SitesBLAST
Comparing WP_072905713.1 NCBI__GCF_900142125.1:WP_072905713.1 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)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
54% identity, 100% coverage: 3:1150/1150 of query aligns to 1:1146/1150 of A0A0H3JRU9
- R21 (= R23) mutation to A: Complete loss of catalytic activity.
- K119 (= K121) binding ATP
- K161 (= K163) binding ATP
- H211 (= H213) binding ATP
- E278 (= E280) binding ATP
- K411 (≠ T414) mutation to A: Complete loss of catalytic activity.
- RDAHQ 541:545 (= RDAHQ 546:550) binding substrate
- D542 (= D547) binding Mn(2+)
- A580 (= A585) mutation to T: Complete loss of catalytic activity.
- R614 (= R619) mutation to A: Complete loss of catalytic activity.
- Y621 (= Y626) mutation to A: Complete loss of catalytic activity.
- K712 (= K716) binding Mn(2+)
- H741 (= H745) binding Mn(2+)
- H743 (= H747) binding Mn(2+)
- Q838 (= Q842) mutation to A: About 2.5-fold loss of catalytic activity.
- T876 (= T880) mutation to A: Complete loss of catalytic activity.
- S879 (= S883) mutation to A: About 2-fold loss of catalytic activity.
- K880 (= K884) mutation to T: Complete loss of catalytic activity.
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
53% identity, 100% coverage: 5:1150/1150 of query aligns to 1:1137/1137 of 3bg5A
- active site: K117 (= K121), K159 (= K163), S189 (= S200), H202 (= H213), R228 (= R239), T267 (= T278), E269 (= E280), E281 (= E293), N283 (= N295), R285 (= R297), E289 (= E301), R337 (= R349), D533 (= D547), D639 (= D653), K703 (= K716), H732 (= H745), H734 (= H747), I755 (≠ V768), S761 (= S774), M762 (≠ V775), T801 (= T814), T867 (= T880), S869 (= S882), V881 (≠ I894), N883 (= N896), Q888 (≠ E901)
- binding adenosine-5'-triphosphate: K117 (= K121), M157 (≠ I161), K159 (= K163), Y196 (= Y207), I197 (= I208), H202 (= H213), Q226 (= Q237), H229 (= H240), E269 (= E280), L271 (= L282), E281 (= E293), N283 (= N295)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y463 (= Y475), G471 (= G483), F472 (≠ Y484), P473 (= P485), F579 (= F593)
- binding manganese (ii) ion: D533 (= D547), H732 (= H745), H734 (= H747)
- binding pyruvic acid: L603 (= L617), K703 (= K716)
3hb9A Crystal structure of s. Aureus pyruvate carboxylase a610t mutant (see paper)
53% identity, 100% coverage: 5:1150/1150 of query aligns to 1:1133/1133 of 3hb9A
- active site: K117 (= K121), K159 (= K163), H198 (= H213), R224 (= R239), T263 (= T278), E265 (= E280), E277 (= E293), N279 (= N295), R281 (= R297), E285 (= E301), R333 (= R349), D529 (= D547), D635 (= D653), K699 (= K716), H728 (= H745), H730 (= H747), I751 (≠ V768), S757 (= S774), M758 (≠ V775), T797 (= T814), T863 (= T880), S865 (= S882), V877 (≠ I894), N879 (= N896), Q884 (≠ E901)
- binding adenosine-5'-diphosphate: K117 (= K121), M157 (≠ I161), Y192 (= Y207), I193 (= I208), H198 (= H213), Q222 (= Q237), H225 (= H240), L267 (= L282), I276 (= I292), E277 (= E293)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y459 (= Y475), N462 (≠ Y478), G467 (= G483), F468 (≠ Y484), F575 (= F593), K577 (≠ R595)
- binding manganese (ii) ion: D529 (= D547), H728 (= H745), H730 (= H747)
4qshC Crystal structure of l. Monocytogenes pyruvate carboxylase in complex with cyclic-di-amp (see paper)
52% identity, 100% coverage: 3:1147/1150 of query aligns to 3:1077/1081 of 4qshC
- active site: K650 (= K716)
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: Y662 (≠ E728), Y689 (≠ A755), A693 (≠ M759), S696 (≠ Q762)
- binding manganese (ii) ion: D481 (= D547), H679 (= H745), H681 (= H747)
5vyzA Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
52% identity, 99% coverage: 6:1147/1150 of query aligns to 8:1141/1144 of 5vyzA
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: Q719 (≠ F725), Y722 (≠ E728), S752 (≠ M758), G753 (≠ M759), Q756 (= Q762)
- binding adenosine-5'-diphosphate: K123 (= K121), M162 (≠ I161), K164 (= K163), G168 (= G167), G170 (= G169), G171 (= G170), M174 (= M173), Y208 (= Y207), I209 (= I208), H214 (= H213), Q238 (= Q237), N241 (≠ H240), L283 (= L282), E293 (= E293), T449 (= T450)
- binding magnesium ion: E281 (= E280), E293 (= E293)
- binding manganese (ii) ion: D541 (= D547), K710 (= K716), H739 (= H745), H741 (= H747)
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
