SitesBLAST
Comparing WP_011383893.1 NCBI__GCF_000009985.1:WP_011383893.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1dgjA Crystal structure of the aldehyde oxidoreductase from desulfovibrio desulfuricans atcc 27774 (see paper)
31% identity, 99% coverage: 1:905/913 of query aligns to 1:905/906 of 1dgjA
- active site: V391 (≠ Q369), F427 (≠ L404), R503 (= R480), Y507 (≠ H484), R535 (= R512), E869 (= E869), M870 (≠ Q870)
- binding molybdenum (iv)oxide: G424 (= G401), R535 (= R512), G698 (≠ S676), E869 (= E869)
- binding fe2/s2 (inorganic) cluster: V38 (= V38), G39 (= G39), C40 (= C40), G41 (≠ D41), G43 (= G43), Q44 (≠ D44), C45 (= C45), G46 (= G46), C48 (= C48), R58 (≠ C58), C60 (= C60), C100 (= C99), G101 (= G100), C103 (= C102), C137 (= C134), C139 (= C136)
- binding pterin cytosine dinucleotide: Q99 (= Q98), C139 (= C136), F423 (= F400), G424 (= G401), R535 (= R512), W652 (≠ A633), H655 (≠ I636), G656 (= G637), Q657 (= Q638), G658 (= G639), A697 (≠ T675), G698 (≠ S676), S700 (= S678), S702 (≠ Q680), Q703 (≠ T681), C799 (≠ I801), N800 (= N802), V803 (≠ L805), V804 (≠ L806), Q807 (= Q809), S865 (≠ K865), G866 (= G866), V867 (≠ I867), G868 (= G868), E869 (= E869)
4usaA Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with trans-cinnamaldehyde (see paper)
31% identity, 99% coverage: 1:907/913 of query aligns to 1:907/907 of 4usaA
- active site: I390 (vs. gap), F425 (≠ L404), R501 (= R480), F505 (≠ H484), R533 (= R512), E869 (= E869), L870 (≠ Q870)
- binding bicarbonate ion: R460 (= R439), A531 (= A510), F532 (= F511), Y535 (≠ F514), Q539 (= Q518)
- binding fe2/s2 (inorganic) cluster: V38 (= V38), C40 (= C40), E41 (≠ D41), G43 (= G43), C45 (= C45), G46 (= G46), C48 (= C48), R58 (≠ C58), C60 (= C60), C100 (= C99), G101 (= G100), C103 (= C102), C137 (= C134), C139 (= C136)
- binding hydrocinnamic acid: I255 (vs. gap), F425 (≠ L404), F494 (≠ W473), L497 (≠ T476), Y535 (≠ F514), L626 (≠ T609)
- binding magnesium ion: E899 (≠ D899), E903 (≠ A903)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): Q99 (= Q98), C139 (= C136), T420 (≠ G399), F421 (= F400), G422 (= G401), R533 (= R512), W650 (≠ A633), H653 (≠ I636), G654 (= G637), Q655 (= Q638), G656 (= G639), S695 (≠ T675), G696 (≠ S676), G697 (≠ A677), Q700 (= Q680), Q701 (≠ T681), C799 (≠ I801), N800 (= N802), T804 (≠ L806), Q807 (= Q809), S865 (≠ K865), G866 (= G866), V867 (≠ I867), G868 (= G868), E869 (= E869)
4us9A Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with 3- phenylpropionaldehyde (see paper)
31% identity, 99% coverage: 1:907/913 of query aligns to 1:907/907 of 4us9A
- active site: I390 (vs. gap), F425 (≠ L404), R501 (= R480), F505 (≠ H484), R533 (= R512), E869 (= E869), L870 (≠ Q870)
- binding 3-phenylpropanal: I255 (vs. gap), F257 (≠ I241), P258 (= P242), H752 (≠ E754)
- binding bicarbonate ion: R460 (= R439), L498 (≠ V477), A531 (= A510), F532 (= F511), Y535 (≠ F514), Q539 (= Q518), R890 (≠ T890), Y892 (≠ R892)
- binding fe2/s2 (inorganic) cluster: V38 (= V38), C40 (= C40), E41 (≠ D41), G43 (= G43), C45 (= C45), G46 (= G46), C48 (= C48), R58 (≠ C58), C60 (= C60), C100 (= C99), G101 (= G100), C103 (= C102), C137 (= C134), C139 (= C136)
