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Comparing RR42_RS25130 FitnessBrowser__Cup4G11:RR42_RS25130 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)
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
60% identity, 99% coverage: 5:1162/1167 of query aligns to 2:1129/1129 of 3tw6B
- active site: K124 (= K121), K162 (= K163), H212 (= H213), R238 (= R239), T277 (= T278), E279 (= E280), E293 (= E294), N295 (= N296), R297 (= R298), E301 (= E302), R349 (= R363), D544 (= D560), D650 (= D666), K713 (= K729), H742 (= H758), H744 (= H760), A877 (≠ T893)
- binding adenosine-5'-diphosphate: K124 (= K121), K162 (= K163), G167 (= G168), G169 (= G170), M172 (= M173), E204 (= E205), L206 (= L207), V207 (= V208), H212 (= H213), Q236 (= Q237), N239 (= N240), L281 (= L282), E293 (= E294), T450 (= T464)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: R349 (= R363), D395 (= D409), K1102 (= K1132)
- binding magnesium ion: E279 (= E280), E293 (= E294), M529 (= M545), R530 (≠ L546), E532 (≠ Q548), D763 (= D779)
- binding zinc ion: D544 (= D560), K713 (= K729), H742 (= H758), H744 (= H760)
3tw6C Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
60% identity, 91% coverage: 5:1070/1167 of query aligns to 2:1038/1044 of 3tw6C
- active site: K124 (= K121), K166 (= K163), H200 (= H213), R226 (= R239), T265 (= T278), E267 (= E280), E281 (= E294), N283 (= N296), R285 (= R298), E289 (= E302), R337 (= R363), D528 (= D560), D634 (= D666), K697 (= K729), H726 (= H758), H728 (= H760), A861 (≠ T893)
- binding adenosine-5'-diphosphate: K166 (= K163), M169 (= M173), V195 (= V208), H200 (= H213), Q224 (= Q237), E281 (= E294), T438 (= T464)
- binding coenzyme a: R411 (= R437), R413 (= R439), R453 (= R479), Q454 (= Q480), D455 (= D481), R456 (= R482), L1011 (= L1043)
- binding magnesium ion: E267 (= E280), E281 (= E294)
- binding phosphonoacetic acid: K229 (= K242), R285 (= R298), Q287 (= Q300), V288 (= V301), E289 (= E302)
- binding zinc ion: D528 (= D560), K697 (= K729), H726 (= H758), H728 (= H760)
2qf7B Crystal structure of a complete multifunctional pyruvate carboxylase from rhizobium etli (see paper)
58% identity, 92% coverage: 5:1078/1167 of query aligns to 2:1016/1017 of 2qf7B
- active site: K123 (= K121), K150 (= K163), H169 (= H213), R195 (= R239), T234 (= T278), E236 (= E280), E250 (= E294), N252 (= N296), R254 (= R298), E258 (= E302), R306 (= R363), D498 (= D560), D604 (= D666), K667 (= K729), H696 (= H758), H698 (= H760), T831 (= T893)
- binding phosphothiophosphoric acid-adenylate ester: M148 (= M161), K150 (= K163), M153 (= M173), E161 (= E205), V164 (= V208), H169 (= H213), Q193 (= Q237), E236 (= E280), L238 (= L282), I249 (= I293), E250 (= E294), T407 (= T464)
- binding magnesium ion: E236 (= E280), E250 (= E294), M483 (= M545), R484 (≠ L546), E486 (≠ Q548), D717 (= D779)
- binding zinc ion: D498 (= D560), K667 (= K729), H696 (= H758), H698 (= H760)
2qf7A Crystal structure of a complete multifunctional pyruvate carboxylase from rhizobium etli (see paper)
56% identity, 99% coverage: 5:1162/1167 of query aligns to 2:1073/1076 of 2qf7A
- active site: K124 (≠ E179), H147 (= H213), R173 (= R239), T212 (= T278), E214 (= E280), E228 (= E294), N230 (= N296), R232 (= R298), E236 (= E302), R284 (= R363), D479 (= D560), D585 (= D666), K648 (= K729), H677 (= H758), H679 (= H760), T812 (= T893)
- binding phosphothiophosphoric acid-adenylate ester: H147 (= H213), Q171 (= Q237), E214 (= E280), L216 (= L282), E228 (= E294), T385 (= T464)
- binding coenzyme a: R400 (= R479), Q401 (= Q480), D402 (= D481), R403 (= R482), A404 (= A483), I956 (≠ L1037), K960 (= K1041), L962 (= L1043), N985 (= N1066)
- binding magnesium ion: E214 (= E280), E228 (= E294), M464 (= M545), R465 (≠ L546), E467 (≠ Q548), D698 (= D779)
