HrXHD5Lx3GLl7+e5ZxREVClJvc0
15668173
2492842
2127774
1592252

aspartate aminotransferase (aspB1) [Methanococcus jannaschii]

375

1041

1202

1200

ohLF5H8cOB9R98gbUZGNRmxsLAE	6980405 1B8G 6980404 1B8G	429	E: 2E-6	Ident: 53/250	Ident% 21	Q: 82-300 (375) S: 108-344 (429)	Chain B, 1-Aminocyclopropane-1-Carboxylate Synthase	Pos: 109/250	Gap: 44/250
gHxQ3IT2TFptxc/V64VNDQqOQTc	5107512 1BQA 5107513 1BQA	396	E: 2E-11	Ident: 62/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Chain A, Aspartate Aminotransferase P195a Mutant	Pos: 126/342	Gap: 36/342
drCuFjwkkjjR6+EvUgvMbKR3lP8	14719481 1JG8 14719482 1JG8 14719483 1JG8 14719484 1JG8	347	E: 5E-11	Ident: 63/357	Ident% 17	Q: 37-374 (375) S: 16-343 (347)	Chain A, Crystal Structure Of Threonine Aldolase (Low-Specificity)	Pos: 124/357	Gap: 48/357
s3GlLi6LbAr9Mci+F1AlKcQTkME	1311171 1ARH 1311172 1ARH	396	E: 2E-12	Ident: 63/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Chain A, Aspartate Aminotransferase, Y225rR386A MUTANT	Pos: 127/342	Gap: 36/342
RlUP3PRTeQU74OLipmmIyMzgdtY	11513367 1G7X	396	E: 1E-12	Ident: 62/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Chain A, Aspartate Aminotransferase Active Site Mutant N194aR292LR386L	Pos: 126/342	Gap: 36/342
D91tdRa0+7H2gKj/VonpQbaHdq8	640141 1AIA 640142 1AIA 640145 1AIC 640146 1AIC 640143 1AIB 640144 1AIB	396	E: 1E-12	Ident: 63/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Chain A, Aspartate Aminotransferase (E.C.2.6.1.1) (Holo Form) Mutant With Lys 258 Replaced By His (K258h) Complexed With Pyridoxamine-5'-Phosphate	Pos: 127/342	Gap: 36/342
JytjoighgJ/+gBmng0EhKAfMjRU	11513365 1G7W	396	E: 1E-12	Ident: 63/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Chain A, Aspartate Aminotransferase Active Site Mutant N194aR386L	Pos: 127/342	Gap: 36/342
+O0fUKjFgC4o318GXWCZ/1M+rgM	230414 2AAT	396	E: 1E-12	Ident: 63/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Aspartate Aminotransferase (E.C.2.6.1.1) Mutant K258a Complex With Pyridoxamine Phosphate (PMP)	Pos: 127/342	Gap: 36/342
MpMUPmCqEK6BG734qDkyG9RD1qk	11513598 1G4X	396	E: 1E-12	Ident: 62/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Chain A, Aspartate Aminotransferase Active Site Mutant N194aR292L	Pos: 126/342	Gap: 36/342
8Gv2V2OpHxhqLhJtdffyhcRqGTI	443270 1SPA 515079 1ASC 515078 1ASB	396	E: 2E-12	Ident: 63/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Aspartate Aminotransferase (E.C.2.6.1.1) Mutant With Asp 222 Replaced By Ala (D222a) Reconstructed With N(1)-Methylated Pyridoxal-5'-Phosphate	Pos: 127/342	Gap: 36/342
XXOWx1YGehjQNzRBGGwvKHzNxRw	515082 1ASF 515083 1ASG	396	E: 4E-13	Ident: 63/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Aspartate Aminotransferase (E.C.2.6.1.1) Mutant With Tyr 226 Replaced By Phe (Y226f) And Complexed With Pyridoxal-5'-Phosphate And Sulfate	Pos: 128/342	Gap: 36/342
UDhCZLUNw7nWqgFavYvZsIc5mps	9257157 1QIS	396	E: 1E-13	Ident: 64/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Chain A, Aspartate Aminotransferase From Escherichia Coli, C191f Mutation, With Bound Maleate	Pos: 128/342	Gap: 36/342
tjekh6sC/HOE0HaXtu9EkWJgudI	1127184 1AHX 1127185 1AHX 1127190 1AHF 1127191 1AHF 1127192 1AHE 1127193 1AHE 1127182 1AHY 1127183 1AHY 1127186 1AHG 1127188 1AHG	396	E: 2E-13	Ident: 64/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Chain A, Aspartate Aminotransferase Hexamutant	Pos: 126/342	Gap: 36/342
oSjHF2vTuYqZZNKQiI29DStm4ps	1311169 1ARI 1311170 1ARI	396	E: 2E-13	Ident: 64/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Chain A, Aspartate Aminotransferase, W140h Mutant, Maleate Complex	Pos: 127/342	Gap: 36/342
Dhkg56hgr782H8TpVtbaMUZpFZo	9257158 1QIT	396	E: 2E-13	Ident: 64/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Chain A, Aspartate Aminotransferase From Escherichia Coli, C191w Mutation, With Bound Maleate	Pos: 129/342	Gap: 36/342
Krx0OFqyc6XMLVux5iWbJXw1Im8	442597 1AAM	396	E: 8E-14	Ident: 64/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Aspartate Aminotransferase (E.C.2.6.1.1) Mutant With Arg 292 Replaced By Asp (R292d) Complex With Pyridoxal-5'-Phosphate And Sulfate	Pos: 127/342	Gap: 36/342
B+ukkWeVrKW1dfjeLyqqLBkYB9M	11514255 1B4X 11514273 5EAA	396	E: 4E-14	Ident: 65/342	Ident% 19	Q: 10-315 (375) S: 9-350 (396)	Chain A, Aspartate Aminotransferase From E. Coli, C191s Mutation, With Bound Maleate	Pos: 129/342	Gap: 36/342
2oU6eHNBapXMxHj3Gac1WwrptwE	230800 3AAT	396	E: 4E-14	Ident: 69/371	Ident% 18	Q: 10-344 (375) S: 9-374 (396)	Aspartate Aminotransferase (E.C.2.6.1.1) (Mutant With Arg 386 Replaced By Phe) (R386F) Complex With Pyridoxal-5'-Phosphate And Sulfate	Pos: 135/371	Gap: 41/371
6WhBFC2PNI/UDhtJ+6ABISXA6CI	12084330 1C9C 12084331 1CQ6 12084332 1CQ7 12084333 1CQ8 640164 1ARS 640152 1AMR 1311173 1ARG 1311174 1ARG 515080 1ASD 640151 1AMQ 493833 1ASM 493834 1ASM 515077 1ASA 442601 1AAW 493835 1ASN 493836 1ASN 515081 1ASE 493831 1ASL 493832 1ASL 640153 1AMS	396	E: 7E-14	Ident: 64/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	aspartate aminotransferase [Escherichia coli K12]	Pos: 128/342	Gap: 36/342
w6eRGiF7KfxInSCTRerYPiscGZ0	9257156 1QIR	396	E: 8E-14	Ident: 64/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Chain A, Aspartate Aminotransferase From Escherichia Coli, C191y Mutation, With Bound Maleate	Pos: 128/342	Gap: 36/342
dUxE/fHW1CKXotXNs9Plo3YNJNs	640165 1ART	398	E: 7E-14	Ident: 64/342	Ident% 18	Q: 10-315 (375) S: 9-350 (398)	Aspartate Aminotransferase (E.C.2.6.1.1) Complexed With Pyridoxal-5'-Phosphate And 2-Methylaspartate	Pos: 128/342	Gap: 36/342
5pEUkygwKF1cKHntDBKLu5g7c+8	7245555 1CZE 7245554 1CZC	396	E: 8E-15	Ident: 63/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Chain A, Aspartate Aminotransferase Mutant Atb17139S142N WITH Succinic Acid	Pos: 130/342	Gap: 36/342
ogRNjwTo2lqHuun0hp81SSwmlwc	13786765 1IAX 13786766 1IAX 13786767 1IAY	428	E: 6E-15	Ident: 67/260	Ident% 25	Q: 55-291 (375) S: 78-328 (428)	Chain A, Crystal Structure Of Acc Synthase Complexed With Plp	Pos: 124/260	Gap: 32/260
JkwqZ/v6aB4/Mpzkj7rqTUP98RU	4388895 1YOO	396	E: 9E-15	Ident: 62/342	Ident% 18	Q: 10-315 (375) S: 9-350 (396)	Aspartate Aminotransferase Mutant Atb17 With Isovaleric Acid	Pos: 129/342	Gap: 36/342
h/njSI9CWOVVjuNBa5Cbwc1A8qI	14278152 1FC4 14278153 1FC4	401	E: 1E-17	Ident: 50/367	Ident% 13	Q: 21-373 (375) S: 43-393 (401)	Chain A, 2-Amino-3-Ketobutyrate Coa Ligase	Pos: 110/367	Gap: 30/367
dXwRA/kDPpzUpF1QjSlGeJE25gQ	3660282 1YAA 3660283 1YAA 3660284 1YAA 3660285 1YAA	412	E: 2E-21	Ident: 61/419	Ident% 14	Q: 2-374 (375) S: 4-408 (412)	Chain A, Aspartate Aminotransferase From Saccharomyces Cerevisiae Cytoplasm	Pos: 126/419	Gap: 60/419
iA0yc7LdsUWoyX8k+1tHx2048u0	6137419 1BW0 6137418 1BW0	416	E: 9E-22	Ident: 78/323	Ident% 24	Q: 26-323 (375) S: 36-357 (416)	Chain B, Crystal Structure Of Tyrosine Aminotransferase From Trypanosoma Cruzi	Pos: 149/323	Gap: 26/323
Y75wiOEQ7h6YYfHcJcRx5kEzle0	2392159 1AJS 2392156 1AJR 2392157 1AJR	412	E: 1E-23	Ident: 53/367	Ident% 14	Q: 14-340 (375) S: 21-383 (412)	Chain B, Refinement And Comparison Of The Crystal Structures Of Pig Cytosolic Aspartate Aminotransferase And Its Complex With 2-Methylaspartate	Pos: 113/367	Gap: 44/367
3Rq42uMCHJG6dJrsBhwNCEYEzD4	229661 1AAT	411	E: 3E-24	Ident: 63/417	Ident% 15	Q: 2-374 (375) S: 4-407 (411)	Cytosolic Aspartate Aminotransferase (E.C.2.6.1.1) Complex With 2-Oxo-Glutaric Acid	Pos: 131/417	Gap: 57/417
4f3BrVveYoNeb8uD+4i+g0iObFc	2392158 1AJS	412	E: 2E-24	Ident: 54/367	Ident% 14	Q: 14-340 (375) S: 21-383 (412)	Chain A, Refinement And Comparison Of The Crystal Structures Of Pig Cytosolic Aspartate Aminotransferase And Its Complex With 2-Methylaspartate	Pos: 114/367	Gap: 44/367
OJVm9kV5SZiIlYIaSv5/eTCZA+M	809192 2CST 809193 2CST	411	E: 6E-24	Ident: 63/417	Ident% 15	Q: 2-374 (375) S: 4-407 (411)	Chain A, Aspartate Aminotransferase (Caspat) (E.C.2.6.1.1) Complexed With Pyridoxal-5'-Phosphate And Maleate	Pos: 133/417	Gap: 57/417
Z8x29SoBVLzmgn3ow+xiwazk1hc	5107514 1BQD 5107515 1BQD	396	E: 2E-25	Ident: 65/411	Ident% 15	Q: 1-374 (375) S: 1-396 (396)	Chain A, Aspartate Aminotransferase P138aP195A DOUBLE MUTANT	Pos: 134/411	Gap: 52/411
n5jGv6jOfqoxyKnRZiiVimlpAjU	443542 7AAT 443543 7AAT 494624 1TAR 494625 1TAR 443572 9AAT 443573 9AAT 1633522 1OXO 1633523 1OXO 443556 8AAT 443557 8AAT 442634 1AMA 494312 1MAQ 2392380 1IVR 494311 1MAP 1633521 1OXP 494626 1TAS 494627 1TAS 494628 1TAT 494629 1TAT	401	E: 2E-25	Ident: 54/346	Ident% 15	Q: 10-327 (375) S: 11-354 (401)	Chain A, Aspartate Aminotransferase (E.C.2.6.1.1) Complex With Pyridoxal-5'-Phosphate At Ph 7.5	Pos: 119/346	Gap: 30/346
mv4okDRFYzPznF0FRmwLW6vxdjo	5822524 3TAT 5822525 3TAT 5822526 3TAT 5822527 3TAT 5822528 3TAT 5822529 3TAT	397	E: 9E-27	Ident: 65/381	Ident% 17	Q: 1-341 (375) S: 1-380 (397)	tyrosine aminotransferase, tyrosine repressible [Escherichia coli K12]	Pos: 127/381	Gap: 41/381
mrph4Dyg+WyKmN+42Q/k5c0UfNo	11513597 1G4V	396	E: 7E-27	Ident: 66/411	Ident% 16	Q: 1-374 (375) S: 1-396 (396)	Chain A, Aspartate Aminotransferase Active Site Mutant N194aY225F	Pos: 136/411	Gap: 52/411
P5sd/O6B5cW+aJHpLbOuWX8Xxu4	18655496 1KUS	364	E: 1E-31	Ident: 62/368	Ident% 16	Q: 14-374 (375) S: 12-357 (364)	Chain A, The Three-Dimensional Structure Of L-Threonine-O-3- Phosphate Decarboxylase From Salmonella Enterica (Cobd)	Pos: 135/368	Gap: 29/368
I/EfOzHgu1yHb8NMDM516rPUBQo	15826678 1FG3 15826679 1FG7	356	E: 2E-39	Ident: 57/298	Ident% 19	Q: 67-361 (375) S: 61-343 (356)	Chain A, Crystal Structure Of L-Histidinol Phosphate Aminotransferase Complexed With L-Histidinol	Pos: 122/298	Gap: 18/298
kcfwUY1Nxj/qDoUfH0OQPsZ8QQM	14278468 1GEW 14278469 1GEX 14278520 1GEY 15826616 1IJI	356	E: 8E-40	Ident: 58/298	Ident% 19	Q: 67-361 (375) S: 61-343 (356)	histidinol-phosphate aminotransferase [Escherichia coli K12]	Pos: 117/298	Gap: 18/298
wtp4lBsihJtwBO8bhEvrV/1fe6o	9955069 1C7N 9955070 1C7N 9955071 1C7N 9955072 1C7N 9955073 1C7N 9955074 1C7N 9955075 1C7N 9955076 1C7N 9955077 1C7O 9955078 1C7O 9955079 1C7O 9955080 1C7O 9955081 1C7O 9955082 1C7O 9955083 1C7O 9955084 1C7O	399	E: 4E-41	Ident: 74/368	Ident% 20	Q: 22-375 (375) S: 30-391 (399)	Chain A, Crystal Structure Of Cystalysin From Treponema Denticola Contains A Pyridoxal 5'-Phosphate Cofactor	Pos: 158/368	Gap: 20/368
GL4upeJtZcOqzxk6pjwbKzogexQ	6980640 1D2F 6980639 1D2F	390	E: 5E-53	Ident: 71/363	Ident% 19	Q: 21-370 (375) S: 26-382 (390)	enzyme that may degrade or block biosynthesis of endogenous mal inducer, probably aminotrasferase [Escherichia coli K12]	Pos: 153/363	Gap: 19/363
XKHYQGc0Lc3414IoC1jiWRBfO88	5821836 1BJW 5821837 1BJW	382	E: 3E-69	Ident: 147/380	Ident% 38	Q: 2-367 (375) S: 4-375 (382)	Chain A, Aspartate Aminotransferase From Thermus Thermophilus	Pos: 220/380	Gap: 22/380
9aJ1OTTTmR0pUhLKzdeWrkW2dRQ	5821839 1BKG 5821840 1BKG 5821841 1BKG 5821842 1BKG	385	E: 7E-70	Ident: 148/380	Ident% 38	Q: 2-367 (375) S: 4-375 (385)	ASPARTATE AMINOTRANSFERASE (TRANSAMINASE A) (ASPAT)	Pos: 221/380	Gap: 22/380
iukf7T5MyibqAm7irZnekB2LVHQ	17942613 1GCK 17942614 1GCK	385	E: 2E-70	Ident: 149/380	Ident% 39	Q: 2-367 (375) S: 4-375 (385)	Chain A, Thermus Thermophilus Aspartate Aminotransferase Double Mutant 1 Complexed With Aspartate	Pos: 223/380	Gap: 22/380
reEHGK1K7q8aPRrAaPsXYutdj9c	15826454 1GC3 15826455 1GC3 15826456 1GC3 15826457 1GC3 15826458 1GC3 15826459 1GC3 15826460 1GC3 15826461 1GC3 15826462 1GC4 15826463 1GC4 15826464 1GC4 15826465 1GC4	385	E: 2E-70	Ident: 148/380	Ident% 38	Q: 2-367 (375) S: 4-375 (385)	Chain A, Thermus Thermophilus Aspartate Aminotransferase Tetra Mutant 2 Complexed With Tryptophan	Pos: 223/380	Gap: 22/380
Jo+xdQnKoZhXXYJH/sJpngRUxqs	14278621 1DJU 14278622 1DJU	388	E: 1E-77	Ident: 161/388	Ident% 41	Q: 2-375 (375) S: 2-383 (388)	Chain A, Crystal Structure Of Aromatic Aminotransferase From Pyrococcus Horikoshii Ot3	Pos: 241/388	Gap: 20/388
XkWRXJzNfcfCM8fechNEwydT0Kg	15988223 1GDE 15988224 1GDE 15988238 1GD9 15988239 1GD9	389	E: 9E-78	Ident: 161/388	Ident% 41	Q: 2-375 (375) S: 3-384 (389)	aspartate aminotransferase [Pyrococcus horikoshii]	Pos: 241/388	Gap: 20/388

yssLYKjsljfYJnMWy/NMc8/i1TI
15668174
2495732
2128074
1498759

M. jannaschii predicted coding region MJ0002 [Methanococcus jannaschii]

243

0RRSa/IUgB8cGJLVI5LSrgSbpS4
15668175
2495733
2128075
1498760

M. jannaschii predicted coding region MJ0003 [Methanococcus jannaschii]

156

vRFp0E5dVjjpXhtlEwlXL0AP/F0
15668176
2495734
2127708
1590817

(R)-2-hydroxyglutaryl-CoA dehydratase activator [Methanococcus jannaschii]

243

294

316

bfRvFJW7PL4H1rgKKRgM6zI4Ob0

13786981 1HUX
13786982 1HUX

270

E: 1E-73

Ident: 89/247

Ident% 36

Q: 2-239 (243) S: 5-249 (270)

Chain A, Crystal Structure Of The Acidaminococcus Fermentans (R)-2- Hydroxyglutaryl-Coa Dehydratase Component A

Pos: 139/247

Gap: 11/247

dAHAjoA7LQB1RcMGWVt7jw8tnFE
15668177
2494429
2127908
1590818

formate dehydrogenase, beta subunit [Methanococcus jannaschii]

379

172

548

1242

VzH5n6t+6j1FiRcfHsybOkdExyA	18158649 1KEK 18158650 1KEK 4558091 1B0P 4558092 1B0P 4558221 2PDA 4558222 2PDA	1231	E: 3.8E0	Ident: 20/83	Ident% 24	Q: 269-341 (379) S: 679-755 (1231)	Chain A, Crystal Structure Of The Free Radical Intermediate Of Pyruvate:ferredoxin Oxidoreductase	Pos: 32/83	Gap: 16/83
iMyNepb8nMkabZXk9/tTA9EaMzA	4139441 1FEH 6730137 1C4A 6730138 1C4C	574	E: .08E0	Ident: 21/107	Ident% 19	Q: 242-342 (379) S: 108-202 (574)	PERIPLASMIC [FE] HYDROGENASE 1	Pos: 39/107	Gap: 18/107
yQysezpIgy5EXPkgq9y3NH3Gpgo	6729719 1BQX 6729750 1BWE	77	E: 9.2E0	Ident: 20/75	Ident% 26	Q: 280-352 (379) S: 8-57 (77)	Chain A, Artificial Fe8s8 Ferredoxin: The D13c Variant Of Bacillus Schlegelii Fe7s8 Ferredoxin	Pos: 30/75	Gap: 27/75
5xSPy+cFzzfqHehaKELq/fFwonw	1310890 1CLF	55	E: .23E0	Ident: 14/70	Ident% 20	Q: 277-346 (379) S: 5-53 (55)	Clostridium Pasteurianum Ferredoxin	Pos: 24/70	Gap: 21/70
CgruAQnSEgW+lL5k+XYzHmwctEk	7546410 1DUR	55	E: .24E0	Ident: 17/68	Ident% 25	Q: 278-345 (379) S: 6-51 (55)	ferredoxin 2[4Fe-4S] [validated] - Peptostreptococcus asaccharolyticus	Pos: 25/68	Gap: 22/68
qxiEu8o08o1qDoLq6yI134Srrrg	4930042 1HFE 4930044 1HFE	421	E: .093E0	Ident: 17/65	Ident% 26	Q: 279-343 (379) S: 34-79 (421)	PERIPLASMIC [FE] HYDROGENASE LARGE SUBUNIT (FE HYDROGENLYASE)	Pos: 21/65	Gap: 19/65
2xxTpjvmscJ469r9dxRPOLjaLsc	3318893 1BD6	77	E: 9.2E0	Ident: 15/75	Ident% 20	Q: 278-350 (379) S: 6-59 (77)	7-Fe Ferredoxin From Bacillus Schlegelii, Nmr, Minimized Average Structure	Pos: 20/75	Gap: 23/75
nf4y4bxj9elJZrW7KKNrL67NMOs	13399647 1H7W 13399648 1H7W 13399649 1H7W 13399650 1H7W 13399647 1H7W 13399648 1H7W 13399649 1H7W 13399650 1H7W	1025	E: 5.2E0	Ident: 9/45	Ident% 20	Q: 266-309 (379) S: 972-1016 (1025)	Chain A, Dihydropyrimidine Dehydrogenase (Dpd) From Pig	Pos: 16/45	Gap: 1/45
g2pwKD1gqMG5wMsDpC0bBSKM3oI	3114424 2FDN 640397 1FDN	55	E: 4.6E0	Ident: 17/67	Ident% 25	Q: 280-346 (379) S: 8-53 (55)	FERREDOXIN	Pos: 24/67	Gap: 21/67
SOPRvn2QaOUjkvQ5O3SLtRBKRyQ	15825930 1JB0	80	E: .002E0	Ident: 17/67	Ident% 25	Q: 277-343 (379) S: 7-60 (80)	Chain C, Crystal Structure Of Photosystem I: A Photosynthetic Reaction Center And Core Antenna System From Cyanobacteria	Pos: 24/67	Gap: 13/67
GEAQAaM8LuOiwqWmvUIP/ujr8Xw	1065197 1FCA	55	E: 9.3E0	Ident: 19/67	Ident% 28	Q: 280-346 (379) S: 8-53 (55)	Ferredoxin	Pos: 26/67	Gap: 21/67
fFNH9v5dE+qaDKIs3YFhzTaIlxY	5542236 1FUM 5542240 1FUM	243	E: 6.6E0	Ident: 17/78	Ident% 21	Q: 277-347 (379) S: 145-221 (243)	Chain B, Structure Of The E. Coli Fumarate Reductase Respiratory Complex	Pos: 26/78	Gap: 8/78
Q125RpMho9EZQi8VTwB6VThNPNw	3318886 1BC6	77	E: 8.6E0	Ident: 15/75	Ident% 20	Q: 278-350 (379) S: 6-59 (77)	7-Fe Ferredoxin From Bacillus Schlegelii, Nmr, 20 Structures	Pos: 20/75	Gap: 23/75
8ymp5ZKp2+2BBBERbg3oODedPNk	2554684 1XER	103	E: .046E0	Ident: 15/68	Ident% 22	Q: 276-342 (379) S: 41-95 (103)	Structure Of Ferredoxin	Pos: 24/68	Gap: 14/68
uSp4lyNDaZPY+UVPBME4WnK5nzc	13399651 1H7X 13399652 1H7X 13399653 1H7X 13399654 1H7X 13399651 1H7X 13399652 1H7X 13399653 1H7X 13399654 1H7X	1025	E: 5E0	Ident: 9/45	Ident% 20	Q: 266-309 (379) S: 972-1016 (1025)	Chain A, Dihydropyrimidine Dehydrogenase (Dpd) From Pig, Ternary Complex Of A Mutant Enzyme (C671a), Nadph And 5-Fluorouracil	Pos: 16/45	Gap: 1/45
6RNObzCsQZH9QGgMNOD/Mu3sPwM	14278676 1E7P 14278679 1E7P 14278682 1E7P 14278685 1E7P 6730465 1QLA 6730468 1QLA 6730471 1QLB 6730474 1QLB	239	E: 1E-4	Ident: 35/208	Ident% 16	Q: 178-357 (379) S: 55-235 (239)	Fumarate reductase iron-sulfur protein	Pos: 63/208	Gap: 55/208

USMo9IP13ZW9L/r/PpAe7HrWgts
15668178
2497966
2127906
1498763

formate dehydrogenase, alpha subunit [Methanococcus jannaschii]

378

557

839

898

ORzYqtxvJkYlNB7B+7nZpYV8EEg	2392333 1FDO 2392332 1FDI 2392039 1AA6 2392333 1FDO 2392332 1FDI 2392039 1AA6 2392333 1FDO 2392332 1FDI 2392039 1AA6	715	E: .9E0	Ident: 26/162	Ident% 16	Q: 158-307 (378) S: 54-213 (715)	Oxidized Form Of Formate Dehydrogenase H From E. Coli	Pos: 53/162	Gap: 14/162
H8ID5u8jlOaIydqZOaUWP08FaDc	9954924 1EU1 9954924 1EU1 9954924 1EU1	780	E: .8E0	Ident: 17/50	Ident% 34	Q: 53-87 (378) S: 49-98 (780)	Chain A, The Crystal Structure Of Rhodobacter Sphaeroides Dimethylsulfoxide Reductase Reveals Two Distinct Molybdenum Coordination Environments	Pos: 24/50	Gap: 15/50
DVo5gQHYz7Kvd67OLH+AlvvCbUI	14278228 1ICI 14278229 1ICI	256	E: 4.6E0	Ident: 12/60	Ident% 20	Q: 141-200 (378) S: 184-241 (256)	Chain A, Crystal Structure Of A Sir2 Homolog-Nad Complex	Pos: 25/60	Gap: 2/60
6NnR4ymDzHMwlDG/4UKXj3Nx6tA	6137474 2NAP 6137474 2NAP	723	E: 6E-4	Ident: 24/70	Ident% 34	Q: 302-368 (378) S: 451-520 (723)	Chain A, Dissimilatory Nitrate Reductase (Nap) From Desulfovibrio Desulfuricans	Pos: 35/70	Gap: 3/70
8w8z9uHy1KOV1r08SECOgrivDpo	10120735 1E5V 10120736 1E5V 2981779 1DMR 2981904 3DMR 2981898 2DMR 10120735 1E5V 10120736 1E5V 2981779 1DMR 2981904 3DMR 2981898 2DMR	823	E: 1E-4	Ident: 36/110	Ident% 32	Q: 269-367 (378) S: 468-575 (823)	Chain A, Oxidized Dmso Reductase Exposed To Hepes Buffer	Pos: 53/110	Gap: 13/110
yuuYUyWmLRoetNkCcPrCz9/qVUU	10120737 1E60 10120738 1E60 10120739 1E61 10120740 1E61 10120737 1E60 10120738 1E60 10120739 1E61 10120740 1E61	823	E: 1E-4	Ident: 36/110	Ident% 32	Q: 269-367 (378) S: 468-575 (823)	Chain A, Oxidized Dmso Reductase Exposed To Hepes - Structure Ii Buffer	Pos: 53/110	Gap: 13/110
noOJC/APTXG2dikgGBjwaMMOoh4	2981909 4DMR 2981909 4DMR	823	E: 1E-4	Ident: 36/110	Ident% 32	Q: 269-367 (378) S: 468-575 (823)	Reduced Dmso Reductase From Rhodobacter Capsulatus With Bound Dmso Substrate	Pos: 53/110	Gap: 13/110
k4bo4EClIdlvI4jDH4y4XExSx/o	3318672 1DMS 3318672 1DMS	781	E: 3E-4	Ident: 35/110	Ident% 31	Q: 269-367 (378) S: 426-533 (781)	Structure Of Dmso Reductase	Pos: 53/110	Gap: 13/110
INHGFuM/BUeYAj7/cj2R0H05Dms	9257120 1E18 9257120 1E18	823	E: 2E-4	Ident: 36/110	Ident% 32	Q: 269-367 (378) S: 468-575 (823)	Chain A, Tungsten-Susbstituted Dmso Reductase From Rhodobacter Capsulatus	Pos: 53/110	Gap: 13/110
6iMgA68hCKyADDpScehcQDC1U7I	12084495 1G8J 12084497 1G8J 12084495 1G8J 12084497 1G8J	825	E: 3E-11	Ident: 29/154	Ident% 18	Q: 233-371 (378) S: 454-604 (825)	Chain A, Crystal Structure Analysis Of Arsenite Oxidase From Alcaligenes Faecalis	Pos: 51/154	Gap: 18/154
zkCfS+rPYloj48jagG0Dp9LnvsE	12084499 1G8K 12084501 1G8K 12084503 1G8K 12084505 1G8K 12084499 1G8K 12084501 1G8K 12084503 1G8K 12084505 1G8K	825	E: 3E-11	Ident: 29/154	Ident% 18	Q: 233-371 (378) S: 454-604 (825)	Chain A, Crystal Structure Analysis Of Arsenite Oxidase From Alcaligenes Faecalis	Pos: 51/154	Gap: 18/154
af2Z1bQsiqO5L/M/p9RLoPfskos	4699615 1TMO 4699615 1TMO	829	E: 1E-18	Ident: 27/132	Ident% 20	Q: 252-372 (378) S: 449-578 (829)	TRIMETHYLAMINE-N-OXIDE REDUCTASE PRECURSOR (TMAO REDUCTASE) (TRIMETHYLAMINE OXIDASE)	Pos: 53/132	Gap: 13/132

GpBJwuHbh1sJIq9OAhAsaewMdrE
15668179
2495735
2127712
1592253

2-hydroxyglutaryl-CoA dehydratase, subunit beta (hgdB) [Methanococcus jannaschii]

373

1
32-54

FfVMwb1e6OtGGmK+vXGV1YGmB4Y
15668180
2495736
2128076
1592254

M. jannaschii predicted coding region MJ0008 [Methanococcus jannaschii]

220

6oqYk4biwFAmm/CQJzUKrxIeOog
15668181
2495737
2128077
1498767

M. jannaschii predicted coding region MJ0009 [Methanococcus jannaschii]

276

vMLqx16Sz0byxVzC1PUAiRzI8mo
15668182
2495738
2129193
1590821

BcpC phosphonopyruvate decarboxylase [Methanococcus jannaschii]

428

190

226

3KHdf/vEliPuG4JwdLroQhKZiis

13399528 1EJJ
14278698 1EQJ

511

E: 2E-6

Ident: 23/91

Ident% 25

Q: 287-367 (428) S: 387-477 (511)

Chain A, Crystal Structural Analysis Of Phosphoglycerate Mutase Cocrystallized With 3-Phosphoglycerate

Pos: 38/91

Gap: 10/91

S6bSylyWyiIG+TOt8bpK1Sofsck
15668183
2495739
2128078
1590822

M. jannaschii predicted coding region MJ0011 [Methanococcus jannaschii]

197

0CvwWQUVUQCfkh155dz4OPmWbDQ
15668184
2495741
2128080
1498771

M. jannaschii predicted coding region MJ0013 [Methanococcus jannaschii]

162

c1z4McfPWVVQIk3dwdxcyvtNx4A
15668185
2495742
2128081
1590824

conserved hypothetical protein [Methanococcus jannaschii]

213

459

724

Cks4rrta5g4JevpCGErajDz+GaQ	1421516 1GDT 1421517 1GDT	183	E: .002E0	Ident: 34/123	Ident% 27	Q: 63-182 (213) S: 2-115 (183)	100 pct identical to gp:ECOTNPA_2[gamma delta resolvase(Tn1000)] [Plasmid F]	Pos: 62/123	Gap: 12/123
U5OGwd/Nfhdv74e3A5gtl3wFoes	15825913 1GHT 18655826 1HX7	105	E: .002E0	Ident: 30/109	Ident% 27	Q: 63-168 (213) S: 2-102 (105)	Chain A, Solution Structure Of The Catalytic Domain Of Gamma Delta Resolvase	Pos: 53/109	Gap: 11/109
4hUfNnt0swoOKzY0MXeUUGYuBOc	515293 2RSL 515294 2RSL 515292 2RSL 515128 1GDR	140	E: .003E0	Ident: 34/123	Ident% 27	Q: 63-182 (213) S: 2-115 (140)	Chain B, Gamma Delta Resolvase (Large Fragment, Catalytic Domain)	Pos: 62/123	Gap: 12/123
lGsStdQxpSYdAskUt5QpBWp1F6w	13096363 1EXI 13096365 1EXJ	278	E: .17E0	Ident: 17/57	Ident% 29	Q: 4-58 (213) S: 2-58 (278)	Chain A, Crystal Structure Of Transcription Activator Bmrr, From B. Subtilis, Bound To 21 Base Pair Bmr Operator And Tpsb	Pos: 28/57	Gap: 2/57
3Qz7WQ8Pec92/wnLKZKNtzL9plY	17942827 1JBG	109	E: .01E0	Ident: 14/47	Ident% 29	Q: 8-53 (213) S: 3-49 (109)	Chain A, Crystal Structure Of Mtan, The Bacillus Subtilis Multidrug Transporter Activator, N-Terminus	Pos: 27/47	Gap: 1/47

y7QOQo+pHgscclTQiKpoqqAUVQE
15668186
2495743
2128082
1590825

conserved hypothetical protein [Methanococcus jannaschii]

124

x5+U+7xEPehLfDwh0TQYImMKKoI
15668187
15669818
2495744
2128083
1498774
2826441

M. jannaschii predicted coding region MJ0016 [Methanococcus jannaschii]

*TARGET
Z9yfspqFnQM2QCG7kPSk6HcWIyc
15668188
2495745
2129326
1498775

transposase, similar to IS240 [Methanococcus jannaschii]

214

120

516

1173

o1/riZWMpH7d8z0NVvsRlwhcE2c
15668189
2495746
2128084
1498776

M. jannaschii predicted coding region MJ0018 [Methanococcus jannaschii]

524

1
10-32

*TARGET
dt7qY89QOpxD5UvSA8Jmuk3P+yY
15668190
2499483
2128085
1498777

Glu-tRNA amidotransferase (gatB) [Methanococcus jannaschii]

630

184

267

231

0rVcRBVt2mexXUHJyu1uBSg5FoA
15668191
2492981
2129091
1592255

asparaginase (ansA) [Methanococcus jannaschii]

417

206

240

260

Fq7XCjKIbdkwqoyi61KoMwOufdw	809338 3PGA 809339 3PGA 809340 3PGA 809341 3PGA 809338 3PGA 809339 3PGA 809340 3PGA 809341 3PGA	337	E: 3E-14	Ident: 65/188	Ident% 34	Q: 72-248 (417) S: 8-184 (337)	Chain 1, Glutaminase-Asparaginase (E.C.3.5.1.1) (Amidohydrolase, Asparaginase)	Pos: 92/188	Gap: 22/188
vDAr+YwlWuNrENqcIa1hyxfUeNk	6980434 1DJP 6980435 1DJP 6980432 1DJO 6980433 1DJO 6980434 1DJP 6980435 1DJP 6980432 1DJO 6980433 1DJO	330	E: 9E-15	Ident: 66/188	Ident% 35	Q: 72-248 (417) S: 1-177 (330)	Chain A, Crystal Structure Of Pseudomonas 7a Glutaminase- Asparaginase With The Inhibitor Don Covalently Bound In The Active Site	Pos: 94/188	Gap: 22/188
N0vVMvcO8bChdUhGDAlfOsk7cCg	2392795 4PGA 2392796 4PGA 2392795 4PGA 2392796 4PGA	337	E: 1E-15	Ident: 67/193	Ident% 34	Q: 67-248 (417) S: 3-184 (337)	Chain A, Glutaminase-Asparaginase From Pseudomonas 7a	Pos: 97/193	Gap: 22/193
dPiKdryJDWSCfkS8RfOrhEUpIBE	809177 1AGX 809177 1AGX	331	E: 1E-18	Ident: 94/345	Ident% 27	Q: 76-401 (417) S: 4-326 (331)	GLUTAMINASE-ASPARAGINASE	Pos: 158/345	Gap: 41/345
B35nudwhKWrLb9lHuPZBIi/6ImI	12084598 1HFJ 12084599 1HFJ 12084600 1HFK 12084601 1HFK 15825842 1HFW 15825843 1HFW 15825844 1HFW 15825845 1HFW 15825846 1HG0 15825847 1HG0 15825848 1HG0 15825849 1HG0 15825850 1HG1 15825851 1HG1 15825852 1HG1 15825853 1HG1 18158634 1JSL 18158635 1JSL 18158636 1JSL 18158637 1JSL 18158638 1JSR 18158639 1JSR 18158640 1JSR 18158641 1JSR 12084598 1HFJ 12084599 1HFJ 12084600 1HFK 12084601 1HFK 15825842 1HFW 15825843 1HFW 15825844 1HFW 15825845 1HFW 15825846 1HG0 15825847 1HG0 15825848 1HG0 15825849 1HG0 15825850 1HG1 15825851 1HG1 15825852 1HG1 15825853 1HG1 18158634 1JSL 18158635 1JSL 18158636 1JSL 18158637 1JSL 18158638 1JSR 18158639 1JSR 18158640 1JSR 18158641 1JSR	327	E: 1E-22	Ident: 92/296	Ident% 31	Q: 71-353 (417) S: 2-284 (327)	Chain A, Asparaginase From Erwinia Chrysanthemi, Hexagonal Form With Sulfate	Pos: 142/296	Gap: 26/296
Ty+TTJnoRtj5XcPclXxpAcOrv4k	2098425 1WSA 2098424 1WSA 2098425 1WSA 2098424 1WSA	330	E: 2E-25	Ident: 96/325	Ident% 29	Q: 76-388 (417) S: 6-314 (330)	L-asparaginase (L-asparagine amidohydrolase) (L-ASNase)	Pos: 162/325	Gap: 28/325
FKAfvrSTJna7swypstldwj6e0t0	443453 3ECA 443455 3ECA 443457 3ECA 443459 3ECA 443453 3ECA 443455 3ECA 443457 3ECA 443459 3ECA	326	E: 2E-28	Ident: 108/342	Ident% 31	Q: 73-402 (417) S: 1-325 (326)	Chain A, Asparaginase Type Ii (E.C.3.5.1.1) (Eca)	Pos: 171/342	Gap: 29/342
UNV5wc4Zk6gw0d0VttsediPUf60	2392782 4ECA 2392783 4ECA 2392784 4ECA 2392785 4ECA 2392782 4ECA 2392783 4ECA 2392784 4ECA 2392785 4ECA	326	E: 1E-28	Ident: 106/342	Ident% 30	Q: 73-402 (417) S: 1-325 (326)	Chain A, Asparaginase From E. Coli, Mutant T89v With Covalently Bound Aspartate	Pos: 169/342	Gap: 29/342
ZR+Ii2H+RXR8ncG91dl8Oj4jdfk	13399487 1HO3 13399488 1HO3 13399487 1HO3 13399488 1HO3	326	E: 7E-28	Ident: 107/342	Ident% 31	Q: 73-402 (417) S: 1-325 (326)	Chain A, Crystal Structure Analysis Of E. Coli L-Asparaginase Ii (Y25f Mutant)	Pos: 171/342	Gap: 29/342

bSnfCRtynU8fjwZN88rXFIxVSS0
15668192
2500057
2128086
1498780

conserved hypothetical protein [Methanococcus jannaschii]

375

417

857

v4ATo4+Ge+q27kVj8F36bTEu2Gw	18158903 1KEE 18158905 1KEE 18158907 1KEE 18158909 1KEE 4929935 1BXR 4929937 1BXR 4929939 1BXR 4929941 1BXR 3318829 1JDB 6730187 1CS0 6730189 1CS0 6730191 1CS0 6730193 1CS0 6730116 1C30 6730118 1C30 6730120 1C30 6730122 1C30 6730126 1C3O 6730128 1C3O 6730130 1C3O 6730132 1C3O 3318817 1JDB 3318821 1JDB 3318825 1JDB	1073	E: 1.1E0	Ident: 11/104	Ident% 10	Q: 88-179 (375) S: 619-716 (1073)	carbamoyl-phosphate synthase large subunit [Escherichia coli K12]	Pos: 31/104	Gap: 18/104
OAFz1nQovRbK4W7vpGOU9QIDPpo	5821976 1CE8 5821978 1CE8 5821980 1CE8 5821982 1CE8	1073	E: 1.1E0	Ident: 11/104	Ident% 10	Q: 88-179 (375) S: 619-716 (1073)	Chain A, Carbamoyl Phosphate Synthetase From Escherichis Coli With Complexed With The Allosteric Ligand Imp	Pos: 31/104	Gap: 18/104
potEbycYVN6+6+FUdxgmXLLd4J8	3891747 1A9X 3891749 1A9X 3891751 1A9X 3891753 1A9X	1058	E: 1.7E0	Ident: 10/102	Ident% 9	Q: 88-177 (375) S: 619-714 (1058)	Chain A, Carbamoyl Phosphate Synthetase: Caught In The Act Of Glutamine Hydrolysis	Pos: 30/102	Gap: 18/102

wWH0uL0cQ8Ob84kvHHzkMF3cH8Q
15668193
2495747
2127815
1592256

cobalamin biosynthesis protein (cbiD) [Methanococcus jannaschii]

362

2EPhBwFFwoqd31KWQph/wxtQvU8
15668194
2495748
2128087
1498782

M. jannaschii predicted coding region MJ0023 [Methanococcus jannaschii]

118

1
92-114

dDEZnDNT7P4fY68KTF+163psAN0
15668195
2495749
2128088
1498783

conserved hypothetical protein [Methanococcus jannaschii]

139

XF26xuXDBfxNDZdYnz0E+DWLjVs
15668196
2500652
2128089
1498784

hypothetical protein [Methanococcus jannaschii]

338

kzcccX3WTL9N0f0Oimv2QotDLD8	13096161 1G6S 13096162 1G6T	427	E: 3.1E0	Ident: 19/72	Ident% 26	Q: 80-150 (338) S: 155-216 (427)	5-enolpyruvylshikimate-3-phosphate synthetase [Escherichia coli O157:H7 EDL933]	Pos: 33/72	Gap: 11/72
Xmoo6GfrpR56e4tLRlXjQZ7cPfQ	442878 1EPS	427	E: 3.1E0	Ident: 19/72	Ident% 26	Q: 80-150 (338) S: 155-216 (427)	5-Enol-Pyruvyl-3-Phosphate Synthase (E.C.2.5.1.9)	Pos: 33/72	Gap: 11/72
z1p83jIZAFQFz193EfzQeaJQruA	6980699 1QMI 6980700 1QMI 6980701 1QMI 6980702 1QMI	347	E: 1E-110	Ident: 112/324	Ident% 34	Q: 4-324 (338) S: 6-329 (347)	Chain A, Crystal Structure Of Rna 3'-Terminal Phosphate Cyclase, An Ubiquitous Enzyme With Unusual Topology	Pos: 169/324	Gap: 3/324
D/RMv3TjEvx1mSdx2sqAe396bzc	6980698 1QMH 6980697 1QMH	347	E: 1E-112	Ident: 112/325	Ident% 34	Q: 3-324 (338) S: 5-329 (347)	Chain B, Crystal Structure Of Rna 3'-Terminal Phosphate Cyclase, An Ubiquitous Enzyme With Unusual Topology	Pos: 170/325	Gap: 3/325

O1yK63DqJYiEjljMqR+8VN89RlQ
15668197
2500953
2127710
1592257

proliferating-cell nucleolar antigen, FMU/NOL1/NOP2 family [Methanococcus jannaschii]

274

176

690

1221

5yacVXeX24KA2VAxDdq6jBcMkd4	9955209 1DUS	194	E: .006E0	Ident: 34/193	Ident% 17	Q: 17-207 (274) S: 6-153 (194)	Chain A, Mj0882-A Hypothetical Protein From M. Jannaschii	Pos: 70/193	Gap: 47/193
vA+2H/nVRtry7DbEZBMzWESzqAU	12084575 1DL5 12084576 1DL5	317	E: 2E0	Ident: 15/56	Ident% 26	Q: 87-142 (274) S: 79-134 (317)	L-isoaspartate(D-aspartate) O-methyltransferase [Thermotoga maritima]	Pos: 31/56	Gap: -1/-1
lM2+ripCwRk/MZZDqFHy17GXCMQ	17942640 1JG4 17942641 1JG3 17942642 1JG3 17942645 1JG2 17942646 1JG1	235	E: .53E0	Ident: 31/163	Ident% 19	Q: 11-164 (274) S: 20-166 (235)	Chain A, Crystal Structure Of L-Isoaspartyl (D-Aspartyl) O- Methyltransferase With S-Adenosylmethionine	Pos: 63/163	Gap: 25/163
sdLvp9C2Zy6Jo9DOLsgrTNL4ftA	1942357 1AQJ 1942356 1AQJ	421	E: .92E0	Ident: 27/168	Ident% 16	Q: 74-229 (274) S: 31-183 (421)	MODIFICATION METHYLASE TAQI (ADENINE-SPECIFIC METHYLTRANSFERASE TAQI) (M.TAQI)	Pos: 49/168	Gap: 27/168
tdDIHGJll8WLyentzVrJ4a2dJF8	10120640 1EIZ 10120641 1EJ0	180	E: .6E0	Ident: 15/76	Ident% 19	Q: 82-143 (274) S: 21-96 (180)	Chain A, Ftsj Rna Methyltransferase Complexed With S- Adenosylmethionine	Pos: 33/76	Gap: 14/76
hi8Q6/nV02EB1TFFVLhaW6G9Jqc	1942410 2ADM 1942411 2ADM 1942354 1AQI 1942355 1AQI	421	E: .92E0	Ident: 27/168	Ident% 16	Q: 74-229 (274) S: 31-183 (421)	Chain A, Adenine-N6-Dna-Methyltransferase Taqi	Pos: 49/168	Gap: 27/168
hIoOPKoCj6Ik/GPsGHPUsmrYKzg	15988176 1I9G	280	E: 5E-5	Ident: 31/237	Ident% 13	Q: 36-269 (274) S: 53-257 (280)	hypothetical protein Rv2118c [Mycobacterium tuberculosis H37Rv]	Pos: 69/237	Gap: 35/237
4rKE3UX+X/Imm9Mpan7bWusBMGE	13399509 1G38 13399510 1G38	393	E: 3E-5	Ident: 29/168	Ident% 17	Q: 74-229 (274) S: 11-163 (393)	Chain A, Adenine-Specific Methyltransferase M. Taq IDNA COMPLEX	Pos: 48/168	Gap: 27/168

7k5sT1dsKe+SKIiIoTDffHMfM9c
15668198
2495750
2128090
1498786

M. jannaschii predicted coding region MJ0027 [Methanococcus jannaschii]

184

4
26-48,89-111,117-139,149-171

VCyFtvFjSrn2HpnonJWkBMYHBRU
15668199
2495751
2127988
1590830

thiamine monphosphate kinase (thiL) [Methanococcus jannaschii]

319

165

358

416

JVldkQE2x96QYpRNVN79S417ub8

6137337 1CLI
6137339 1CLI
6137338 1CLI
6137340 1CLI

345

E: 5E-13

Ident: 40/224

Ident% 17

Q: 15-222 (319) S: 32-251 (345)

Chain A, X-Ray Crystal Structure Of Aminoimidazole Ribonucleotide Synthetase (Purm), From The E. Coli Purine Biosynthetic Pathway, At 2.5 A Resolution

Pos: 82/224

Gap: 20/224

ZiFpk0KwWPP+u01Lhcxml0J6vnU
15668200
2495440
2127828
1590832

coenzyme F420-reducing hydrogenase, delta subunit (frcD) [Methanococcus jannaschii]

183

zVtMJrI/lfeKkzM4jPxlWPBuLn8

7546418 1CFZ
7546419 1CFZ
7546420 1CFZ
7546421 1CFZ
7546422 1CFZ
7546423 1CFZ

162

E: 6E-35

Ident: 37/158

Ident% 23

Q: 27-181 (183) S: 2-150 (162)

hybD protein - Escherichia coli

Pos: 74/158

Gap: 12/158

45ofW8El/bhi2fWrxnbjW2YstUQ
15668201
2494431
2127831
1590833

coenzyme F420-reducing hydrogenase, gamma subunit [Methanococcus jannaschii]

230

715

1721

1855

aGGKUqjNEv24fhTGLQy+jpCJRvI	640409 1FRI 640409 1FRI	106	E: 1.2E0	Ident: 13/52	Ident% 25	Q: 151-201 (230) S: 11-62 (106)	Ferredoxin (Fdi) Mutant With Asp 23 Replaced By Asn (D23n)	Pos: 20/52	Gap: 1/52
VzH5n6t+6j1FiRcfHsybOkdExyA	18158649 1KEK 18158650 1KEK 4558091 1B0P 4558092 1B0P 4558221 2PDA 4558222 2PDA 18158649 1KEK 18158650 1KEK 4558091 1B0P 4558092 1B0P 4558221 2PDA 4558222 2PDA	1231	E: .17E0	Ident: 10/31	Ident% 32	Q: 200-230 (230) S: 681-711 (1231)	Chain A, Crystal Structure Of The Free Radical Intermediate Of Pyruvate:ferredoxin Oxidoreductase	Pos: 15/31	Gap: -1/-1
2hG8JJNBvGLy4OK+bdlHFYT4mUo	640413 1FRL 640413 1FRL	106	E: 1.5E0	Ident: 11/43	Ident% 25	Q: 178-218 (230) S: 8-50 (106)	Ferredoxin (Fdi) Mutant With Glu 38 Replaced By Ser (E38s)	Pos: 15/43	Gap: 2/43
iMyNepb8nMkabZXk9/tTA9EaMzA	4139441 1FEH 6730137 1C4A 6730138 1C4C	574	E: .27E0	Ident: 19/97	Ident% 19	Q: 138-218 (230) S: 113-201 (574)	PERIPLASMIC [FE] HYDROGENASE 1	Pos: 31/97	Gap: 24/97
/cf4aWnHhUUbQzJYlalc/Pt/YAs	442904 1FDD 442904 1FDD	106	E: 1.3E0	Ident: 13/52	Ident% 25	Q: 151-201 (230) S: 11-62 (106)	Ferredoxin Mutant With Asp 15 Replaced By Asn (D15n)	Pos: 19/52	Gap: 1/52
I72Dln91KCIeVbXqmZyKxz1tYE4	640408 1FRH 640408 1FRH	106	E: 1.6E0	Ident: 13/52	Ident% 25	Q: 151-201 (230) S: 11-62 (106)	Ferredoxin (Fdi) Mutant With Phe 2 Replaced By Tyr (F2y)	Pos: 20/52	Gap: 1/52
yQysezpIgy5EXPkgq9y3NH3Gpgo	6729719 1BQX 6729750 1BWE 6729719 1BQX 6729750 1BWE	77	E: 7.6E0	Ident: 15/43	Ident% 34	Q: 178-218 (230) S: 8-50 (77)	Chain A, Artificial Fe8s8 Ferredoxin: The D13c Variant Of Bacillus Schlegelii Fe7s8 Ferredoxin	Pos: 22/43	Gap: 2/43
o4BqKin2wnGOOqLgLsXsVHFoTWM	6729695 1B0T 6729695 1B0T	106	E: 1.3E0	Ident: 11/43	Ident% 25	Q: 178-218 (230) S: 8-50 (106)	Chain A, D15kK84D MUTANT OF AZOTOBACTER VINELANDII FDI	Pos: 15/43	Gap: 2/43
+GJCcAELu5pZiM784UWQAyxpDqQ	6729852 7FD1 2624426 6FD1 6729851 6FDR 6729853 7FDR 443515 5FD1 2914395 1AXQ 442901 1FDA 442902 1FDB 349883 1FER 6729852 7FD1 2624426 6FD1 6729851 6FDR 6729853 7FDR 443515 5FD1 2914395 1AXQ 442901 1FDA 442902 1FDB 349883 1FER	106	E: 1.5E0	Ident: 13/52	Ident% 25	Q: 151-201 (230) S: 11-62 (106)	Chain A, 7-Fe Ferredoxin From Azotobacter Vinelandii At Ph 8.5, 100 K, 1.35 A	Pos: 20/52	Gap: 1/52
jKdyEAp/MhaKX3+iz1lBCe/77h0	9256974 1F5C 9256974 1F5C	106	E: .007E0	Ident: 12/54	Ident% 22	Q: 171-222 (230) S: 1-54 (106)	Chain A, Crystal Structure Of F25h Ferredoxin 1 Mutant From Azotobacter Vinelandii At 1.75 Angstrom Resolution	Pos: 16/54	Gap: 2/54
gKvs7La5SfJ/Y+chhsg97cy8zys	3212403 1A6L 3212403 1A6L	106	E: 1.3E0	Ident: 13/52	Ident% 25	Q: 151-201 (230) S: 11-62 (106)	T14c Mutant Of Azotobacter Vinelandii Fdi	Pos: 20/52	Gap: 1/52
nge+kG6iYzQQt7xGjSFdcKQ6Rt8	1943573 1BLU	82	E: .22E0	Ident: 14/47	Ident% 29	Q: 178-218 (230) S: 8-54 (82)	Structure Of The 2[4fe-4s] Ferredoxin From Chromatium Vinosum	Pos: 17/47	Gap: 6/47
CgruAQnSEgW+lL5k+XYzHmwctEk	7546410 1DUR	55	E: .26E0	Ident: 17/47	Ident% 36	Q: 172-218 (230) S: 3-47 (55)	ferredoxin 2[4Fe-4S] [validated] - Peptostreptococcus asaccharolyticus	Pos: 24/47	Gap: 2/47
iQSEJwYITV2R3WJvDblYKM46o0Q	6435688 1D3W 6435688 1D3W	106	E: 1.7E0	Ident: 14/52	Ident% 26	Q: 151-201 (230) S: 11-62 (106)	Chain A, Crystal Structure Of Ferredoxin 1 D15e Mutant From Azotobacter Vinelandii At 1.7 Angstrom Resolution	Pos: 20/52	Gap: 1/52
2xxTpjvmscJ469r9dxRPOLjaLsc	3318893 1BD6 3318893 1BD6	77	E: 3.4E0	Ident: 15/45	Ident% 33	Q: 162-201 (230) S: 18-62 (77)	7-Fe Ferredoxin From Bacillus Schlegelii, Nmr, Minimized Average Structure	Pos: 21/45	Gap: 5/45
wDKdFxGv1xPRgAjyOhfuIaElFYo	10120847 1FF2	106	E: .041E0	Ident: 11/54	Ident% 20	Q: 171-222 (230) S: 1-54 (106)	Chain A, Crystal Structure Of The C42d Mutant Of Azotobacter Vinelandii 7fe Ferredoxin (Fdi)	Pos: 15/54	Gap: 2/54
nf4y4bxj9elJZrW7KKNrL67NMOs	13399647 1H7W 13399648 1H7W 13399649 1H7W 13399650 1H7W	1025	E: 1.4E0	Ident: 20/96	Ident% 20	Q: 129-220 (230) S: 911-999 (1025)	Chain A, Dihydropyrimidine Dehydrogenase (Dpd) From Pig	Pos: 38/96	Gap: 11/96
JfVoTFlIZRcJlQyFWNh5fHC5xkM	12084520 1GAO 12084521 1GAO 12084522 1GAO 12084523 1GAO 12084520 1GAO 12084521 1GAO 12084522 1GAO 12084523 1GAO	106	E: 2.4E0	Ident: 13/52	Ident% 25	Q: 151-201 (230) S: 11-62 (106)	Chain A, Crystal Structure Of The L44s Mutant Of Ferredoxin I	Pos: 21/52	Gap: 1/52
loGLj57l5LgQ64JlcN8+ghK6O5Q	640412 1FRK 640412 1FRK	106	E: .67E0	Ident: 13/52	Ident% 25	Q: 151-201 (230) S: 11-62 (106)	Ferredoxin (Fdi) Mutant With His 35 Replaced By Asp (H35d)	Pos: 20/52	Gap: 1/52
kIg48lQG1hbdSxu8W2Z+7HJLxQ0	640411 1FRJ 640411 1FRJ	106	E: .49E0	Ident: 12/43	Ident% 27	Q: 178-218 (230) S: 8-50 (106)	Ferredoxin (Fdi) Mutant With Phe 25 Replaced By Ile (F25i)	Pos: 16/43	Gap: 2/43
DQZRu/1iO/Xkv1jEgQ0v7P4lT0c	2098504 1FTC 2098505 1FTC 2098504 1FTC 2098505 1FTC	106	E: 2.4E0	Ident: 12/52	Ident% 23	Q: 151-201 (230) S: 11-62 (106)	Chain A, Y13c Mutant Of Azotobacter Vinelandii Fdi	Pos: 19/52	Gap: 1/52
fFNH9v5dE+qaDKIs3YFhzTaIlxY	5542236 1FUM 5542240 1FUM	243	E: .04E0	Ident: 26/111	Ident% 23	Q: 136-219 (230) S: 106-216 (243)	Chain B, Structure Of The E. Coli Fumarate Reductase Respiratory Complex	Pos: 38/111	Gap: 27/111
fGvF3SwaFFk9Bk7s0WH1Zlguxx4	640414 1FRM 640414 1FRM	106	E: 1.3E0	Ident: 14/52	Ident% 26	Q: 151-201 (230) S: 11-62 (106)	Ferredoxin (Fdi) Mutant With Glu 46 Replaced By Ala (E46a)	Pos: 21/52	Gap: 1/52
z1LxZZWfFIAH0OSD5kYo6tqQAhk	230509 2FD2 230509 2FD2	106	E: .34E0	Ident: 12/43	Ident% 27	Q: 178-218 (230) S: 8-50 (106)	Ferredoxin (Mutant With Cys 24 Replaced By Ala) (C24A)	Pos: 16/43	Gap: 2/43
Q125RpMho9EZQi8VTwB6VThNPNw	3318886 1BC6 3318886 1BC6	77	E: .72E0	Ident: 11/29	Ident% 37	Q: 173-201 (230) S: 34-62 (77)	7-Fe Ferredoxin From Bacillus Schlegelii, Nmr, 20 Structures	Pos: 15/29	Gap: -1/-1
qQplKtyoIwG7exLqldeSrI1Eksg	229911 1FD2 229911 1FD2	106	E: 2E0	Ident: 13/52	Ident% 25	Q: 151-201 (230) S: 11-62 (106)	Ferredoxin (Mutant With Cys 20 Replaced By Ala) (C20A)	Pos: 20/52	Gap: 1/52
8ymp5ZKp2+2BBBERbg3oODedPNk	2554684 1XER	103	E: .2E0	Ident: 19/55	Ident% 34	Q: 173-218 (230) S: 40-94 (103)	Structure Of Ferredoxin	Pos: 25/55	Gap: 9/55
uSp4lyNDaZPY+UVPBME4WnK5nzc	13399651 1H7X 13399652 1H7X 13399653 1H7X 13399654 1H7X	1025	E: 1.2E0	Ident: 20/96	Ident% 20	Q: 129-220 (230) S: 911-999 (1025)	Chain A, Dihydropyrimidine Dehydrogenase (Dpd) From Pig, Ternary Complex Of A Mutant Enzyme (C671a), Nadph And 5-Fluorouracil	Pos: 38/96	Gap: 11/96
3tCQS5D57iL+uq4Eep83G/7nRrM	17942775 1H98 17942775 1H98	78	E: .23E0	Ident: 15/45	Ident% 33	Q: 176-218 (230) S: 6-50 (78)	Ferredoxin	Pos: 19/45	Gap: 2/45
l7/cipYNUBBLIxzO5Q8s7ITvXw8	9256973 1F5B 9256973 1F5B	106	E: 1.6E0	Ident: 13/52	Ident% 25	Q: 151-201 (230) S: 11-62 (106)	Chain A, Crystal Structure Of F2h Ferredoxin 1 Mutant From Azotobacter Vinelandii At 1.75 Angstrom Resolution	Pos: 20/52	Gap: 1/52
SH16zLMC8lDzlqTrXLFPPEJa3ig	6980482 1B0V 6980483 1B0V 6980484 1B0V 6980485 1B0V 6980482 1B0V 6980483 1B0V 6980484 1B0V 6980485 1B0V	106	E: 3.4E0	Ident: 13/52	Ident% 25	Q: 151-201 (230) S: 11-62 (106)	Chain A, I40n Mutant Of Azotobacter Vinelandii Fdi	Pos: 19/52	Gap: 1/52
Fn7/sGzV6eWR/IpHLC0xu5v/5L4	6730011 1FRF	264	E: .067E0	Ident: 44/153	Ident% 28	Q: 15-143 (230) S: 17-162 (264)	Chain S, Crystal Structure Of The Ni-Fe Hydrogenase From Desulfovibrio Fructosovorans	Pos: 69/153	Gap: 31/153
6Ekbo0SCjFYvxg39JnwnmbJ7Vbs	11514021 1G3O 11514021 1G3O	106	E: 1.4E0	Ident: 13/52	Ident% 25	Q: 151-201 (230) S: 11-62 (106)	Chain A, Crystal Structure Of V19e Mutant Of Ferredoxin I	Pos: 21/52	Gap: 1/52
Qe3jBXA3OcrgzBJbOuL4CTe/9j0	640415 1FRX 640415 1FRX	106	E: 3.2E0	Ident: 13/52	Ident% 25	Q: 151-201 (230) S: 11-62 (106)	Ferredoxin (Fdi) Mutant With Cys 20 Replaced By Ser (C20s)	Pos: 20/52	Gap: 1/52
iWtrpMuYsuB5Jn+pd4gDE0Gq3J8	11513606 1G6B 11513606 1G6B	106	E: 1.3E0	Ident: 13/52	Ident% 25	Q: 151-201 (230) S: 11-62 (106)	Chain A, Crystal Structure Of P47s Mutant Of Ferredoxin I	Pos: 21/52	Gap: 1/52
OOWAhk3eEBubDxv212qaSBtoyKU	1943535 1FRV 1943537 1FRV	264	E: 5E-4	Ident: 46/169	Ident% 27	Q: 7-150 (230) S: 9-170 (264)	Chain A, Crystal Structure Of The Oxidized Form Of Ni-Fe Hydrogenase	Pos: 71/169	Gap: 32/169
5xSPy+cFzzfqHehaKELq/fFwonw	1310890 1CLF	55	E: 2E-4	Ident: 17/41	Ident% 41	Q: 178-218 (230) S: 8-48 (55)	Clostridium Pasteurianum Ferredoxin	Pos: 22/41	Gap: -1/-1
qxiEu8o08o1qDoLq6yI134Srrrg	4930042 1HFE 4930044 1HFE	421	E: 5E-4	Ident: 20/48	Ident% 41	Q: 173-218 (230) S: 30-77 (421)	PERIPLASMIC [FE] HYDROGENASE LARGE SUBUNIT (FE HYDROGENLYASE)	Pos: 28/48	Gap: 2/48
b1rBpheqIkjxsAqyFWaMyjvtNSk	6730442 1H2R	267	E: 2E-5	Ident: 44/160	Ident% 27	Q: 7-139 (230) S: 9-161 (267)	Chain S, Three-Dimensional Structure Of Ni-Fe Hydrogenase From Desulfivibrio Vulgaris Miyazaki F In The Reduced Form At 1.4 A Resolution	Pos: 71/160	Gap: 34/160
GEAQAaM8LuOiwqWmvUIP/ujr8Xw	1065197 1FCA	55	E: 2E-5	Ident: 18/48	Ident% 37	Q: 171-218 (230) S: 1-48 (55)	Ferredoxin	Pos: 22/48	Gap: -1/-1
r3SKYz68fEUvC9wB9naYhzhXhv8	4558286 1H2A	317	E: 2E-5	Ident: 44/160	Ident% 27	Q: 7-139 (230) S: 59-211 (317)	Periplasmic [NiFe] hydrogenase small subunit precursor (NiFe hydrogenlyase small chain)	Pos: 71/160	Gap: 34/160
g2pwKD1gqMG5wMsDpC0bBSKM3oI	3114424 2FDN 640397 1FDN	55	E: 4E-6	Ident: 19/48	Ident% 39	Q: 171-218 (230) S: 1-48 (55)	FERREDOXIN	Pos: 23/48	Gap: -1/-1
VDFNleDSeLeyQwOwCFf6o6VSlRc	14719750 1E3D 14719752 1E3D	266	E: 2E-7	Ident: 45/162	Ident% 27	Q: 7-145 (230) S: 9-167 (266)	Chain A, [nife] Hydrogenase From Desulfovibrio Desulfuricans Atcc 27774	Pos: 77/162	Gap: 26/162
czV/rIdZrHmyt64iUiJoFZXvvH4	5542157 1CC1	283	E: 1E-24	Ident: 46/194	Ident% 23	Q: 2-160 (230) S: 5-197 (283)	Chain S, Crystal Structure Of A Reduced, Active Form Of The Ni-Fe-Se Hydrogenase From Desulfomicrobium Baculatum	Pos: 78/194	Gap: 36/194
64efpAuP2rO1sLcE2FcRKyPt2FA	3318796 2FRV 3318798 2FRV 3318800 2FRV 3318802 2FRV 3318804 2FRV 3318794 2FRV	264	E: 2E-27	Ident: 44/170	Ident% 25	Q: 7-151 (230) S: 9-171 (264)	Chain A, Crystal Structure Of The Oxidized Form Of Ni-Fe Hydrogenase	Pos: 70/170	Gap: 32/170

h3IJInxhhnUfatGXWA7W/s+78bs
15668202
2494430
2127826
1590834

coenzyme F420-reducing hydrogenase, beta subunit (frhB) [Methanococcus jannaschii]

287

Esb3BYj7E8ikClWxF6YeF8TktLc
15668203
2495752
2129293
1592258

succinate dehydrogenase, flavoprotein subunit (sdhA) [Methanococcus jannaschii]

539

269

1271

1322

aySqkN6tr7T16IggfUEc83vfxvs	10120751 1F8R 10120752 1F8R 10120753 1F8R 10120754 1F8R 10120755 1F8S 10120756 1F8S 10120757 1F8S 10120758 1F8S 10120759 1F8S 10120760 1F8S 10120761 1F8S 10120762 1F8S	498	E: .55E0	Ident: 8/34	Ident% 23	Q: 5-38 (539) S: 36-69 (498)	Chain A, Crystal Structure Of L-Amino Acid Oxidase From Calloselasma Rhodostoma Complexed With Citrate	Pos: 13/34	Gap: -1/-1
99lsAZqKxk9drWJZmkUDUqNs6+0	15826394 1JEH 15826395 1JEH	478	E: .037E0	Ident: 16/45	Ident% 35	Q: 3-47 (539) S: 6-50 (478)	Chain A, Crystal Structure Of Yeast E3, Lipoamide Dehydrogenase	Pos: 20/45	Gap: -1/-1
bcSIuqWauc8rQ1ZoQBkq/y6W6Ew	12084636 1EL5 12084637 1EL5 12084638 1EL7 12084639 1EL7 12084640 1EL8 12084641 1EL8	389	E: .91E0	Ident: 5/28	Ident% 17	Q: 3-30 (539) S: 4-31 (389)	Chain A, Complex Of Monomeric Sarcosine Oxidase With The Inhibitor Dimethylglycine	Pos: 12/28	Gap: -1/-1
T3GRldPoe/Xj/hPVaPoWUqK4I5E	13786943 1FL2	310	E: .13E0	Ident: 12/28	Ident% 42	Q: 337-364 (539) S: 256-283 (310)	Chain A, Catalytic Core Component Of The Alkylhydroperoxide Reductase Ahpf From E.Coli	Pos: 19/28	Gap: -1/-1
BFpuGMdRUW+aYjtA5aBaXTNFZnw	13399974 1HYU	521	E: .095E0	Ident: 16/61	Ident% 26	Q: 337-397 (539) S: 467-520 (521)	alkyl hydroperoxide reductase, F52a subunit; detoxification of hydroperoxides [Salmonella typhimurium LT2]	Pos: 28/61	Gap: 7/61
6z31CtPMzPqNTVNQTXcXqZ2zrQ0	494262 1LPF 494263 1LPF	477	E: .021E0	Ident: 15/52	Ident% 28	Q: 2-52 (539) S: 3-52 (477)	Chain A, Dihydrolipoamide Dehydrogenase (E.C.1.8.1.4) Complex With Flavin-Adenine-Dinucleotide (Fad)	Pos: 22/52	Gap: 3/52
/n1/Romv01YH+rNsFbfBDTcVsvA	7245699 1B3M 7245700 1B3M	389	E: .91E0	Ident: 5/28	Ident% 17	Q: 3-30 (539) S: 4-31 (389)	Chain A, Monomeric Sarcosine Oxidase From Bacillus Sp. B-0618	Pos: 12/28	Gap: -1/-1
CvHHwDHAWs6UuVe0qpUqcdmXK3w	15988005 1I8T 15988006 1I8T	367	E: .059E0	Ident: 19/85	Ident% 22	Q: 3-78 (539) S: 2-86 (367)	UDP-galactopyranose mutase [Escherichia coli K12]	Pos: 30/85	Gap: 9/85
Jrc5VzWIN01LjxxSdwmypL2A1wc	494878 3LAD 494879 3LAD 494878 3LAD 494879 3LAD	476	E: .33E0	Ident: 14/51	Ident% 27	Q: 338-388 (539) S: 298-345 (476)	Chain A, Dihydrolipoamide Dehydrogenase (E.C.1.8.1.4)	Pos: 26/51	Gap: 3/51
mz9RhkfQTct1nxKGT5aPyiDe8nI	10835765 1E39	571	E: 5E-30	Ident: 136/457	Ident% 29	Q: 4-391 (539) S: 128-567 (571)	Chain A, Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated To Alanine	Pos: 207/457	Gap: 86/457
IQmcogHy5OnTk1G+JfQE/Puc6qU	16974904 1JRZ 16974905 1JRZ	571	E: 1E-31	Ident: 136/450	Ident% 30	Q: 4-391 (539) S: 128-567 (571)	Chain A, Crystal Structure Of Arg402tyr Mutant Flavocytochrome C3 From Shewanella Frigidimarina	Pos: 208/450	Gap: 72/450
yy1w9FkFU5kFQ/fkXvs9AUrdaAQ	16974902 1JRY 16974903 1JRY	571	E: 7E-31	Ident: 138/450	Ident% 30	Q: 4-391 (539) S: 128-567 (571)	Chain A, Crystal Structure Of Arg402lys Mutant Flavocytochrome C3 From Shewanella Frigidimarina	Pos: 206/450	Gap: 72/450
xLCFrHiVLYYVYUaznOcvVDtw1zg	16974900 1JRX 16974901 1JRX	571	E: 8E-31	Ident: 138/450	Ident% 30	Q: 4-391 (539) S: 128-567 (571)	Chain A, Crystal Structure Of Arg402ala Mutant Flavocytochrome C3 From Shewanella Frigidimarina	Pos: 206/450	Gap: 72/450
/xTLJv1U0zd8Fh1PQ7BUU/Uc2FA	6573457 1QJD	571	E: 3E-31	Ident: 137/457	Ident% 29	Q: 4-391 (539) S: 128-567 (571)	Chain A, Flavocytochrome C3 From Shewanella Frigidimarina	Pos: 208/457	Gap: 86/457
FIhfGFYR144H7UUPm/QVZF7ckSA	6573311 1D4D 6573312 1D4E	572	E: 6E-32	Ident: 142/463	Ident% 30	Q: 3-395 (539) S: 127-572 (572)	Chain A, Crystal Structure Of The Succinate Complexed Form Of The Flavocytochrome C Fumarate Reductase Of Shewanella Putrefaciens Strain Mr-1	Pos: 214/463	Gap: 87/463
zpSdJKboRiws+pB0szDHX0JSe2s	6573307 1D4C 6573310 1D4C 6573308 1D4C 6573309 1D4C	572	E: 5E-32	Ident: 143/463	Ident% 30	Q: 3-395 (539) S: 127-572 (572)	Chain A, Crystal Structure Of The Uncomplexed Form Of The Flavocytochrome C Fumarate Reductase Of Shewanella Putrefaciens Strain Mr-1	Pos: 214/463	Gap: 87/463
ZI1M+0S0t7Qr9Bih7LiEVqVI+FU	11514094 1QO8 11514095 1QO8	566	E: 2E-35	Ident: 142/454	Ident% 31	Q: 3-388 (539) S: 122-559 (566)	Chain A, The Structure Of The Open Conformation Of A Flavocytochrome C3 Fumarate Reductase	Pos: 210/454	Gap: 84/454
Fej328Jn3gT8j9OqJgVAZfzPyEY	14278681 1E7P 14278684 1E7P	655	E: 1E-140	Ident: 195/562	Ident% 34	Q: 3-519 (539) S: 6-566 (655)	Chain G, Quinol:fumarate Reductase From Wolinella Succinogenes	Pos: 289/562	Gap: 46/562
4Ptic6N/XQlG//sT8ZnFmPddNSI	14278675 1E7P 14278678 1E7P	656	E: 1E-140	Ident: 195/562	Ident% 34	Q: 3-519 (539) S: 6-566 (656)	Chain A, Quinol:fumarate Reductase From Wolinella Succinogenes	Pos: 289/562	Gap: 46/562
XTodYn1AwnfgT5s2DWz8KwWlBI8	6730464 1QLA 6730467 1QLA 6730470 1QLB 6730473 1QLB	656	E: 1E-140	Ident: 194/562	Ident% 34	Q: 3-519 (539) S: 6-566 (656)	Fumarate reductase flavoprotein subunit	Pos: 289/562	Gap: 46/562
IfSIu66IH1ZstDNONYyvmHcXH0w	5542180 1CHU	540	E: 1E-160	Ident: 178/534	Ident% 33	Q: 4-521 (539) S: 10-534 (540)	L-ASPARTATE OXIDASE (QUINOLINATE SYNTHETASE B)	Pos: 275/534	Gap: 25/534
WeBcKgAGYESGloudS7RiQadXvSc	5542235 1FUM 5542239 1FUM	601	E: 1E-168	Ident: 186/547	Ident% 34	Q: 4-518 (539) S: 6-552 (601)	Chain A, Structure Of The E. Coli Fumarate Reductase Respiratory Complex	Pos: 292/547	Gap: 32/547

PhhyHmmAleF+oz/eJcZwmeQKl2c
15668204
2495753
2127989
1590837

conserved hypothetical protein [Methanococcus jannaschii]

316

141

gag9P6g0WLTBIbWvnru3ACo8Y3U
15668205
2492573
2127733
1590838

ABC transporter subunit [Methanococcus jannaschii]

250

1367

1361

1344

q9VJg++DTI4s/+pcNr24LsU/ZBE	6573453 1B0U	262	E: 4E-17	Ident: 75/244	Ident% 30	Q: 1-231 (250) S: 1-240 (262)	Chain A, Atp-Binding Subunit Of The Histidine Permease From Salmonella Typhimurium	Pos: 124/244	Gap: 17/244
vwZlRCrw/davJk0PIngo3RbJxdw	15988440 1JSQ 15988441 1JSQ 15988442 1JSQ 15988443 1JSQ 15988444 1JSQ 15988445 1JSQ 15988446 1JSQ 15988447 1JSQ	582	E: 1E-53	Ident: 62/233	Ident% 26	Q: 7-234 (250) S: 342-568 (582)	ATP-binding transport protein; multicopy suppressor of htrB [Escherichia coli O157:H7 EDL933]	Pos: 108/233	Gap: 11/233
bHzMC4Gxg64/bRB+N8ytSV+FEa0	15826057 1F3O	235	E: 1E-61	Ident: 53/229	Ident% 23	Q: 7-225 (250) S: 2-226 (235)	Chain A, Crystal Structure Of Mj0796 Atp-Binding Cassette	Pos: 105/229	Gap: 14/229
ImYhpWAkHn8eI11by5jCV4ScHuA	12084694 1G29 12084695 1G29	372	E: 2E-69	Ident: 54/253	Ident% 21	Q: 4-248 (250) S: 1-244 (372)	Chain 1, Malk	Pos: 117/253	Gap: 17/253

iCs+tcx4wk48iXnIIY0DM4wC10o
15668206
3334491
2826237

SSU ribosomal protein S15P (rpsO) [Methanococcus jannaschii]

153

107

133

156

Naye02yGV4zuauJDEpIZ7E1s5gY	3212289 1A32	88	E: 1E0	Ident: 24/67	Ident% 35	Q: 69-134 (153) S: 8-74 (88)	30S RIBOSOMAL PROTEIN S15 (BS18)	Pos: 37/67	Gap: 1/67
HWbxjDsJCKiN1X/OBpc2Bk4D40g	6137692 1QD7	85	E: .77E0	Ident: 24/67	Ident% 35	Q: 69-134 (153) S: 7-73 (85)	Chain H, Partial Model For 30s Ribosomal Subunit	Pos: 37/67	Gap: 1/67

fjvkakbAYdEkWczB3r1vB5Bxs2Q
15668207
2495754
2128091
1498797

conserved hypothetical protein [Methanococcus jannaschii]

238

191

OPWkBZtYqLJdsppwRLWTTASiCTw

14488686 1II7
14488687 1II7

333

E: 2E-4

Ident: 24/85

Ident% 28

Q: 26-109 (238) S: 6-86 (333)

Chain A, Crystal Structure Of P. Furiosus Mre11 With Manganese And Damp

Pos: 43/85

Gap: 5/85

sDEJ+dW9DskKVKcM4ai7rkqgSWA
15668208
2495755
2128092
1498798

conserved hypothetical protein [Methanococcus jannaschii]

217

mbnCIcATdwdCev+Fl+XOZWVvzgo
15668209
2495756
2128093
1590840

conserved hypothetical protein [Methanococcus jannaschii]

115

GHYCbIkMEjmM5VDyczlJC+1mt78

17943305 1GO3
17943307 1GO3

107

E: 2E-29

Ident: 107/107

Ident% 100

Q: 9-115 (115) S: 1-107 (107)

Chain F, Structure Of An Archeal Homolog Of The Eukaryotic Rna Polymerase Ii Rpb4RPB7 COMPLEX

Pos: 107/107

Gap: -1/-1

hcennMUlanr8ce1j4TCMB9T0G7s
15668210
3334485
2826238

LSU ribosomal protein L21E [Methanococcus jannaschii]

123

141

lgmYwMIUH/aBB7oRy9IMAnM6yT0

10120933 1FFK
15825958 1JJ2

E: 2E-25

Ident: 49/90

Ident% 54

Q: 5-94 (98) S: 3-92 (95)

ribosomal protein L21.eR [validated] - Haloarcula marismortui

Pos: 56/90

Gap: -1/-1

eHLWBQkPyqjl6JeWFvIiXIQqrh0
15668211
2495757
2128094
1498801

conserved hypothetical protein [Methanococcus jannaschii]

454

129

XlWeX2fOJdm9FCvWqxfz2vTFmI0	13096179 1HQM	1265	E: 6.8E0	Ident: 39/201	Ident% 19	Q: 217-405 (454) S: 924-1114 (1265)	Chain D, Crystal Structure Of Thermus Aquaticus Core Rna Polymerase- Includes Complete Structure With Side-Chains (Except For Disordered Regions)-Further Refined From Original Deposition-Contains Additional Sequence Information	Pos: 72/201	Gap: 22/201
rPpnuC2TTnfm6Xqb4lzpvfXroC0	14278484 1I6V	1264	E: 6.4E0	Ident: 39/201	Ident% 19	Q: 217-405 (454) S: 923-1113 (1264)	Chain D, Thermus Aquaticus Core Rna Polymerase-Rifampicin Complex	Pos: 72/201	Gap: 22/201
SsxLEsqR28tFTlsjArSbRRrw2c0	18158779 1K8W	327	E: .89E0	Ident: 16/67	Ident% 23	Q: 379-445 (454) S: 160-218 (327)	Chain A, Crystal Structure Of The E. Coli Pseudouridine Synthase Trub Bound To A T Stem-Loop Rna	Pos: 26/67	Gap: 8/67

8e0WHEOaIqcQFD8692xwnytKhPw
15668212
2495758
2128095
1498802

M. jannaschii predicted coding region MJ0042 [Methanococcus jannaschii]

215

nOGJ1vvKfMG0QrneXFS6++S7/Mw
15668213
2495759
2127759
1498803

intein containing hypothetical protein [Methanococcus jannaschii]

785

165

280

MLUfiHyXe/IydoBlTA7leQ4RjyU	6435708 1QQC	773	E: 6.7E0	Ident: 19/94	Ident% 20	Q: 77-158 (785) S: 448-540 (773)	Chain A, Crystal Structure Of An Archaebacterial Dna Polymerase D.Tok	Pos: 32/94	Gap: 13/94
SfdHsvySBlfGWQ8PlDIoTF4X8w0	7546394 1D5A	733	E: 6.4E0	Ident: 19/94	Ident% 20	Q: 77-158 (785) S: 448-540 (733)	Chain A, Crystal Structure Of An Archaebacterial Dna Polymerase D.Tok. Deposition Of Second Native Structure At 2.4 Angstro	Pos: 32/94	Gap: 13/94
M76KckTzNUez3wDx6DvgNH9pPfY	8569297 1QHT	775	E: .012E0	Ident: 17/94	Ident% 18	Q: 77-158 (785) S: 448-540 (775)	Chain A, Dna Polymerase From Thermococcus Sp. 9on-7 Archaeon	Pos: 33/94	Gap: 13/94
TRSpfie2PYCVWwJS6lohQ9xsEsM	9256860 1DQ3	454	E: 4E-4	Ident: 42/279	Ident% 15	Q: 149-375 (785) S: 48-323 (454)	Chain A, Crystal Structure Of An Archaeal Intein-Encoded Homing Endonuclease Pi-Pfui	Pos: 86/279	Gap: 55/279
7tpsTHWm2nwYvG0rZSX5TMfXVWA	4699806 1TGO	773	E: 3E-4	Ident: 20/94	Ident% 21	Q: 77-158 (785) S: 448-540 (773)	DNA POLYMERASE (TO POL)	Pos: 33/94	Gap: 13/94
FcPIpltXAv/v3gZfrBXQ9XgiUsY	9257100 1EF0 9257101 1EF0	462	E: 5E-5	Ident: 55/401	Ident% 13	Q: 129-456 (785) S: 5-398 (462)	Chain A, Crystal Structure Of Pi-Scei Miniprecursor	Pos: 123/401	Gap: 80/401
deFFXMyGiKsoSK+VKqVS+6pD5Lo	3114410 1VDE 3114411 1VDE 6730322 1DFA	454	E: 1E-5	Ident: 56/401	Ident% 13	Q: 129-456 (785) S: 1-394 (454)	Chain A, Pi-Scei, A Homing Endonuclease With Protein Splicing Activity	Pos: 124/401	Gap: 80/401

4IvYCHmYSGWOUkFq0apqfPfKlEY
15668214
2495760
2127990
1590842

conserved hypothetical protein [Methanococcus jannaschii]

260

278

437

wjJ9vbHDCm++ufOc/u+2GSeg7ic	6980398 1B7B 6980399 1B7B 6980400 1B7B 6980401 1B7B	310	E: 2E-5	Ident: 43/317	Ident% 13	Q: 2-256 (260) S: 4-308 (310)	CARBAMATE KINASE	Pos: 88/317	Gap: 74/317
NL7cRLgoPLaobFNirUviJ4sIRhs	9955156 1E19 9955157 1E19	314	E: 4E-8	Ident: 46/325	Ident% 14	Q: 2-256 (260) S: 4-312 (314)	Carbamate kinase (Carbamate kinase-like carbamoylphosphate synthetase)	Pos: 103/325	Gap: 86/325

q+qiyJBTvCW6uyFzBf2rLkaq5hM
15668215
2495761
2128096
1590843

conserved hypothetical protein [Methanococcus jannaschii]

221

144

lsDOKDxRRzUnctTdboLRaQNAQAI
15668216
2495762
2128097
1590844

conserved hypothetical protein [Methanococcus jannaschii]

261

282

2426

2450

lvV9EWMq77UqxJ8kc84I2Mjac+g	13787051 1F3L 13787051 1F3L	321	E: .001E0	Ident: 25/76	Ident% 32	Q: 86-161 (261) S: 47-118 (321)	Chain A, Crystal Structure Of The Conserved Core Of Protein Arginine Methyltransferase Prmt3	Pos: 36/76	Gap: 4/76
THMXI+EwFWrStxZxMR/rZMoqaoM	12084699 1G6Q 12084700 1G6Q 12084701 1G6Q 12084702 1G6Q 12084703 1G6Q 12084704 1G6Q 12084699 1G6Q 12084700 1G6Q 12084701 1G6Q 12084702 1G6Q 12084703 1G6Q 12084704 1G6Q	328	E: 6E-4	Ident: 22/74	Ident% 29	Q: 88-161 (261) S: 42-111 (328)	Chain 1, Crystal Structure Of Yeast Arginine Methyltransferase, Hmt1	Pos: 34/74	Gap: 4/74
KvA/gFgwGTZo3udIfCuYDUYMKok	1942407 1XVA 1942408 1XVA 4139415 1BHJ 4139416 1BHJ 6137381 1D2C 6137382 1D2C 1942407 1XVA 1942408 1XVA 4139415 1BHJ 4139416 1BHJ 6137381 1D2C 6137382 1D2C	292	E: 1E-7	Ident: 19/159	Ident% 11	Q: 68-222 (261) S: 42-175 (292)	Chain A, Methyltransferase	Pos: 53/159	Gap: 29/159
6WRUmfFkUHO5q8JMb4xzwfMupbI	6435570 1D2G 6435571 1D2G 6435572 1D2H 6435573 1D2H 6435574 1D2H 6435575 1D2H 6435570 1D2G 6435571 1D2G 6435572 1D2H 6435573 1D2H 6435574 1D2H 6435575 1D2H	292	E: 1E-7	Ident: 20/159	Ident% 12	Q: 68-222 (261) S: 42-175 (292)	Chain A, Crystal Structure Of R175k Mutant Glycine N- Methyltransferase From Rat Liver	Pos: 53/159	Gap: 29/159
5yacVXeX24KA2VAxDdq6jBcMkd4	9955209 1DUS 9955209 1DUS	194	E: 6E-11	Ident: 46/186	Ident% 24	Q: 70-251 (261) S: 37-187 (194)	Chain A, Mj0882-A Hypothetical Protein From M. Jannaschii	Pos: 81/186	Gap: 39/186
4rKE3UX+X/Imm9Mpan7bWusBMGE	13399509 1G38 13399510 1G38 13399509 1G38 13399510 1G38	393	E: 1E-14	Ident: 33/212	Ident% 15	Q: 61-261 (261) S: 1-194 (393)	Chain A, Adenine-Specific Methyltransferase M. Taq IDNA COMPLEX	Pos: 64/212	Gap: 29/212
sdLvp9C2Zy6Jo9DOLsgrTNL4ftA	1942357 1AQJ 1942356 1AQJ 1942357 1AQJ 1942356 1AQJ	421	E: 6E-15	Ident: 33/212	Ident% 15	Q: 61-261 (261) S: 21-214 (421)	MODIFICATION METHYLASE TAQI (ADENINE-SPECIFIC METHYLTRANSFERASE TAQI) (M.TAQI)	Pos: 64/212	Gap: 29/212
hi8Q6/nV02EB1TFFVLhaW6G9Jqc	1942410 2ADM 1942411 2ADM 1942354 1AQI 1942355 1AQI 1942410 2ADM 1942411 2ADM 1942354 1AQI 1942355 1AQI	421	E: 6E-15	Ident: 33/212	Ident% 15	Q: 61-261 (261) S: 21-214 (421)	Chain A, Adenine-N6-Dna-Methyltransferase Taqi	Pos: 64/212	Gap: 29/212

0sF/CvkaN+rx/jOokILGr8UMl3c
15668217
3915921
2826239

putative mRNA 3'-end processing factor 1 [Methanococcus jannaschii]

428

210

819

1053

jBPYMibRSGOmLbz0ZI1phniYAcc	6729916 1BVT 3891961 1BC2 3891962 1BC2	227	E: .036E0	Ident: 22/82	Ident% 26	Q: 15-94 (428) S: 42-121 (227)	Chain A, Metallo-Beta-Lactamase From Bacillus Cereus 569H9	Pos: 37/82	Gap: 4/82
N0abiif/C4AGjZWV9KgD2/hPC2c	5542575 4ZNB 5542576 4ZNB	232	E: .28E0	Ident: 15/82	Ident% 18	Q: 12-91 (428) S: 35-114 (232)	Chain A, Metallo-Beta-Lactamase (C181s Mutant)	Pos: 29/82	Gap: 4/82
XBv3Q77UHx7Kuox4rVYxBZr3vl8	17942983 1HLK 17942984 1HLK	227	E: .35E0	Ident: 15/82	Ident% 18	Q: 12-91 (428) S: 32-111 (227)	Chain A, Metallo-Beta-Lactamase From Bacteroides Fragilis In Complex With A Tricyclic Inhibitor	Pos: 29/82	Gap: 4/82
MJ3ASArKoA9Vi9zCKlk1qfaYiPo	11513751 1DDK	220	E: 1.5E0	Ident: 12/40	Ident% 30	Q: 50-89 (428) S: 69-106 (220)	Chain A, Crystal Structure Of Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa	Pos: 20/40	Gap: 2/40
5TH1bP3JnMZYWyRrIJwXj59CGOg	1942529 1ZNB 1942528 1ZNB 2914226 3ZNB 2914208 2ZNB 2914207 2ZNB 2914225 3ZNB	232	E: .26E0	Ident: 15/82	Ident% 18	Q: 12-91 (428) S: 35-114 (232)	Chain B, Metallo-Beta-Lactamase	Pos: 29/82	Gap: 4/82
e2ndT+OghztoJLRAeuKoIbL7IFE	3660296 2BMI 3660295 2BMI	232	E: .32E0	Ident: 15/82	Ident% 18	Q: 12-91 (428) S: 35-114 (232)	Chain B, Metallo-Beta-Lactamase	Pos: 27/82	Gap: 4/82
C0g4SqX/1BDxS4MgMEisEXpPjvY	6137439 1QH5 6137440 1QH5 6137437 1QH3 6137438 1QH3	260	E: .068E0	Ident: 17/156	Ident% 10	Q: 16-166 (428) S: 14-135 (260)	hydroxyacyl glutathione hydrolase; hydroxyacyl glutathione hydrolase; glyoxalase 2; Hydroxyacyl glutathione hydrolase; glyoxalase II; hydroxyacylglutathione hydroxylase [Homo sapiens]	Pos: 39/156	Gap: 39/156
dFy3rKag6gYWYFxCBbnmcMTR0II	15825822 1JJE 15825823 1JJE	222	E: 1.5E0	Ident: 12/40	Ident% 30	Q: 50-89 (428) S: 70-107 (222)	Chain A, Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa In Complex With A Biaryl Succinic Acid Inhibitor (11)	Pos: 20/40	Gap: 2/40
jAZBIe/yywfB4Hh7zonVgaCQqWo	3891997 1A8T 3891998 1A8T 3318914 1A7T 3318915 1A7T	232	E: .3E0	Ident: 15/82	Ident% 18	Q: 12-91 (428) S: 35-114 (232)	Chain A, Metallo-Beta-Lactamase In Complex With L-159,061	Pos: 27/82	Gap: 4/82
DcaWGtOZ17Q2xedscaYiU07BkPg	11513648 1E5D 11513649 1E5D	402	E: 4.6E0	Ident: 16/66	Ident% 24	Q: 15-69 (428) S: 36-91 (402)	Rubredoxin-oxygen oxidoreductase (ROO) (Rubredoxin oxidase)	Pos: 26/66	Gap: 21/66
XT8+3JO2FsX22qeiVs94XDmThLQ	10120734 1DXK	227	E: .039E0	Ident: 22/82	Ident% 26	Q: 15-94 (428) S: 42-121 (227)	Chain A, Metallo-Beta-Lactamase From Bacillus Cereus 569H9 C168S Mutant	Pos: 37/82	Gap: 4/82
cIKbi2bj5zVKnVqOWbQw91qCE6o	4930171 2BC2 4930172 2BC2 4930212 3BC2	227	E: .039E0	Ident: 22/82	Ident% 26	Q: 15-94 (428) S: 42-121 (227)	Chain A, Metallo Beta-Lactamase Ii From Bacillus Cereus 569H9 AT Ph 6.0, Trigonal Crystal Form	Pos: 37/82	Gap: 4/82
Fxm0w1DnZDWiDNXZ9FMIUnpYdGk	11513826 1DD6 11513827 1DD6 15825825 1JJT 15825826 1JJT	228	E: .003E0	Ident: 27/180	Ident% 15	Q: 12-189 (428) S: 31-183 (228)	Chain A, Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa In Complex With A Mercaptocarboxylate Inhibitor	Pos: 49/180	Gap: 29/180
3ov5UKBHdok9NXtZhkxOKk9lBHE	1827826 1BMC	221	E: .038E0	Ident: 22/82	Ident% 26	Q: 15-94 (428) S: 36-115 (221)	Structure Of A Zinc Metallo-Beta-Lactamase From Bacillus Cereus	Pos: 37/82	Gap: 4/82
L6FiZs6SzpVm9VZrMR2dpe8EXfU	6137470 1SML	269	E: 6E-7	Ident: 32/150	Ident% 21	Q: 16-160 (428) S: 40-178 (269)	Chain A, Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia	Pos: 56/150	Gap: 16/150

beCOKzOxKibBXd6QS4zywFb0O3Y
15668218
3219870
2826240

M. jannaschii predicted coding region MJ0047.1 [Methanococcus jannaschii]

105

3TSKkyDoqwhG3RQJqclRk3wMxH8
15668219
2495764
2127991
11513603
11513604
1498809

conserved hypothetical protein [Methanococcus jannaschii]

228

X486V8k72QgcalcMsFtL2euEdFA	494086 1HCY 494080 1HC1 494081 1HC2 494082 1HC3 494083 1HC4 494084 1HC5 494085 1HC6	657	E: 6.7E0	Ident: 9/48	Ident% 18	Q: 79-126 (228) S: 12-59 (657)	Arthropodan Hemocyanin (Deoxygenated) Refined Using Constrained 32 Point Group Symmetry	Pos: 24/48	Gap: -1/-1
h0SPXE2HUXYVDQCGkF1dq6asgi8	11513605 1G62	224	E: 2E-86	Ident: 74/228	Ident% 32	Q: 3-227 (228) S: 1-224 (224)	Chain A, Crystal Structure Of S.Cerevisiae Eif6	Pos: 121/228	Gap: 7/228
3TSKkyDoqwhG3RQJqclRk3wMxH8	11513603 1G61 11513604 1G61	228	E: 1E-111	Ident: 228/228	Ident% 100	Q: 1-228 (228) S: 1-228 (228)	conserved hypothetical protein [Methanococcus jannaschii]	Pos: 228/228	Gap: -1/-1

yRpCQ6dC8PqI5N8Q6EkLYdi7Bf0
15668220
1710536
2129255
1590847

LSU ribosomal protein L31E [Methanococcus jannaschii]

RkwcdThd6J22TVg1FzHXLhCSVl0

10120940 1FFK
15825965 1JJ2

E: 6E-4

Ident: 27/72

Ident% 37

Q: 7-76 (87) S: 6-76 (91)

Chain U, Crystal Structure Of The Large Ribosomal Subunit From Haloarcula Marismortui At 2.4 Angstrom Resolution

Pos: 42/72

Gap: 3/72

C4xCKlCK2fTRg+E1IkDL4LiZPTA
15668221
2495765
2128098
1498811

group II decarboxylase [Methanococcus jannaschii]

396

595

1201

1246

y10FF70dbma7+D4MV7qNwwsqWBY	7767011 1ELU 7767012 1ELU 7767009 1ELQ 7767010 1ELQ	390	E: 1E-5	Ident: 52/343	Ident% 15	Q: 71-387 (396) S: 62-382 (390)	Chain A, Complex Between The Cystine C-S Lyase C-Des And Its Reaction Product Cysteine Persulfide.	Pos: 98/343	Gap: 48/343
gA6Hu9AQn739J1mcf5oaOBPelYk	9955228 1C0N	406	E: 1E-7	Ident: 34/201	Ident% 16	Q: 66-261 (396) S: 66-241 (406)	Chain A, Csdb Protein, Nifs Homologue	Pos: 63/201	Gap: 30/201
s91RgYu2Tcj+lwvjlimuh+sXLF0	14719479 1JF9	408	E: 1E-8	Ident: 34/201	Ident% 16	Q: 66-261 (396) S: 68-243 (408)	Chain A, Crystal Structure Of Selenocysteine Lyase	Pos: 64/201	Gap: 30/201
drCuFjwkkjjR6+EvUgvMbKR3lP8	14719481 1JG8 14719482 1JG8 14719483 1JG8 14719484 1JG8	347	E: 2E-8	Ident: 68/377	Ident% 18	Q: 41-395 (396) S: 16-344 (347)	Chain A, Crystal Structure Of Threonine Aldolase (Low-Specificity)	Pos: 128/377	Gap: 70/377
x35DV18uKEjGNw2ftquF754grXg	18158926 1KMJ 18158927 1KMK	406	E: 2E-8	Ident: 34/201	Ident% 16	Q: 66-261 (396) S: 66-241 (406)	Chain A, E. Coli NifsCSDB PROTEIN AT 2.0A WITH THE CYSTEINE Persulfide Intermediate (Residue Css).	Pos: 64/201	Gap: 30/201
XkWRXJzNfcfCM8fechNEwydT0Kg	15988223 1GDE 15988224 1GDE 15988238 1GD9 15988239 1GD9	389	E: 1E-12	Ident: 45/371	Ident% 12	Q: 45-396 (396) S: 44-385 (389)	aspartate aminotransferase [Pyrococcus horikoshii]	Pos: 111/371	Gap: 48/371
I/EfOzHgu1yHb8NMDM516rPUBQo	15826678 1FG3 15826679 1FG7	356	E: 1E-12	Ident: 46/353	Ident% 13	Q: 57-391 (396) S: 33-352 (356)	Chain A, Crystal Structure Of L-Histidinol Phosphate Aminotransferase Complexed With L-Histidinol	Pos: 97/353	Gap: 51/353
Jo+xdQnKoZhXXYJH/sJpngRUxqs	14278621 1DJU 14278622 1DJU	388	E: 1E-12	Ident: 46/371	Ident% 12	Q: 45-396 (396) S: 43-384 (388)	Chain A, Crystal Structure Of Aromatic Aminotransferase From Pyrococcus Horikoshii Ot3	Pos: 111/371	Gap: 48/371
kcfwUY1Nxj/qDoUfH0OQPsZ8QQM	14278468 1GEW 14278469 1GEX 14278520 1GEY 15826616 1IJI	356	E: 4E-13	Ident: 46/353	Ident% 13	Q: 57-391 (396) S: 33-352 (356)	histidinol-phosphate aminotransferase [Escherichia coli K12]	Pos: 98/353	Gap: 51/353
h/njSI9CWOVVjuNBa5Cbwc1A8qI	14278152 1FC4 14278153 1FC4	401	E: 3E-14	Ident: 50/285	Ident% 17	Q: 122-395 (396) S: 129-395 (401)	Chain A, 2-Amino-3-Ketobutyrate Coa Ligase	Pos: 84/285	Gap: 29/285
iukf7T5MyibqAm7irZnekB2LVHQ	17942613 1GCK 17942614 1GCK	385	E: 1E-15	Ident: 42/378	Ident% 11	Q: 35-394 (396) S: 38-382 (385)	Chain A, Thermus Thermophilus Aspartate Aminotransferase Double Mutant 1 Complexed With Aspartate	Pos: 100/378	Gap: 51/378
9aJ1OTTTmR0pUhLKzdeWrkW2dRQ	5821839 1BKG 5821840 1BKG 5821841 1BKG 5821842 1BKG	385	E: 4E-15	Ident: 42/378	Ident% 11	Q: 35-394 (396) S: 38-382 (385)	ASPARTATE AMINOTRANSFERASE (TRANSAMINASE A) (ASPAT)	Pos: 99/378	Gap: 51/378
reEHGK1K7q8aPRrAaPsXYutdj9c	15826454 1GC3 15826455 1GC3 15826456 1GC3 15826457 1GC3 15826458 1GC3 15826459 1GC3 15826460 1GC3 15826461 1GC3 15826462 1GC4 15826463 1GC4 15826464 1GC4 15826465 1GC4	385	E: 1E-15	Ident: 42/378	Ident% 11	Q: 35-394 (396) S: 38-382 (385)	Chain A, Thermus Thermophilus Aspartate Aminotransferase Tetra Mutant 2 Complexed With Tryptophan	Pos: 100/378	Gap: 51/378
XKHYQGc0Lc3414IoC1jiWRBfO88	5821836 1BJW 5821837 1BJW	382	E: 4E-15	Ident: 42/378	Ident% 11	Q: 35-394 (396) S: 38-382 (382)	Chain A, Aspartate Aminotransferase From Thermus Thermophilus	Pos: 99/378	Gap: 51/378
wHIpYtiNFZOilicGTrWvdnAtV6U	7546281 1EG5 7546280 1EG5	384	E: 1E-18	Ident: 63/356	Ident% 17	Q: 68-394 (396) S: 44-373 (384)	Chain B, Nifs-Like Protein	Pos: 119/356	Gap: 55/356
2rXX9OSCRSAQ9Rd7XR9WIFN0ESA	7546480 1ECX 7546479 1ECX	384	E: 3E-18	Ident: 62/353	Ident% 17	Q: 71-394 (396) S: 47-373 (384)	Chain B, Nifs-Like Protein	Pos: 119/353	Gap: 55/353
zoaFc/QKTfLHZTU91lg4kWVJ0A8	16975044 1JS3 16975045 1JS3 16975046 1JS6 16975047 1JS6	486	E: 3E-69	Ident: 70/397	Ident% 17	Q: 12-373 (396) S: 54-436 (486)	Aromatic-L-amino-acid decarboxylase (AADC) (DOPA decarboxylase) (DDC)	Pos: 137/397	Gap: 49/397

8NoTBli6WptSdKId3/H3gjwVmpY
15668222
2495766
2129070
1590848

conserved hypothetical protein [Methanococcus jannaschii]

115

MFGc+6jjASLSLwpB8KxNQ02RDZQ
15668223
2495767
2128099
1498813

conserved hypothetical protein [Methanococcus jannaschii]

222

104

382

549

atG1yQwke2RG6n3lgdv1xiWOSTM	1311283 1ORB	296	E: .011E0	Ident: 29/199	Ident% 14	Q: 43-216 (222) S: 102-278 (296)	Thiosulfate:cyanide Sulfurtransferase Mol_id: 1; Molecule: Carboxymethylated Rhodanese; Chain: Null; Ec: 2.8.1.1	Pos: 54/199	Gap: 47/199
ienyYmKsU7Df16Pkk4ayntOmvwM	2914481 1RHS	296	E: .28E0	Ident: 28/199	Ident% 14	Q: 43-216 (222) S: 102-278 (296)	Sulfur-Substituted Rhodanese	Pos: 53/199	Gap: 47/199
n/4bZwOvrwu49faWIPhpaAx3omQ	12084448 1DP2	293	E: .28E0	Ident: 28/199	Ident% 14	Q: 43-216 (222) S: 102-278 (293)	Chain A, Crystal Structure Of The Complex Between Rhodanese And Lipoate	Pos: 53/199	Gap: 47/199
LSPsfuAeo6tQ5g5tDvnHLESETQU	3660166 1C25	161	E: .002E0	Ident: 15/66	Ident% 22	Q: 99-164 (222) S: 38-101 (161)	Human Cdc25a Catalytic Domain	Pos: 29/66	Gap: 2/66
1QUfhPz3q4J9npwgJIAa70Ix6r0	10120629 1CWT	178	E: .22E0	Ident: 12/32	Ident% 37	Q: 106-137 (222) S: 46-77 (178)	Chain A, Human Cdc25b Catalytic Domain With Methyl Mercury	Pos: 19/32	Gap: -1/-1
sCu6KUzLch9Bz5PcPBuPbU2I4Hc	10120628 1CWS 10120709 1CWR 7766892 1QB0	211	E: .22E0	Ident: 12/32	Ident% 37	Q: 106-137 (222) S: 64-95 (211)	Chain A, Human Cdc25b Catalytic Domain With Tungstate	Pos: 19/32	Gap: -1/-1
7EFkDbowYNlS+vvghnMVdVC3p4E	230290 1RHD	293	E: .028E0	Ident: 29/199	Ident% 14	Q: 43-216 (222) S: 102-278 (293)	Rhodanese (E.C.2.8.1.1)	Pos: 54/199	Gap: 47/199
kmQFV2tUJAd5DWO2uEFiEyVbA9g	1827843 2ORA 4929921 1BOH 4929922 1BOI	296	E: .28E0	Ident: 28/199	Ident% 14	Q: 43-216 (222) S: 102-278 (296)	Rhodanese (Thiosulfate: Cyanide Sulfurtransferase)	Pos: 53/199	Gap: 47/199
/lLj0soUNR6u6+/y5irVJ7OKTjE	18655646 1HZM	154	E: .16E0	Ident: 18/119	Ident% 15	Q: 103-219 (222) S: 29-142 (154)	Chain A, Structure Of Erk2 Binding Domain Of Mapk Phosphatase Mkp-3: Structural Insights Into Mkp-3 Activation By Erk2	Pos: 37/119	Gap: 7/119
ffXQB53ysNxeRCkuohWeig2LJTU	8569460 1E0C 8569460 1E0C	271	E: 3E-5	Ident: 23/124	Ident% 18	Q: 94-216 (222) S: 11-120 (271)	Chain A, Sulfurtransferase From Azotobacter Vinelandii	Pos: 46/124	Gap: 15/124
ICnL3kHpKms7K1nziijzSu0MtrQ	17942861 1GMX	108	E: 2E-6	Ident: 22/127	Ident% 17	Q: 94-219 (222) S: 7-99 (108)	Chain A, Escherichia Coli Glpe Sulfurtransferase	Pos: 46/127	Gap: 35/127
h21GmVJobyHj7ztF+RslQ6bNaLQ	17942915 1GN0	108	E: 8E-8	Ident: 23/127	Ident% 18	Q: 94-219 (222) S: 7-99 (108)	protein of glp regulon [Escherichia coli K12]	Pos: 47/127	Gap: 35/127

h0338TFB10nBD4dw/shn1qO6FFI
15668224
2495768
2128100
1498814

M. jannaschii predicted coding region MJ0053 [Methanococcus jannaschii]

227

VagpzKcyyt1qg6h+GZxChvwDy20
15668225
2495769
2128101
1498815

conserved hypothetical protein [Methanococcus jannaschii]

281

9PVMVbWd7yAy/tXt44Urasjd6IM
15668226
2497761
2127946
1590849

GTP cyclohydrolase II (ribA) [Methanococcus jannaschii]

227

6+1iX1mkd28Rr85UYfsp2fHIcQA	14278251 1G57 14278252 1G57 14278253 1G58 14278254 1G58	217	E: 7E-21	Ident: 65/217	Ident% 29	Q: 4-219 (227) S: 16-208 (217)	Chain A, Crystal Structure Of 3,4-Dihydroxy-2-Butanone 4-Phosphate Synthase	Pos: 107/217	Gap: 25/217
JnF07jJZMJS4H+L/dRlafFM2fTg	16974815 1IEZ	217	E: 7E-21	Ident: 65/217	Ident% 29	Q: 4-219 (227) S: 16-208 (217)	3,4 dihydroxy-2-butanone-4-phosphate synthase [Escherichia coli O157:H7 EDL933]	Pos: 107/217	Gap: 25/217

OQ6smSOcMBU07FNmU+Rboiwk22g
15668227
2495770
2128102
1590850

conserved hypothetical protein [Methanococcus jannaschii]

136

*TARGET
8OKiZAlIULzm8LZmfIfsiznOsws
15668228
2495771
2127992
1498818

Na+/H+ antiporter [Methanococcus jannaschii]

426

12
3-25,28-50,60-81,90-112,151-173,181-203,213-235,242-264,275-297,305-327,341-363,383-405

130

350

431

*TARGET
3aAxFuFQzeusZ4J1piPsQ/I9zoI
15668229
2492880
2127758
1590851

ammonium transporter (amtB) [Methanococcus jannaschii]

391

10
9-31,50-72,88-110,112-134,152-174,185-207,216-238,255-277,298-320,339-361

167

259

266

/mCaP4liBl9vYJFbKbFm2G+fLkQ
15668230
2494778
2120008
1592259

nitrogen regulatory protein P-II (glnB) [Methanococcus jannaschii]

112

125

141

150

7Y22MiBZJLsv/Tt1bYG/rQFqOVw	1633299 2PII 1127243 1PIL	112	E: 7E-24	Ident: 63/112	Ident% 56	Q: 1-112 (112) S: 1-112 (112)	regulatory protein P-II for glutamine synthetase [Escherichia coli O157:H7]	Pos: 82/112	Gap: -1/-1
ExtUxkiu3MOYZRwihOXGNyNnqyU	5822483 2GNK	112	E: 1E-39	Ident: 59/112	Ident% 52	Q: 1-112 (112) S: 1-112 (112)	Chain A, Glnk, A Signal Protein From E. Coli	Pos: 79/112	Gap: -1/-1
21OIwpXK/wkNBAQQqc3la9wtP0U	5822079 1GNK 5822078 1GNK	112	E: 5E-42	Ident: 59/112	Ident% 52	Q: 1-112 (112) S: 1-112 (112)	nitrogen regulatory protein P-II 2 [Escherichia coli O157:H7 EDL933]	Pos: 79/112	Gap: -1/-1

/j4tlQW3vQS2ag+g+H62vkJaeSE
15668231
2494055
2127724
1498822

methylthioadenosine phosphorylase (mtaP) [Methanococcus jannaschii]

252

104

132

205

v+WYCgvR0ZUW+Y/kH1bnYvFX2VE	16975349 1K3F 16975350 1K3F 16975351 1K3F 16975352 1K3F 16975353 1K3F 16975354 1K3F	253	E: 3.1E0	Ident: 25/188	Ident% 13	Q: 62-234 (252) S: 78-252 (253)	uridine phosphorylase [Escherichia coli K12]	Pos: 56/188	Gap: 28/188
pPTOxqagLhVVYa4ARnYSQY3bUiU	17942804 1K9S 17942805 1K9S 17942806 1K9S 17942807 1K9S 17942808 1K9S 17942809 1K9S	237	E: .007E0	Ident: 29/191	Ident% 15	Q: 45-228 (252) S: 53-233 (237)	Chain A, Purine Nucleoside Phosphorylase From E. Coli In Complex With Formycin A Derivative And Phosphate	Pos: 58/191	Gap: 17/191
lPEybi+fP3L0KCOIogXYaraP5t0	1633413 1ECP 1633414 1ECP 1633415 1ECP 1633416 1ECP 1633417 1ECP 1633418 1ECP 3892013 1A69 3892015 1A69 3892014 1A69	238	E: .007E0	Ident: 29/191	Ident% 15	Q: 45-228 (252) S: 53-233 (238)	Chain A, Purine Nucleoside Phosphorylase	Pos: 58/191	Gap: 17/191
VOPO8T3cRFsR2ygNp77bKdNpJYs	6730447 1QE5 6730448 1QE5 6730449 1QE5 6730134 1C3X 6730135 1C3X 6730136 1C3X	266	E: 3E-43	Ident: 50/243	Ident% 20	Q: 3-233 (252) S: 33-266 (266)	Chain A, Purine Nucleoside Phosphorylase From Cellulomonas Sp. In Complex With Phosphate	Pos: 93/243	Gap: 21/243
iHKyNLnOJswUn0cYWaovNrMqDQk	15825908 1G2O 15825909 1G2O 15825910 1G2O 15825923 1I80 15825924 1I80 15825925 1I80	268	E: 7E-49	Ident: 55/222	Ident% 24	Q: 14-233 (252) S: 65-267 (268)	deoD [Mycobacterium tuberculosis H37Rv]	Pos: 95/222	Gap: 21/222
AMIrmk+S4cwesa6NeX2Az1nxSEY	3402090 1A9P 3402089 1A9O 3402093 1A9S	289	E: 2E-71	Ident: 56/257	Ident% 21	Q: 2-235 (252) S: 27-283 (289)	Bovine Purine Nucleoside Phosphorylase Complexed With 9-Deazainosine And Phosphate	Pos: 95/257	Gap: 23/257
xrO6PTCD5FftycZTZfHuhc7ufMg	4558114 1B8O 4558113 1B8N	284	E: 2E-71	Ident: 57/257	Ident% 22	Q: 2-235 (252) S: 27-283 (284)	Chain A, Purine Nucleoside Phosphorylase	Pos: 95/257	Gap: 23/257
l5jIyWsDnTDOx2Nj/BkTLnGRAcs	3318947 1A9T	284	E: 2E-71	Ident: 56/257	Ident% 21	Q: 2-235 (252) S: 27-283 (284)	Bovine Purine Nucleoside Phosphorylase Complexed With 9-Deazainosine And Phosphate	Pos: 95/257	Gap: 23/257
Yd/oqFc5JzoBN2wSgpbp66IUX2Y	3402091 1A9Q 3402092 1A9R	282	E: 5E-71	Ident: 56/256	Ident% 21	Q: 2-234 (252) S: 27-282 (282)	Bovine Purine Nucleoside Phosphorylase Complexed With Inosine	Pos: 95/256	Gap: 23/256
HrPWvmQ4bDL82gt/i5tDl8m+WwM	230388 1ULB 230387 1ULA	289	E: 3E-71	Ident: 54/257	Ident% 21	Q: 2-235 (252) S: 27-283 (289)	purine nucleoside phosphorylase [Homo sapiens]	Pos: 89/257	Gap: 23/257
+cvjAQDLyQTDU5xQSm90M1xXiIY	1311143 1PBN 4699623 4PNP 4699622 3PNP	289	E: 3E-71	Ident: 56/257	Ident% 21	Q: 2-235 (252) S: 27-283 (289)	Purine Nucleoside Phosphorylase	Pos: 95/257	Gap: 23/257
/jpO705SPnpblBGMy+2FYR9QC2s	11514560 1FXU	289	E: 4E-72	Ident: 56/257	Ident% 21	Q: 2-235 (252) S: 27-283 (289)	Chain A, Purine Nucleoside Phosphorylase From Calf Spleen In Complex With N(7)-Acycloguanosine Inhibitor And A Phosphate Ion	Pos: 95/257	Gap: 23/257
6IaWoOseRRKdn7Y3944IE9oFlTU	2624420 1VFN	281	E: 6E-72	Ident: 57/257	Ident% 22	Q: 2-235 (252) S: 24-280 (281)	Purine Nucleoside Phosphorylase	Pos: 95/257	Gap: 23/257
YQYb6o+mNKPtlSdUKveEOo7fpHE	5542176 1CG6 5542154 1CB0	283	E: 1E-76	Ident: 99/261	Ident% 37	Q: 2-248 (252) S: 12-272 (283)	5'-methylthioadenosine phosphorylase [Homo sapiens]	Pos: 147/261	Gap: 14/261

kS7A3rPgvaoiDuRkrXSjlUDDOfc
15668232
2494418
2127888
1498823

ferredoxin [Methanococcus jannaschii]

274

1800

2232

+GJCcAELu5pZiM784UWQAyxpDqQ	6729852 7FD1 2624426 6FD1 6729851 6FDR 6729853 7FDR 443515 5FD1 2914395 1AXQ 442901 1FDA 442902 1FDB 349883 1FER	106	E: .18E0	Ident: 13/48	Ident% 27	Q: 30-75 (80) S: 8-54 (106)	Chain A, 7-Fe Ferredoxin From Azotobacter Vinelandii At Ph 8.5, 100 K, 1.35 A	Pos: 18/48	Gap: 3/48
wDKdFxGv1xPRgAjyOhfuIaElFYo	10120847 1FF2	106	E: 2.6E0	Ident: 12/48	Ident% 25	Q: 30-75 (80) S: 8-54 (106)	Chain A, Crystal Structure Of The C42d Mutant Of Azotobacter Vinelandii 7fe Ferredoxin (Fdi)	Pos: 17/48	Gap: 3/48
kIg48lQG1hbdSxu8W2Z+7HJLxQ0	640411 1FRJ	106	E: .24E0	Ident: 12/48	Ident% 25	Q: 30-75 (80) S: 8-54 (106)	Ferredoxin (Fdi) Mutant With Phe 25 Replaced By Ile (F25i)	Pos: 17/48	Gap: 3/48
/cf4aWnHhUUbQzJYlalc/Pt/YAs	442904 1FDD	106	E: .36E0	Ident: 13/48	Ident% 27	Q: 30-75 (80) S: 8-54 (106)	Ferredoxin Mutant With Asp 15 Replaced By Asn (D15n)	Pos: 19/48	Gap: 3/48
iMyNepb8nMkabZXk9/tTA9EaMzA	4139441 1FEH 6730137 1C4A 6730138 1C4C	574	E: 1E0	Ident: 21/79	Ident% 26	Q: 10-75 (80) S: 127-205 (574)	PERIPLASMIC [FE] HYDROGENASE 1	Pos: 34/79	Gap: 13/79
yQysezpIgy5EXPkgq9y3NH3Gpgo	6729719 1BQX 6729750 1BWE 6729719 1BQX 6729750 1BWE	77	E: 2.2E0	Ident: 7/25	Ident% 28	Q: 25-49 (80) S: 34-58 (77)	Chain A, Artificial Fe8s8 Ferredoxin: The D13c Variant Of Bacillus Schlegelii Fe7s8 Ferredoxin	Pos: 13/25	Gap: -1/-1
o4BqKin2wnGOOqLgLsXsVHFoTWM	6729695 1B0T	106	E: .15E0	Ident: 13/48	Ident% 27	Q: 30-75 (80) S: 8-54 (106)	Chain A, D15kK84D MUTANT OF AZOTOBACTER VINELANDII FDI	Pos: 18/48	Gap: 3/48
loGLj57l5LgQ64JlcN8+ghK6O5Q	640412 1FRK 640412 1FRK	106	E: .17E0	Ident: 13/48	Ident% 27	Q: 30-75 (80) S: 8-54 (106)	Ferredoxin (Fdi) Mutant With His 35 Replaced By Asp (H35d)	Pos: 18/48	Gap: 3/48
5xSPy+cFzzfqHehaKELq/fFwonw	1310890 1CLF 1310890 1CLF	55	E: .01E0	Ident: 14/45	Ident% 31	Q: 30-74 (80) S: 8-51 (55)	Clostridium Pasteurianum Ferredoxin	Pos: 22/45	Gap: 1/45
DQZRu/1iO/Xkv1jEgQ0v7P4lT0c	2098504 1FTC 2098505 1FTC	106	E: .2E0	Ident: 13/48	Ident% 27	Q: 30-75 (80) S: 8-54 (106)	Chain A, Y13c Mutant Of Azotobacter Vinelandii Fdi	Pos: 18/48	Gap: 3/48
nge+kG6iYzQQt7xGjSFdcKQ6Rt8	1943573 1BLU	82	E: 1.5E0	Ident: 15/55	Ident% 27	Q: 28-76 (80) S: 6-59 (82)	Structure Of The 2[4fe-4s] Ferredoxin From Chromatium Vinosum	Pos: 25/55	Gap: 7/55
CgruAQnSEgW+lL5k+XYzHmwctEk	7546410 1DUR	55	E: .004E0	Ident: 14/53	Ident% 26	Q: 22-74 (80) S: 1-50 (55)	ferredoxin 2[4Fe-4S] [validated] - Peptostreptococcus asaccharolyticus	Pos: 21/53	Gap: 3/53
iQSEJwYITV2R3WJvDblYKM46o0Q	6435688 1D3W	106	E: .27E0	Ident: 13/48	Ident% 27	Q: 30-75 (80) S: 8-54 (106)	Chain A, Crystal Structure Of Ferredoxin 1 D15e Mutant From Azotobacter Vinelandii At 1.7 Angstrom Resolution	Pos: 18/48	Gap: 3/48
2xxTpjvmscJ469r9dxRPOLjaLsc	3318893 1BD6 3318893 1BD6	77	E: 1.5E0	Ident: 7/25	Ident% 28	Q: 25-49 (80) S: 34-58 (77)	7-Fe Ferredoxin From Bacillus Schlegelii, Nmr, Minimized Average Structure	Pos: 13/25	Gap: -1/-1
qxiEu8o08o1qDoLq6yI134Srrrg	4930042 1HFE 4930044 1HFE	421	E: 1.3E0	Ident: 16/54	Ident% 29	Q: 23-75 (80) S: 28-81 (421)	PERIPLASMIC [FE] HYDROGENASE LARGE SUBUNIT (FE HYDROGENLYASE)	Pos: 24/54	Gap: 1/54
nf4y4bxj9elJZrW7KKNrL67NMOs	13399647 1H7W 13399648 1H7W 13399649 1H7W 13399650 1H7W	1025	E: 2.9E0	Ident: 22/68	Ident% 32	Q: 6-70 (80) S: 932-996 (1025)	Chain A, Dihydropyrimidine Dehydrogenase (Dpd) From Pig	Pos: 31/68	Gap: 6/68
JfVoTFlIZRcJlQyFWNh5fHC5xkM	12084520 1GAO 12084521 1GAO 12084522 1GAO 12084523 1GAO	106	E: .074E0	Ident: 13/48	Ident% 27	Q: 30-75 (80) S: 8-54 (106)	Chain A, Crystal Structure Of The L44s Mutant Of Ferredoxin I	Pos: 18/48	Gap: 3/48
g2pwKD1gqMG5wMsDpC0bBSKM3oI	3114424 2FDN 640397 1FDN	55	E: .002E0	Ident: 15/53	Ident% 28	Q: 22-74 (80) S: 1-51 (55)	FERREDOXIN	Pos: 23/53	Gap: 2/53
SOPRvn2QaOUjkvQ5O3SLtRBKRyQ	15825930 1JB0 15825930 1JB0	80	E: .012E0	Ident: 11/58	Ident% 18	Q: 27-77 (80) S: 7-64 (80)	Chain C, Crystal Structure Of Photosystem I: A Photosynthetic Reaction Center And Core Antenna System From Cyanobacteria	Pos: 17/58	Gap: 7/58
GEAQAaM8LuOiwqWmvUIP/ujr8Xw	1065197 1FCA	55	E: .002E0	Ident: 13/53	Ident% 24	Q: 22-74 (80) S: 1-51 (55)	Ferredoxin	Pos: 21/53	Gap: 2/53
fGvF3SwaFFk9Bk7s0WH1Zlguxx4	640414 1FRM	106	E: .17E0	Ident: 13/48	Ident% 27	Q: 30-75 (80) S: 8-54 (106)	Ferredoxin (Fdi) Mutant With Glu 46 Replaced By Ala (E46a)	Pos: 18/48	Gap: 3/48
Q125RpMho9EZQi8VTwB6VThNPNw	3318886 1BC6 3318886 1BC6	77	E: 1.4E0	Ident: 7/25	Ident% 28	Q: 25-49 (80) S: 34-58 (77)	7-Fe Ferredoxin From Bacillus Schlegelii, Nmr, 20 Structures	Pos: 13/25	Gap: -1/-1
qQplKtyoIwG7exLqldeSrI1Eksg	229911 1FD2	106	E: .002E0	Ident: 12/53	Ident% 22	Q: 25-75 (80) S: 3-54 (106)	Ferredoxin (Mutant With Cys 20 Replaced By Ala) (C20A)	Pos: 19/53	Gap: 3/53
uSp4lyNDaZPY+UVPBME4WnK5nzc	13399651 1H7X 13399652 1H7X 13399653 1H7X 13399654 1H7X	1025	E: 2.7E0	Ident: 22/68	Ident% 32	Q: 6-70 (80) S: 932-996 (1025)	Chain A, Dihydropyrimidine Dehydrogenase (Dpd) From Pig, Ternary Complex Of A Mutant Enzyme (C671a), Nadph And 5-Fluorouracil	Pos: 31/68	Gap: 6/68
3tCQS5D57iL+uq4Eep83G/7nRrM	17942775 1H98 17942775 1H98	78	E: .8E0	Ident: 6/28	Ident% 21	Q: 25-52 (80) S: 34-61 (78)	Ferredoxin	Pos: 11/28	Gap: -1/-1
l7/cipYNUBBLIxzO5Q8s7ITvXw8	9256973 1F5B	106	E: .18E0	Ident: 13/48	Ident% 27	Q: 30-75 (80) S: 8-54 (106)	Chain A, Crystal Structure Of F2h Ferredoxin 1 Mutant From Azotobacter Vinelandii At 1.75 Angstrom Resolution	Pos: 18/48	Gap: 3/48
MsAAgplcdI2MFIMRV6p5sw4bcTo	1633514 1ROF 1942765 1VJW	60	E: 2.7E0	Ident: 11/58	Ident% 18	Q: 23-79 (80) S: 3-60 (60)	ferredoxin [Thermotoga maritima]	Pos: 21/58	Gap: 1/58
SH16zLMC8lDzlqTrXLFPPEJa3ig	6980482 1B0V 6980483 1B0V 6980484 1B0V 6980485 1B0V	106	E: .72E0	Ident: 13/48	Ident% 27	Q: 30-75 (80) S: 8-54 (106)	Chain A, I40n Mutant Of Azotobacter Vinelandii Fdi	Pos: 18/48	Gap: 3/48
6Ekbo0SCjFYvxg39JnwnmbJ7Vbs	11514021 1G3O	106	E: .7E0	Ident: 12/48	Ident% 25	Q: 30-75 (80) S: 8-54 (106)	Chain A, Crystal Structure Of V19e Mutant Of Ferredoxin I	Pos: 17/48	Gap: 3/48
Qe3jBXA3OcrgzBJbOuL4CTe/9j0	640415 1FRX	106	E: .002E0	Ident: 12/53	Ident% 22	Q: 25-75 (80) S: 3-54 (106)	Ferredoxin (Fdi) Mutant With Cys 20 Replaced By Ser (C20s)	Pos: 19/53	Gap: 3/53
iWtrpMuYsuB5Jn+pd4gDE0Gq3J8	11513606 1G6B 11513606 1G6B	106	E: .22E0	Ident: 13/48	Ident% 27	Q: 30-75 (80) S: 8-54 (106)	Chain A, Crystal Structure Of P47s Mutant Of Ferredoxin I	Pos: 18/48	Gap: 3/48
aGGKUqjNEv24fhTGLQy+jpCJRvI	640409 1FRI	106	E: 2E-4	Ident: 14/53	Ident% 26	Q: 25-75 (80) S: 3-54 (106)	Ferredoxin (Fdi) Mutant With Asp 23 Replaced By Asn (D23n)	Pos: 20/53	Gap: 3/53
2hG8JJNBvGLy4OK+bdlHFYT4mUo	640413 1FRL	106	E: 3E-4	Ident: 13/53	Ident% 24	Q: 25-75 (80) S: 3-54 (106)	Ferredoxin (Fdi) Mutant With Glu 38 Replaced By Ser (E38s)	Pos: 21/53	Gap: 3/53
gKvs7La5SfJ/Y+chhsg97cy8zys	3212403 1A6L	106	E: 5E-4	Ident: 13/53	Ident% 24	Q: 25-75 (80) S: 3-54 (106)	T14c Mutant Of Azotobacter Vinelandii Fdi	Pos: 20/53	Gap: 3/53
jKdyEAp/MhaKX3+iz1lBCe/77h0	9256974 1F5C	106	E: 5E-4	Ident: 12/53	Ident% 22	Q: 25-75 (80) S: 3-54 (106)	Chain A, Crystal Structure Of F25h Ferredoxin 1 Mutant From Azotobacter Vinelandii At 1.75 Angstrom Resolution	Pos: 19/53	Gap: 3/53
I72Dln91KCIeVbXqmZyKxz1tYE4	640408 1FRH	106	E: 3E-4	Ident: 13/53	Ident% 24	Q: 25-75 (80) S: 3-54 (106)	Ferredoxin (Fdi) Mutant With Phe 2 Replaced By Tyr (F2y)	Pos: 20/53	Gap: 3/53
z1LxZZWfFIAH0OSD5kYo6tqQAhk	230509 2FD2	106	E: 9E-5	Ident: 13/53	Ident% 24	Q: 25-75 (80) S: 3-54 (106)	Ferredoxin (Mutant With Cys 24 Replaced By Ala) (C24A)	Pos: 20/53	Gap: 3/53
8ymp5ZKp2+2BBBERbg3oODedPNk	2554684 1XER	103	E: 4E-7	Ident: 18/68	Ident% 26	Q: 19-78 (80) S: 34-101 (103)	Structure Of Ferredoxin	Pos: 25/68	Gap: 8/68
VzH5n6t+6j1FiRcfHsybOkdExyA	18158649 1KEK 18158650 1KEK 4558091 1B0P 4558092 1B0P 4558221 2PDA 4558222 2PDA	1231	E: 5E-8	Ident: 13/84	Ident% 15	Q: 22-77 (80) S: 680-763 (1231)	Chain A, Crystal Structure Of The Free Radical Intermediate Of Pyruvate:ferredoxin Oxidoreductase	Pos: 25/84	Gap: 28/84

78QT/A516j3SKhxWLIEggGg7snk
15668233
2500922
2128103
1498824

hypothetical protein [Methanococcus jannaschii]

207

143

185

159

ChcEMZLKcA3YNdjNPlatNQDcTSs

13096287 1HRU
13096288 1HRU

188

E: 7E-8

Ident: 38/140

Ident% 27

Q: 28-158 (207) S: 15-154 (188)

Chain A, The Structure Of The Yrdc Gene Product From E.Coli

Pos: 72/140

Gap: 9/140

WcssMiy7b7dk8gZeN75MQO8yolA
15668234
2495772
2128104
1590854

M. jannaschii predicted coding region MJ0063 [Methanococcus jannaschii]

181

324

6QSnlqRelWe0xtS3XEh3L5ipn+E

9955321 1DXL
9955322 1DXL
9955323 1DXL
9955324 1DXL

470

E: 3E0

Ident: 34/126

Ident% 26

Q: 20-132 (181) S: 54-170 (470)

Chain A, Dihydrolipoamide Dehydrogenase Of Glycine Decarboxylase From Pisum Sativum

Pos: 56/126

Gap: 22/126

*TARGET
M+tWL8fphPeaX/OzNzZMAAdPyl8
15668235
2495773
2128105
1590855

M. jannaschii predicted coding region MJ0064 [Methanococcus jannaschii]

189

1
163-185

456

640

1352

EHxOTtDRMWwW2F82isCZi9gmzuw
15668236
2495774
2128106
1498827

conserved hypothetical protein [Methanococcus jannaschii]

363

xWEKtPd9H4KgqVnF0xWiJhMTtJw
15668237
2495775
2128107
1590856

sulfate adenylate transferase, subunit 2 (cysD) [Methanococcus jannaschii]

480

244

449

653

v7t/rHfd9FYzTF2fbeXEoIyXI4o	18158792 1JGT 18158793 1JGT	513	E: .006E0	Ident: 39/274	Ident% 14	Q: 153-403 (480) S: 148-401 (513)	Chain A, Crystal Structure Of Beta-Lactam Synthetase	Pos: 76/274	Gap: 43/274
EM3OuV6sPyIcrOaDRgrnnXhsiiw	1310841 1GPM 1310843 1GPM 1310842 1GPM 1310844 1GPM	525	E: 2E-11	Ident: 40/193	Ident% 20	Q: 242-421 (480) S: 216-404 (525)	GMP synthetase (glutamine-hydrolyzing) [Escherichia coli K12]	Pos: 72/193	Gap: 17/193
P46QX2zhccQaG7bm/hbu1uWLBnE	5107693 1SUR	215	E: 5E-36	Ident: 45/211	Ident% 21	Q: 222-424 (480) S: 10-212 (215)	Phospho-Adenylyl-Sulfate Reductase	Pos: 93/211	Gap: 16/211

DRNQSLGWheWZOrt/1tXQwS9L3xY
15668238
2495776
2128108
1498829

M. jannaschii predicted coding region MJ0067 [Methanococcus jannaschii]

103

1
32-54

UXl70xL/aU7x95hJbmU3qo7oO90
15668239
2495777
2128109
1498830

conserved hypothetical protein [Methanococcus jannaschii]

115

1
58-79

o2znh0RAtJxCqUhqLSbVlND/Yuk
15668240
2498154
2127737
1592260

acetylglutamate kinase (argB) [Methanococcus jannaschii]

300

147

364

482

NL7cRLgoPLaobFNirUviJ4sIRhs	9955156 1E19 9955157 1E19	314	E: 4E-11	Ident: 58/294	Ident% 19	Q: 27-275 (300) S: 2-295 (314)	Carbamate kinase (Carbamate kinase-like carbamoylphosphate synthetase)	Pos: 112/294	Gap: 45/294
wjJ9vbHDCm++ufOc/u+2GSeg7ic	6980398 1B7B 6980399 1B7B 6980400 1B7B 6980401 1B7B	310	E: 8E-12	Ident: 65/312	Ident% 20	Q: 27-299 (300) S: 2-310 (310)	CARBAMATE KINASE	Pos: 118/312	Gap: 42/312

75NB2a22wXqLjC7mrC3g19+BWrA
15668241
2495778
2128110
1498832

M. jannaschii predicted coding region MJ0070 [Methanococcus jannaschii]

103

Y3KHNMhTIt2eh2aKQFj+YDjpseQ
15668242
2495779
2128111
1498833

conserved hypothetical protein [Methanococcus jannaschii]

CiYY9VS7SYhJFn6JkqazVaavVW4
15668243
2495780
2128112
1590858

M. jannaschii predicted coding region MJ0072 [Methanococcus jannaschii]

ZrCa3k7rmu2hP3RwBYIggyDMxAM
15668244
2495781
2128113
1590859

M. jannaschii predicted coding region MJ0073 [Methanococcus jannaschii]

199

1030

1193

J14DK6NIUBoatmiCeKSLYXRkLz8	14719642 1F5S 14719643 1F5S	211	E: .034E0	Ident: 20/80	Ident% 25	Q: 2-81 (93) S: 137-207 (211)	phosphoserine phosphatase (serB) [Methanococcus jannaschii]	Pos: 36/80	Gap: 9/80
UmNScvLZOzPyvpSWM8cKs4hFVNY	9257145 1EUL 18159010 1KJU	994	E: .003E0	Ident: 22/62	Ident% 35	Q: 15-76 (93) S: 684-740 (994)	Chain A, Crystal Structure Of Calcium Atpase With Two Bound Calcium Ions	Pos: 36/62	Gap: 5/62
Vdj+Ws9/lKWLm+lO3xOedqPRMv0	15826095 1J97 15826096 1J97	211	E: .031E0	Ident: 20/80	Ident% 25	Q: 2-81 (93) S: 137-207 (211)	Chain A, Phospho-Aspartyl Intermediate Analogue Of Phosphoserine Phosphatase	Pos: 36/80	Gap: 9/80

5/nZjulHJ4AC3aBfXQQ+CbELIOg
15668245
2496243
2128114
1590860

M. jannaschii predicted coding region MJ0074 [Methanococcus jannaschii]

358

101

QD09v6y3LcDnVAIJ+ubGqgD4DzQ
15668246
2496244
2128115
1590862

M. jannaschii predicted coding region MJ0075 [Methanococcus jannaschii]

365

QSHtrwNAYXYVxcLYQNuyJSFygKU
15668247
2495783
2128116
1498840

conserved hypothetical protein [Methanococcus jannaschii]

382

180

570

ao28Ox3MjwDQzIIgYB2Jdn7fb8w	2982054 1ATZ 2982053 1ATZ	189	E: 9.8E0	Ident: 12/97	Ident% 12	Q: 219-310 (382) S: 1-96 (189)	Chain B, Human Von Willebrand Factor A3 Domain	Pos: 32/97	Gap: 6/97
1epdOVYFFBXDAEOJ9zf3RpOxzzw	13786657 1FE8 13786660 1FE8 13786663 1FE8	196	E: 4E0	Ident: 12/98	Ident% 12	Q: 218-310 (382) S: 6-102 (196)	Chain A, Crystal Structure Of The Von Willebrand Factor A3 Domain In Complex With A Fab Fragment Of Igg Ru5 That Inhibits Collagen Binding	Pos: 32/98	Gap: 6/98
zLveicgS7MwhsicXMA+ZaM+EVEQ	1942623 1JLM	192	E: 2.8E0	Ident: 20/120	Ident% 16	Q: 220-321 (382) S: 3-118 (192)	I-Domain From Integrin Cr3, Mn2+ Bound	Pos: 40/120	Gap: 22/120
1aDp9g/huZAZnBa94zeEjntr7Hc	3891525 1BHQ 3891526 1BHQ 3891523 1BHO 3891524 1BHO 3891487 1IDN 3891488 1IDN	190	E: 7E0	Ident: 20/115	Ident% 17	Q: 225-321 (382) S: 3-113 (190)	Chain 1, Mac-1 I Domain Cadmium Complex	Pos: 39/115	Gap: 22/115
EqJX3eM+zQXIyivwyM6xqiaAy44	1827901 1IDO	192	E: 5E0	Ident: 20/115	Ident% 17	Q: 225-321 (382) S: 11-121 (192)	I-Domain From Integrin Cr3, Mg2+ Bound	Pos: 39/115	Gap: 22/115

nm5rpYg+XzL/j5OslbLIj1dVZkA
15668248
2495782
2127993
1498839

conserved hypothetical protein) [Methanococcus jannaschii]

113

8Dp8WW2c9GMizW4zYAd9ldzRBng
15668249
2495784
2128117
1498841

M. jannaschii predicted coding region MJ0078 [Methanococcus jannaschii]

207

3L5GOWagA+TJ5nWpLiOf3VlhIFU
15668250
2495785
2127994
1590863

regulatory protein, putative (moxR) [Methanococcus jannaschii]

380

1371

1536

8F6wQyvxO46gAOLmeQaqijmCKdc	15825804 1IN4	334	E: .002E0	Ident: 35/183	Ident% 19	Q: 19-186 (380) S: 27-190 (334)	Holliday junction DNA helicase [Thermotoga maritima]	Pos: 63/183	Gap: 34/183
DOuiLI2/wYqdbPHHEdikg1RBHbk	7245635 1DO2 7245636 1DO2 7245637 1DO2 7245638 1DO2 7245733 1DO0 7245734 1DO0 7245735 1DO0 7245736 1DO0 7245737 1DO0 7245738 1DO0	442	E: .002E0	Ident: 39/276	Ident% 14	Q: 7-239 (380) S: 4-275 (442)	Chain A, Trigonal Crystal Form Of Heat Shock Locus U (Hslu) From Escherichia Coli	Pos: 92/276	Gap: 47/276
y6DmWiIH9AALWyOIwRl3tNpm6BY	15825807 1IN7	334	E: .002E0	Ident: 30/149	Ident% 20	Q: 19-152 (380) S: 27-159 (334)	Chain A, Thermotoga Maritima Ruvb R170a	Pos: 53/149	Gap: 31/149
EERS/16O3gptXoyz8uOxjqZiY48	13399751 1G4A 13399752 1G4A 13399757 1G4B 13399758 1G4B 13399759 1G4B 13399760 1G4B	443	E: .002E0	Ident: 42/282	Ident% 14	Q: 1-239 (380) S: 1-276 (443)	heat shock protein hslVU, ATPase subunit, homologous to chaperones [Escherichia coli O157:H7 EDL933]	Pos: 96/282	Gap: 49/282
ipw07lpZfhwgzuJP8x0KG5aq2DM	15825813 1J7K	334	E: .002E0	Ident: 35/183	Ident% 19	Q: 19-186 (380) S: 27-190 (334)	Chain A, Thermotoga Maritima Ruvb P216g Mutant	Pos: 63/183	Gap: 34/183
RUQqaY/E17zzAKWGrj92sCRoIa0	15825806 1IN6	334	E: .008E0	Ident: 34/183	Ident% 18	Q: 19-186 (380) S: 27-190 (334)	Chain A, Thermotoga Maritima Ruvb K64r Mutant	Pos: 63/183	Gap: 34/183
jT16rmsWK4wzWla7stQfYxFKzc4	11513635 1E94 11513636 1E94 17942585 1HT2 17942586 1HT2 17942591 1HT2 17942592 1HT2 17942603 1HT1 17942604 1HT1 17942605 1HT1 17942606 1HT1 17942611 1HQY 17942612 1HQY	449	E: .002E0	Ident: 39/276	Ident% 14	Q: 7-239 (380) S: 11-282 (449)	Chain E, Hslv-Hslu From E.Coli	Pos: 92/276	Gap: 47/276
0MEvOkKr8OI2856yiCCRa6FaiGk	15825805 1IN5	334	E: 2E-16	Ident: 31/221	Ident% 14	Q: 11-215 (380) S: 19-221 (334)	Chain A, Thermogota Maritima Ruvb A156s Mutant	Pos: 65/221	Gap: 34/221
yLaGm9IiCwHDwP9FpN6bZ4qVoUA	15825808 1IN8	334	E: 3E-16	Ident: 31/211	Ident% 14	Q: 11-206 (380) S: 19-211 (334)	Chain A, Thermotoga Maritima Ruvb T158v	Pos: 63/211	Gap: 33/211
7p31udcsdEo83MCeJFYMQz922a8	14488635 1E32	458	E: 9E-20	Ident: 29/214	Ident% 13	Q: 30-238 (380) S: 232-435 (458)	Chain A, Structure Of The N-Terminal Domain And The D1 Aaa Domain Of Membrane Fusion Atpase P97	Pos: 67/214	Gap: 15/214
0B8TwyQpQ7qbXEdQmvS8QbF0gbg	15825870 1G8P	350	E: 2E-28	Ident: 46/314	Ident% 14	Q: 18-278 (380) S: 25-334 (350)	Magnesium-chelatase 38 kDa subunit (Mg-protoporphyrin IX chelatase)	Pos: 94/314	Gap: 57/314

7Q6uo53T/iaEqmK+seeogGvsrn0
15668251
2495786
2128118
1498843

conserved hypothetical protein [Methanococcus jannaschii]

127

134

ZAS5GR0qeGzAKHGHniiIK+atJbI	6573449 2CPG 6573448 2CPG 6573450 2CPG	45	E: 5.1E0	Ident: 10/37	Ident% 27	Q: 2-38 (127) S: 3-39 (45)	Chain B, Transcriptional Repressor Copg	Pos: 26/37	Gap: -1/-1
XU4bf+rzVk8oMnZmZTxlVmC121A	16975419 1EA4 16975420 1EA4 16975421 1EA4 16975422 1EA4 16975423 1EA4 16975424 1EA4 16975426 1EA4 16975427 1EA4 16975428 1EA4 6573432 1B01 6573433 1B01	45	E: 4.5E0	Ident: 10/37	Ident% 27	Q: 2-38 (127) S: 3-39 (45)	replication protein A [Plasmid pLS1]	Pos: 26/37	Gap: -1/-1
TYDTAc5WqpO7Ka93SfxTmGs/JNw	16975425 1EA4	44	E: 4.5E0	Ident: 10/37	Ident% 27	Q: 2-38 (127) S: 2-38 (44)	Chain H, Transcriptional Repressor Copg22BP DSDNA COMPLEX	Pos: 26/37	Gap: -1/-1

AuiZSkYF6zb0mhH6E30XrfatVls
15668252
3915770
2826241

methyl coenzyme M reductase II, subunit beta (mrtB) [Methanococcus jannaschii]

447

0T9gn9FRBXs4ZhVfqa/fl1yLSGo	11514434 1E6Y 11514437 1E6Y	433	E: 1E-135	Ident: 249/429	Ident% 58	Q: 6-434 (447) S: 2-430 (433)	Chain B, Methyl-Coenzyme M Reductase From Methanosarcina Barkeri	Pos: 316/429	Gap: -1/-1
92HGU6BYATm6rHxGzQ9txXP77qk	12084787 1E6V 12084788 1E6V	443	E: 1E-149	Ident: 282/435	Ident% 64	Q: 5-439 (447) S: 6-439 (443)	Chain B, Methyl-Coenzyme M Reductase From Methanopyrus Kandleri	Pos: 349/435	Gap: 1/435
N7nOYbU4eT3b2kxETN27sr8xNUc	15826789 1HBM 15826792 1HBM 15826795 1HBN 15826798 1HBN 15826801 1HBO 15826804 1HBO 15826807 1HBU 15826810 1HBU 3891379 1MRO 3891382 1MRO	442	E: 1E-155	Ident: 293/440	Ident% 66	Q: 4-443 (447) S: 3-441 (442)	Chain B, Methyl-Coenzyme M Reductase Enzyme Product Complex	Pos: 358/440	Gap: 1/440

GMQOE2GS2yMVEVMzGOijOumOXeA
15668253
2497838
2117588
1498845

methyl coenzyme M reductase II, subunit gamma (mtrG) [Methanococcus jannaschii]

266

k4fVocq22F9Nq2UzwdEfLLTd67o	11514435 1E6Y 11514438 1E6Y	247	E: 2E-61	Ident: 128/249	Ident% 51	Q: 2-250 (266) S: 1-244 (247)	Chain C, Methyl-Coenzyme M Reductase From Methanosarcina Barkeri	Pos: 166/249	Gap: 5/249
0aFBrJD2CS2DNDjRPQg/6N4NFKY	11514427 1E6V 11514430 1E6V	258	E: 4E-76	Ident: 162/251	Ident% 64	Q: 1-250 (266) S: 1-250 (258)	Chain C, Methyl-Coenzyme M Reductase From Methanopyrus Kandleri	Pos: 196/251	Gap: 2/251
iKlJIIDUGoGqqv/Tgx6Rb9eNOTQ	3891380 1MRO 3891383 1MRO	247	E: 2E-81	Ident: 158/247	Ident% 63	Q: 6-252 (266) S: 2-247 (247)	Chain C, Methyl-Coenzyme M Reductase	Pos: 194/247	Gap: 1/247
LHNqSLyNIKIMFRmt+++ZrhKGYSc	15826790 1HBM 15826793 1HBM 15826796 1HBN 15826799 1HBN 15826802 1HBO 15826805 1HBO 15826808 1HBU 15826811 1HBU	248	E: 8E-82	Ident: 159/248	Ident% 64	Q: 6-253 (266) S: 2-248 (248)	Chain C, Methyl-Coenzyme M Reductase Enzyme Product Complex	Pos: 195/248	Gap: 1/248

K3FVzSPrPFgNhaK4QRu/Yry8nZI
15668254
2497836
2117586
1590865

methyl coenzyme M reductase II, subunit alpha (mtrA) [Methanococcus jannaschii]

552

178

184

oohPJFzGNu5SaBwytnVJoHr7MdQ	11514425 1E6V 11514428 1E6V	553	E: 0E0	Ident: 420/550	Ident% 76	Q: 3-551 (552) S: 4-552 (553)	METHYL-COENZYME M REDUCTASE I ALPHA SUBUNIT (MCR I ALPHA)	Pos: 478/550	Gap: 2/550
lTEL5HVV9wZMqfwBqOsHltzsJuM	3891378 1MRO 3891381 1MRO	548	E: 0E0	Ident: 384/547	Ident% 70	Q: 6-551 (552) S: 3-548 (548)	Chain A, Methyl-Coenzyme M Reductase	Pos: 441/547	Gap: 2/547
pM1oMicIxOcy7Rhbjtsu6+wPN7s	12084789 1E6Y 12084790 1E6Y	569	E: 0E0	Ident: 345/542	Ident% 63	Q: 19-551 (552) S: 29-568 (569)	Chain A, Methyl-Coenzyme M Reductase From Methanosarcina Barkeri	Pos: 409/542	Gap: 11/542
UGmGgZef0RBle9P6OvvPdHbzqPk	15826788 1HBM 15826791 1HBM 15826794 1HBN 15826797 1HBN 15826800 1HBO 15826803 1HBO 15826806 1HBU 15826809 1HBU	549	E: 0E0	Ident: 384/547	Ident% 70	Q: 6-551 (552) S: 3-548 (549)	Chain A, Methyl-Coenzyme M Reductase Enzyme Product Complex	Pos: 441/547	Gap: 2/547

L/RTYZgLoRZ5EAqC8MiWqGMg9sc
15668255
2495787
2129170
1590866

CODH nickel-insertion accessory protein (cooC) [Methanococcus jannaschii]

249

338

1215

1237

3BgeMZ6BFNupbalw/pdyB3sGeMk	15988243 1ION	243	E: .018E0	Ident: 55/231	Ident% 23	Q: 5-230 (249) S: 8-210 (243)	Chain A, The Septum Site-Determining Protein Mind Complexed With Mg- Adp From Pyrococcus Horikoshii Ot3	Pos: 102/231	Gap: 33/231
CFG4EQfHlw3zH0XXCLdJgxtkLRg	10835832 1F48 15988419 1IHU 15988420 1II0 15988421 1II0 15988422 1II9 15988423 1II9 10835832 1F48 15988419 1IHU 15988420 1II0 15988421 1II0 15988422 1II9 15988423 1II9	589	E: 5.2E0	Ident: 14/34	Ident% 41	Q: 7-40 (249) S: 15-48 (589)	Chain A, Crystal Structure Of The Escherichia Coli Arsenite- Translocating Atpase	Pos: 22/34	Gap: -1/-1
fTIoJyO/Shrp4BpYo6Y5RjFX/yg	13096247 1G1M 13096248 1G1M 13096265 1G5P 13096266 1G5P 13096555 1FP6 13096556 1FP6 13096557 1FP6 13096558 1FP6 3891309 2NIP 3891308 2NIP 2624433 1N2C 2624434 1N2C 2624435 1N2C 2624436 1N2C 443146 1NIP 443147 1NIP	289	E: 2E-26	Ident: 35/252	Ident% 13	Q: 4-243 (249) S: 6-237 (289)	Chain A, All-Ferrous Nitrogenase Iron Protein From Azotobacter Vinelandii	Pos: 73/252	Gap: 32/252
6+6tZ8GkUvkHE9qMU8axELktGHw	7245830 1DE0 7245831 1DE0	289	E: 2E-26	Ident: 34/252	Ident% 13	Q: 4-243 (249) S: 6-237 (289)	Chain A, Modulating The Midpoint Potential Of The [4fe-4s] Cluster Of The Nitrogenase Fe Protein	Pos: 73/252	Gap: 32/252
R4Ntx/udi4KTYO32Y8h1br8qvtw	13096253 1G20 13096254 1G20 13096255 1G20 13096256 1G20 13096261 1G21 13096262 1G21 13096263 1G21 13096264 1G21	289	E: 8E-26	Ident: 35/251	Ident% 13	Q: 4-243 (249) S: 7-237 (289)	Chain E, Mgatp-Bound And Nucleotide-Free Structures Of A Nitrogenase Protein Complex Between Leu127del-Fe Protein And The Mofe Protein	Pos: 73/251	Gap: 31/251
KQ/jNVW6vykvnLTmvBrQa2jm5iA	3891564 1CP2 3891565 1CP2	269	E: 2E-26	Ident: 41/263	Ident% 15	Q: 2-247 (249) S: 3-244 (269)	Chain A, Nitrogenase Iron Protein From Clostridium Pasteurianum	Pos: 86/263	Gap: 38/263
F+MPUjh6i9STg8Qe0jMlH4bw5GI	13787126 1HYQ	263	E: 1E-30	Ident: 53/253	Ident% 20	Q: 2-246 (249) S: 5-228 (263)	cell division inhibitor (minD-1) [Archaeoglobus fulgidus]	Pos: 103/253	Gap: 37/253
O6LNgse0G/wKFmgauvTlwbE7CxE	14278418 1G3Q 14278419 1G3R	237	E: 7E-33	Ident: 55/243	Ident% 22	Q: 4-241 (249) S: 7-221 (237)	Chain A, Crystal Structure Analysis Of Pyrococcus Furiosus Cell Division Atpase Mind	Pos: 100/243	Gap: 33/243

vBeLHSjs0AKSIlI3odG1csOhxgA
15668256
2495788
2129082
1590868

iron transport periplasmic binding protein, putative (ceuE) [Methanococcus jannaschii]

373

1
5-27

304

361

yeUd0C0K/dIerNuEQ7n14gDUcAw

7546212 1EFD

266

E: .003E0

Ident: 43/265

Ident% 16

Q: 56-311 (373) S: 5-245 (266)

Chain N, Periplasmic Ferric Siderophore Binding Protein Fhud Complexed With Gallichrome

Pos: 87/265

Gap: 33/265

a2kCk7xsmLzI7masC3T1aF3n89g
15668257
2495789
2128119
1498850

unspecified methyltransferase [Methanococcus jannaschii]

372

411

1213

CLwBDHjwMBl6r+Evx1ZsEsKT2pE	13399462 1FP1	372	E: 3.5E0	Ident: 54/226	Ident% 23	Q: 29-208 (372) S: 40-246 (372)	isoliquiritigenin 2'-O-methyltransferase - alfalfa	Pos: 91/226	Gap: 65/226
1C5GcqvpAIv9PkNHXFVCgS2x3Bc	13399464 1FPQ	372	E: .073E0	Ident: 64/320	Ident% 20	Q: 29-305 (372) S: 40-343 (372)	Chain A, Crystal Structure Analysis Of Selenomethionine Substituted Chalcone O-Methyltransferase	Pos: 115/320	Gap: 59/320
KvA/gFgwGTZo3udIfCuYDUYMKok	1942407 1XVA 1942408 1XVA 4139415 1BHJ 4139416 1BHJ 6137381 1D2C 6137382 1D2C	292	E: .002E0	Ident: 22/185	Ident% 11	Q: 149-314 (372) S: 37-201 (292)	Chain A, Methyltransferase	Pos: 57/185	Gap: 39/185
6WRUmfFkUHO5q8JMb4xzwfMupbI	6435570 1D2G 6435571 1D2G 6435572 1D2H 6435573 1D2H 6435574 1D2H 6435575 1D2H	292	E: .002E0	Ident: 22/185	Ident% 11	Q: 149-314 (372) S: 37-201 (292)	Chain A, Crystal Structure Of R175k Mutant Glycine N- Methyltransferase From Rat Liver	Pos: 57/185	Gap: 39/185
Wddivj6xnNcTc3wDunDAYHxkp/0	16974818 1IM8 16974819 1IM8	244	E: 7.6E0	Ident: 27/143	Ident% 18	Q: 177-308 (372) S: 64-205 (244)	Chain A, Crystal Structure Of Yeco From Haemophilus Influenzae (Hi0319), A Methyltransferase With A Bound S- Adenosylhomocysteine	Pos: 53/143	Gap: 12/143
lvV9EWMq77UqxJ8kc84I2Mjac+g	13787051 1F3L	321	E: 8E-4	Ident: 13/75	Ident% 17	Q: 173-245 (372) S: 47-120 (321)	Chain A, Crystal Structure Of The Conserved Core Of Protein Arginine Methyltransferase Prmt3	Pos: 28/75	Gap: 3/75
THMXI+EwFWrStxZxMR/rZMoqaoM	12084699 1G6Q 12084700 1G6Q 12084701 1G6Q 12084702 1G6Q 12084703 1G6Q 12084704 1G6Q	328	E: 3E-5	Ident: 28/192	Ident% 14	Q: 151-340 (372) S: 18-173 (328)	Chain 1, Crystal Structure Of Yeast Arginine Methyltransferase, Hmt1	Pos: 58/192	Gap: 38/192
vA+2H/nVRtry7DbEZBMzWESzqAU	12084575 1DL5 12084576 1DL5	317	E: 1E-6	Ident: 24/126	Ident% 19	Q: 149-270 (372) S: 53-173 (317)	L-isoaspartate(D-aspartate) O-methyltransferase [Thermotoga maritima]	Pos: 45/126	Gap: 9/126
lM2+ripCwRk/MZZDqFHy17GXCMQ	17942640 1JG4 17942641 1JG3 17942642 1JG3 17942645 1JG2 17942646 1JG1	235	E: 2E-8	Ident: 39/188	Ident% 20	Q: 103-270 (372) S: 4-187 (235)	Chain A, Crystal Structure Of L-Isoaspartyl (D-Aspartyl) O- Methyltransferase With S-Adenosylmethionine	Pos: 68/188	Gap: 24/188
haJpE3oCsT1VwDwRhiFFet7yd6A	13399467 1FPX	352	E: 5E-27	Ident: 58/366	Ident% 15	Q: 8-341 (372) S: 8-349 (352)	Chain A, Crystal Structure Analysis Of Selenomethionine Substituted Isoflavone O-Methyltransferase	Pos: 112/366	Gap: 56/366
P+3IE1q+NiZA4sbw1/YGgJtxJSA	13399463 1FP2	352	E: 3E-31	Ident: 58/366	Ident% 15	Q: 8-341 (372) S: 8-349 (352)	isoflavone-O-methytransferase (EC 2.1.1.-) - alfalfa	Pos: 113/366	Gap: 56/366

*TARGET
cJ3NEutQx0dTGCfg9Pb3L/Rlkyc
15668258
2501404
2127961
1590869

hemin permease (hemU) [Methanococcus jannaschii]

349

8
21-43,62-84,131-153,162-184,204-225,258-280,292-314,319-341

534

642

666

oUezaTEbqhJqJYd90Z/nuU04f0k
15668259
2495790
2128120
1590870

M. jannaschii predicted coding region MJ0088 [Methanococcus jannaschii]

180

cg4xI4aG0O0CCa2lVaafPu0xv1c
15668260
2492574
2127897
1498853

ferric enterobactin transport ATP-binding protein [Methanococcus jannaschii]

254

1302

1316

1343

vwZlRCrw/davJk0PIngo3RbJxdw	15988440 1JSQ 15988441 1JSQ 15988442 1JSQ 15988443 1JSQ 15988444 1JSQ 15988445 1JSQ 15988446 1JSQ 15988447 1JSQ	582	E: 6E-57	Ident: 59/227	Ident% 25	Q: 6-226 (254) S: 342-565 (582)	ATP-binding transport protein; multicopy suppressor of htrB [Escherichia coli O157:H7 EDL933]	Pos: 112/227	Gap: 9/227
bHzMC4Gxg64/bRB+N8ytSV+FEa0	15826057 1F3O	235	E: 1E-64	Ident: 77/226	Ident% 34	Q: 6-220 (254) S: 2-226 (235)	Chain A, Crystal Structure Of Mj0796 Atp-Binding Cassette	Pos: 118/226	Gap: 12/226
ImYhpWAkHn8eI11by5jCV4ScHuA	12084694 1G29 12084695 1G29	372	E: 1E-72	Ident: 61/234	Ident% 26	Q: 3-229 (254) S: 1-230 (372)	Chain 1, Malk	Pos: 115/234	Gap: 11/234

/xzH5pJpzLugaDInzwpMSjMczXg
15668261
2499893
2127834
1590871

collagenase (prtC) [Methanococcus jannaschii]

407

101

163

161

+2NC+m7KRbQs8Wn2+h2U7EdMjCM	1941991 1QAP 1941992 1QAP	296	E: 8.8E0	Ident: 15/86	Ident% 17	Q: 12-97 (407) S: 216-280 (296)	Chain A, Quinolinic Acid Phosphoribosyltransferase With Bound Quinolinic Acid	Pos: 27/86	Gap: 21/86
Txx0Eudc/mdkXNnEvo8P0g/UoP4	576250 1PMY	123	E: 4.6E0	Ident: 13/48	Ident% 27	Q: 346-393 (407) S: 24-71 (123)	PSEUDOAZURIN	Pos: 19/48	Gap: -1/-1

*TARGET
oBtb1C9ewd1o/uqSQeU8dDJ+auA
15668262
2495791
2129153
1590872

Na+/Ca+ exchanger protein, putative [Methanococcus jannaschii]

302

8
1-23,37-59,73-95,111-133,159-181,193-215,227-249,265-287

252

571

601

CmX0UAtP2XtfrsfT86wy5/HwAKk
15668263
2494622
2127928
1498856

heterodisulfide reductase, subunit D (hdrD) [Methanococcus jannaschii]

489

382

817

1099

e8bS99K9p4eSI3JDsqRrfPGZwEw	2914607 1QOB 2914608 1QOB	98	E: 6.6E0	Ident: 14/55	Ident% 25	Q: 3-57 (489) S: 2-50 (98)	Chain A, Ferredoxin Mutation D62k	Pos: 23/55	Gap: 6/55
LHAkXqnextvfeofA6qcvyTkQj0o	2914612 1QOF 2914613 1QOF	98	E: 7.5E0	Ident: 14/55	Ident% 25	Q: 3-57 (489) S: 2-50 (98)	Chain A, Ferredoxin Mutation Q70k	Pos: 23/55	Gap: 6/55
VzH5n6t+6j1FiRcfHsybOkdExyA	18158649 1KEK 18158650 1KEK 4558091 1B0P 4558092 1B0P 4558221 2PDA 4558222 2PDA	1231	E: .25E0	Ident: 18/70	Ident% 25	Q: 132-197 (489) S: 686-755 (1231)	Chain A, Crystal Structure Of The Free Radical Intermediate Of Pyruvate:ferredoxin Oxidoreductase	Pos: 25/70	Gap: 4/70
rw3G5f1ie3rmBruRop1hiFlpWVQ	14488782 1J7A	98	E: 6.6E0	Ident: 14/55	Ident% 25	Q: 3-57 (489) S: 2-50 (98)	Chain A, Structure Of The Anabaena Ferredoxin D68k Mutant	Pos: 23/55	Gap: 6/55
iMyNepb8nMkabZXk9/tTA9EaMzA	4139441 1FEH 6730137 1C4A 6730138 1C4C	574	E: .001E0	Ident: 39/204	Ident% 19	Q: 19-199 (489) S: 11-203 (574)	PERIPLASMIC [FE] HYDROGENASE 1	Pos: 67/204	Gap: 34/204
5xSPy+cFzzfqHehaKELq/fFwonw	1310890 1CLF	55	E: .043E0	Ident: 14/74	Ident% 18	Q: 128-201 (489) S: 2-52 (55)	Clostridium Pasteurianum Ferredoxin	Pos: 19/74	Gap: 23/74
bmhWcf8690L3kwB6MyUxDRL/SsM	2914614 1QOG 2914615 1QOG	98	E: 6E0	Ident: 14/55	Ident% 25	Q: 3-57 (489) S: 2-50 (98)	Chain A, Ferredoxin Mutation S47a	Pos: 23/55	Gap: 6/55
i3bPyLxbnYDERJnRz49tJHHKCWY	2914605 1QOA 2914606 1QOA	98	E: 7.3E0	Ident: 13/55	Ident% 23	Q: 3-57 (489) S: 2-50 (98)	Chain A, Ferredoxin Mutation C49s	Pos: 19/55	Gap: 6/55
CgruAQnSEgW+lL5k+XYzHmwctEk	7546410 1DUR	55	E: 1.3E0	Ident: 14/74	Ident% 18	Q: 132-205 (489) S: 6-55 (55)	ferredoxin 2[4Fe-4S] [validated] - Peptostreptococcus asaccharolyticus	Pos: 20/74	Gap: 24/74
qxiEu8o08o1qDoLq6yI134Srrrg	4930042 1HFE 4930044 1HFE	421	E: 1.2E0	Ident: 16/97	Ident% 16	Q: 101-197 (489) S: 6-77 (421)	PERIPLASMIC [FE] HYDROGENASE LARGE SUBUNIT (FE HYDROGENLYASE)	Pos: 29/97	Gap: 25/97
1+2luvestDL/mf4m7gOmAWoHlkU	13096128 1EWY 6980569 1CZP 6980570 1CZP 6730558 1QT9 229927 1FXA 229928 1FXA	98	E: 6.4E0	Ident: 14/55	Ident% 25	Q: 3-57 (489) S: 2-50 (98)	Chain C, Anabaena Pcc7119 Ferredoxin:ferredoxin-Nadp+-Reductase Complex	Pos: 23/55	Gap: 6/55
g2pwKD1gqMG5wMsDpC0bBSKM3oI	3114424 2FDN 640397 1FDN	55	E: 6.5E0	Ident: 15/71	Ident% 21	Q: 132-202 (489) S: 6-53 (55)	FERREDOXIN	Pos: 21/71	Gap: 23/71
SOPRvn2QaOUjkvQ5O3SLtRBKRyQ	15825930 1JB0	80	E: 8.4E0	Ident: 13/71	Ident% 18	Q: 129-199 (489) S: 5-60 (80)	Chain C, Crystal Structure Of Photosystem I: A Photosynthetic Reaction Center And Core Antenna System From Cyanobacteria	Pos: 18/71	Gap: 15/71
fpelcJxSyXI/xO2bTSWP912/8mw	2914662 1AWD	94	E: 5.7E0	Ident: 21/55	Ident% 38	Q: 3-57 (489) S: 2-46 (94)	FERREDOXIN	Pos: 29/55	Gap: 10/55
GEAQAaM8LuOiwqWmvUIP/ujr8Xw	1065197 1FCA	55	E: 1.2E0	Ident: 14/70	Ident% 20	Q: 132-201 (489) S: 6-52 (55)	Ferredoxin	Pos: 19/70	Gap: 23/70
c5ODEIele1P0/tmwsw93szDlSvI	349931 2PIA	321	E: 1.9E0	Ident: 15/43	Ident% 34	Q: 18-60 (489) S: 248-284 (321)	Phthalate Dioxygenase Reductase (E.C.1.18.1.)	Pos: 24/43	Gap: 6/43
WxTPgTPhB9S8A7HbaxDkyPdB3zU	14488784 1J7C	98	E: 6.3E0	Ident: 14/55	Ident% 25	Q: 3-57 (489) S: 2-50 (98)	Chain A, Structure Of The Anabaena Ferredoxin Mutant E95k	Pos: 23/55	Gap: 6/55
8ymp5ZKp2+2BBBERbg3oODedPNk	2554684 1XER	103	E: .28E0	Ident: 18/70	Ident% 25	Q: 130-199 (489) S: 41-96 (103)	Structure Of Ferredoxin	Pos: 21/70	Gap: 14/70
uYoKXBigdez+L2OsDQIxMbotzKg	1310945 4FXC	98	E: 8.1E0	Ident: 12/55	Ident% 21	Q: 3-57 (489) S: 2-50 (98)	FERREDOXIN	Pos: 21/55	Gap: 6/55
qr9o4LcQsLySlJp4s5mArM2wQ0o	18158824 1HLR	907	E: 3.4E0	Ident: 16/42	Ident% 38	Q: 45-83 (489) S: 37-78 (907)	Chain A, Structure Refinement Of The Aldehyde Oxidoreductase From Desulfovibrio Gigas At 1.28 A	Pos: 23/42	Gap: 3/42
Cjyty8uUCjoQ6+jUSSx4B2Amaps	494032 1FRR 494033 1FRR	95	E: .25E0	Ident: 18/84	Ident% 21	Q: 18-83 (489) S: 14-91 (95)	FERREDOXIN I	Pos: 26/84	Gap: 24/84
nPBjq/Bk6cbQl841Sa+GpMRVQYk	14488783 1J7B	98	E: 6.3E0	Ident: 14/55	Ident% 25	Q: 3-57 (489) S: 2-50 (98)	Chain A, Structure Of The Anabaena Ferredoxin Mutant E94k	Pos: 23/55	Gap: 6/55
6RNObzCsQZH9QGgMNOD/Mu3sPwM	14278676 1E7P 14278679 1E7P 14278682 1E7P 14278685 1E7P 6730465 1QLA 6730468 1QLA 6730471 1QLB 6730474 1QLB	239	E: 2E-18	Ident: 65/221	Ident% 29	Q: 1-202 (489) S: 4-224 (239)	Fumarate reductase iron-sulfur protein	Pos: 111/221	Gap: 19/221
fFNH9v5dE+qaDKIs3YFhzTaIlxY	5542236 1FUM 5542240 1FUM	243	E: 2E-25	Ident: 73/214	Ident% 34	Q: 2-201 (489) S: 6-219 (243)	Chain B, Structure Of The E. Coli Fumarate Reductase Respiratory Complex	Pos: 114/214	Gap: 14/214

jMytaJlbeMMY6p1Qhfuj+GZ/QLI
15668264
2495792
2128121
1498857

M. jannaschii predicted coding region MJ0093 [Methanococcus jannaschii]

142

112

fIrI+kRVpRIxAtfxfPfYr1GIGlY	1943063 1DKZ 1943059 1DKY 1943060 1DKY 1943063 1DKZ 1943059 1DKY 1943060 1DKY	219	E: 4.3E0	Ident: 35/127	Ident% 27	Q: 17-136 (142) S: 76-168 (219)	Chain A, The Substrate Binding Domain Of Dnak In Complex With A Substrate Peptide, Determined From Type 1 Native Crystals	Pos: 53/127	Gap: 41/127
9MimyTqf3l2TzAL6LeMHLWxezyA	4557941 1BPR 4557961 2BPR 4557941 1BPR 4557961 2BPR	191	E: 4.3E0	Ident: 35/127	Ident% 27	Q: 17-136 (142) S: 94-186 (191)	Nmr Structure Of The Substrate Binding Domain Of Dnak, Minimized Average Structure	Pos: 53/127	Gap: 41/127
ScByE0pBM26vORE5bBnGz93AEvg	1943057 1DKX 1943057 1DKX	219	E: 4.3E0	Ident: 35/127	Ident% 27	Q: 17-136 (142) S: 76-168 (219)	Chain A, The Substrate Binding Domain Of Dnak In Complex With A Substrate Peptide, Determined From Type 1 Selenomethionyl Crystals	Pos: 53/127	Gap: 41/127

6F81fT8FszX3gAviEKIyjLW+wkY
15668265
2495793
2128122
1590873

methyl coenzyme M reductase II, operon protein C (mtrC) [Methanococcus jannaschii]

310

Na9vl/JUCF7MPUB8npwpKwCpEo0
15668266
2495794
2128123
1592261

M. jannaschii predicted coding region MJ0095 [Methanococcus jannaschii]

126

rnLIkpdiwNwQquJA3k+3vyNEeUI
15668267
2495795
2128124
1498861

M. jannaschii predicted coding region MJ0096 [Methanococcus jannaschii]

262

5
24-46,90-112,134-156,167-189,203-225

Wxq26ROS8GgHCuEnwrLfdTSVakY
15668268
2495796
2129319
1498862

translation initiation factor aIF-2, subunit beta, putative (aIF2B) [Methanococcus jannaschii]

143

E3kujTH1B4esT3FLzHO5y3w86Jg
15668269
1710548
2119125
1590876

LSU ribosomal protein L37E [Methanococcus jannaschii]

120

138

141

r8yuj0q+TuGHj5GFThAbLByExYg

10120943 1FFK
15825968 1JJ2
10120943 1FFK
15825968 1JJ2
10120943 1FFK
15825968 1JJ2

E: 5E-4

Ident: 25/54

Ident% 46

Q: 2-54 (61) S: 2-54 (56)

50S ribosomal protein L37E (L35E)

Pos: 36/54

Gap: 2/54

XBUsz7vdY6r1WpKL0IlJpLo4DuU
15668270
2494419
2127887
1590877

ferredoxin II [Methanococcus jannaschii]

131

1235

2316

2164

aGGKUqjNEv24fhTGLQy+jpCJRvI	640409 1FRI	106	E: 8.1E0	Ident: 6/28	Ident% 21	Q: 75-102 (131) S: 32-59 (106)	Ferredoxin (Fdi) Mutant With Asp 23 Replaced By Asn (D23n)	Pos: 15/28	Gap: -1/-1
2hG8JJNBvGLy4OK+bdlHFYT4mUo	640413 1FRL 640413 1FRL	106	E: 8.7E0	Ident: 14/50	Ident% 28	Q: 80-127 (131) S: 6-54 (106)	Ferredoxin (Fdi) Mutant With Glu 38 Replaced By Ser (E38s)	Pos: 25/50	Gap: 3/50
VzH5n6t+6j1FiRcfHsybOkdExyA	18158649 1KEK 18158650 1KEK 4558091 1B0P 4558092 1B0P 4558221 2PDA 4558222 2PDA	1231	E: 7.2E0	Ident: 17/72	Ident% 23	Q: 80-125 (131) S: 686-757 (1231)	Chain A, Crystal Structure Of The Free Radical Intermediate Of Pyruvate:ferredoxin Oxidoreductase	Pos: 25/72	Gap: 26/72
/cf4aWnHhUUbQzJYlalc/Pt/YAs	442904 1FDD	106	E: 8.1E0	Ident: 6/28	Ident% 21	Q: 75-102 (131) S: 32-59 (106)	Ferredoxin Mutant With Asp 15 Replaced By Asn (D15n)	Pos: 15/28	Gap: -1/-1
iMyNepb8nMkabZXk9/tTA9EaMzA	4139441 1FEH 6730137 1C4A 6730138 1C4C	574	E: .092E0	Ident: 21/73	Ident% 28	Q: 68-127 (131) S: 133-205 (574)	PERIPLASMIC [FE] HYDROGENASE 1	Pos: 35/73	Gap: 13/73
yQysezpIgy5EXPkgq9y3NH3Gpgo	6729719 1BQX 6729750 1BWE 6729719 1BQX 6729750 1BWE	77	E: .28E0	Ident: 9/25	Ident% 36	Q: 77-101 (131) S: 34-58 (77)	Chain A, Artificial Fe8s8 Ferredoxin: The D13c Variant Of Bacillus Schlegelii Fe7s8 Ferredoxin	Pos: 15/25	Gap: -1/-1
o4BqKin2wnGOOqLgLsXsVHFoTWM	6729695 1B0T	106	E: 8.3E0	Ident: 6/28	Ident% 21	Q: 75-102 (131) S: 32-59 (106)	Chain A, D15kK84D MUTANT OF AZOTOBACTER VINELANDII FDI	Pos: 15/28	Gap: -1/-1
MsAAgplcdI2MFIMRV6p5sw4bcTo	1633514 1ROF 1942765 1VJW	60	E: 5.8E0	Ident: 7/20	Ident% 35	Q: 104-123 (131) S: 2-21 (60)	ferredoxin [Thermotoga maritima]	Pos: 9/20	Gap: -1/-1
5xSPy+cFzzfqHehaKELq/fFwonw	1310890 1CLF 1310890 1CLF	55	E: .006E0	Ident: 18/47	Ident% 38	Q: 80-126 (131) S: 6-51 (55)	Clostridium Pasteurianum Ferredoxin	Pos: 24/47	Gap: 1/47
nge+kG6iYzQQt7xGjSFdcKQ6Rt8	1943573 1BLU	82	E: .017E0	Ident: 14/54	Ident% 25	Q: 80-127 (131) S: 6-58 (82)	Structure Of The 2[4fe-4s] Ferredoxin From Chromatium Vinosum	Pos: 22/54	Gap: 7/54
iWtrpMuYsuB5Jn+pd4gDE0Gq3J8	11513606 1G6B 11513606 1G6B	106	E: 3.3E0	Ident: 15/50	Ident% 30	Q: 80-127 (131) S: 6-54 (106)	Chain A, Crystal Structure Of P47s Mutant Of Ferredoxin I	Pos: 26/50	Gap: 3/50
CgruAQnSEgW+lL5k+XYzHmwctEk	7546410 1DUR	55	E: 4.7E0	Ident: 7/23	Ident% 30	Q: 74-96 (131) S: 28-50 (55)	ferredoxin 2[4Fe-4S] [validated] - Peptostreptococcus asaccharolyticus	Pos: 12/23	Gap: -1/-1
Qe3jBXA3OcrgzBJbOuL4CTe/9j0	640415 1FRX 640415 1FRX	106	E: 7.5E0	Ident: 6/29	Ident% 20	Q: 74-102 (131) S: 31-59 (106)	Ferredoxin (Fdi) Mutant With Cys 20 Replaced By Ser (C20s)	Pos: 15/29	Gap: -1/-1
I72Dln91KCIeVbXqmZyKxz1tYE4	640408 1FRH	106	E: 4.1E0	Ident: 15/50	Ident% 30	Q: 80-127 (131) S: 6-54 (106)	Ferredoxin (Fdi) Mutant With Phe 2 Replaced By Tyr (F2y)	Pos: 26/50	Gap: 3/50
2xxTpjvmscJ469r9dxRPOLjaLsc	3318893 1BD6 3318893 1BD6	77	E: .22E0	Ident: 9/25	Ident% 36	Q: 77-101 (131) S: 34-58 (77)	7-Fe Ferredoxin From Bacillus Schlegelii, Nmr, Minimized Average Structure	Pos: 15/25	Gap: -1/-1
+GJCcAELu5pZiM784UWQAyxpDqQ	6729852 7FD1 2624426 6FD1 6729851 6FDR 6729853 7FDR 443515 5FD1 2914395 1AXQ 442901 1FDA 442902 1FDB 349883 1FER	106	E: 8.3E0	Ident: 6/28	Ident% 21	Q: 75-102 (131) S: 32-59 (106)	Chain A, 7-Fe Ferredoxin From Azotobacter Vinelandii At Ph 8.5, 100 K, 1.35 A	Pos: 15/28	Gap: -1/-1
loGLj57l5LgQ64JlcN8+ghK6O5Q	640412 1FRK 640412 1FRK	106	E: 3.4E0	Ident: 7/29	Ident% 24	Q: 74-102 (131) S: 31-59 (106)	Ferredoxin (Fdi) Mutant With His 35 Replaced By Asp (H35d)	Pos: 16/29	Gap: -1/-1
DQZRu/1iO/Xkv1jEgQ0v7P4lT0c	2098504 1FTC 2098505 1FTC	106	E: 2.7E0	Ident: 15/50	Ident% 30	Q: 80-127 (131) S: 6-54 (106)	Chain A, Y13c Mutant Of Azotobacter Vinelandii Fdi	Pos: 26/50	Gap: 3/50
SOPRvn2QaOUjkvQ5O3SLtRBKRyQ	15825930 1JB0	80	E: .061E0	Ident: 20/60	Ident% 33	Q: 80-130 (131) S: 8-67 (80)	Chain C, Crystal Structure Of Photosystem I: A Photosynthetic Reaction Center And Core Antenna System From Cyanobacteria	Pos: 29/60	Gap: 9/60
GEAQAaM8LuOiwqWmvUIP/ujr8Xw	1065197 1FCA	55	E: .4E0	Ident: 15/47	Ident% 31	Q: 80-126 (131) S: 6-51 (55)	Ferredoxin	Pos: 22/47	Gap: 1/47
fGvF3SwaFFk9Bk7s0WH1Zlguxx4	640414 1FRM 640414 1FRM	106	E: 2.5E0	Ident: 15/50	Ident% 30	Q: 80-127 (131) S: 6-54 (106)	Ferredoxin (Fdi) Mutant With Glu 46 Replaced By Ala (E46a)	Pos: 26/50	Gap: 3/50
Q125RpMho9EZQi8VTwB6VThNPNw	3318886 1BC6 3318886 1BC6	77	E: .2E0	Ident: 9/25	Ident% 36	Q: 77-101 (131) S: 34-58 (77)	7-Fe Ferredoxin From Bacillus Schlegelii, Nmr, 20 Structures	Pos: 15/25	Gap: -1/-1
z1LxZZWfFIAH0OSD5kYo6tqQAhk	230509 2FD2 230509 2FD2	106	E: 2.8E0	Ident: 15/50	Ident% 30	Q: 80-127 (131) S: 6-54 (106)	Ferredoxin (Mutant With Cys 24 Replaced By Ala) (C24A)	Pos: 26/50	Gap: 3/50
qQplKtyoIwG7exLqldeSrI1Eksg	229911 1FD2 229911 1FD2	106	E: 7.9E0	Ident: 6/29	Ident% 20	Q: 74-102 (131) S: 31-59 (106)	Ferredoxin (Mutant With Cys 20 Replaced By Ala) (C20A)	Pos: 15/29	Gap: -1/-1
8ymp5ZKp2+2BBBERbg3oODedPNk	2554684 1XER 2554684 1XER	103	E: 8.7E0	Ident: 6/29	Ident% 20	Q: 103-131 (131) S: 36-64 (103)	Structure Of Ferredoxin	Pos: 13/29	Gap: -1/-1
3tCQS5D57iL+uq4Eep83G/7nRrM	17942775 1H98 17942775 1H98	78	E: 1.4E0	Ident: 16/40	Ident% 40	Q: 88-127 (131) S: 16-54 (78)	Ferredoxin	Pos: 21/40	Gap: 1/40
l7/cipYNUBBLIxzO5Q8s7ITvXw8	9256973 1F5B	106	E: 3.9E0	Ident: 15/50	Ident% 30	Q: 80-127 (131) S: 6-54 (106)	Chain A, Crystal Structure Of F2h Ferredoxin 1 Mutant From Azotobacter Vinelandii At 1.75 Angstrom Resolution	Pos: 26/50	Gap: 3/50
wDKdFxGv1xPRgAjyOhfuIaElFYo	10120847 1FF2	106	E: 2E-4	Ident: 13/54	Ident% 24	Q: 80-131 (131) S: 6-58 (106)	Chain A, Crystal Structure Of The C42d Mutant Of Azotobacter Vinelandii 7fe Ferredoxin (Fdi)	Pos: 25/54	Gap: 3/54
gKvs7La5SfJ/Y+chhsg97cy8zys	3212403 1A6L	106	E: 2E-4	Ident: 16/54	Ident% 29	Q: 74-127 (131) S: 3-54 (106)	T14c Mutant Of Azotobacter Vinelandii Fdi	Pos: 28/54	Gap: 2/54
JfVoTFlIZRcJlQyFWNh5fHC5xkM	12084520 1GAO 12084521 1GAO 12084522 1GAO 12084523 1GAO	106	E: 2E-4	Ident: 14/50	Ident% 28	Q: 80-127 (131) S: 6-54 (106)	Chain A, Crystal Structure Of The L44s Mutant Of Ferredoxin I	Pos: 26/50	Gap: 3/50
SH16zLMC8lDzlqTrXLFPPEJa3ig	6980482 1B0V 6980483 1B0V 6980484 1B0V 6980485 1B0V	106	E: 8E-4	Ident: 14/50	Ident% 28	Q: 80-127 (131) S: 6-54 (106)	Chain A, I40n Mutant Of Azotobacter Vinelandii Fdi	Pos: 24/50	Gap: 3/50
iQSEJwYITV2R3WJvDblYKM46o0Q	6435688 1D3W	106	E: 2E-5	Ident: 14/54	Ident% 25	Q: 80-131 (131) S: 6-58 (106)	Chain A, Crystal Structure Of Ferredoxin 1 D15e Mutant From Azotobacter Vinelandii At 1.7 Angstrom Resolution	Pos: 26/54	Gap: 3/54
g2pwKD1gqMG5wMsDpC0bBSKM3oI	3114424 2FDN 640397 1FDN	55	E: 7E-5	Ident: 17/47	Ident% 36	Q: 80-126 (131) S: 6-51 (55)	FERREDOXIN	Pos: 22/47	Gap: 1/47
jKdyEAp/MhaKX3+iz1lBCe/77h0	9256974 1F5C	106	E: 5E-5	Ident: 14/54	Ident% 25	Q: 80-131 (131) S: 6-58 (106)	Chain A, Crystal Structure Of F25h Ferredoxin 1 Mutant From Azotobacter Vinelandii At 1.75 Angstrom Resolution	Pos: 26/54	Gap: 3/54
kIg48lQG1hbdSxu8W2Z+7HJLxQ0	640411 1FRJ	106	E: 2E-5	Ident: 15/54	Ident% 27	Q: 80-131 (131) S: 6-58 (106)	Ferredoxin (Fdi) Mutant With Phe 25 Replaced By Ile (F25i)	Pos: 27/54	Gap: 3/54
6Ekbo0SCjFYvxg39JnwnmbJ7Vbs	11514021 1G3O	106	E: 6E-5	Ident: 14/54	Ident% 25	Q: 80-131 (131) S: 6-58 (106)	Chain A, Crystal Structure Of V19e Mutant Of Ferredoxin I	Pos: 27/54	Gap: 3/54
qxiEu8o08o1qDoLq6yI134Srrrg	4930042 1HFE 4930044 1HFE	421	E: 4E-9	Ident: 17/56	Ident% 30	Q: 74-128 (131) S: 27-82 (421)	PERIPLASMIC [FE] HYDROGENASE LARGE SUBUNIT (FE HYDROGENLYASE)	Pos: 23/56	Gap: 1/56
nf4y4bxj9elJZrW7KKNrL67NMOs	13399647 1H7W 13399648 1H7W 13399649 1H7W 13399650 1H7W	1025	E: 3E-15	Ident: 29/84	Ident% 34	Q: 52-130 (131) S: 922-1005 (1025)	Chain A, Dihydropyrimidine Dehydrogenase (Dpd) From Pig	Pos: 40/84	Gap: 5/84
uSp4lyNDaZPY+UVPBME4WnK5nzc	13399651 1H7X 13399652 1H7X 13399653 1H7X 13399654 1H7X	1025	E: 3E-15	Ident: 29/84	Ident% 34	Q: 52-130 (131) S: 922-1005 (1025)	Chain A, Dihydropyrimidine Dehydrogenase (Dpd) From Pig, Ternary Complex Of A Mutant Enzyme (C671a), Nadph And 5-Fluorouracil	Pos: 40/84	Gap: 5/84

IUYWZvfgFhHZfx/VVkuvqNEGmkY
15668271
2495797
2128125
1498865

conserved hypothetical protein [Methanococcus jannaschii]

509

733

1638

1611

hyvgTEArBXmHlAVUX4ZR9eQrCNU	2554679 1AK5 2554679 1AK5	503	E: .038E0	Ident: 23/89	Ident% 25	Q: 420-503 (509) S: 129-217 (503)	INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE (IMP DEHYDROGENASE) (IMPDH) (IMPD)	Pos: 47/89	Gap: 5/89
BZHE0WVqR6RKYWkKVAdnKYdeJ4Q	7546367 1ZFJ	491	E: .28E0	Ident: 30/92	Ident% 32	Q: 353-444 (509) S: 126-209 (491)	Chain A, Inosine Monophosphate Dehydrogenase (Impdh; Ec 1.1.1.205) From Streptococcus Pyogenes	Pos: 43/92	Gap: 8/92
17x5TlulZYrUf1UY7XPKS/h/P+U	7546357 1EEP 7546356 1EEP	404	E: 1E-6	Ident: 12/77	Ident% 15	Q: 303-379 (509) S: 18-88 (404)	IMP dehydrogenase (guaB) [Borrelia burgdorferi]	Pos: 32/77	Gap: 6/77
qGPwBxhEgtYik3OetHZbpyktoLE	4929871 1B3O 4929870 1B3O	514	E: 4E-19	Ident: 37/198	Ident% 18	Q: 313-503 (509) S: 48-229 (514)	Inosine-5'-monophosphate dehydrogenase 2 (IMP dehydrogenase 2) (IMPDH-II) (IMPD 2)	Pos: 73/198	Gap: 23/198
Bb8+hjv3PzEAhjIQ5/MfXUmtP9c	15826575 1JR1 15826576 1JR1	514	E: 2E-19	Ident: 37/198	Ident% 18	Q: 313-503 (509) S: 48-229 (514)	INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE 2 (IMP DEHYDROGENASE 2) (IMPDH-II) (IMPD 2)	Pos: 75/198	Gap: 23/198

UycXI0IeHyE25ooIjH1maghS4mE
15668272
2500886
2129283
1590878

signal recognition particle, subunit SRP54 [Methanococcus jannaschii]

451

384

1209

1212

NhHBeSLYZh0HfuciYkIi09emX1Y	7245564 1DUL	69	E: .021E0	Ident: 26/67	Ident% 38	Q: 361-426 (451) S: 2-68 (69)	Chain A, Structure Of The Ribonucleoprotein Core Of The E. Coli Signal Recognition Particle	Pos: 39/67	Gap: 1/67
6+6tZ8GkUvkHE9qMU8axELktGHw	7245830 1DE0 7245831 1DE0	289	E: .43E0	Ident: 10/32	Ident% 31	Q: 107-138 (451) S: 9-40 (289)	Chain A, Modulating The Midpoint Potential Of The [4fe-4s] Cluster Of The Nitrogenase Fe Protein	Pos: 15/32	Gap: -1/-1
R4Ntx/udi4KTYO32Y8h1br8qvtw	13096253 1G20 13096254 1G20 13096255 1G20 13096256 1G20 13096261 1G21 13096262 1G21 13096263 1G21 13096264 1G21	289	E: .51E0	Ident: 10/32	Ident% 31	Q: 107-138 (451) S: 10-41 (289)	Chain E, Mgatp-Bound And Nucleotide-Free Structures Of A Nitrogenase Protein Complex Between Leu127del-Fe Protein And The Mofe Protein	Pos: 15/32	Gap: -1/-1
fTIoJyO/Shrp4BpYo6Y5RjFX/yg	13096247 1G1M 13096248 1G1M 13096265 1G5P 13096266 1G5P 13096555 1FP6 13096556 1FP6 13096557 1FP6 13096558 1FP6 3891309 2NIP 3891308 2NIP 2624433 1N2C 2624434 1N2C 2624435 1N2C 2624436 1N2C 443146 1NIP 443147 1NIP	289	E: .48E0	Ident: 10/32	Ident% 31	Q: 107-138 (451) S: 9-40 (289)	Chain A, All-Ferrous Nitrogenase Iron Protein From Azotobacter Vinelandii	Pos: 15/32	Gap: -1/-1
lN+uiuEA0xZJDUa4dT51vvYfiQg	15988434 1JJ7	260	E: 5.3E0	Ident: 16/41	Ident% 39	Q: 93-133 (451) S: 36-76 (260)	Chain A, Crystal Structure Of The C-Terminal Atpase Domain Of Human Tap1	Pos: 19/41	Gap: -1/-1
CFG4EQfHlw3zH0XXCLdJgxtkLRg	10835832 1F48 15988419 1IHU 15988420 1II0 15988421 1II0 15988422 1II9 15988423 1II9 10835832 1F48 15988419 1IHU 15988420 1II0 15988421 1II0 15988422 1II9 15988423 1II9	589	E: 2.1E0	Ident: 9/38	Ident% 23	Q: 100-137 (451) S: 8-45 (589)	Chain A, Crystal Structure Of The Escherichia Coli Arsenite- Translocating Atpase	Pos: 18/38	Gap: -1/-1
oLYbTq239jH4G5zkfpQoUp7BEuo	13399857 1HQC 13399858 1HQC	324	E: .34E0	Ident: 28/152	Ident% 18	Q: 75-225 (451) S: 17-125 (324)	Chain A, Structure Of Ruvb From Thermus Thermophilus Hb8	Pos: 45/152	Gap: 44/152
+9Qu9Jrqbo8MyKpHGzaGNMO1IQg	16975072 1G3U	214	E: .39E0	Ident: 25/116	Ident% 21	Q: 103-198 (451) S: 3-113 (214)	tmk [Mycobacterium tuberculosis H37Rv]	Pos: 41/116	Gap: 25/116
oqTA0ELuFgtlYffrmwcX3jQsY4U	6435763 1QB2 6435762 1QB2	109	E: 2E-8	Ident: 39/109	Ident% 35	Q: 325-427 (451) S: 1-109 (109)	Chain B, Crystal Structure Of The Conserved Subdomain Of Human Protein Srp54m At 2.1a Resolution: Evidence For The Mechanism Of Signal Peptide Binding	Pos: 58/109	Gap: 6/109
x51cD0vSvOBMm0qWOpu4bMdLAls	12084139 1HQ1	105	E: 4E-10	Ident: 36/93	Ident% 38	Q: 326-418 (451) S: 2-94 (105)	Chain A, Structural And Energetic Analysis Of Rna Recognition By A Universally Conserved Protein From The Signal Recognition Particle	Pos: 55/93	Gap: -1/-1
yVI7rYMyOQqMpsibLvUoem3lDgk	14719791 1J8Y	297	E: 9E-63	Ident: 149/294	Ident% 50	Q: 4-293 (451) S: 2-293 (297)	Chain F, Signal Recognition Particle Conserved Gtpase Domain From A. Ambivalens T112a Mutant	Pos: 202/294	Gap: 6/294
A8TJ1hg6eRZGrfIl35wTsecdB+Y	14719790 1J8M	297	E: 2E-63	Ident: 150/294	Ident% 51	Q: 4-293 (451) S: 2-293 (297)	Chain F, Signal Recognition Particle Conserved Gtpase Domain From A. Ambivalens	Pos: 203/294	Gap: 6/294
HefF++6NQxlXerB660D0HmspgxA	5822474 2FFH 5822475 2FFH 5822476 2FFH	425	E: 2E-66	Ident: 168/433	Ident% 38	Q: 1-431 (451) S: 1-420 (425)	Chain A, The Signal Sequence Binding Protein Ffh From Thermus Aquaticus	Pos: 266/433	Gap: 15/433
ideeNON6D4q5fmHSRq7zy6Hgrv0	3212531 1FTS	295	E: 4E-79	Ident: 107/297	Ident% 36	Q: 7-293 (451) S: 1-292 (295)	Signal Recognition Particle Receptor From E. Coli	Pos: 160/297	Gap: 15/297
xsIiilj9u3g15WyfdHD8tPYIHCE	5822137 1NG1 5822519 3NG1 5822520 3NG1	294	E: 3E-88	Ident: 123/298	Ident% 41	Q: 1-296 (451) S: 1-294 (294)	N And Gtpase Domains Of The Signal Sequence Recognition Protein Ffh From Thermus Aquaticus	Pos: 189/298	Gap: 6/298
yLMpOVjZ8yJyfap6qopERT9MPUk	5822489 2NG1	293	E: 8E-88	Ident: 122/297	Ident% 41	Q: 2-296 (451) S: 1-293 (293)	N And Gtpase Domains Of The Signal Sequence Recognition Protein Ffh From Thermus Aquaticus	Pos: 188/297	Gap: 6/297
GHPCDNYeEtS63+H8ww8i8ImDW50	2780884 1FFH	294	E: 2E-88	Ident: 123/298	Ident% 41	Q: 2-297 (451) S: 1-294 (294)	N And Gtpase Domains Of The Signal Sequence Recognition Protein Ffh From Thermus Aquaticus	Pos: 189/298	Gap: 6/298
YPInVWlXLw6SotfD/oRqKNpKnPo	18655505 1JPJ 18655506 1JPN 18655507 1JPN	296	E: 1E-89	Ident: 125/300	Ident% 41	Q: 1-298 (451) S: 1-296 (296)	Chain A, Gmppnp Complex Of Srp Gtpase Ng Domain	Pos: 191/300	Gap: 6/300

q5aYP/AhPhtMcfZpBJxrnXFi2Lo
15668273
2495798
2129181
1590879

Phenylacrylic acid decarboxylase [Methanococcus jannaschii]

184

154

162

YH/P5zVPknqCX2V7hFjr4DMYaCQ	14278170 1G5Q 14278172 1G5Q 14278174 1G5Q 14278176 1G5Q	181	E: .021E0	Ident: 15/40	Ident% 37	Q: 80-119 (184) S: 78-114 (181)	Chain A, Epid H67n Complexed With Substrate Peptide Dsytc	Pos: 22/40	Gap: 3/40
85S00NXOSLUKkjlFDqIpmaF+RCI	14278129 1G63 14278130 1G63 14278131 1G63 14278132 1G63 14278133 1G63 14278134 1G63 14278135 1G63 14278136 1G63 14278137 1G63 14278138 1G63 14278139 1G63 14278140 1G63	181	E: .021E0	Ident: 15/40	Ident% 37	Q: 80-119 (184) S: 78-114 (181)	EPIDERMIN MODIFYING ENZYME EPID	Pos: 22/40	Gap: 3/40
s3NarHdsnpEBAD7F2NjcIIf4yYc	10835869 1E20	209	E: 2E-26	Ident: 32/153	Ident% 20	Q: 2-146 (184) S: 21-169 (209)	HAL3A protein [Arabidopsis thaliana]	Pos: 60/153	Gap: 12/153

*TARGET
BKMPCFy9DeeT7pY5/Y8LihRpfBU
15668274
2495799
2128126
1498868

conserved hypothetical protein [Methanococcus jannaschii]

433

148

794

1202

MEVA2M4avfU/lFzZiRPBgqp4to8
15668275
2498043
2129217
1590880

DNA-binding protein, probably DNA helicase [Methanococcus jannaschii]

663

275

1155

1431

8F6wQyvxO46gAOLmeQaqijmCKdc	15825804 1IN4	334	E: .082E0	Ident: 40/210	Ident% 19	Q: 155-357 (663) S: 12-213 (334)	Holliday junction DNA helicase [Thermotoga maritima]	Pos: 62/210	Gap: 15/210
cHD7ceBUq0NJx9gs5pUKnO1BbnE	7766820 1D9Z	657	E: .41E0	Ident: 21/79	Ident% 26	Q: 189-263 (663) S: 17-91 (657)	Chain A, Crystal Structure Of The Dna Repair Protein Uvrb In Complex With Atp	Pos: 28/79	Gap: 8/79
L6Zej5XIgGIyzODreof09Mwi8AU	7766819 1D9X	658	E: .4E0	Ident: 21/79	Ident% 26	Q: 189-263 (663) S: 17-91 (658)	Chain A, Crystal Structure Of The Dna Repair Protein Uvrb	Pos: 28/79	Gap: 8/79
ipw07lpZfhwgzuJP8x0KG5aq2DM	15825813 1J7K	334	E: .08E0	Ident: 40/210	Ident% 19	Q: 155-357 (663) S: 12-213 (334)	Chain A, Thermotoga Maritima Ruvb P216g Mutant	Pos: 62/210	Gap: 15/210
OywkgtnrKYZgrHDw0oK3/JjbTNc	5542368 1QHH	167	E: .12E0	Ident: 21/84	Ident% 25	Q: 175-255 (663) S: 2-82 (167)	Chain A, Structure Of Dna Helicase With Adpnp	Pos: 34/84	Gap: 6/84
vS7p6yY9Q2BLX2+ZRvf4PC3Y01Y	7546428 1D2M	665	E: .98E0	Ident: 15/63	Ident% 23	Q: 193-255 (663) S: 22-80 (665)	Excinuclease ABC subunit B	Pos: 24/63	Gap: 4/63
0MEvOkKr8OI2856yiCCRa6FaiGk	15825805 1IN5	334	E: .063E0	Ident: 40/210	Ident% 19	Q: 155-357 (663) S: 12-213 (334)	Chain A, Thermogota Maritima Ruvb A156s Mutant	Pos: 62/210	Gap: 15/210
RUQqaY/E17zzAKWGrj92sCRoIa0	15825806 1IN6	334	E: .59E0	Ident: 39/210	Ident% 18	Q: 155-357 (663) S: 12-213 (334)	Chain A, Thermotoga Maritima Ruvb K64r Mutant	Pos: 62/210	Gap: 15/210
dVuo353q2ifLcqdHLtkIJHYn0fU	3318689 1UAA 3318688 1UAA	673	E: .58E0	Ident: 19/68	Ident% 27	Q: 185-249 (663) S: 3-67 (673)	rep helicase, a single-stranded DNA dependent ATPase [Escherichia coli K12]	Pos: 32/68	Gap: 6/68
yLaGm9IiCwHDwP9FpN6bZ4qVoUA	15825808 1IN8	334	E: .094E0	Ident: 40/210	Ident% 19	Q: 155-357 (663) S: 12-213 (334)	Chain A, Thermotoga Maritima Ruvb T158v	Pos: 62/210	Gap: 15/210
y6DmWiIH9AALWyOIwRl3tNpm6BY	15825807 1IN7	334	E: .17E0	Ident: 39/210	Ident% 18	Q: 155-357 (663) S: 12-213 (334)	Chain A, Thermotoga Maritima Ruvb R170a	Pos: 61/210	Gap: 15/210
Tsr6FhcK7loOvr53qoIEKdJh6ew	5542369 1QHH	273	E: 8E-17	Ident: 44/268	Ident% 16	Q: 365-618 (663) S: 16-250 (273)	Chain B, Structure Of Dna Helicase With Adpnp	Pos: 85/268	Gap: 47/268
jrsWTJdvlm00IVv8Matr4c/09Z0	9257172 2PJR 9257173 2PJR	548	E: 7E-38	Ident: 72/459	Ident% 15	Q: 178-618 (663) S: 5-417 (548)	Chain A, Helicase Product Complex	Pos: 146/459	Gap: 64/459
nYqJS99/vmU+0u1oE0nOKascVJw	15988533 1QHG 4930230 3PJR 2781090 1PJR	724	E: 9E-40	Ident: 72/459	Ident% 15	Q: 178-618 (663) S: 5-417 (724)	ATP-dependent DNA helicase pcrA	Pos: 146/459	Gap: 64/459

EbLDXgXfUiezuOsq9vrHzCkUX5E
15668276
2495800
2128127
1590881

conserved hypothetical protein [Methanococcus jannaschii]

152

FVEjS2gOYT/5rlt8/G+NldMA+wI
15668277
2495801
2128128
1590883

conserved hypothetical protein [Methanococcus jannaschii]

238

6acDAHpvmqSzHBZtbPovJRmBGGg
15668278
2495802
2128129
1590884

dihydropteroate synthase [Methanococcus jannaschii]

525

282

296

ROrDd7vWz1TXFPUBLVjo/GqAo5M	10120607 1F6Y 10120608 1F6Y	262	E: 7E-8	Ident: 38/225	Ident% 16	Q: 160-366 (525) S: 1-222 (262)	5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase - Clostridium thermaceticum	Pos: 92/225	Gap: 21/225
A31B7k9s+lxL1ZlLpgIQhzC4jO0	11514674 1EYE	280	E: 6E-10	Ident: 37/210	Ident% 17	Q: 157-340 (525) S: 3-210 (280)	folP [Mycobacterium tuberculosis H37Rv]	Pos: 82/210	Gap: 28/210
yLi89rb9axVkEwq+uyO0OGozOWQ	3212431 1AJ0 3212432 1AJ2 3212443 1AJZ	282	E: 1E-14	Ident: 42/233	Ident% 18	Q: 173-376 (525) S: 36-260 (282)	DIHYDROPTEROATE SYNTHASE (DHPS) (DIHYDROPTEROATE PYROPHOSPHORYLASE)	Pos: 85/233	Gap: 37/233
GFj6Pl4dJD9XCf033nn5QHTBl3g	3212424 1AD1 3212425 1AD1 3212426 1AD4 3212427 1AD4	266	E: 5E-41	Ident: 45/244	Ident% 18	Q: 160-375 (525) S: 3-242 (266)	Chain A, Dihydropteroate Synthetase (Apo Form) From Staphylococcus Aureus	Pos: 82/244	Gap: 32/244

/RhqUtzvVa9mhBTGP4f5IRUPiAs
15668279
2497544
2129228
1590885

pyruvate kinase [Methanococcus jannaschii]

447

246

305

327

7ITnFiei3xs9Wcp3H3Na8wjH1Ls	10120730 1DXE 10120731 1DXE	256	E: .002E0	Ident: 20/78	Ident% 25	Q: 185-254 (447) S: 135-212 (256)	orf, hypothetical protein [Escherichia coli K12]	Pos: 35/78	Gap: 8/78
T9r1dRl2Iz1DGcElo8lo+/dDktE	10120732 1DXF 10120733 1DXF	256	E: .002E0	Ident: 20/78	Ident% 25	Q: 185-254 (447) S: 135-212 (256)	Chain A, 2-Dehydro-3-Deoxy-Galactarate Aldolase From Escherichia Coli In Complex With Pyruvate	Pos: 35/78	Gap: 8/78
k1lv/J9OT79kGMpKzvva8N0muqk	3212328 1A3W 3212329 1A3W 3212330 1A3X 3212331 1A3X	500	E: 1E-50	Ident: 162/487	Ident% 33	Q: 5-447 (447) S: 18-500 (500)	Required for START A in the cell cycle and sporulation; Cdc19p [Saccharomyces cerevisiae]	Pos: 245/487	Gap: 48/487
ObMfqlxHi4k1+ewZoaKKvNfGq7k	3660268 1PKL 3660264 1PKL 3660265 1PKL 3660263 1PKL 3660267 1PKL 3660261 1PKL 3660266 1PKL 3660262 1PKL	499	E: 1E-54	Ident: 140/430	Ident% 32	Q: 2-401 (447) S: 16-444 (499)	Chain G, The Structure Of Leishmania Pyruvate Kinase	Pos: 228/430	Gap: 31/430
uocQUIsRe0YAQxzX7rIza+qtK7M	9955371 1E0U 9955372 1E0U 9955373 1E0U 9955374 1E0U	470	E: 1E-56	Ident: 160/445	Ident% 35	Q: 5-417 (447) S: 1-437 (470)	Chain A, Structure R271l Mutant Of E. Coli Pyruvate Kinase	Pos: 245/445	Gap: 40/445
Zx2oGB39piV6uUXgql8LiG9Wup8	9955367 1E0T 9955368 1E0T 9955369 1E0T 9955370 1E0T	470	E: 5E-56	Ident: 159/445	Ident% 35	Q: 5-417 (447) S: 1-437 (470)	Chain A, R292d Mutant Of E. Coli Pyruvate Kinase	Pos: 244/445	Gap: 40/445
8kt+nJo9CAZHt2wFi1teUcyZwKs	1310978 1PKY 1310979 1PKY 1310981 1PKY 1310980 1PKY	470	E: 7E-57	Ident: 160/445	Ident% 35	Q: 5-417 (447) S: 1-437 (470)	Chain A, Pyruvate Kinase From E. Coli In The T-State	Pos: 245/445	Gap: 40/445
xyozgvL1onnI787K+p9jz8A34iI	999572 1PKN	530	E: 1E-167	Ident: 157/489	Ident% 32	Q: 6-447 (447) S: 42-529 (530)	Pyruvate Kinase (E.C.2.7.1.40) Complexed With Manganese, Potassium, And Pyruvate	Pos: 251/489	Gap: 48/489
ItUs6SAyasoNivNJZqVrZlFATTI	15987978 1F3X 15987979 1F3X 15987980 1F3X 15987981 1F3X 15987982 1F3X 15987983 1F3X 15987984 1F3X 15987985 1F3X	530	E: 1E-168	Ident: 159/488	Ident% 32	Q: 6-447 (447) S: 42-529 (530)	Chain A, S402p Mutant Of Rabbit Muscle Pyruvate Kinase	Pos: 251/488	Gap: 46/488
1xkBUWrgyceLEcvS5u7IXNPUKLE	1311281 1PKM	530	E: 1E-168	Ident: 158/488	Ident% 32	Q: 6-447 (447) S: 42-529 (530)	PYRUVATE KINASE, M1 ISOZYME (PYRUVATE KINASE MUSCLE ISOZYME)	Pos: 250/488	Gap: 46/488
S5b2p5SMZEHcb+8rpeRZ2FdHPkc	4929839 1A49 4929840 1A49 4929841 1A49 4929842 1A49 4929843 1A49 4929844 1A49 4929845 1A49 4929846 1A49 4557921 1A5U 4557922 1A5U 4557923 1A5U 4557924 1A5U 4557925 1A5U 4557926 1A5U 4557927 1A5U 4557928 1A5U 3659945 1AQF 3659946 1AQF 3659947 1AQF 3659948 1AQF 3659950 1AQF 3659951 1AQF 3659952 1AQF 3659949 1AQF	530	E: 1E-168	Ident: 157/489	Ident% 32	Q: 6-447 (447) S: 42-529 (530)	Chain A, Bis Mg-Atp-K-Oxalate Complex Of Pyruvate Kinase	Pos: 251/489	Gap: 48/489
JUwNRhkAKe6LrT870ks2QHc1MxI	15987970 1F3W 15987971 1F3W 15987972 1F3W 15987973 1F3W 15987974 1F3W 15987975 1F3W 15987976 1F3W 15987977 1F3W	530	E: 1E-168	Ident: 159/488	Ident% 32	Q: 6-447 (447) S: 42-529 (530)	Chain A, Recombinant Rabbit Muscle Pyruvate Kinase	Pos: 251/488	Gap: 46/488

2xrhRG14Mn0F4uZOluKI+DcylVg
15668280
2497355
2128130
11513829
11513830
13787079
13787080
13787081
13787082
1498875

extragenic suppressor (suhB) [Methanococcus jannaschii]