52% identity, 99% coverage: 6:1147/1150 of query aligns to 2:1135/1138 of 7zz3A
- binding acetyl coenzyme *a: N22 (≠ T26), F43 (≠ Y47), K44 (= K48), A45 (= A49), D46 (= D50), S48 (≠ A52), R363 (= R370), H413 (≠ Q420), E414 (= E421), R416 (= R423), R418 (= R425), R459 (≠ K466), R461 (= R468), K1016 (= K1028), T1017 (= T1029), L1018 (= L1030), R1045 (= R1057)
- binding adenosine-5'-triphosphate: K117 (= K121), M156 (≠ I161), K158 (= K163), G163 (= G168), G164 (= G169), G165 (= G170), M168 (= M173), E200 (= E205), Y202 (= Y207), I203 (= I208), H208 (= H213), Q232 (= Q237), N235 (≠ H240), L277 (= L282), E287 (= E293), N289 (= N295), T443 (= T450)
- binding bicarbonate ion: K237 (= K242), R291 (= R297), Q293 (= Q299), E295 (= E301)
- binding biotin: G84 (= G88), V294 (= V300), R342 (= R349), K1104 (= K1116)
- binding magnesium ion: E275 (= E280), E287 (= E293), V520 (≠ T532), T523 (≠ N535), D754 (= D766)
- binding manganese (ii) ion: D535 (= D547), K704 (= K716), H733 (= H745), H735 (= H747)
- binding pyruvic acid: R534 (= R546), Q538 (= Q550), L605 (= L617), K704 (= K716), T868 (= T880)
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
52% identity, 99% coverage: 6:1146/1150 of query aligns to 3:1129/1129 of 3tw6B
- active site: K124 (= K121), K162 (= K163), H212 (= H213), R238 (= R239), T277 (= T278), E279 (= E280), E293 (= E293), N295 (= N295), R297 (= R297), E301 (= E301), R349 (= R349), D544 (= D547), D650 (= D653), K713 (= K716), H742 (= H745), H744 (= H747), A877 (≠ T880)
- binding adenosine-5'-diphosphate: K124 (= K121), K162 (= K163), G167 (= G168), G169 (= G170), M172 (= M173), E204 (= E205), L206 (≠ Y207), V207 (≠ I208), H212 (= H213), Q236 (= Q237), N239 (≠ H240), L281 (= L282), E293 (= E293), T450 (= T450)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: R349 (= R349), D395 (= D395), K1102 (= K1116)
- binding magnesium ion: E279 (= E280), E293 (= E293), M529 (≠ T532), R530 (= R533), E532 (≠ N535), D763 (= D766)
- binding zinc ion: D544 (= D547), K713 (= K716), H742 (= H745), H744 (= H747)
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
52% identity, 100% coverage: 4:1150/1150 of query aligns to 3:1146/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K163), G167 (= G168), G168 (= G169), F206 (≠ Y207), Q236 (= Q237), H239 (= H240), E292 (= E293)
- binding coenzyme a: F21 (= F22), R22 (= R23), T25 (= T26), R45 (= R46), Q46 (≠ Y47), K47 (= K48), A48 (= A49), D49 (= D50), E50 (= E51), R366 (= R370), R413 (= R417), A416 (≠ Q420), R419 (= R423), Q462 (≠ K466), R464 (= R468), A465 (= A469), Q466 (≠ N470), K1024 (= K1028), R1053 (= R1057)
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
52% identity, 100% coverage: 4:1150/1150 of query aligns to 4:1147/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (= F22), T26 (= T26), R46 (= R46), Q47 (≠ Y47), K48 (= K48), A49 (= A49), D50 (= D50), R367 (= R370), R414 (= R417), E418 (= E421), R420 (= R423), R422 (= R425), A462 (≠ K465), Q463 (≠ K466), R465 (= R468), K1025 (= K1028)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K163), G168 (= G168), G169 (= G169), M173 (= M173), F207 (≠ Y207), I208 (= I208), P211 (= P211), H240 (= H240)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: D582 (= D588), Q839 (= Q842), T877 (= T880), S880 (= S883), K881 (= K884)
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
52% identity, 100% coverage: 4:1150/1150 of query aligns to 35:1178/1178 of P11498
- V145 (≠ I114) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (= R125) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (= R239) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y273) to C: in PC deficiency
- R451 (= R423) to C: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs113994143
- D572 (= D547) binding Mn(2+)
- R583 (= R558) to L: in PC deficiency; dbSNP:rs119103242
- A610 (= A585) to T: in PC deficiency; mild; dbSNP:rs28940589
- R631 (= R606) to Q: in PC deficiency; dbSNP:rs113994145
- K741 (= K716) binding via carbamate group; modified: N6-carboxylysine
- M743 (= M718) to I: in PC deficiency; mild; dbSNP:rs28940590
- H771 (= H745) binding Mn(2+)
- H773 (= H747) binding Mn(2+)
- F1077 (≠ Y1049) mutation F->A,E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer.
- VAK 1131:1133 (≠ VKE 1103:1105) natural variant: Missing (in PC deficiency)
- K1144 (= K1116) modified: N6-biotinyllysine
7zyyA Cryo-em structure of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
53% identity, 92% coverage: 6:1068/1150 of query aligns to 2:1056/1056 of 7zyyA
- binding acetyl coenzyme *a: R19 (= R23), N22 (≠ T26), F43 (≠ Y47), K44 (= K48), A45 (= A49), R363 (= R370), E414 (= E421), R416 (= R423), R418 (= R425), R459 (≠ K466), D460 (= D467), R461 (= R468), K1016 (= K1028), T1017 (= T1029), L1018 (= L1030), N1041 (= N1053), R1045 (= R1057)
- binding adenosine-5'-diphosphate: K158 (= K163), G163 (= G168), G164 (= G169), M168 (= M173), E200 (= E205), K201 (= K206), Y202 (= Y207), I203 (= I208), H208 (= H213), Q232 (= Q237), N235 (≠ H240), E275 (= E280), L277 (= L282), E287 (= E293), T443 (= T450)
- binding bicarbonate ion: R291 (= R297), Q293 (= Q299), V294 (= V300), E295 (= E301)
- binding magnesium ion: E275 (= E280), E287 (= E293), V520 (≠ T532), T523 (≠ N535), D754 (= D766)
- binding manganese (ii) ion: D535 (= D547), K704 (= K716), H733 (= H745), H735 (= H747)
- binding pyruvic acid: Q538 (= Q550), G572 (= G584), L605 (= L617), R607 (= R619), K704 (= K716), T868 (= T880)
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
51% identity, 100% coverage: 4:1150/1150 of query aligns to 35:1178/1178 of Q05920
- K35 (= K4) modified: N6-acetyllysine
- K39 (= K8) modified: N6-acetyllysine
- K79 (= K48) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ Q117) modified: N6-acetyllysine
- K152 (= K121) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ N210) modified: N6-acetyllysine
- K434 (≠ L406) modified: N6-acetyllysine
- K589 (≠ R564) modified: N6-acetyllysine
- K717 (= K692) modified: N6-acetyllysine
- K748 (= K723) modified: N6-acetyllysine; mutation to Q: Reduced pyruvate carboxylase activity.
- K892 (≠ E864) modified: N6-acetyllysine
- K969 (= K941) modified: N6-acetyllysine
8gk8A R21a staphylococcus aureus pyruvate carboxylase (see paper)
53% identity, 92% coverage: 5:1064/1150 of query aligns to 1:1037/1041 of 8gk8A
- binding acetyl coenzyme *a: E400 (= E421), R402 (= R423), R404 (= R425), L445 (≠ K466), R447 (= R468), N1026 (= N1053), R1030 (= R1057)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: N457 (≠ Y478), G462 (= G483), F463 (≠ Y484), P464 (= P485), F570 (= F593), K572 (≠ R595)
- binding coenzyme a: R42 (= R46), Y43 (= Y47), A45 (= A49), D46 (= D50), E47 (= E51), S48 (≠ A52)
- binding manganese (ii) ion: D524 (= D547), K694 (= K716), H723 (= H745), H725 (= H747)
3tw6C Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
52% identity, 92% coverage: 6:1063/1150 of query aligns to 3:1044/1044 of 3tw6C
- active site: K124 (= K121), K166 (= K163), H200 (= H213), R226 (= R239), T265 (= T278), E267 (= E280), E281 (= E293), N283 (= N295), R285 (= R297), E289 (= E301), R337 (= R349), D528 (= D547), D634 (= D653), K697 (= K716), H726 (= H745), H728 (= H747), A861 (≠ T880)
- binding adenosine-5'-diphosphate: K166 (= K163), M169 (= M173), V195 (≠ I208), H200 (= H213), Q224 (= Q237), E281 (= E293), T438 (= T450)
- binding coenzyme a: R411 (= R423), R413 (= R425), R453 (≠ K465), Q454 (≠ K466), D455 (= D467), R456 (= R468), L1011 (= L1030)
- binding magnesium ion: E267 (= E280), E281 (= E293)
- binding phosphonoacetic acid: K229 (= K242), R285 (= R297), Q287 (= Q299), V288 (= V300), E289 (= E301)
- binding zinc ion: D528 (= D547), K697 (= K716), H726 (= H745), H728 (= H747)
2qf7B Crystal structure of a complete multifunctional pyruvate carboxylase from rhizobium etli (see paper)
52% identity, 92% coverage: 6:1065/1150 of query aligns to 3:1016/1017 of 2qf7B
- active site: K123 (= K121), K150 (= K163), H169 (= H213), R195 (= R239), T234 (= T278), E236 (= E280), E250 (= E293), N252 (= N295), R254 (= R297), E258 (= E301), R306 (= R349), D498 (= D547), D604 (= D653), K667 (= K716), H696 (= H745), H698 (= H747), T831 (= T880)
- binding phosphothiophosphoric acid-adenylate ester: M148 (≠ I161), K150 (= K163), M153 (= M173), E161 (= E205), V164 (≠ I208), H169 (= H213), Q193 (= Q237), E236 (= E280), L238 (= L282), I249 (= I292), E250 (= E293), T407 (= T450)
- binding magnesium ion: E236 (= E280), E250 (= E293), M483 (≠ T532), R484 (= R533), E486 (≠ N535), D717 (= D766)
- binding zinc ion: D498 (= D547), K667 (= K716), H696 (= H745), H698 (= H747)
P11154 Pyruvate carboxylase 1; Pyruvic carboxylase 1; PCB 1; EC 6.4.1.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
50% identity, 99% coverage: 8:1150/1150 of query aligns to 21:1169/1178 of P11154
- K1135 (= K1116) modified: N6-biotinyllysine
3bg5B Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
54% identity, 82% coverage: 208:1150/1150 of query aligns to 134:1074/1074 of 3bg5B
- active site: H139 (= H213), R165 (= R239), T204 (= T278), E206 (= E280), E218 (= E293), N220 (= N295), R222 (= R297), E226 (= E301), R274 (= R349), D470 (= D547), D576 (= D653), K640 (= K716), H669 (= H745), H671 (= H747), I692 (≠ V768), S698 (= S774), M699 (≠ V775), T738 (= T814), T804 (= T880), S806 (= S882), V818 (≠ I894), N820 (= N896), Q825 (≠ E901)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: N403 (≠ Y478), G408 (= G483), F409 (≠ Y484), P410 (= P485), F516 (= F593), K518 (≠ R595)
- binding manganese (ii) ion: D470 (= D547), H669 (= H745), H671 (= H747)
- binding pyruvic acid: Q473 (= Q550), K640 (= K716), T804 (= T880)
Sites not aligning to the query:
5vyzC Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
52% identity, 82% coverage: 203:1147/1150 of query aligns to 143:1080/1083 of 5vyzC
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: P657 (= P724), Y661 (≠ E728), S691 (≠ M758), Q695 (= Q762)
- binding adenosine-5'-diphosphate: Y147 (= Y207), H153 (= H213), Q177 (= Q237), L222 (= L282), E232 (= E293), T388 (= T450)
- binding magnesium ion: E220 (= E280), E232 (= E293)
- binding manganese (ii) ion: D480 (= D547), K649 (= K716), H678 (= H745), H680 (= H747)
2qf7A Crystal structure of a complete multifunctional pyruvate carboxylase from rhizobium etli (see paper)
52% identity, 82% coverage: 206:1149/1150 of query aligns to 140:1076/1076 of 2qf7A
- active site: H147 (= H213), R173 (= R239), T212 (= T278), E214 (= E280), E228 (= E293), N230 (= N295), R232 (= R297), E236 (= E301), R284 (= R349), D479 (= D547), D585 (= D653), K648 (= K716), H677 (= H745), H679 (= H747), T812 (= T880)
- binding phosphothiophosphoric acid-adenylate ester: H147 (= H213), Q171 (= Q237), E214 (= E280), L216 (= L282), E228 (= E293), T385 (= T450)
- binding coenzyme a: R400 (≠ K465), Q401 (≠ K466), D402 (= D467), R403 (= R468), A404 (= A469), I956 (= I1024), K960 (= K1028), L962 (= L1030), N985 (= N1053)
- binding magnesium ion: E214 (= E280), E228 (= E293), M464 (≠ T532), R465 (= R533), E467 (≠ N535), D698 (= D766)
- binding zinc ion: D479 (= D547), K648 (= K716), H677 (= H745), H679 (= H747)
Sites not aligning to the query:
3ho8A Crystal structure of s. Aureus pyruvate carboxylase in complex with coenzyme a (see paper)
55% identity, 75% coverage: 205:1065/1150 of query aligns to 136:994/994 of 3ho8A
- active site: H144 (= H213), R170 (= R239), T209 (= T278), E211 (= E280), E223 (= E293), N225 (= N295), R227 (= R297), E231 (= E301), R279 (= R349), D475 (= D547), D581 (= D653), K645 (= K716), H674 (= H745), H676 (= H747), I697 (≠ V768), S703 (= S774), M704 (≠ V775), T743 (= T814), T809 (= T880), S811 (= S882), V823 (≠ I894), N825 (= N896), Q830 (≠ E901)
- binding coenzyme a: E351 (= E421), R353 (= R423), R355 (= R425), S395 (≠ K465), L396 (≠ K466), R398 (= R468), K957 (= K1028), M981 (≠ L1052), R986 (= R1057)
- binding manganese (ii) ion: D475 (= D547), H674 (= H745), H676 (= H747)
Sites not aligning to the query:
Query Sequence
>WP_072905713.1 NCBI__GCF_900142125.1:WP_072905713.1
MGVKKFKKIMAANRGEIAIRIFRACTELGISTVAIYSEEDRLSLHRYKADEAYQIGKGKG
PIDAYLSIDEIIDLARKKDVDAIHPGYGFLSENAEFAEACERAGISFIGPTPEIQRQLGD
KISGRQVAIEAGVPIVPGTENPVQTEEEALIFAKDCGYPIIVKASSGGGGRGMRVVNNKK
ELLEGIRSAASEAQAAFGDSTVFLEKYIENPKHVEVQILGDAHGNLVHFYERDCSIQRRH
QKVIEIAPSLYLTKKKREELCGYALKLASAVNYRNAGTVEFLMDKDQNFYFIEVNPRIQV
EHTVTELVTMRNLVQAQILIAEGHKLSDPCIGIKSQKDIELRGYAIQSRITTEDPANNFS
PDFGTIKAYRTAAGFGVRLDAAAGYAGALITPHYDSLLVKVSTWGLSFECAARTMHRALQ
EFRIRGVKTNIGFLEKVITHPTFLEGKCDTSFLDKHPEVFDLKIKKDRANKILNYIGYTT
VNGYPGIAPEKALRFKNLREAEVPEIPYGQPHPRGTRDILREKGPKGLAEWTRKNKQLLL
TDTTMRDAHQSLMATRFRTYDLDRIAEATAHLGGGLWSLEMWGGATYDVSMRFLREDPWD
RLERLREKIPNILFQMLLRGSNAVGYTNYPDNVVQDFVAKAAEKGIDVFRVFDSLNWTTG
MKVAMEAVQKSGAICEAAICYTGDILDPKRDKYPLEYYVNMAKELETMGADVLAIKDMAG
LLKPFAAEKLVKALKNETGLPIHLHTHDTSSNGVAMLMMAAQAGCDVVDAALSSVSGLTA
QPNMNALLAALEGTIWDPKVDMQGLQKLANYWETCRTYYAPFESELRSGTAQVYEHEIPG
GQYSNYKPQVEGLGLGHRWEECKEMYRKVNDMFGDLVKVTPSSKIVGDMAMFMIQNNLEP
EDVYERGHDLAFPQGVVDFFKGMIGQPYGGFPEKLQKIILKGEQPLTCRPGELLEPVDFV
LKKDELEKKLGHKVRDEDVLSAVLYPGVYEEYDRFRQEHSDTSVLPTPVFFYGLDIGDEV
TIDIEAGKTLIVKLNAVGRVREDGTRNIYFELNGEPRTVVVKDESVESDESSHVKADPDN
GHEIGAPMPGKIFKMNVNIGDEVKEGDVMLVTEAMKMETNVKAKKDGVIKEIVFGEGDQV
DQGDLLLVFE
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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