- binding zinc ion: D479 (= D560), K648 (= K729), H677 (= H758), H679 (= H760)
3tw6A Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
57% identity, 92% coverage: 5:1083/1167 of query aligns to 2:1006/1007 of 3tw6A
- active site: K124 (= K121), H152 (= H213), R178 (= R239), T217 (= T278), E219 (= E280), E233 (= E294), N235 (= N296), R237 (= R298), E241 (= E302), R289 (= R363), D485 (= D560), D591 (= D666), K654 (= K729), H683 (= H758), H685 (= H760), A818 (≠ T893)
- binding adenosine-5'-diphosphate: L146 (= L207), V147 (= V208), H152 (= H213), Q176 (= Q237), N179 (= N240), L221 (= L282)
- binding coenzyme a: R365 (= R439), R405 (= R479), Q406 (= Q480), D407 (= D481), R408 (= R482), T967 (= T1042), L968 (= L1043)
- binding magnesium ion: E219 (= E280), E233 (= E294), M470 (= M545), R471 (≠ L546), E473 (≠ Q548), D704 (= D779)
- binding zinc ion: D485 (= D560), K654 (= K729), H683 (= H758), H685 (= H760)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
50% identity, 99% coverage: 6:1165/1167 of query aligns to 4:1145/1150 of A0A0H3JRU9
- R21 (= R23) mutation to A: Complete loss of catalytic activity.
- K119 (= K121) binding
- K161 (= K163) binding
- H211 (= H213) binding
- E278 (= E280) binding
- K411 (≠ R428) mutation to A: Complete loss of catalytic activity.
- RDAHQ 541:545 (= RDAHQ 559:563) binding
- D542 (= D560) binding
- A580 (= A598) mutation to T: Complete loss of catalytic activity.
- R614 (= R632) mutation to A: Complete loss of catalytic activity.
- Y621 (= Y639) mutation to A: Complete loss of catalytic activity.
- K712 (= K729) binding
- H741 (= H758) binding
- H743 (= H760) binding
- Q838 (= Q855) mutation to A: About 2.5-fold loss of catalytic activity.
- T876 (= T893) mutation to A: Complete loss of catalytic activity.
- S879 (= S896) mutation to A: About 2-fold loss of catalytic activity.
- K880 (= K897) mutation to T: Complete loss of catalytic activity.
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
49% identity, 99% coverage: 6:1165/1167 of query aligns to 2:1136/1137 of 3bg5A
- active site: K117 (= K121), K159 (= K163), S189 (≠ D200), H202 (= H213), R228 (= R239), T267 (= T278), E269 (= E280), E281 (= E294), N283 (= N296), R285 (= R298), E289 (= E302), R337 (= R363), D533 (= D560), D639 (= D666), K703 (= K729), H732 (= H758), H734 (= H760), I755 (≠ V781), S761 (≠ A787), M762 (= M788), T801 (≠ G827), T867 (= T893), S869 (≠ T895), V881 (= V907), N883 (= N909), Q888 (≠ A914)
- binding adenosine-5'-triphosphate: K117 (= K121), M157 (= M161), K159 (= K163), Y196 (≠ L207), I197 (≠ V208), H202 (= H213), Q226 (= Q237), H229 (≠ N240), E269 (= E280), L271 (= L282), E281 (= E294), N283 (= N296)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y463 (= Y489), G471 (= G497), F472 (≠ H498), P473 (= P499), F579 (= F606)
- binding manganese (ii) ion: D533 (= D560), H732 (= H758), H734 (= H760)
- binding pyruvic acid: L603 (= L630), K703 (= K729)
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
49% identity, 99% coverage: 6:1165/1167 of query aligns to 2:1137/1138 of 7zz3A
- binding acetyl coenzyme *a: N22 (≠ A26), F43 (= F47), K44 (= K48), A45 (= A49), D46 (= D50), S48 (= S52), R363 (= R384), H413 (≠ R434), E414 (= E435), R416 (= R437), R418 (= R439), R459 (≠ Q480), R461 (= R482), K1016 (= K1041), T1017 (= T1042), L1018 (= L1043), R1045 (= R1070)
- binding adenosine-5'-triphosphate: K117 (= K121), M156 (= M161), K158 (= K163), G163 (= G168), G164 (= G169), G165 (= G170), M168 (= M173), E200 (= E205), Y202 (≠ L207), I203 (≠ V208), H208 (= H213), Q232 (= Q237), N235 (= N240), L277 (= L282), E287 (= E294), N289 (= N296), T443 (= T464)
- binding bicarbonate ion: K237 (= K242), R291 (= R298), Q293 (= Q300), E295 (= E302)
- binding biotin: G84 (= G88), V294 (= V301), R342 (= R363), K1104 (= K1132)
- binding magnesium ion: E275 (= E280), E287 (= E294), V520 (≠ M545), T523 (≠ Q548), D754 (= D779)
- binding manganese (ii) ion: D535 (= D560), K704 (= K729), H733 (= H758), H735 (= H760)
- binding pyruvic acid: R534 (= R559), Q538 (= Q563), L605 (= L630), K704 (= K729), T868 (= T893)
5vyzA Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
49% identity, 99% coverage: 6:1165/1167 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 (= Q738), Y722 (≠ A741), S752 (≠ L771), G753 (≠ A772), Q756 (≠ D775)
- binding adenosine-5'-diphosphate: K123 (= K121), M162 (= M161), K164 (= K163), G168 (= G167), G170 (= G169), G171 (= G170), M174 (= M173), Y208 (≠ L207), I209 (≠ V208), H214 (= H213), Q238 (= Q237), N241 (= N240), L283 (= L282), E293 (= E294), T449 (= T464)
- binding magnesium ion: E281 (= E280), E293 (= E294)
- binding manganese (ii) ion: D541 (= D560), K710 (= K729), H739 (= H758), H741 (= H760)
3hb9A Crystal structure of s. Aureus pyruvate carboxylase a610t mutant (see paper)
49% identity, 99% coverage: 6:1165/1167 of query aligns to 2:1132/1133 of 3hb9A
- active site: K117 (= K121), K159 (= K163), H198 (= H213), R224 (= R239), T263 (= T278), E265 (= E280), E277 (= E294), N279 (= N296), R281 (= R298), E285 (= E302), R333 (= R363), D529 (= D560), D635 (= D666), K699 (= K729), H728 (= H758), H730 (= H760), I751 (≠ V781), S757 (≠ A787), M758 (= M788), T797 (≠ G827), T863 (= T893), S865 (≠ T895), V877 (= V907), N879 (= N909), Q884 (≠ A914)
- binding adenosine-5'-diphosphate: K117 (= K121), M157 (= M161), Y192 (≠ L207), I193 (≠ V208), H198 (= H213), Q222 (= Q237), H225 (≠ N240), L267 (= L282), I276 (= I293), E277 (= E294)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y459 (= Y489), N462 (≠ D492), G467 (= G497), F468 (≠ H498), F575 (= F606), K577 (= K608)
- binding manganese (ii) ion: D529 (= D560), H728 (= H758), H730 (= H760)
7zyyA Cryo-em structure of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
50% identity, 92% coverage: 6:1078/1167 of query aligns to 2:1053/1056 of 7zyyA
- binding acetyl coenzyme *a: R19 (= R23), N22 (≠ A26), F43 (= F47), K44 (= K48), A45 (= A49), R363 (= R384), E414 (= E435), R416 (= R437), R418 (= R439), R459 (≠ Q480), D460 (= D481), R461 (= R482), K1016 (= K1041), T1017 (= T1042), L1018 (= L1043), N1041 (= N1066), R1045 (= R1070)
- binding adenosine-5'-diphosphate: K158 (= K163), G163 (= G168), G164 (= G169), M168 (= M173), E200 (= E205), K201 (= K206), Y202 (≠ L207), I203 (≠ V208), H208 (= H213), Q232 (= Q237), N235 (= N240), E275 (= E280), L277 (= L282), E287 (= E294), T443 (= T464)
- binding bicarbonate ion: R291 (= R298), Q293 (= Q300), V294 (= V301), E295 (= E302)
- binding magnesium ion: E275 (= E280), E287 (= E294), V520 (≠ M545), T523 (≠ Q548), D754 (= D779)
- binding manganese (ii) ion: D535 (= D560), K704 (= K729), H733 (= H758), H735 (= H760)
- binding pyruvic acid: Q538 (= Q563), G572 (= G597), L605 (= L630), R607 (= R632), K704 (= K729), T868 (= T893)
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
48% identity, 100% coverage: 1:1165/1167 of query aligns to 32:1177/1178 of P11498
- V145 (= V114) 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 (= R437) to C: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs113994143
- D572 (= D560) binding
- R583 (= R571) to L: in PC deficiency; dbSNP:rs119103242
- A610 (= A598) to T: in PC deficiency; mild; dbSNP:rs28940589
- R631 (= R619) to Q: in PC deficiency; dbSNP:rs113994145
- K741 (= K729) binding via carbamate group; modified: N6-carboxylysine
- M743 (= M731) to I: in PC deficiency; mild; dbSNP:rs28940590
- H771 (= H758) binding
- H773 (= H760) binding
- F1077 (≠ Q1062) mutation F->A,E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer.
