SitesBLAST
Comparing YP_001312744.1 NCBI__GCF_000017145.1:YP_001312744.1 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)
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
34% identity, 97% coverage: 19:766/772 of query aligns to 3:757/761 of 1rm6A
- active site: Q206 (= Q229), T241 (≠ Q264), Y318 (≠ G342), L322 (= L346), R350 (= R373), E718 (= E727), G719 (≠ D728)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G235 (= G258), G236 (= G259), F237 (= F260), G238 (= G261), R350 (= R373), I473 (≠ L495), G474 (= G496), Q475 (≠ T497), G476 (= G498), Y513 (≠ F535), S514 (≠ A536), S515 (= S537), V517 (≠ T539), T518 (= T540), L646 (≠ I652), N647 (≠ H653), V651 (≠ A657), Q654 (= Q660), K714 (= K723), E715 (≠ G724), A716 (≠ V725), S717 (≠ G726), E718 (= E727)
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
34% identity, 97% coverage: 19:766/772 of query aligns to 11:765/769 of O33819
- Q214 (= Q229) binding Mo-molybdopterin cytosine dinucleotide
- GF 244:245 (= GF 259:260) binding Mo-molybdopterin cytosine dinucleotide
- SSRVT 522:526 (≠ ASHTT 536:540) binding Mo-molybdopterin cytosine dinucleotide
- VGKALN 650:655 (≠ IGRVIH 648:653) binding Mo-molybdopterin cytosine dinucleotide
- KEAS 722:725 (≠ KGVG 723:726) binding Mo-molybdopterin cytosine dinucleotide
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
31% identity, 97% coverage: 19:766/772 of query aligns to 14:785/786 of 1t3qB
- active site: Q224 (= Q229), A259 (≠ Q264), E336 (vs. gap), V343 (≠ A345), R371 (= R373), E743 (= E727), S744 (≠ D728)
- binding pterin cytosine dinucleotide: G254 (= G259), F255 (= F260), R371 (= R373), S506 (≠ L495), G507 (= G496), Q508 (≠ T497), H510 (≠ A499), T513 (≠ A502), Y545 (≠ F535), S547 (= S537), G549 (≠ T539), A550 (≠ T540), C666 (≠ I648), I670 (= I652), I674 (≠ A656), V675 (≠ A657), Q678 (= Q660), K739 (= K723), G740 (= G724), M741 (≠ V725), G742 (= G726)
7dqxD Crystal structure of xanthine dehydrogenase family protein
30% identity, 96% coverage: 19:761/772 of query aligns to 6:764/770 of 7dqxD
- binding pterin cytosine dinucleotide: G247 (= G258), S248 (≠ G259), F249 (= F260), R363 (= R373), V491 (≠ L495), G492 (= G496), Q493 (≠ T497), G494 (= G498), V498 (≠ A502), S530 (≠ A534), W531 (≠ F535), S532 (≠ A536), S533 (= S537), R534 (≠ H538), S535 (≠ T539), T536 (= T540), T658 (≠ A656), T659 (≠ A657), Q662 (= Q660), G725 (= G724), L726 (≠ V725), G727 (= G726), E728 (= E727)
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)
38% identity, 55% coverage: 14:435/772 of query aligns to 3:414/425 of Q0QLF2
- Q208 (= Q229) binding Se-Mo-molybdopterin cytosine dinucleotide
- GFG 238:240 (= GFG 259:261) binding Se-Mo-molybdopterin cytosine dinucleotide
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)
38% identity, 55% coverage: 14:435/772 of query aligns to 2:413/420 of 3hrdE