- binding magnesium ion: E899 (≠ D899), E903 (≠ A903)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): Q99 (= Q98), C139 (= C136), T420 (≠ G399), F421 (= F400), G422 (= G401), R533 (= R512), W650 (≠ A633), H653 (≠ I636), G654 (= G637), Q655 (= Q638), G656 (= G639), S695 (≠ T675), G696 (≠ S676), G697 (≠ A677), Q700 (= Q680), Q701 (≠ T681), C799 (≠ I801), N800 (= N802), T804 (≠ L806), Q807 (= Q809), S865 (≠ K865), G866 (= G866), V867 (≠ I867), G868 (= G868), E869 (= E869)
4us8A Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with benzaldehyde (see paper)
31% identity, 99% coverage: 1:907/913 of query aligns to 1:907/907 of 4us8A
- active site: I390 (vs. gap), F425 (≠ L404), R501 (= R480), F505 (≠ H484), R533 (= R512), E869 (= E869), L870 (≠ Q870)
- binding bicarbonate ion: R460 (= R439), L498 (≠ V477), A531 (= A510), F532 (= F511), Y535 (≠ F514), Q539 (= Q518)
- binding fe2/s2 (inorganic) cluster: V38 (= V38), C40 (= C40), E41 (≠ D41), G43 (= G43), C45 (= C45), G46 (= G46), C48 (= C48), R58 (≠ C58), C60 (= C60), C100 (= C99), G101 (= G100), C103 (= C102), C137 (= C134), C139 (= C136)
- binding benzaldehyde: I255 (vs. gap), I255 (vs. gap), L394 (≠ M373), F425 (≠ L404), F425 (≠ L404), F425 (≠ L404), F425 (≠ L404), L497 (≠ T476), L497 (≠ T476), R501 (= R480), A531 (= A510), Y535 (≠ F514), Y535 (≠ F514), L626 (≠ T609), L626 (≠ T609), L626 (≠ T609), P694 (≠ K674), G696 (≠ S676), G697 (≠ A677)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): Q99 (= Q98), C139 (= C136), T420 (≠ G399), F421 (= F400), G422 (= G401), R533 (= R512), H653 (≠ I636), G654 (= G637), Q655 (= Q638), G656 (= G639), S695 (≠ T675), G696 (≠ S676), G697 (≠ A677), Q700 (= Q680), Q701 (≠ T681), C799 (≠ I801), N800 (= N802), T804 (≠ L806), Q807 (= Q809), S865 (≠ K865), G866 (= G866), V867 (≠ I867), G868 (= G868), E869 (= E869)
4c7yA Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with sodium dithionite and sodium sulfide (see paper)
31% identity, 99% coverage: 1:907/913 of query aligns to 1:907/907 of 4c7yA
- active site: I390 (vs. gap), F425 (≠ L404), R501 (= R480), F505 (≠ H484), R533 (= R512), E869 (= E869), L870 (≠ Q870)
- binding bicarbonate ion: R460 (= R439), L498 (≠ V477), A531 (= A510), Y535 (≠ F514), Q539 (= Q518)
- binding fe2/s2 (inorganic) cluster: C40 (= C40), E41 (≠ D41), G43 (= G43), C45 (= C45), G46 (= G46), C48 (= C48), R58 (≠ C58), C60 (= C60), C100 (= C99), G101 (= G100), C103 (= C102), C137 (= C134), C139 (= C136)
- binding magnesium ion: E899 (≠ D899), E903 (≠ A903)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): Q99 (= Q98), C139 (= C136), T420 (≠ G399), F421 (= F400), G422 (= G401), R533 (= R512), W650 (≠ A633), H653 (≠ I636), G654 (= G637), Q655 (= Q638), G656 (= G639), S695 (≠ T675), G696 (≠ S676), Q700 (= Q680), Q701 (≠ T681), C799 (≠ I801), N800 (= N802), T804 (≠ L806), Q807 (= Q809), S865 (≠ K865), G866 (= G866), V867 (≠ I867), G868 (= G868), E869 (= E869)
- binding hydrogen peroxide: G696 (≠ S676), G697 (≠ A677), E869 (= E869)