- VAK 1131:1133 (≠ VAA 1119:1121) natural variant: Missing (in PC deficiency)
- K1144 (= K1132) modified: N6-biotinyllysine
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
48% identity, 100% coverage: 1:1165/1167 of query aligns to 1:1146/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ M22), T26 (≠ A26), R46 (= R46), Q47 (≠ F47), K48 (= K48), A49 (= A49), D50 (= D50), R367 (= R384), R414 (= R431), E418 (= E435), R420 (= R437), R422 (= R439), A462 (≠ R479), Q463 (= Q480), R465 (= R482), K1025 (= K1041)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K163), G168 (= G168), G169 (= G169), M173 (= M173), F207 (≠ L207), I208 (≠ V208), P211 (≠ A211), H240 (≠ N240)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: D582 (= D601), Q839 (= Q855), T877 (= T893), S880 (= S896), K881 (= K897)
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
48% identity, 100% coverage: 2:1165/1167 of query aligns to 1:1145/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K163), G167 (= G168), G168 (= G169), F206 (≠ L207), Q236 (= Q237), H239 (≠ N240), E292 (= E294)
- binding coenzyme a: F21 (≠ M22), R22 (= R23), T25 (≠ A26), R45 (= R46), Q46 (≠ F47), K47 (= K48), A48 (= A49), D49 (= D50), E50 (= E51), R366 (= R384), R413 (= R431), A416 (≠ R434), R419 (= R437), Q462 (= Q480), R464 (= R482), A465 (= A483), Q466 (≠ T484), K1024 (= K1041), R1053 (= R1070)
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
47% identity, 100% coverage: 1:1165/1167 of query aligns to 32:1177/1178 of Q05920
- K35 (≠ T4) modified: N6-acetyllysine
- K39 (≠ S8) modified: N6-acetyllysine
- K79 (= K48) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (= K117) modified: N6-acetyllysine
- K152 (= K121) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ N210) modified: N6-acetyllysine
- K434 (≠ P420) modified: N6-acetyllysine
- K589 (≠ P577) modified: N6-acetyllysine
- K717 (= K705) modified: N6-acetyllysine
- K748 (≠ R736) modified: N6-acetyllysine; mutation to Q: Reduced pyruvate carboxylase activity.
- K892 (≠ R877) modified: N6-acetyllysine
- K969 (≠ R954) modified: N6-acetyllysine
8gk8A R21a staphylococcus aureus pyruvate carboxylase
49% identity, 92% coverage: 6:1075/1167 of query aligns to 2:1035/1041 of 8gk8A
- binding acetyl coenzyme *a: E400 (= E435), R402 (= R437), R404 (= R439), L445 (≠ Q480), R447 (= R482), N1026 (= N1066), R1030 (= R1070)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: N457 (≠ D492), G462 (= G497), F463 (≠ H498), P464 (= P499), F570 (= F606), K572 (= K608)
- binding coenzyme a: R42 (= R46), Y43 (≠ F47), A45 (= A49), D46 (= D50), E47 (= E51), S48 (= S52)
- binding manganese (ii) ion: D524 (= D560), K694 (= K729), H723 (= H758), H725 (= H760)
5vyzC Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
45% identity, 99% coverage: 6:1165/1167 of query aligns to 9:1082/1083 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 (= P737), Y661 (≠ A741), S691 (≠ L771), Q695 (≠ D775)