- active site: Q207 (= Q229), L242 (≠ Q264), R318 (≠ V341), H322 (≠ A345), R350 (= R373)
- binding calcium ion: T206 (= T228), N208 (≠ S230), D212 (≠ V234), K241 (= K263), L242 (≠ Q264), D243 (= D265)
- binding pterin cytosine dinucleotide: G237 (= G259), F238 (= F260), R350 (= R373)
- binding selenium atom: F238 (= F260), A348 (= A371), F349 (= F372), R350 (= R373)
3hrdA Crystal structure of nicotinate dehydrogenase (see paper)
38% identity, 55% coverage: 14:435/772 of query aligns to 2:413/420 of 3hrdA
- active site: Q207 (= Q229), L242 (≠ Q264), R318 (≠ V341), H322 (≠ A345), R350 (= R373)
- binding pterin cytosine dinucleotide: G236 (= G258), G237 (= G259), F238 (= F260), R350 (= R373)
- binding magnesium ion: T206 (= T228), N208 (≠ S230), D212 (≠ V234), K241 (= K263), L242 (≠ Q264), D243 (= D265), T305 (≠ S328), Y308 (= Y331), A309 (≠ G332), S346 (≠ A369)
- binding nicotinic acid: A314 (≠ G337), R318 (≠ V341), F352 (≠ Y375)
- binding selenium atom: F238 (= F260), G239 (= G261), A348 (= A371), F349 (= F372), R350 (= R373)
P19919 Carbon monoxide dehydrogenase large chain; CO dehydrogenase subunit L; CO-DH L; EC 1.2.5.3 from Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5) (Oligotropha carboxidovorans) (see 2 papers)
29% identity, 96% coverage: 1:744/772 of query aligns to 1:780/809 of P19919
- C388 (vs. gap) binding Cu(+)
- E763 (= E727) binding Mo-molybdopterin cytosine dinucleotide
1n60B Crystal structure of the cu,mo-co dehydrogenase (codh); cyanide- inactivated form (see paper)
29% identity, 94% coverage: 19:744/772 of query aligns to 15:774/803 of 1n60B
- active site: Q234 (= Q229), V269 (≠ Q264), P346 (= P336), I352 (≠ V341), R381 (= R373), C382 (vs. gap), E757 (= E727), S758 (≠ D728)
- binding pterin cytosine dinucleotide: G264 (= G259), F265 (= F260), R381 (= R373), Q522 (≠ L495), G523 (= G496), Q524 (≠ T497), H526 (≠ A499), T529 (≠ A502), T561 (≠ A534), Y562 (≠ F535), G563 (≠ A536), S564 (= S537), S566 (≠ T539), T567 (= T540), C680 (≠ I648), I684 (= I652), I688 (≠ A656), I689 (≠ A657), Q692 (= Q660), K753 (= K723), G754 (= G724), V755 (= V725), E757 (= E727)
- binding mo(vi)(=o)(oh)2 cluster: F265 (= F260), G266 (= G261), Y562 (≠ F535), G563 (≠ A536), E757 (= E727)
1n63B Crystal structure of the cu,mo-co dehydrogenase (codh); carbon monoxide reduced state (see paper)
29% identity, 94% coverage: 19:744/772 of query aligns to 17:776/805 of 1n63B
- active site: Q236 (= Q229), V271 (≠ Q264), P348 (= P336), I354 (≠ V341), R383 (= R373), C384 (vs. gap), E759 (= E727), S760 (≠ D728)
- binding cu(i)-s-mo(iv)(=o)oh cluster: G268 (= G261), A381 (= A371), R383 (= R373), C384 (vs. gap), Y564 (≠ F535), G565 (≠ A536), E759 (= E727)
- binding pterin cytosine dinucleotide: G266 (= G259), F267 (= F260), R383 (= R373), Q524 (≠ L495), G525 (= G496), Q526 (≠ T497), H528 (≠ A499), T531 (≠ A502), T563 (≠ A534), Y564 (≠ F535), S566 (= S537), S568 (≠ T539), T569 (= T540), C682 (≠ I648), I686 (= I652), I690 (≠ A656), I691 (≠ A657), Q694 (= Q660), K755 (= K723), G756 (= G724), V757 (= V725), E759 (= E727)