3fc4A Ethylene glycol inhibited form of aldehyde oxidoreductase from desulfovibrio gigas (see paper)
31% identity, 99% coverage: 1:907/913 of query aligns to 1:907/907 of 3fc4A
- active site: I390 (vs. gap), F425 (≠ L404), R501 (= R480), F505 (≠ H484), R533 (= R512), E869 (= E869), L870 (≠ Q870)
- binding 1,2-ethanediol: Y535 (≠ F514), Y622 (= Y604), G696 (≠ S676), G697 (≠ A677), E869 (= E869)
- binding fe2/s2 (inorganic) cluster: V38 (= V38), C40 (= C40), E41 (≠ D41), G43 (= G43), C45 (= C45), G46 (= G46), C48 (= C48), R58 (≠ C58), C60 (= C60), C100 (= C99), G101 (= G100), C103 (= C102), C137 (= C134), C139 (= C136)
- binding magnesium ion: E899 (≠ D899), E903 (≠ A903)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): Q99 (= Q98), C139 (= C136), G419 (= G398), T420 (≠ G399), F421 (= F400), G422 (= G401), R533 (= R512), W650 (≠ A633), H653 (≠ I636), G654 (= G637), Q655 (= Q638), G656 (= G639), S695 (≠ T675), G696 (≠ S676), Q700 (= Q680), Q701 (≠ T681), C799 (≠ I801), N800 (= N802), T804 (≠ L806), Q807 (= Q809), S865 (≠ K865), G866 (= G866), V867 (≠ I867), G868 (= G868), E869 (= E869)
3fahA Glycerol inhibited form of aldehyde oxidoreductase from desulfovibrio gigas (see paper)
31% identity, 99% coverage: 1:907/913 of query aligns to 1:907/907 of 3fahA
- active site: I390 (vs. gap), F425 (≠ L404), R501 (= R480), F505 (≠ H484), R533 (= R512), E869 (= E869), L870 (≠ Q870)
- binding fe2/s2 (inorganic) cluster: V38 (= V38), C40 (= C40), E41 (≠ D41), G43 (= G43), C45 (= C45), G46 (= G46), C48 (= C48), R58 (≠ C58), C60 (= C60), C100 (= C99), G101 (= G100), C103 (= C102), C137 (= C134), C139 (= C136)
- binding glycerol: P416 (≠ A395), Y535 (≠ F514), Y622 (= Y604), W683 (≠ M663), G696 (≠ S676), G697 (≠ A677), E869 (= E869), K884 (≠ R884), V889 (= V889), R890 (≠ T890), Y892 (≠ R892)
- binding magnesium ion: E899 (≠ D899), E903 (≠ A903)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): Q99 (= Q98), C139 (= C136), G419 (= G398), T420 (≠ G399), F421 (= F400), G422 (= G401), R533 (= R512), W650 (≠ A633), H653 (≠ I636), G654 (= G637), Q655 (= Q638), G656 (= G639), S695 (≠ T675), G696 (≠ S676), Q700 (= Q680), Q701 (≠ T681), C799 (≠ I801), N800 (= N802), T804 (≠ L806), Q807 (= Q809), S865 (≠ K865), G866 (= G866), V867 (≠ I867), G868 (= G868), E869 (= E869)
1sijA Crystal structure of the aldehyde dehydrogenase (a.K.A. Aor or mop) of desulfovibrio gigas covalently bound to [aso3]- (see paper)
31% identity, 99% coverage: 1:907/913 of query aligns to 1:907/907 of 1sijA
- active site: I390 (vs. gap), F425 (≠ L404), R501 (= R480), F505 (≠ H484), R533 (= R512), E869 (= E869), L870 (≠ Q870)
- binding arsenite: Y535 (≠ F514), G696 (≠ S676), G697 (≠ A677), E869 (= E869)
- binding fe2/s2 (inorganic) cluster: V38 (= V38), C40 (= C40), E41 (≠ D41), G43 (= G43), C45 (= C45), G46 (= G46), C48 (= C48), R58 (≠ C58), C60 (= C60), Q99 (= Q98), C100 (= C99), G101 (= G100), C103 (= C102), C137 (= C134), C139 (= C136)