- binding adenosine-5'-diphosphate: Y147 (≠ M175), H153 (≠ D181), Q177 (≠ E205), L222 (= L282), E232 (= E294), T388 (= T464)
- binding magnesium ion: E220 (= E280), E232 (= E294)
- binding manganese (ii) ion: D480 (= D560), K649 (= K729), H678 (= H758), H680 (= H760)
4qshC Crystal structure of l. Monocytogenes pyruvate carboxylase in complex with cyclic-di-amp (see paper)
49% identity, 83% coverage: 202:1166/1167 of query aligns to 140:1080/1081 of 4qshC
- active site: K650 (= K729)
- 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 (≠ A741), Y689 (≠ A768), A693 (= A772), S696 (≠ D775)
- binding manganese (ii) ion: D481 (= D560), H679 (= H758), H681 (= H760)
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)
46% identity, 99% coverage: 7:1165/1167 of query aligns to 20:1168/1178 of P11154
- K1135 (= K1132) modified: N6-biotinyllysine
3bg5B Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
48% identity, 82% coverage: 208:1165/1167 of query aligns to 134:1073/1074 of 3bg5B
- active site: H139 (= H213), R165 (= R239), T204 (= T278), E206 (= E280), E218 (= E294), N220 (= N296), R222 (= R298), E226 (= E302), R274 (= R363), D470 (= D560), D576 (= D666), K640 (= K729), H669 (= H758), H671 (= H760), I692 (≠ V781), S698 (≠ A787), M699 (= M788), T738 (≠ G827), T804 (= T893), S806 (≠ T895), V818 (= V907), N820 (= N909), Q825 (≠ A914)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: N403 (≠ D492), G408 (= G497), F409 (≠ H498), P410 (= P499), F516 (= F606), K518 (= K608)
- binding manganese (ii) ion: D470 (= D560), H669 (= H758), H671 (= H760)
- binding pyruvic acid: Q473 (= Q563), K640 (= K729), T804 (= T893)
Sites not aligning to the query:
Query Sequence
>RR42_RS25130 FitnessBrowser__Cup4G11:RR42_RS25130
MDYTPIKSLLIANRSEIAIRVMRAAAEMNIRTVAIYSKEDRLALHRFKADESYLVGEGKK
PLAAYLDIDDILRIARQAKVDAIHPGYGFLSENPDFAQAVMDAGIRWIGPSPEVMRKLGN
KVAARNAAIEAGVPVMPATDPLPRDLDECKRLAAGIGYPLMLKASWGGGGRGMRMLENEQ
DLETALPAARREALSAFGNDEVYVEKLVRNARHVEVQALGDAHGNLVHLYERDCTVQRRN
QKVVERAPAPYLDDAGRAALCDAAMRLMRAVGYTHAGTIEFLMDADSGQFYFIEVNPRIQ
VEHTVTELVTGVDIVKAQIRITEGGHIGMTENTRDADGKIVVRAAGVPEQAGISLNGHAL
QCRITTEDPENGFLPDYGRLSAYRSAAGFGVRLDAGTAYGGAVITPYYDSLLVKVTTWAP
TAPESIRRMDRALREFRIRGVASNLQFLENVINHPAFRSGDVTTRFIDKTPELLAFTKRQ
DRATKLLRYLGDVCVNGHPEMSGRSLPALPLPTPVLPAVDTTGPLPTGTRDLLRELGAEK
FSRWMLEQKRVLLTDTTMRDAHQSLFATRMRTADMLPIAPFYARELPQLFSMECWGGATF
DVALRFLKEDPWQRLEQLRERVPNILFQMLLRGSNAVGYTNYADNVVKFFVRQAASAGVD
VFRVFDSLNWVRNMRVAIDAVCDSGALCEGAICYTGDIFDGSRPKYDLKYYVGIARELQA
AGVHVLGIKDMAEICRPQAAAALVKALKEETGLPVHFHTHDTSGISAASALAAIDAGCDA
VDGALDAMSGLTSQPNLSSIAAALAGSERASGLDLERLHEASMYWEGVRRYYAPFESEIR
AGTADVYRHEMPGGQYTNLREQARSLGIEHRWTEVSRAYADVNKMFGDIVKVTPTSKVVG
DMALMMVANDMSAADVCDPGKEIAFPESVVSLFKGELGFPPDGFPAALSRKVLRGEPPAP
YRPGDQIPAVDLAAARAAGEAACEQALDDRQLASYLMYPKQAIAYHAHVRTYSDTSVVPT
PAFLYGLQPQEETAVDLEPGKTLLVSLQGMHPDAEEGNIKVQFELNGQSRTALVEQRSAA
HAAVVRHSRPVAEPGNPLHVAAPMPGAIVTVAVQPGQRVAAGTTLLALEAMKMETHIAAD
RDCEIAAVHVQQGDRVAAKDLLIELRL
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