1n62B Crystal structure of the mo,cu-co dehydrogenase (codh), n- butylisocyanide-bound state (see paper)
29% identity, 94% coverage: 19:744/772 of query aligns to 16:775/804 of 1n62B
- active site: Q235 (= Q229), V270 (≠ Q264), P347 (= P336), I353 (≠ V341), R382 (= R373), C383 (vs. gap), E758 (= E727), S759 (≠ D728)
- binding cu(i)-s-mo(iv)(=o)o-nbic cluster: G267 (= G261), V379 (vs. gap), A380 (= A371), R382 (= R373), C383 (vs. gap), F385 (≠ Y375), Y563 (≠ F535), G564 (≠ A536), E758 (= E727)
- binding pterin cytosine dinucleotide: G265 (= G259), F266 (= F260), R382 (= R373), Q523 (≠ L495), G524 (= G496), Q525 (≠ T497), H527 (≠ A499), T530 (≠ A502), T562 (≠ A534), Y563 (≠ F535), G564 (≠ A536), S565 (= S537), S567 (≠ T539), T568 (= T540), C681 (≠ I648), I685 (= I652), I689 (≠ A656), I690 (≠ A657), Q693 (= Q660), K754 (= K723), G755 (= G724), V756 (= V725), G757 (= G726), E758 (= E727)
1n5wB Crystal structure of the cu,mo-co dehydrogenase (codh); oxidized form (see paper)
29% identity, 94% coverage: 19:744/772 of query aligns to 16:775/804 of 1n5wB
- active site: Q235 (= Q229), V270 (≠ Q264), P347 (= P336), I353 (≠ V341), R382 (= R373), C383 (vs. gap), E758 (= E727), S759 (≠ D728)
- binding cu(i)-s-mo(vi)(=o)oh cluster: G267 (= G261), A380 (= A371), R382 (= R373), C383 (vs. gap), Y563 (≠ F535), G564 (≠ A536), E758 (= E727)
- binding pterin cytosine dinucleotide: G265 (= G259), F266 (= F260), R382 (= R373), Q523 (≠ L495), G524 (= G496), Q525 (≠ T497), H527 (≠ A499), T530 (≠ A502), T562 (≠ A534), Y563 (≠ F535), S565 (= S537), S567 (≠ T539), T568 (= T540), C681 (≠ I648), I685 (= I652), I689 (≠ A656), I690 (≠ A657), Q693 (= Q660), K754 (= K723), G755 (= G724), V756 (= V725), E758 (= E727)
1zxiB Reconstituted co dehydrogenase from oligotropha carboxidovorans (see paper)
29% identity, 94% coverage: 19:744/772 of query aligns to 16:775/804 of 1zxiB
- active site: Q235 (= Q229), V270 (≠ Q264), P347 (= P336), I353 (≠ V341), R382 (= R373), C383 (vs. gap), E758 (= E727), S759 (≠ D728)
- binding copper (ii) ion: C383 (vs. gap), S384 (≠ G374), E758 (= E727)
- binding cu(i)-s-mo(vi)(=o)oh cluster: F266 (= F260), G267 (= G261), A380 (= A371), Y381 (≠ F372), R382 (= R373), C383 (vs. gap), Y563 (≠ F535), G564 (≠ A536), E758 (= E727)
- binding pterin cytosine dinucleotide: G265 (= G259), F266 (= F260), R382 (= R373), Q523 (≠ L495), G524 (= G496), Q525 (≠ T497), H527 (≠ A499), T530 (≠ A502), T562 (≠ A534), Y563 (≠ F535), S565 (= S537), S567 (≠ T539), T568 (= T540), C681 (≠ I648), I685 (= I652), I689 (≠ A656), I690 (≠ A657), Q693 (= Q660), K754 (= K723), G755 (= G724), V756 (= V725), E758 (= E727)
4usaA Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with trans-cinnamaldehyde (see paper)
30% identity, 97% coverage: 15:764/772 of query aligns to 172:906/907 of 4usaA
- active site: I390 (≠ Q229), F425 (≠ Q264), R501 (≠ V341), F505 (≠ A345), R533 (= R373), E869 (= E727), L870 (≠ D728)
- binding bicarbonate ion: R460 (= R300), A531 (= A371), F532 (= F372), Y535 (= Y375), Q539 (= Q379)
- binding hydrocinnamic acid: I255 (≠ S93), F425 (≠ Q264), F494 (≠ H334), L497 (≠ G337), Y535 (= Y375), L626 (≠ I470)
- binding magnesium ion: E899 (= E757), E903 (≠ N761)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ G259), F421 (= F260), G422 (= G261), R533 (= R373), W650 (≠ T492), H653 (≠ L495), G654 (= G496), Q655 (≠ T497), G656 (= G498), S695 (≠ L542), G696 (= G543), G697 (= G544), Q700 (≠ A547), Q701 (= Q548), C799 (≠ I652), N800 (≠ H653), T804 (≠ A657), Q807 (= Q660), S865 (≠ K723), G866 (= G724), V867 (= V725), G868 (= G726), E869 (= E727)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 38, 40, 41, 43, 45, 46, 48, 58, 60, 100, 101, 103, 137, 139
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
4us9A Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with 3- phenylpropionaldehyde (see paper)
30% identity, 97% coverage: 15:764/772 of query aligns to 172:906/907 of 4us9A
- active site: I390 (≠ Q229), F425 (≠ Q264), R501 (≠ V341), F505 (≠ A345), R533 (= R373), E869 (= E727), L870 (≠ D728)
- binding 3-phenylpropanal: I255 (≠ S93), F257 (≠ H95), P258 (= P96), H752 (≠ Q606)
- binding bicarbonate ion: R460 (= R300), L498 (≠ V338), A531 (= A371), F532 (= F372), Y535 (= Y375), Q539 (= Q379), R890 (= R748), Y892 (≠ H750)
- binding magnesium ion: E899 (= E757), E903 (≠ N761)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ G259), F421 (= F260), G422 (= G261), R533 (= R373), W650 (≠ T492), H653 (≠ L495), G654 (= G496), Q655 (≠ T497), G656 (= G498), S695 (≠ L542), G696 (= G543), G697 (= G544), Q700 (≠ A547), Q701 (= Q548), C799 (≠ I652), N800 (≠ H653), T804 (≠ A657), Q807 (= Q660), S865 (≠ K723), G866 (= G724), V867 (= V725), G868 (= G726), E869 (= E727)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 38, 40, 41, 43, 45, 46, 48, 58, 60, 100, 101, 103, 137, 139
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
4us8A Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with benzaldehyde (see paper)
30% identity, 97% coverage: 15:764/772 of query aligns to 172:906/907 of 4us8A
- active site: I390 (≠ Q229), F425 (≠ Q264), R501 (≠ V341), F505 (≠ A345), R533 (= R373), E869 (= E727), L870 (≠ D728)
- binding bicarbonate ion: R460 (= R300), L498 (≠ V338), A531 (= A371), F532 (= F372), Y535 (= Y375), Q539 (= Q379)
- binding benzaldehyde: I255 (≠ S93), I255 (≠ S93), L394 (≠ M233), F425 (≠ Q264), F425 (≠ Q264), F425 (≠ Q264), F425 (≠ Q264), L497 (≠ G337), L497 (≠ G337), R501 (≠ V341), A531 (= A371), Y535 (= Y375), Y535 (= Y375), L626 (≠ I470), L626 (≠ I470), L626 (≠ I470), P694 (≠ Y541), G696 (= G543), G697 (= G544)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ G259), F421 (= F260), G422 (= G261), R533 (= R373), H653 (≠ L495), G654 (= G496), Q655 (≠ T497), G656 (= G498), S695 (≠ L542), G696 (= G543), G697 (= G544), Q700 (≠ A547), Q701 (= Q548), C799 (≠ I652), N800 (≠ H653), T804 (≠ A657), Q807 (= Q660), S865 (≠ K723), G866 (= G724), V867 (= V725), G868 (= G726), E869 (= E727)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 38, 40, 41, 43, 45, 46, 48, 58, 60, 100, 101, 103, 137, 139
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
4c7yA Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with sodium dithionite and sodium sulfide (see paper)
30% identity, 97% coverage: 15:764/772 of query aligns to 172:906/907 of 4c7yA
- active site: I390 (≠ Q229), F425 (≠ Q264), R501 (≠ V341), F505 (≠ A345), R533 (= R373), E869 (= E727), L870 (≠ D728)
- binding bicarbonate ion: R460 (= R300), L498 (≠ V338), A531 (= A371), Y535 (= Y375), Q539 (= Q379)
- binding magnesium ion: E899 (= E757), E903 (≠ N761)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ G259), F421 (= F260), G422 (= G261), R533 (= R373), W650 (≠ T492), H653 (≠ L495), G654 (= G496), Q655 (≠ T497), G656 (= G498), S695 (≠ L542), G696 (= G543), Q700 (≠ A547), Q701 (= Q548), C799 (≠ I652), N800 (≠ H653), T804 (≠ A657), Q807 (= Q660), S865 (≠ K723), G866 (= G724), V867 (= V725), G868 (= G726), E869 (= E727)
- binding hydrogen peroxide: G696 (= G543), G697 (= G544), E869 (= E727)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 40, 41, 43, 45, 46, 48, 58, 60, 100, 101, 103, 137, 139
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
3fc4A Ethylene glycol inhibited form of aldehyde oxidoreductase from desulfovibrio gigas (see paper)
30% identity, 97% coverage: 15:764/772 of query aligns to 172:906/907 of 3fc4A
- active site: I390 (≠ Q229), F425 (≠ Q264), R501 (≠ V341), F505 (≠ A345), R533 (= R373), E869 (= E727), L870 (≠ D728)
- binding 1,2-ethanediol: Y535 (= Y375), Y622 (≠ H462), G696 (= G543), G697 (= G544), E869 (= E727)
- binding magnesium ion: E899 (= E757), E903 (≠ N761)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G419 (= G258), T420 (≠ G259), F421 (= F260), G422 (= G261), R533 (= R373), W650 (≠ T492), H653 (≠ L495), G654 (= G496), Q655 (≠ T497), G656 (= G498), S695 (≠ L542), G696 (= G543), Q700 (≠ A547), Q701 (= Q548), C799 (≠ I652), N800 (≠ H653), T804 (≠ A657), Q807 (= Q660), S865 (≠ K723), G866 (= G724), V867 (= V725), G868 (= G726), E869 (= E727)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 38, 40, 41, 43, 45, 46, 48, 58, 60, 100, 101, 103, 137, 139
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
3fahA Glycerol inhibited form of aldehyde oxidoreductase from desulfovibrio gigas (see paper)
30% identity, 97% coverage: 15:764/772 of query aligns to 172:906/907 of 3fahA