- binding magnesium ion: E899 (≠ D899), E903 (≠ A903)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): Q99 (= Q98), C139 (= C136), T420 (≠ G399), F421 (= F400), G422 (= G401), R533 (= R512), H653 (≠ I636), G654 (= G637), Q655 (= Q638), G656 (= G639), S695 (≠ T675), G696 (≠ S676), S698 (= S678), Q700 (= Q680), Q701 (≠ T681), C799 (≠ I801), N800 (= N802), T804 (≠ L806), Q807 (= Q809), S865 (≠ K865), G866 (= G866), V867 (≠ I867), G868 (= G868), E869 (= E869)
Q46509 Aldehyde oxidoreductase; Molybdenum iron sulfur protein; EC 1.2.99.7 from Megalodesulfovibrio gigas (Desulfovibrio gigas) (see paper)
31% identity, 99% coverage: 1:907/913 of query aligns to 1:907/907 of Q46509
- C40 (= C40) binding
- C45 (= C45) binding
- C48 (= C48) binding
- C60 (= C60) binding
- C100 (= C99) binding
- C103 (= C102) binding
- C137 (= C134) binding
- C139 (= C136) binding
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
33% identity, 82% coverage: 156:901/913 of query aligns to 3:758/769 of O33819
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
33% identity, 81% coverage: 164:901/913 of query aligns to 2:750/761 of 1rm6A
- active site: Q206 (= Q369), T241 (≠ L404), Y318 (≠ R480), L322 (≠ H484), R350 (= R512), E718 (= E869), G719 (≠ Q870)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G235 (= G398), G236 (= G399), F237 (= F400), G238 (= G401), R350 (= R512), I473 (= I636), G474 (= G637), Q475 (= Q638), G476 (= G639), Y513 (≠ S676), S514 (≠ A677), S515 (= S678), V517 (≠ Q680), T518 (= T681), L646 (≠ I801), N647 (= N802), V651 (≠ L806), Q654 (= Q809), K714 (= K865), E715 (≠ G866), A716 (≠ I867), S717 (≠ G868), E718 (= E869)
Q0QLF2 Nicotinate dehydrogenase large molybdopterin subunit; NDH; Nicotinic acid hydroxylase large molybdopterin subunit; NAH; EC 1.17.1.5 from Eubacterium barkeri (Clostridium barkeri) (see 2 papers)
39% identity, 44% coverage: 165:564/913 of query aligns to 8:403/425 of Q0QLF2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2:425 modified: mature protein, Nicotinate dehydrogenase large molybdopterin subunit
3hrdE Crystal structure of nicotinate dehydrogenase (see paper)
39% identity, 44% coverage: 165:564/913 of query aligns to 7:402/420 of 3hrdE
- active site: Q207 (= Q369), L242 (= L404), R318 (= R480), H322 (= H484), R350 (= R512)
- binding calcium ion: T206 (= T368), N208 (≠ A370), D212 (= D374), K241 (= K403), L242 (= L404), D243 (= D405)
- binding pterin cytosine dinucleotide: G237 (= G399), F238 (= F400), R350 (= R512)
- binding selenium atom: F238 (= F400), A348 (= A510), F349 (= F511), R350 (= R512)
3hrdA Crystal structure of nicotinate dehydrogenase (see paper)
39% identity, 44% coverage: 165:564/913 of query aligns to 7:402/420 of 3hrdA
- active site: Q207 (= Q369), L242 (= L404), R318 (= R480), H322 (= H484), R350 (= R512)
- binding pterin cytosine dinucleotide: G236 (= G398), G237 (= G399), F238 (= F400), R350 (= R512)
- binding magnesium ion: T206 (= T368), N208 (≠ A370), D212 (= D374), K241 (= K403), L242 (= L404), D243 (= D405), T305 (= T467), Y308 (= Y470), A309 (= A471), S346 (= S508)
- binding nicotinic acid: A314 (≠ T476), R318 (= R480), F352 (= F514)
