SitesBLAST
Comparing WP_013011594.1 NCBI__GCF_000025725.1:WP_013011594.1 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)
52% identity, 100% coverage: 2:1143/1144 of query aligns to 3:1145/1150 of A0A0H3JRU9
- R21 (= R20) mutation to A: Complete loss of catalytic activity.
- K119 (= K118) binding ATP
- K161 (= K160) binding ATP
- H211 (= H210) binding ATP
- E278 (= E277) binding ATP
- K411 (= K411) mutation to A: Complete loss of catalytic activity.
- RDAHQ 541:545 (= RDAHQ 540:544) binding substrate
- D542 (= D541) binding Mn(2+)
- A580 (= A579) mutation to T: Complete loss of catalytic activity.
- R614 (= R613) mutation to A: Complete loss of catalytic activity.
- Y621 (= Y620) mutation to A: Complete loss of catalytic activity.
- K712 (= K710) binding Mn(2+)
- H741 (= H739) binding Mn(2+)
- H743 (= H741) binding Mn(2+)
- Q838 (= Q836) mutation to A: About 2.5-fold loss of catalytic activity.
- T876 (= T874) mutation to A: Complete loss of catalytic activity.
- S879 (= S877) mutation to A: About 2-fold loss of catalytic activity.
- K880 (= K878) mutation to T: Complete loss of catalytic activity.
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
52% identity, 100% coverage: 3:1143/1144 of query aligns to 2:1137/1138 of 7zz3A
- binding acetyl coenzyme *a: N22 (≠ T23), F43 (≠ Y44), K44 (= K45), A45 (= A46), D46 (= D47), S48 (≠ A49), R363 (= R367), H413 (≠ S417), E414 (= E418), R416 (= R420), R418 (= R422), R459 (≠ Q463), R461 (= R465), K1016 (= K1022), T1017 (= T1023), L1018 (= L1024), R1045 (= R1051)
- binding adenosine-5'-triphosphate: K117 (= K118), M156 (≠ L158), K158 (= K160), G163 (= G165), G164 (= G166), G165 (= G167), M168 (≠ I170), E200 (= E202), Y202 (= Y204), I203 (= I205), H208 (= H210), Q232 (= Q234), N235 (≠ H237), L277 (= L279), E287 (= E290), N289 (= N292), T443 (= T447)
- binding bicarbonate ion: K237 (= K239), R291 (= R294), Q293 (= Q296), E295 (= E298)
- binding biotin: G84 (= G85), V294 (= V297), R342 (= R346), K1104 (= K1110)
- binding magnesium ion: E275 (= E277), E287 (= E290), V520 (= V526), T523 (≠ S529), D754 (= D760)
- binding manganese (ii) ion: D535 (= D541), K704 (= K710), H733 (= H739), H735 (= H741)
- binding pyruvic acid: R534 (= R540), Q538 (= Q544), L605 (= L611), K704 (= K710), T868 (= T874)
5vyzA Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
52% identity, 100% coverage: 3:1143/1144 of query aligns to 8:1143/1144 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 (≠ Y719), Y722 (≠ K722), S752 (≠ L752), G753 (≠ M753), Q756 (≠ E756)
- binding adenosine-5'-diphosphate: K123 (= K118), M162 (≠ L158), K164 (= K160), G168 (= G164), G170 (= G166), G171 (= G167), M174 (≠ I170), Y208 (= Y204), I209 (= I205), H214 (= H210), Q238 (= Q234), N241 (≠ H237), L283 (= L279), E293 (= E290), T449 (= T447)
- binding magnesium ion: E281 (= E277), E293 (= E290)
- binding manganese (ii) ion: D541 (= D541), K710 (= K710), H739 (= H739), H741 (= H741)
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
52% identity, 100% coverage: 2:1143/1144 of query aligns to 1:1136/1137 of 3bg5A
- active site: K117 (= K118), K159 (= K160), S189 (≠ D197), H202 (= H210), R228 (= R236), T267 (= T275), E269 (= E277), E281 (= E290), N283 (= N292), R285 (= R294), E289 (= E298), R337 (= R346), D533 (= D541), D639 (= D647), K703 (= K710), H732 (= H739), H734 (= H741), I755 (= I762), S761 (= S768), M762 (= M769), T801 (≠ R808), T867 (= T874), S869 (= S876), V881 (= V888), N883 (= N890), Q888 (≠ D895)