- active site: I390 (≠ Q229), F425 (≠ Q264), R501 (≠ V341), F505 (≠ A345), R533 (= R373), E869 (= E727), L870 (≠ D728)
- binding glycerol: P416 (≠ H255), Y535 (= Y375), Y622 (≠ H462), W683 (≠ Q522), G696 (= G543), G697 (= G544), E869 (= E727), K884 (≠ Y742), V889 (= V747), R890 (= R748), Y892 (≠ H750)
- binding magnesium ion: E899 (= E757), E903 (≠ N761)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G419 (= G258), T420 (≠ G259), F421 (= F260), G422 (= G261), R533 (= R373), W650 (≠ T492), H653 (≠ L495), G654 (= G496), Q655 (≠ T497), G656 (= G498), S695 (≠ L542), G696 (= G543), Q700 (≠ A547), Q701 (= Q548), C799 (≠ I652), N800 (≠ H653), T804 (≠ A657), Q807 (= Q660), S865 (≠ K723), G866 (= G724), V867 (= V725), G868 (= G726), E869 (= E727)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 38, 40, 41, 43, 45, 46, 48, 58, 60, 100, 101, 103, 137, 139
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
1sijA Crystal structure of the aldehyde dehydrogenase (a.K.A. Aor or mop) of desulfovibrio gigas covalently bound to [aso3]- (see paper)
30% identity, 97% coverage: 15:764/772 of query aligns to 172:906/907 of 1sijA
- active site: I390 (≠ Q229), F425 (≠ Q264), R501 (≠ V341), F505 (≠ A345), R533 (= R373), E869 (= E727), L870 (≠ D728)
- binding arsenite: Y535 (= Y375), G696 (= G543), G697 (= G544), E869 (= E727)
- binding magnesium ion: E899 (= E757), E903 (≠ N761)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ G259), F421 (= F260), G422 (= G261), R533 (= R373), H653 (≠ L495), G654 (= G496), Q655 (≠ T497), G656 (= G498), S695 (≠ L542), G696 (= G543), S698 (≠ R545), Q700 (≠ A547), Q701 (= Q548), C799 (≠ I652), N800 (≠ H653), T804 (≠ A657), Q807 (= Q660), S865 (≠ K723), G866 (= G724), V867 (= V725), G868 (= G726), E869 (= E727)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 38, 40, 41, 43, 45, 46, 48, 58, 60, 99, 100, 101, 103, 137, 139
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
Query Sequence
>YP_001312744.1 NCBI__GCF_000017145.1:YP_001312744.1
MNTHERIDRDLSERDFTVVGKSVKRSDTLEKVTGAARYAGDVALPGMLYAKMKRSNIAHA
RIKSIDTSKALALQGVKAVLTHQDVPRVLHAGSPHPRSASVTKDQYILDERVRYWGEGVA
AVAAVSEEIAERAVALIEVEYDPLPGLFTIEAASDPAAPPIHENGLGQNYVLPPVFVTRG
DVDKGFGEADLVIEREYDLGRPTPAYMEPNVCVSQWDGNGKLTMWTSTQSAFMVRGTLAE
VLGVPLNKVRVIVDHMGGGFGAKQDLFQNEFLCALLARRTGRPVKMEFSRKETFVGGRSR
HPGKIWLKQGFTRDGRIVAREARVTFNSGAYGSHGPGVTNVGTAALTSLYRCENVRLEGR
CIYTNSPIAGAFRGYGVVQTYYALDLMMDEAAEKLGFDPAEFKLMNAVREGDMAPSGHPI
VGHGLVDCIRRVMEETNWHELRRREKPETVKRRGIGIGCEMHGSSAYPGIKEQGNAIVKM
NEDGTVTLITGTAGLGTGAHTALSQIVAEELGVPFEAVSVVQGDTDMVPWDIGAFASHTT
YLGGRAAQLAAADVRRQVLEHAAPLLKAEPGDLAIRDGFVVVANGSNQSLRLSEAVGPQR
GMPAVQLVGVGTYMPTKSYSFAAHFAEVEVDTETGEVAVLEVVPVHEIGRVIHPIAAAGQ
IEGGIQQGIGHTLSEDYVIDLTDGRSLNPSFVDYKMPLSMDMPSIRTIIIETAPDPGGPY
GAKGVGEDPIIAIGPAIANAIYDAIGVRFHHYPITPEQVLNALKTKANETRQ
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