- binding selenium atom: F238 (= F400), G239 (= G401), A348 (= A510), F349 (= F511), R350 (= R512)
2ckjA Human milk xanthine oxidoreductase
28% identity, 84% coverage: 137:904/913 of query aligns to 489:1252/1264 of 2ckjA
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 228, 230, 231, 232, 233, 234, 308, 309, 317, 318, 321, 322, 324, 325, 331, 375
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 71, 111, 112, 114, 146, 147, 148
2e1qA Crystal structure of human xanthine oxidoreductase mutant, glu803val (see paper)
29% identity, 81% coverage: 165:904/913 of query aligns to 548:1283/1307 of 2e1qA
- active site: Q742 (= Q369), V777 (≠ L404), R855 (= R480), H859 (= H484), R887 (= R512), G1235 (= G868), E1236 (= E869)
- binding bicarbonate ion: R814 (= R439), H815 (= H440), I852 (≠ V477), F886 (= F511), F889 (= F514), G890 (= G515), Q893 (= Q518)
- binding calcium ion: E715 (= E344), H716 (= H345), Y718 (= Y347), T741 (= T368), T747 (≠ D374), S780 (= S407), T781 (vs. gap), S784 (≠ Q409), T811 (≠ S436), G812 (≠ T437)
- binding fe2/s2 (inorganic) cluster: L719 (≠ I348)
- binding hydroxy(dioxo)molybdenum: F773 (= F400), G774 (= G401), R887 (= R512), A1053 (≠ S676), A1054 (= A677), E1236 (= E869)
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 43, 44, 230, 231, 232, 233, 234, 235, 236, 237, 238, 311, 312, 316, 320, 321, 324, 325, 327, 328, 333, 334, 377, 378
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 71, 110, 111, 112, 114, 146, 148
P47989 Xanthine dehydrogenase/oxidase; EC 1.17.1.4; EC 1.17.3.2 from Homo sapiens (Human) (see 4 papers)
29% identity, 81% coverage: 165:904/913 of query aligns to 574:1309/1333 of P47989
- D584 (≠ R175) to A: in dbSNP:rs45491693
- R607 (= R197) to Q: in dbSNP:rs45442092
- K617 (≠ R207) to N: in dbSNP:rs45442398
- T623 (≠ L213) to I: in dbSNP:rs45448694
- I646 (≠ L237) to V: in dbSNP:rs17323225
- I703 (≠ T297) to V: in dbSNP:rs17011368
- L763 (≠ I364) to F: in a breast cancer sample; somatic mutation
- R791 (≠ I392) to G: in a breast cancer sample; somatic mutation; dbSNP:rs775646772
- T910 (≠ G509) to M: in dbSNP:rs669884
- C993 (≠ G591) modified: Disulfide link with 536, In oxidase form
- V1091 (≠ S688) to L: in dbSNP:rs45619033
- N1109 (≠ R710) to T: in dbSNP:rs45547640
- P1150 (= P764) to R: in dbSNP:rs1042036
- R1176 (≠ K790) to C: in dbSNP:rs45624433
- R1296 (vs. gap) to W: in dbSNP:rs45564939
Sites not aligning to the query:
- 133 E → K: in dbSNP:rs45447191
- 172 G → R: in dbSNP:rs45523133
- 235 T → M: in dbSNP:rs45469499
- 257:264 binding
- 337 binding
- 347:351 binding
- 360 binding
- 395 K → M: in dbSNP:rs34929837
- 422 binding
- 509 modified: Disulfide link with 1318, In oxidase form
- 536 modified: Disulfide link with 993, In oxidase form
- 555 P → S: in dbSNP:rs45577338
- 1318 modified: Disulfide link with 509, In oxidase form
3ax7A Bovine xanthine oxidase, protease cleaved form (see paper)
29% identity, 82% coverage: 157:904/913 of query aligns to 464:1207/1225 of 3ax7A
- active site: Q666 (= Q369), E701 (≠ L404), R779 (= R480), H783 (= H484), R811 (= R512), G1159 (= G868), E1160 (= E869)