252

436

636

616

ZBF94QJ3EzWaQ+Gfgwy7vnJRUhQ	1942590 1RDZ 1942591 1RDZ 1942588 1RDY 1942589 1RDY 1942586 1RDX 1942587 1RDX 1942590 1RDZ 1942591 1RDZ 1942588 1RDY 1942589 1RDY 1942586 1RDX 1942587 1RDX	337	E: .71E0	Ident: 22/78	Ident% 28	Q: 36-106 (252) S: 66-142 (337)	Chain A, T-State Structure Of The Arg 243 To Ala Mutant Of Pig Kidney Fructose 1,6-Bisphosphatase Expressed In E. Coli	Pos: 40/78	Gap: 8/78
4X8UtYorUcUT/8Ip2FtySKz7tSw	231009 4FBP 231010 4FBP 231011 4FBP 231012 4FBP 442899 1FBH 999828 1FPD 999829 1FPD 999834 1FPF 999835 1FPF 999832 1FPE 999833 1FPE 1633399 1FPJ 1633400 1FPJ 1633401 1FPI 1633402 1FPI 1633395 1FPL 1633396 1FPL 999838 1FPG 999839 1FPG 229903 1FBP 229904 1FBP 442898 1FBH 230506 2FBP 230507 2FBP 230854 3FBP 230855 3FBP 231139 5FBP 442889 1FBC 442895 1FBF 442891 1FBD 442893 1FBE 442897 1FBG 442912 1FPB 231138 5FBP 442911 1FPB 442888 1FBC 442894 1FBF 442890 1FBD 442892 1FBE 442896 1FBG 1633397 1FPK 1633398 1FPK 231009 4FBP 231010 4FBP 231011 4FBP 231012 4FBP 442899 1FBH 999828 1FPD 999829 1FPD 999834 1FPF 999835 1FPF 999832 1FPE 999833 1FPE 1633399 1FPJ 1633400 1FPJ 1633401 1FPI 1633402 1FPI 1633395 1FPL 1633396 1FPL 999838 1FPG 999839 1FPG 229903 1FBP 229904 1FBP 442898 1FBH 230506 2FBP 230507 2FBP 230854 3FBP 230855 3FBP 231139 5FBP 442889 1FBC 442895 1FBF 442891 1FBD 442893 1FBE 442897 1FBG 442912 1FPB 231138 5FBP 442911 1FPB 442888 1FBC 442894 1FBF 442890 1FBD 442892 1FBE 442896 1FBG 1633397 1FPK 1633398 1FPK	335	E: .69E0	Ident: 22/78	Ident% 28	Q: 36-106 (252) S: 66-142 (335)	Chain A, Fructose-1,6-Bisphosphatase (Fru-1,6-Pase) (D-Fructose-1,6-Bisphosphate 1-Phosphohydrolase) (E.C.3.1.3.11) Complex With AMP	Pos: 40/78	Gap: 8/78
sqWSVPAo6/n/gkKoDoUzHdooaCM	10121019 1EYI 10121020 1EYJ 10121021 1EYJ 10121022 1EYK 10121023 1EYK 5107572 1CNQ 10121019 1EYI 10121020 1EYJ 10121021 1EYJ 10121022 1EYK 10121023 1EYK 5107572 1CNQ	337	E: .44E0	Ident: 23/78	Ident% 29	Q: 36-106 (252) S: 66-142 (337)	fructose-bisphosphatase (EC 3.1.3.11) - pig	Pos: 40/78	Gap: 8/78
jHhpGfXKtAdW9YhEYoYySCt4wCo	1311146 1FTA 1311149 1FTA 1311147 1FTA 1311148 1FTA 1311146 1FTA 1311149 1FTA 1311147 1FTA 1311148 1FTA	337	E: 1.1E0	Ident: 22/78	Ident% 28	Q: 36-106 (252) S: 66-142 (337)	Chain A, Fructose-1,6-Bisphosphatase(D-Fructose-1,6-Bisphosphate, 1-Phosphohydrolase) (E.C.3.1.3.11) Complexed With The Allosteric Inhibitor Amp	Pos: 39/78	Gap: 8/78
NCh2hZCuzIPvyAjIXVKj+bKz+wY	11514531 1FJ6 11514533 1FJ9 11514534 1FJ9 11514531 1FJ6 11514533 1FJ9 11514534 1FJ9	337	E: .45E0	Ident: 23/78	Ident% 29	Q: 36-106 (252) S: 66-142 (337)	Chain A, Fructose-1,6-Bisphosphatase (Mutant Y57w) ProductZN Complex (R-State)	Pos: 40/78	Gap: 8/78
lBJbkWKoLhEb99Vq7ZeIebYsyxY	809401 1FRP 809402 1FRP 809401 1FRP 809402 1FRP	335	E: .71E0	Ident: 22/78	Ident% 28	Q: 36-106 (252) S: 66-142 (335)	Chain A, Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1-Phosphohydrolase) (E.C.3.1.3.11) Complexed With Fructose-2,6-Bisphosphate, Adenosine Monophosphate (Amp), And Zinc	Pos: 40/78	Gap: 8/78
C3Tcaj+r49rke11LLDsMRdkv1kE	6729708 1BK4 6729708 1BK4	337	E: 2.3E0	Ident: 22/78	Ident% 28	Q: 36-106 (252) S: 66-142 (337)	FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) (FBPASE)	Pos: 39/78	Gap: 8/78
pJTgyjeKPcaK2WT2DguS7p9I/X4	2554912 1FSA 2554913 1FSA 2554912 1FSA 2554913 1FSA	337	E: .4E0	Ident: 25/104	Ident% 24	Q: 10-106 (252) S: 47-142 (337)	Chain A, The T-State Structure Of Lys 42 To Ala Mutant Of The Pig Kidney Fructose 1,6-Bisphosphatase Expressed In E. Coli	Pos: 47/104	Gap: 15/104
q2nBtwlh+LSM5Hv6fLTmGHEhWOM	999485 1INP 999485 1INP	400	E: 5E-4	Ident: 27/184	Ident% 14	Q: 80-219 (252) S: 152-335 (400)	Inositol polyphosphate 1-phosphatase (IPPase) (IPP)	Pos: 49/184	Gap: 44/184
sPZ48//mYjbMRguaY4cpSf4RrMs	16974874 1K9Y 16974875 1K9Z 16974876 1KA0 16974877 1KA1 7245969 1QGX 16974874 1K9Y 16974875 1K9Z 16974876 1KA0 16974877 1KA1 7245969 1QGX	357	E: 4E-19	Ident: 43/217	Ident% 19	Q: 71-251 (252) S: 132-347 (357)	Putative phosphatase gene involved in salt tolerance and methionine biogenesis; halotolerance; Met22p [Saccharomyces cerevisiae]	Pos: 76/217	Gap: 37/217
yzdnxQLKWU1Kw9YLknD7XAfcCIM	15825834 1JP4 15825834 1JP4	308	E: 1E-33	Ident: 43/273	Ident% 15	Q: 10-239 (252) S: 18-287 (308)	Chain A, Crystal Structure Of An Enzyme Displaying Both Inositol- Polyphosphate 1-Phosphatase And 3'-Phosphoadenosine-5'- Phosphate Phosphatase Activities	Pos: 89/273	Gap: 46/273
o/z0MDOegfuflkvtDPoF12LHR/s	996148 1IMB 996149 1IMB 996172 1IME 996173 1IME 996146 1IMA 996147 1IMA 996155 1IMC 996165 1IMD 996154 1IMC 996164 1IMD 996175 1IMF 996148 1IMB 996149 1IMB 996172 1IME 996173 1IME 996146 1IMA 996147 1IMA 996155 1IMC 996165 1IMD 996154 1IMC 996164 1IMD 996175 1IMF	277	E: 2E-54	Ident: 69/263	Ident% 26	Q: 5-249 (252) S: 10-263 (277)	inositol(myo)-1(or 4)-monophosphatase 1 [Homo sapiens]	Pos: 119/263	Gap: 27/263
m11DJoh1krBnlIO0lklYAco5pEk	443382 2HHM 443383 2HHM 2914660 1AWB 2914661 1AWB 443382 2HHM 443383 2HHM 2914660 1AWB 2914661 1AWB	276	E: 1E-58	Ident: 62/267	Ident% 23	Q: 2-250 (252) S: 6-263 (276)	Chain A, Human Inositol Monophosphatase (E.C.3.1.3.25) Dimer Complex With Gadolinium And Sulfate	Pos: 111/267	Gap: 27/267
2xrhRG14Mn0F4uZOluKI+DcylVg	11513829 1DK4 11513830 1DK4 13787079 1G0H 13787080 1G0H 13787081 1G0I 13787082 1G0I 11513829 1DK4 11513830 1DK4 13787079 1G0H 13787080 1G0H 13787081 1G0I 13787082 1G0I	252	E: 1E-135	Ident: 252/252	Ident% 100	Q: 1-252 (252) S: 1-252 (252)	extragenic suppressor (suhB) [Methanococcus jannaschii]	Pos: 252/252	Gap: -1/-1

QhqM2xcO/YmTXFfo2TN6pDRHVKA
15668281
2495803
2128131
1590886

M. jannaschii predicted coding region MJ0110 [Methanococcus jannaschii]

3
6-28,38-60,63-84

*TARGET
4/yaD/z1LdEKM364C7Dt1a9cGwo
15668282
2495804
2129225
1590887

protein translocase, subunit SECD (secD) [Methanococcus jannaschii]

396

5
12-34,239-260,267-289,333-355,360-382

168

582

903

eS82qyUoyIbjbvx67HigBB0Fx5Y
15668283
2144392
1590888

acetyl-CoA decarbonylase/synthase, subunit gamma (cdhE) [Methanococcus jannaschii]

488

120

yLi89rb9axVkEwq+uyO0OGozOWQ

3212431 1AJ0
3212432 1AJ2
3212443 1AJZ

282

E: .74E0

Ident: 27/145

Ident% 18

Q: 152-276 (488) S: 81-217 (282)

DIHYDROPTEROATE SYNTHASE (DHPS) (DIHYDROPTEROATE PYROPHOSPHORYLASE)

Pos: 52/145

Gap: 28/145

hUBGHNTMmdOcmc1QoiQCMpOkz1Y
15668284
2144393
1590889

acetyl-CoA decarbonylase/synthase, subunit delta (cdhD) [Methanococcus jannaschii]

405

yLi89rb9axVkEwq+uyO0OGozOWQ	3212431 1AJ0 3212432 1AJ2 3212443 1AJZ	282	E: 1.9E0	Ident: 30/160	Ident% 18	Q: 165-306 (405) S: 51-204 (282)	DIHYDROPTEROATE SYNTHASE (DHPS) (DIHYDROPTEROATE PYROPHOSPHORYLASE)	Pos: 62/160	Gap: 24/160
ROrDd7vWz1TXFPUBLVjo/GqAo5M	10120607 1F6Y 10120608 1F6Y	262	E: 2.5E0	Ident: 28/149	Ident% 18	Q: 155-291 (405) S: 29-165 (262)	5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase - Clostridium thermaceticum	Pos: 62/149	Gap: 24/149

HEpdIP+h6CfuWo2hvPCMtargAl4
15668285
2495805
2128132
1592262

M. jannaschii predicted coding region MJ0114 [Methanococcus jannaschii]

303

qE9VsASU60nSnLlowqvJV4BuLmk
15668286
2495806
2128133
1498882

conserved hypothetical protein [Methanococcus jannaschii]

155

PF9sWFsQ7QHFTlxQUoskWwNcIWY
15668287
2495807
2128134
1498883

conserved hypothetical protein [Methanococcus jannaschii]

225

M76KckTzNUez3wDx6DvgNH9pPfY

8569297 1QHT

775

E: .12E0

Ident: 27/137

Ident% 19

Q: 109-223 (225) S: 517-646 (775)

Chain A, Dna Polymerase From Thermococcus Sp. 9on-7 Archaeon

Pos: 50/137

Gap: 29/137

ZsbX1SrWkh01X3Gofxxq4KqYBDQ
15668288
3219871
2826246

conserved hypothetical protein [Methanococcus jannaschii]

Oa7Lkv/pQEbIC//s26EUtomrTZk
15668289
2494298
2129323
1592263

translation initiation factor aIF-2, subunit alpha (aif2A) [Methanococcus jannaschii]

266

412

789

853

Mcf1hBjIhKFXMmRNezSZWygaACA	17943304 1GO3 17943306 1GO3	187	E: 3E-4	Ident: 25/112	Ident% 22	Q: 9-96 (266) S: 79-187 (187)	DNA-directed RNA polymerase, subunit E' (rpoE1) [Methanococcus jannaschii]	Pos: 53/112	Gap: 27/112
rtMUPuklsb0slwepoWuy4obNnto	2098462 1SRO	76	E: 4E-5	Ident: 31/74	Ident% 41	Q: 10-83 (266) S: 4-74 (76)	S1 Rna Binding Domain, Nmr, 20 Structures	Pos: 47/74	Gap: 3/74
WiSJOAMMs+NFsrGSfyCDhIl64Kg	11514054 1E3P	757	E: 2E-15	Ident: 34/103	Ident% 33	Q: 3-101 (266) S: 659-756 (757)	Chain A, Tungstate Derivative Of Streptomyces Antibioticus Pnpase Gpsi Enzyme	Pos: 56/103	Gap: 9/103
F/scBK4xHcrObPUhz+nLxau+v8I	11514023 1E3H	757	E: 7E-15	Ident: 34/103	Ident% 33	Q: 3-101 (266) S: 659-756 (757)	Chain A, Semet Derivative Of Streptomyces Antibioticus PnpaseGPSI Enzyme	Pos: 56/103	Gap: 9/103

IEv3nJG3f2I9/ila5ICrXqr6Ck0
15668290
2497839
2129110
1498885

methyl coenzyme M reductase II, operon protein D (mtrD) [Methanococcus jannaschii]

167

6Et7hKdMWC02N62tZRPhyh5oPYg
15668291
2495808
2128135
1498886

carbon monoxide dehydrogenase gamma subunit (cdhE) isolog [Methanococcus jannaschii]

224

FmfXcqym1YwF3pAwPpGxKP3gxXI
15668292
2495809
2128136
1498887

urease accessory protein (ureG) [Methanococcus jannaschii]

233

124

990

1239

YPInVWlXLw6SotfD/oRqKNpKnPo	18655505 1JPJ 18655506 1JPN 18655507 1JPN	296	E: .075E0	Ident: 22/92	Ident% 23	Q: 6-93 (233) S: 103-190 (296)	Chain A, Gmppnp Complex Of Srp Gtpase Ng Domain	Pos: 41/92	Gap: 8/92
HefF++6NQxlXerB660D0HmspgxA	5822474 2FFH 5822475 2FFH 5822476 2FFH	425	E: .057E0	Ident: 22/92	Ident% 23	Q: 6-93 (233) S: 103-190 (425)	Chain A, The Signal Sequence Binding Protein Ffh From Thermus Aquaticus	Pos: 41/92	Gap: 8/92
aEgMwDXBlqcYefrwMoQ7oNDi/ik	515076 1AGP	166	E: .056E0	Ident: 24/184	Ident% 13	Q: 4-183 (233) S: 6-166 (166)	C-H-Ras P21 Protein Mutant With Gly 12 Replaced By Asp (G12d) Complexed With Guanosine-5'-[b,G-Imido] Triphosphate	Pos: 56/184	Gap: 27/184
1hdI1kVU8qaU1oUBGnJTETFFSkw	443432 2REB 443229 1REA	352	E: .051E0	Ident: 15/104	Ident% 14	Q: 2-104 (233) S: 60-158 (352)	The Structure Of The E. Coli Reca Protein Monomer And Polymer	Pos: 35/104	Gap: 6/104
02ez5lI7ve1LX+gMNwKpyOAch+E	4139776 1B23 1942754 1TTT 1942755 1TTT 1942756 1TTT 2392582 1TUI 2392583 1TUI 2392584 1TUI	405	E: .019E0	Ident: 26/226	Ident% 11	Q: 4-202 (233) S: 14-214 (405)	Chain P, E. Coli Cysteinyl-Trna And T. Aquaticus Elongation Factor Ef-Tu:gtp Ternary Complex	Pos: 56/226	Gap: 52/226
gxSU6b8wf9bjSBQdGn8DikMHGI0	2098390 2REC 2098391 2REC 2098392 2REC 2098393 2REC 2098394 2REC 2098395 2REC	353	E: .051E0	Ident: 15/104	Ident% 14	Q: 2-104 (233) S: 61-159 (353)	RecA protein [Escherichia coli O157:H7]	Pos: 35/104	Gap: 6/104
xsIiilj9u3g15WyfdHD8tPYIHCE	5822137 1NG1 5822519 3NG1 5822520 3NG1	294	E: .073E0	Ident: 22/92	Ident% 23	Q: 6-93 (233) S: 103-190 (294)	N And Gtpase Domains Of The Signal Sequence Recognition Protein Ffh From Thermus Aquaticus	Pos: 41/92	Gap: 8/92
aINNm1qx4WRZBeQP1HU0qUbYCBw	2624675 1AIP 2624671 1AIP 2624672 1AIP 2624676 1AIP	405	E: .23E0	Ident: 26/226	Ident% 11	Q: 4-202 (233) S: 14-214 (405)	Chain E, Ef-Tu Ef-Ts Complex From Thermus Thermophilus	Pos: 56/226	Gap: 52/226
ideeNON6D4q5fmHSRq7zy6Hgrv0	3212531 1FTS	295	E: 7.6E0	Ident: 21/111	Ident% 18	Q: 3-109 (233) S: 95-201 (295)	Signal Recognition Particle Receptor From E. Coli	Pos: 39/111	Gap: 8/111
yLMpOVjZ8yJyfap6qopERT9MPUk	5822489 2NG1	293	E: .073E0	Ident: 22/92	Ident% 23	Q: 6-93 (233) S: 102-189 (293)	N And Gtpase Domains Of The Signal Sequence Recognition Protein Ffh From Thermus Aquaticus	Pos: 41/92	Gap: 8/92
GHPCDNYeEtS63+H8ww8i8ImDW50	2780884 1FFH	294	E: .073E0	Ident: 22/92	Ident% 23	Q: 6-93 (233) S: 102-189 (294)	N And Gtpase Domains Of The Signal Sequence Recognition Protein Ffh From Thermus Aquaticus	Pos: 41/92	Gap: 8/92
2rECtURbut1MQ96XkZ034sun7O8	494936 821P 2392390 1JAI 5107569 1CLU 576244 1PLL 576242 1PLJ	166	E: .48E0	Ident: 29/182	Ident% 15	Q: 4-175 (233) S: 6-154 (166)	C-H-Ras P21 Protein (Residues 1 - 166) Mutant With Gly 12 Replaced By Pro (G12p) Complex With Guanosine-5'-[b,G-Imido] Triphosphate	Pos: 52/182	Gap: 43/182
9Bdj0c9d2ccLnG+rusFqZAbf42k	494886 421P	166	E: .049E0	Ident: 24/184	Ident% 13	Q: 4-183 (233) S: 6-166 (166)	H-Ras P21 Protein Mutant With Gly 12 Replaced By Arg (G12r) Complex With Guanosine-5'-[b,G-Imido] Triphosphate	Pos: 56/184	Gap: 27/184
xdb9mOHWZQGv9S4NgQp+dwK4jA0	2392389 1JAH 576243 1PLK	166	E: .005E0	Ident: 25/184	Ident% 13	Q: 4-183 (233) S: 6-166 (166)	H-Ras P21 Protein Mutant G12p, Complexed With Guanosine-5'-[beta,Gamma-Methylene] Triphosphate And Magnesium	Pos: 56/184	Gap: 27/184
yVI7rYMyOQqMpsibLvUoem3lDgk	14719791 1J8Y	297	E: 1E-9	Ident: 30/151	Ident% 19	Q: 3-139 (233) S: 100-250 (297)	Chain F, Signal Recognition Particle Conserved Gtpase Domain From A. Ambivalens T112a Mutant	Pos: 56/151	Gap: 14/151
A8TJ1hg6eRZGrfIl35wTsecdB+Y	14719790 1J8M	297	E: 1E-10	Ident: 31/151	Ident% 20	Q: 3-139 (233) S: 100-250 (297)	Chain F, Signal Recognition Particle Conserved Gtpase Domain From A. Ambivalens	Pos: 57/151	Gap: 14/151

F93AldKUPWEl1++Thrm8PVmfwMA
15668293
2492575
2129284
1590892

SN-glycerol-3-phosphate transport ATP-binding protein (ugpC) [Methanococcus jannaschii]

261

1241

1325

1373

q9VJg++DTI4s/+pcNr24LsU/ZBE	6573453 1B0U	262	E: 2E-42	Ident: 52/262	Ident% 19	Q: 5-244 (261) S: 6-260 (262)	Chain A, Atp-Binding Subunit Of The Histidine Permease From Salmonella Typhimurium	Pos: 120/262	Gap: 29/262
bHzMC4Gxg64/bRB+N8ytSV+FEa0	15826057 1F3O	235	E: 2E-47	Ident: 54/229	Ident% 23	Q: 1-215 (261) S: 2-225 (235)	Chain A, Crystal Structure Of Mj0796 Atp-Binding Cassette	Pos: 101/229	Gap: 19/229
ImYhpWAkHn8eI11by5jCV4ScHuA	12084694 1G29 12084695 1G29	372	E: 3E-73	Ident: 61/261	Ident% 23	Q: 6-254 (261) S: 4-256 (372)	Chain 1, Malk	Pos: 108/261	Gap: 20/261

Sj1jgKaILGBuzqchwT503xgh6GI
15668294
2494314
2129320
1590893

translation initiation factor aIF-2B, subunit delta, putative [Methanococcus jannaschii]

308

112

132

142

jzU54bGlz1iFvwRWFrcOVqWFUVY
15668295
2495810
2128137
1498890

M. jannaschii predicted coding region MJ0123 [Methanococcus jannaschii]

110

100

iX/PzCqxrREcoCSBxnOZU+aGTP0
3915925
2826244

type I restriction-modification enzyme 2, R subunit [Methanococcus jannaschii]

1075

1
349-367

140

228

361

U1Sr7u8KEdUrROTswxXLwha9phw	9955068 1C4O	664	E: 7.5E0	Ident: 26/207	Ident% 12	Q: 575-774 (1075) S: 433-618 (664)	Chain A, Crystal Structure Of The Dna Nucleotide Excision Repair Enzyme Uvrb From Thermus Thermophilus	Pos: 62/207	Gap: 28/207
cHD7ceBUq0NJx9gs5pUKnO1BbnE	7766820 1D9Z	657	E: 7.1E0	Ident: 32/239	Ident% 13	Q: 584-814 (1075) S: 429-655 (657)	Chain A, Crystal Structure Of The Dna Repair Protein Uvrb In Complex With Atp	Pos: 82/239	Gap: 20/239
L6Zej5XIgGIyzODreof09Mwi8AU	7766819 1D9X	658	E: 6.7E0	Ident: 32/239	Ident% 13	Q: 584-814 (1075) S: 430-656 (658)	Chain A, Crystal Structure Of The Dna Repair Protein Uvrb	Pos: 82/239	Gap: 20/239
vS7p6yY9Q2BLX2+ZRvf4PC3Y01Y	7546428 1D2M	665	E: 7.4E0	Ident: 26/207	Ident% 12	Q: 575-774 (1075) S: 434-619 (665)	Excinuclease ABC subunit B	Pos: 62/207	Gap: 28/207

T5GMuGx/d9f+eBJGhxLrZeIpQ9k
15668296
2495812
2128138
1498892

conserved hypothetical protein [Methanococcus jannaschii]

116

KWzGKig7iqB/SfpcUiD4pX8K+ro
15668297
3915926
2826245

conserved hypothetical protein [Methanococcus jannaschii]

222

255

7zBkXXQKg83FwPakUkjBvhTEPgs	1827771 1KNY 1827772 1KNY	253	E: .002E0	Ident: 18/78	Ident% 23	Q: 3-70 (98) S: 8-85 (253)	Chain A, Kanamycin Nucleotidyltransferase	Pos: 38/78	Gap: 10/78
w45q01fCElMhy7eBkdaNzrDEKPY	640136 1KAN 640137 1KAN	253	E: .002E0	Ident: 18/78	Ident% 23	Q: 3-70 (98) S: 8-85 (253)	Chain A, Kanamycin Nucleotidyltransferase (E.C.2.7.7.-) Mutant With Asp 80 Replaced By Tyr And Thr 130 Replaced By Lys (D80y,T130k)	Pos: 38/78	Gap: 10/78
eSecGa9mEH4XUdGi/UEgJ91dexg	10120664 1FA0 10120665 1FA0	537	E: .59E0	Ident: 13/91	Ident% 14	Q: 3-73 (98) S: 47-137 (537)	Chain A, Structure Of Yeast Poly(A) Polymerase Bound To Manganate And 3'-Datp	Pos: 30/91	Gap: 20/91

urf+7qN/jb1CWswoJpMgVm9b6Pc
15668298
2495814
2128140
1498894

conserved hypothetical protein [Methanococcus jannaschii]

121

whvBf+Uxjbfgryp7n0e/6pzYLIE
15668299
2495815
2128141
1498895

conserved hypothetical protein [Methanococcus jannaschii]

181

239

7zBkXXQKg83FwPakUkjBvhTEPgs	1827771 1KNY 1827772 1KNY	253	E: .31E0	Ident: 15/49	Ident% 30	Q: 1-47 (98) S: 6-54 (253)	Chain A, Kanamycin Nucleotidyltransferase	Pos: 27/49	Gap: 2/49
w45q01fCElMhy7eBkdaNzrDEKPY	640136 1KAN 640137 1KAN	253	E: .32E0	Ident: 15/49	Ident% 30	Q: 1-47 (98) S: 6-54 (253)	Chain A, Kanamycin Nucleotidyltransferase (E.C.2.7.7.-) Mutant With Asp 80 Replaced By Tyr And Thr 130 Replaced By Lys (D80y,T130k)	Pos: 27/49	Gap: 2/49

HZtFtPfdzpA8pKgqgKAySnzsLis
15668300
2495816
2128142
1498897

M. jannaschii predicted coding region MJ0129 [Methanococcus jannaschii]

170

4
1-18,27-49,59-81,133-155

*TARGET
MdqezkVuAjH3t1JTVxng4N0xQ9E
3915927
2826248

type I restriction-modification enzyme 2, S subunit [Methanococcus jannaschii]

343

210

339

351

9Wb8M61+YIGFm7v6mpVgMgTbr+k
15668301
2495818
2128143
1498899

M. jannaschii predicted coding region MJ0131 [Methanococcus jannaschii]

103

3
1-23,26-48,65-87

5jwzvrb0Mh56wATt//XyG0UmK/M
15668302
2495819
2129237
1592267

type I restriction-modification enzyme 2, M subunit [Methanococcus jannaschii]

220

119

135

ZMuMgSwQ7cg0k2V2f0nWlZGNDEM
15668303
2495820
2128144
1498901

conserved hypothetical protein [Methanococcus jannaschii]

273

114

242

8glEnVm47xyTKNr6em7Lto8NfRs	349936 2XIM 349937 2XIM 349938 2XIM 349939 2XIM	393	E: 8.1E0	Ident: 23/160	Ident% 14	Q: 9-145 (273) S: 25-181 (393)	Chain A, D-Xylose Isomerase (E.C.5.3.1.5) Mutant With Lys 253 Replaced By Arg (K253R) Complex With Xylitol-Mg	Pos: 48/160	Gap: 26/160
Q5mr3Oigxl2Jd9lN5gePTzfXiUs	3891531 1BHW 3891532 1BHW 3891533 1BHW 3891534 1BHW 443303 1XIN 443304 1XIN 443305 1XIN 443306 1XIN	393	E: 8.1E0	Ident: 23/160	Ident% 14	Q: 9-145 (273) S: 25-181 (393)	Chain A, Low Temperature Middle Resolution Structure Of Xylose Isomerase From Masc Data	Pos: 48/160	Gap: 26/160
mUgkT1cvLLv0zNmbT24U3OZmJ9M	4930281 1BXB 4930282 1BXB 4930283 1BXB 4930284 1BXB	387	E: .094E0	Ident: 29/273	Ident% 10	Q: 22-251 (273) S: 36-282 (387)	Xylose isomerase	Pos: 65/273	Gap: 69/273
rGf1wG6qHQDHoJVJUgWzWLceV1I	349918 1XIM 349919 1XIM 349920 1XIM 349921 1XIM 443538 6XIM 443539 6XIM 443540 6XIM 443541 6XIM 443522 5XIM 443523 5XIM 443524 5XIM 443525 5XIM 443552 7XIM 443553 7XIM 443554 7XIM 443555 7XIM 443510 4XIM 443511 4XIM 443513 4XIM 443512 4XIM	393	E: 8.5E0	Ident: 23/160	Ident% 14	Q: 9-145 (273) S: 25-181 (393)	Chain A, D-Xylose Isomerase (E.C.5.3.1.5) Complex With Xylitol-Co	Pos: 48/160	Gap: 26/160
SvfV34UzS0wd1qaUFb3VBtJxNeA	443580 9XIM 443581 9XIM 443568 8XIM 443569 8XIM 443582 9XIM 443570 8XIM 443583 9XIM 443571 8XIM	393	E: 6.3E0	Ident: 23/164	Ident% 14	Q: 9-149 (273) S: 25-185 (393)	Chain A, D-Xylose Isomerase (E.C.5.3.1.5) Mutant With Glu 186 Replaced By Gln (E186Q) Complex With Xylose And Mn	Pos: 48/164	Gap: 26/164
Z5+di8bDDG4bjKSGV3Dl1N1J/4U	349950 3XIM 349948 3XIM 349949 3XIM 349947 3XIM	393	E: 7.3E0	Ident: 23/160	Ident% 14	Q: 9-145 (273) S: 25-181 (393)	Chain D, D-Xylose Isomerase (E.C.5.3.1.5) Mutant With Lys 309 Replaced By Arg, Lys 319 Replaced By Arg, Lys 323 Replaced By Arg ((K309r, K319r, K323r) Complex With Sorbitol-Co	Pos: 48/160	Gap: 26/160
+L3WO+PUKTuUSAwUUXM16MthcPg	443526 5XIN 443527 5XIN 443528 5XIN 443529 5XIN	393	E: 8.3E0	Ident: 23/160	Ident% 14	Q: 9-145 (273) S: 25-181 (393)	Chain A, D-Xylose Isomerase (E.C.5.3.1.5) Mutant With Asp 255 Replaced By Ala (D255A) Complex With Xylose And Mg	Pos: 48/160	Gap: 26/160
NEXU2yAxBEB5hq3+typQHW3F96E	443442 2XIN 443443 2XIN 443444 2XIN 443445 2XIN	393	E: 8.1E0	Ident: 23/160	Ident% 14	Q: 9-145 (273) S: 25-181 (393)	Chain A, D-Xylose Isomerase (E.C.5.3.1.5) Mutant With His 290 Replaced By Asn (H290N) Complex With Sorbitol And Co	Pos: 48/160	Gap: 26/160
NPhvWRGCVvv94D97ID+eYiq1400	6137712 1QUM	285	E: 7E-53	Ident: 50/235	Ident% 21	Q: 47-267 (273) S: 49-278 (285)	endonuclease IV [Escherichia coli O157:H7]	Pos: 88/235	Gap: 19/235
X1ooR7s3ctapA8iLG8qCJ2LwkKM	6573704 1QTW	285	E: 8E-53	Ident: 50/235	Ident% 21	Q: 47-267 (273) S: 49-278 (285)	Chain A, High-Resolution Crystal Structure Of The Escherichia Coli Dna Repair Enzyme Endonuclease Iv	Pos: 88/235	Gap: 19/235

kSv81NcSUbv3G7oHljnUTv5zIBU
15668304
2495821
2127995
1590899

L-isoaspartyl protein carboxyl methyltransferase isolog (pimT) [Methanococcus jannaschii]

282

180

1205

1213

sdLvp9C2Zy6Jo9DOLsgrTNL4ftA	1942357 1AQJ 1942356 1AQJ	421	E: .54E0	Ident: 26/171	Ident% 15	Q: 53-215 (282) S: 3-165 (421)	MODIFICATION METHYLASE TAQI (ADENINE-SPECIFIC METHYLTRANSFERASE TAQI) (M.TAQI)	Pos: 53/171	Gap: 16/171
hi8Q6/nV02EB1TFFVLhaW6G9Jqc	1942410 2ADM 1942411 2ADM 1942354 1AQI 1942355 1AQI	421	E: .56E0	Ident: 26/171	Ident% 15	Q: 53-215 (282) S: 3-165 (421)	Chain A, Adenine-N6-Dna-Methyltransferase Taqi	Pos: 53/171	Gap: 16/171
hpZBO1gnbkAUILK+QLhlddzJ/ow	1633081 1VID	221	E: 3E-4	Ident: 11/57	Ident% 19	Q: 91-147 (282) S: 62-118 (221)	Catechol O-Methyltransferase	Pos: 27/57	Gap