- binding adenosine-5'-triphosphate: K117 (= K118), M157 (≠ L158), K159 (= K160), Y196 (= Y204), I197 (= I205), H202 (= H210), Q226 (= Q234), H229 (= H237), E269 (= E277), L271 (= L279), E281 (= E290), N283 (= N292)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y463 (≠ F472), G471 (≠ N480), F472 (vs. gap), P473 (= P481), F579 (= F587)
- binding manganese (ii) ion: D533 (= D541), H732 (= H739), H734 (= H741)
- binding pyruvic acid: L603 (= L611), K703 (= K710)
3hb9A Crystal structure of s. Aureus pyruvate carboxylase a610t mutant (see paper)
52% identity, 100% coverage: 2:1143/1144 of query aligns to 1:1132/1133 of 3hb9A
- active site: K117 (= K118), K159 (= K160), H198 (= H210), R224 (= R236), T263 (= T275), E265 (= E277), E277 (= E290), N279 (= N292), R281 (= R294), E285 (= E298), R333 (= R346), D529 (= D541), D635 (= D647), K699 (= K710), H728 (= H739), H730 (= H741), I751 (= I762), S757 (= S768), M758 (= M769), T797 (≠ R808), T863 (= T874), S865 (= S876), V877 (= V888), N879 (= N890), Q884 (≠ D895)
- binding adenosine-5'-diphosphate: K117 (= K118), M157 (≠ L158), Y192 (= Y204), I193 (= I205), H198 (= H210), Q222 (= Q234), H225 (= H237), L267 (= L279), I276 (≠ L289), E277 (= E290)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y459 (≠ F472), N462 (= N475), G467 (≠ N480), F468 (vs. gap), F575 (= F587), K577 (= K589)
- binding manganese (ii) ion: D529 (= D541), H728 (= H739), H730 (= H741)
7zyyA Cryo-em structure of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
52% identity, 92% coverage: 3:1060/1144 of query aligns to 2:1054/1056 of 7zyyA
- binding acetyl coenzyme *a: R19 (= R20), N22 (≠ T23), F43 (≠ Y44), K44 (= K45), A45 (= A46), R363 (= R367), E414 (= E418), R416 (= R420), R418 (= R422), R459 (≠ Q463), D460 (= D464), R461 (= R465), K1016 (= K1022), T1017 (= T1023), L1018 (= L1024), N1041 (= N1047), R1045 (= R1051)
- binding adenosine-5'-diphosphate: K158 (= K160), G163 (= G165), G164 (= G166), M168 (≠ I170), E200 (= E202), K201 (= K203), Y202 (= Y204), I203 (= I205), H208 (= H210), Q232 (= Q234), N235 (≠ H237), E275 (= E277), L277 (= L279), E287 (= E290), T443 (= T447)
- binding bicarbonate ion: R291 (= R294), Q293 (= Q296), V294 (= V297), E295 (= E298)
- binding magnesium ion: E275 (= E277), E287 (= E290), V520 (= V526), T523 (≠ S529), D754 (= D760)
- binding manganese (ii) ion: D535 (= D541), K704 (= K710), H733 (= H739), H735 (= H741)
- binding pyruvic acid: Q538 (= Q544), G572 (= G578), L605 (= L611), R607 (= R613), K704 (= K710), T868 (= T874)
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
49% identity, 99% coverage: 3:1140/1144 of query aligns to 3:1129/1129 of 3tw6B
- active site: K124 (= K118), K162 (= K160), H212 (= H210), R238 (= R236), T277 (= T275), E279 (= E277), E293 (= E290), N295 (= N292), R297 (= R294), E301 (= E298), R349 (= R346), D544 (= D541), D650 (= D647), K713 (= K710), H742 (= H739), H744 (= H741), A877 (≠ T874)
- binding adenosine-5'-diphosphate: K124 (= K118), K162 (= K160), G167 (= G165), G169 (= G167), M172 (≠ I170), E204 (= E202), L206 (≠ Y204), V207 (≠ I205), H212 (= H210), Q236 (= Q234), N239 (≠ H237), L281 (= L279), E293 (= E290), T450 (= T447)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: R349 (= R346), D395 (= D392), K1102 (= K1110)
- binding magnesium ion: E279 (= E277), E293 (= E290), M529 (≠ V526), R530 (= R527), E532 (≠ S529), D763 (= D760)
- binding zinc ion: D544 (= D541), K713 (= K710), H742 (= H739), H744 (= H741)
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
49% identity, 100% coverage: 3:1143/1144 of query aligns to 5:1145/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K160), G167 (= G165), G168 (= G166), F206 (≠ Y204), Q236 (= Q234), H239 (= H237), E292 (= E290)
- binding coenzyme a: F21 (= F19), R22 (= R20), T25 (= T23), R45 (= R43), Q46 (≠ Y44), K47 (= K45), A48 (= A46), D49 (= D47), E50 (= E48), R366 (= R367), R413 (= R414), A416 (≠ S417), R419 (= R420), Q462 (= Q463), R464 (= R465), A465 (= A466), Q466 (≠ T467), K1024 (= K1022), R1053 (= R1051)
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
49% identity, 100% coverage: 3:1143/1144 of query aligns to 6:1146/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (= F19), T26 (= T23), R46 (= R43), Q47 (≠ Y44), K48 (= K45), A49 (= A46), D50 (= D47), R367 (= R367), R414 (= R414), E418 (= E418), R420 (= R420), R422 (= R422), A462 (≠ R462), Q463 (= Q463), R465 (= R465), K1025 (= K1022)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K160), G168 (= G165), G169 (= G166), M173 (≠ I170), F207 (≠ Y204), I208 (= I205), P211 (= P208), H240 (= H237)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: D582 (= D582), Q839 (= Q836), T877 (= T874), S880 (= S877), K881 (= K878)
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
49% identity, 100% coverage: 3:1143/1144 of query aligns to 37:1177/1178 of P11498
- V145 (≠ T111) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (≠ K122) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (= R236) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (≠ L270) to C: in PC deficiency
- R451 (= R420) to C: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs113994143
- D572 (= D541) binding Mn(2+)
- R583 (= R552) to L: in PC deficiency; dbSNP:rs119103242
- A610 (= A579) to T: in PC deficiency; mild; dbSNP:rs28940589
- R631 (= R600) to Q: in PC deficiency; dbSNP:rs113994145
- K741 (= K710) binding via carbamate group; modified: N6-carboxylysine
- M743 (= M712) to I: in PC deficiency; mild; dbSNP:rs28940590
- H771 (= H739) binding Mn(2+)
- H773 (= H741) binding Mn(2+)
- F1077 (≠ Y1043) mutation F->A,E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer.
- VAK 1131:1133 (= VAK 1097:1099) natural variant: Missing (in PC deficiency)
- K1144 (= K1110) modified: N6-biotinyllysine
4qshC Crystal structure of l. Monocytogenes pyruvate carboxylase in complex with cyclic-di-amp (see paper)
49% identity, 100% coverage: 2:1143/1144 of query aligns to 5:1079/1081 of 4qshC
- active site: K650 (= K710)
- 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 (≠ K722), Y689 (≠ A749), A693 (≠ M753), S696 (≠ E756)
- binding manganese (ii) ion: D481 (= D541), H679 (= H739), H681 (= H741)
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
49% identity, 100% coverage: 3:1143/1144 of query aligns to 37:1177/1178 of Q05920
- K39 (= K5) modified: N6-acetyllysine
- K79 (= K45) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ M114) modified: N6-acetyllysine
- K152 (= K118) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ E207) modified: N6-acetyllysine
- K434 (≠ H403) modified: N6-acetyllysine
- K589 (≠ D558) modified: N6-acetyllysine
- K717 (= K686) modified: N6-acetyllysine
- K748 (= K717) modified: N6-acetyllysine; mutation to Q: Reduced pyruvate carboxylase activity.
- K892 (≠ Q858) modified: N6-acetyllysine
- K969 (= K935) modified: N6-acetyllysine
Sites not aligning to the query:
- 35 modified: N6-acetyllysine
8gk8A R21a staphylococcus aureus pyruvate carboxylase (see paper)
52% identity, 92% coverage: 2:1058/1144 of query aligns to 1:1037/1041 of 8gk8A
- binding acetyl coenzyme *a: E400 (= E418), R402 (= R420), R404 (= R422), L445 (≠ Q463), R447 (= R465), N1026 (= N1047), R1030 (= R1051)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: N457 (= N475), G462 (≠ N480), F463 (vs. gap), P464 (= P481), F570 (= F587), K572 (= K589)
- binding coenzyme a: R42 (= R43), Y43 (= Y44), A45 (= A46), D46 (= D47), E47 (= E48), S48 (≠ A49)
- binding manganese (ii) ion: D524 (= D541), K694 (= K710), H723 (= H739), H725 (= H741)
3tw6C Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
49% identity, 92% coverage: 3:1057/1144 of query aligns to 3:1044/1044 of 3tw6C
- active site: K124 (= K118), K166 (= K160), H200 (= H210), R226 (= R236), T265 (= T275), E267 (= E277), E281 (= E290), N283 (= N292), R285 (= R294), E289 (= E298), R337 (= R346), D528 (= D541), D634 (= D647), K697 (= K710), H726 (= H739), H728 (= H741), A861 (≠ T874)
- binding adenosine-5'-diphosphate: K166 (= K160), M169 (≠ I170), V195 (≠ I205), H200 (= H210), Q224 (= Q234), E281 (= E290), T438 (= T447)
- binding coenzyme a: R411 (= R420), R413 (= R422), R453 (= R462), Q454 (= Q463), D455 (= D464), R456 (= R465), L1011 (= L1024)
- binding magnesium ion: E267 (= E277), E281 (= E290)
- binding phosphonoacetic acid: K229 (= K239), R285 (= R294), Q287 (= Q296), V288 (= V297), E289 (= E298)
- binding zinc ion: D528 (= D541), K697 (= K710), H726 (= H739), H728 (= H741)
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)
48% identity, 100% coverage: 5:1143/1144 of query aligns to 21:1168/1178 of P11154
- K1135 (= K1110) modified: N6-biotinyllysine
3bg5B Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
48% identity, 100% coverage: 2:1143/1144 of query aligns to 1:1073/1074 of 3bg5B
- active site: K117 (vs. gap), H139 (= H210), R165 (= R236), T204 (= T275), E206 (= E277), E218 (= E290), N220 (= N292), R222 (= R294), E226 (= E298), R274 (= R346), D470 (= D541), D576 (= D647), K640 (= K710), H669 (= H739), H671 (= H741), I692 (= I762), S698 (= S768), M699 (= M769), T738 (≠ R808), T804 (= T874), S806 (= S876), V818 (= V888), N820 (= N890), Q825 (≠ D895)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: N403 (= N475), G408 (≠ N480), F409 (vs. gap), P410 (= P481), F516 (= F587), K518 (= K589)
- binding manganese (ii) ion: D470 (= D541), H669 (= H739), H671 (= H741)
- binding pyruvic acid: Q473 (= Q544), K640 (= K710), T804 (= T874)
2qf7A Crystal structure of a complete multifunctional pyruvate carboxylase from rhizobium etli (see paper)
47% identity, 99% coverage: 3:1140/1144 of query aligns to 3:1073/1076 of 2qf7A
- active site: K124 (= K122), H147 (= H210), R173 (= R236), T212 (= T275), E214 (= E277), E228 (= E290), N230 (= N292), R232 (= R294), E236 (= E298), R284 (= R346), D479 (= D541), D585 (= D647), K648 (= K710), H677 (= H739), H679 (= H741), T812 (= T874)
- binding phosphothiophosphoric acid-adenylate ester: H147 (= H210), Q171 (= Q234), E214 (= E277), L216 (= L279), E228 (= E290), T385 (= T447)
- binding coenzyme a: R400 (= R462), Q401 (= Q463), D402 (= D464), R403 (= R465), A404 (= A466), I956 (= I1018), K960 (= K1022), L962 (= L1024), N985 (= N1047)
- binding magnesium ion: E214 (= E277), E228 (= E290), M464 (≠ V526), R465 (= R527), E467 (≠ S529), D698 (= D760)
- binding zinc ion: D479 (= D541), K648 (= K710), H677 (= H739), H679 (= H741)
2qf7B Crystal structure of a complete multifunctional pyruvate carboxylase from rhizobium etli (see paper)
48% identity, 92% coverage: 3:1057/1144 of query aligns to 3:1014/1017 of 2qf7B
- active site: K123 (= K118), K150 (= K160), H169 (= H210), R195 (= R236), T234 (= T275), E236 (= E277), E250 (= E290), N252 (= N292), R254 (= R294), E258 (= E298), R306 (= R346), D498 (= D541), D604 (= D647), K667 (= K710), H696 (= H739), H698 (= H741), T831 (= T874)
- binding phosphothiophosphoric acid-adenylate ester: M148 (≠ L158), K150 (= K160), M153 (≠ I170), E161 (= E202), V164 (≠ I205), H169 (= H210), Q193 (= Q234), E236 (= E277), L238 (= L279), I249 (≠ L289), E250 (= E290), T407 (= T447)
- binding magnesium ion: E236 (= E277), E250 (= E290), M483 (≠ V526), R484 (= R527), E486 (≠ S529), D717 (= D760)
- binding zinc ion: D498 (= D541), K667 (= K710), H696 (= H739), H698 (= H741)
5vyzC Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
52% identity, 82% coverage: 201:1143/1144 of query aligns to 144:1082/1083 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 (= P718), Y661 (≠ K722), S691 (≠ L752), Q695 (≠ E756)
- binding adenosine-5'-diphosphate: Y147 (= Y204), H153 (= H210), Q177 (= Q234), L222 (= L279), E232 (= E290), T388 (= T447)
- binding magnesium ion: E220 (= E277), E232 (= E290)
- binding manganese (ii) ion: D480 (= D541), K649 (= K710), H678 (= H739), H680 (= H741)
3ho8A Crystal structure of s. Aureus pyruvate carboxylase in complex with coenzyme a (see paper)
48% identity, 92% coverage: 2:1058/1144 of query aligns to 1:993/994 of 3ho8A
- active site: K117 (vs. gap), H144 (= H210), R170 (= R236), T209 (= T275), E211 (= E277), E223 (= E290), N225 (= N292), R227 (= R294), E231 (= E298), R279 (= R346), D475 (= D541), D581 (= D647), K645 (= K710), H674 (= H739), H676 (= H741), I697 (= I762), S703 (= S768), M704 (= M769), T743 (≠ R808), T809 (= T874), S811 (= S876), V823 (= V888), N825 (= N890), Q830 (≠ D895)
- binding coenzyme a: R42 (= R43), Y43 (= Y44), S48 (≠ A49), E351 (= E418), R353 (= R420), R355 (= R422), S395 (≠ R462), L396 (≠ Q463), R398 (= R465), K957 (= K1022), M981 (≠ L1046), R986 (= R1051)
- binding manganese (ii) ion: D475 (= D541), H674 (= H739), H676 (= H741)
Query Sequence
>WP_013011594.1 NCBI__GCF_000025725.1:WP_013011594.1
MRIKKLMSANRGEIAIRTFRACTEMGIRTVALYSEEDKYSLHRYKADEAYLIGKGLDPVA
AYMNIDEIIQLAIHKKIDAIHPGYGFLAENAEFAKACKEAGIIFIGPDSDTINMFGDKKN
AKILAKKCGVPVIEGSVGTVATTEEAASVSESIGYPVLIKAVAGGGGRGIRIAKNKKELL
ENYGSAKSEALKAFGNDEIIIEKYIEEPKHIEVQLLADKHGSIVHLFERDCSIQRRHQKL
IEIAPSISVDDKTLQQMYNAAIEIGKKSKLVNAATVEFLVDKKQDFYFLEVNPRLQVEHT
ITELITGIDIVQSQINIAQGEKLSSPDIDIESQDTIRKNGYAIQCRVTTEDPENNFFPDT
GEIQAYRTAAGFGVRLDAGNGFANAKISPHYDSLLVKVSTHAHSFAQSARKMHRALSEFR
IRGVKTNIQFLEKVISHEKFLNGNFNTTFVDSNKDLCVFKQRQDRATKALKFLANNIINN
PSGSRLSKEIILPSINPPVVPYGVPVPAGTKDILNRRGVQGVIDHVRRSNEAFFTDTTFR
DAHQSLLATRVRTKDMLDIAEYYAHHLNGLFSMEMWGGATYDVAYRFLKESPWDRLIQLR
AKAPNILFQMLLRASNAVGYTNYPDNVVRQFIKLACENGIDIFRIFDCFNWVEQMTPAIE
EVKKNGRIAEAAICYTGDITDPKRTKYSLNYYTGIAKELAEAGTDIIGIKDMAGLLKPYA
AKTLIKAIKEETGLPVHFHTHNTSGNAEAAALMAFEAGADIIDAAVSSMSGLTSQPNMNS
IAAALDGQDKHSTLDKKAMQNVSDYFDRVRRYYFPFESGMKASSAEVYMHEIPGGQYSNL
IVQVEAMGLIDRWEDVRQMYTEVNKELGDIIKVTPSSKVVGDLALFLVRNNLTVDDIYIK
GDTLNFPDSVVSFFKGMLGQPYGGFPKRLQEIVLKGEKPLDCRPGELLEDFDFEAAAKEL
KDMFGRDFSPTELISYALYPAVFKDYVKFNSEYGDPSVFCTRSFFYPLEKEEEIELDIEE
GKTLIIRHMNVSEPDAKGMRKVYFELNGQPRSVTVKDETLTDIIKSNAKGDPANPNEVCA
TMPGSITKVNVKAGDKVAKGDVLLITEAMKMETKIASAADGEVSEVFLHEGDKIESGDLL
IKLV
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