- binding bicarbonate ion: R738 (= R439), H739 (= H440), I776 (≠ V477), T808 (≠ G509), A809 (= A510), G814 (= G515), Q817 (= Q518)
- binding calcium ion: A766 (≠ T467), S769 (≠ Y470), R770 (≠ A471), S773 (≠ G474), S806 (≠ P507), N807 (≠ S508)
- binding fe2/s2 (inorganic) cluster: L643 (≠ I348)
- binding {[(5aR,8R,9aR)-2-amino-4-oxo-6,7-di(sulfanyl-kappaS)-3,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogenato(2-) phosphate}(hydroxy)oxo(thioxo)molybdenum: G695 (= G398), G696 (= G399), F697 (= F400), G698 (= G401), F810 (= F511), R811 (= R512), M937 (≠ I636), G938 (= G637), Q939 (= Q638), A977 (≠ S676), A978 (= A677), S979 (= S678), S981 (≠ Q680), Q1093 (= Q809), E1160 (= E869)
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 45, 197, 198, 199, 200, 201, 202, 203, 204, 205, 278, 279, 283, 287, 288, 291, 292, 294, 295, 300, 301, 345
- binding fe2/s2 (inorganic) cluster: 41, 42, 43, 45, 47, 48, 50, 70, 72, 112, 113, 115, 147, 149
- binding {[(5aR,8R,9aR)-2-amino-4-oxo-6,7-di(sulfanyl-kappaS)-3,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogenato(2-) phosphate}(hydroxy)oxo(thioxo)molybdenum: 111, 149
3hrdB Crystal structure of nicotinate dehydrogenase (see paper)
40% identity, 35% coverage: 593:907/913 of query aligns to 2:327/330 of 3hrdB
- active site: E289 (= E869), P290 (≠ Q870)
- binding pterin cytosine dinucleotide: I45 (= I636), G46 (= G637), Q47 (= Q638), G48 (= G639), S49 (= S640), S85 (= S676), S87 (= S678), Q89 (= Q680), T90 (= T681), I215 (= I801), N216 (= N802), M219 (≠ L805), V220 (≠ L806), Q223 (= Q809), K285 (= K865), G286 (= G866), V287 (≠ I867), G288 (= G868), E289 (= E869)
- binding nicotinic acid: N17 (= N608), T18 (= T609)
Q0QLF1 Nicotinate dehydrogenase medium molybdopterin subunit; NDH; Nicotinic acid hydroxylase medium molybdopterin subunit; NAH; EC 1.17.1.5 from Eubacterium barkeri (Clostridium barkeri) (see paper)
40% identity, 35% coverage: 593:907/913 of query aligns to 2:327/330 of Q0QLF1
Query Sequence
>WP_011383893.1 NCBI__GCF_000009985.1:WP_011383893.1
MKRQTLSINGTSHSLEVPPMRRLSKVLREDLGLRGTKVGCDAGDCGACTVLIDGESVCSC
MIPVGRLTGREIITVEGLSEGAALGRLQRAFEHFGAAQCGICTPGMLNAATALLRSRPRP
SEDEVLDAIGGVLCRCTGYRKIVQAVVESHRFADEPVVPEAGSSVGTRLRRLDGRQRVDG
SEIYGDDVCPPDCLLVRVIRSPHPHARFTIGDLTALRVAYPGIVQVLTAADVPGINLFSV
IPGMEDQPAFAEGLVRYRGEAVAAVVMEADTNDIFQDADFPVLWEVLEPALSMEQATAAD
AVLLHAKRPGNILVRGFVQKGDLDLHWAKAAQVVEDSFTTGFVEHAYIEPEAGYARRVGD
TIEIYACTQAPYMDRDSVAAIMALPPEQVRIIPTAVGGGFGGKLDVSLQPYVALAAWSLG
RPVRCLYTRTESMASSTKRHPAAITARVGAGADGKLTAMEFDGDFNTGAYASWGPTVANR
VPVHCSGPYFIPALRARTRAIHTNNPPSGAFRGFGIPQASIAQESLFDQLADKLGLDRLE
FRRINAITAGQPTATGQILTASVGQQACFDALVPRWQEALAAAEAFNRTAGDRRRGVGVA
GMWYGCGNTSMSNPSTIRVALRADGAVVLFQGAVDIGQGSNTVITQICADALGIEIGKFT
LVMGDTALTADAGKTSASRQTFVSGRASQLAGLDLRDKILRMVNAGADSRLSLDGSILCV
SDGADTHQIDLQSLARDQDGLVMDGEGTFDPPTEKLDANGQGIPYATYGFGAQMAEVEVD
TALGTVKVLKIIAAHDVGRAINPMLLEGQIEGGIAQGLGLALMEEYIQGRTENLHDYLIP
TAGDIPPIETIIIEDAEPLGPFGAKGIGEQALIPTAPAILGAIRHATGVTIRQVPATPDR
VRAAIRAAKGVPS
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory