SitesBLAST
Comparing 5210659 FitnessBrowser__PV4:5210659 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)
Q9NUT2 Mitochondrial potassium channel ATP-binding subunit; ATP-binding cassette sub-family B member 8, mitochondrial; ABCB8; Mitochondrial ATP-binding cassette 1; M-ABC1; Mitochondrial sulfonylurea-receptor; MITOSUR from Homo sapiens (Human) (see 4 papers)
38% identity, 87% coverage: 76:616/620 of query aligns to 187:712/735 of Q9NUT2
- 507:514 (vs. 412:419, 63% identical) binding
- GK 512:513 (= GK 417:418) mutation to AR: Renders the protein unstable.
- K513 (= K418) mutation to A: Abolish binding to ATP.
- A690 (≠ S594) to G: in a breast cancer sample; somatic mutation
Sites not aligning to the query:
- 152 V → I: in dbSNP:rs4148844
- 165 I → T: in a breast cancer sample; somatic mutation
5ochE The crystal structure of human abcb8 in an outward-facing state
38% identity, 86% coverage: 82:616/620 of query aligns to 52:572/576 of 5ochE
- binding adenosine-5'-diphosphate: Y341 (= Y374), C343 (≠ A388), G370 (= G415), G372 (= G417), K373 (= K418), T374 (≠ S419), T375 (= T420)
- binding cholesterol hemisuccinate: P163 (= P196), F238 (≠ V275), S242 (= S279), N243 (≠ I280), F246 (≠ I283), M285 (≠ V318), L288 (≠ I321), V295 (≠ I328)
Q9JI39 ATP-binding cassette sub-family B member 10, mitochondrial; ABC-mitochondrial erythroid protein; ABC-me protein; ATP-binding cassette transporter 10; ABC transporter 10 protein from Mus musculus (Mouse) (see 2 papers)
36% identity, 95% coverage: 24:614/620 of query aligns to 112:698/715 of Q9JI39
- G497 (= G417) mutation to A: Decreases ATP binding about 50%.
- K498 (= K418) mutation to R: Decreases ATP binding about 50%.
- C547 (≠ T467) modified: S-glutathionyl cysteine; mutation to A: Does not affect ABCB10 glutathionylation.
- G602 (= G519) mutation to D: Affects ATP hydrolysis but not binding.; mutation to V: Affects ATP hydrolysis but not binding.
- E624 (= E541) mutation to Q: Affects ATP hydrolysis but not binding.
- C675 (≠ I592) mutation to A: Prevents ABCB10 glutathionylation.
Sites not aligning to the query:
- 1:82 modified: transit peptide, Mitochondrion
Q9NRK6 ATP-binding cassette sub-family B member 10, mitochondrial; ABC-mitochondrial erythroid protein; ABC-me protein; ATP-binding cassette transporter 10; ABC transporter 10 protein; Mitochondrial ATP-binding cassette 2; M-ABC2 from Homo sapiens (Human) (see 5 papers)
36% identity, 93% coverage: 38:614/620 of query aligns to 162:733/738 of Q9NRK6
- C215 (≠ V91) mutation to S: Does not affect ATPase activity; when associated with L-224 and G-582. Activated by Zn (II) mesoporphyrin; when associated with L-224 and G-582.
- C224 (vs. gap) mutation to L: Does not affect ATPase activity; when associated withS-215 and G-582. Activated by Zn (II) mesoporphyrin; when associated with S-215 and G-582.
- R471 (≠ T344) to T: in a breast cancer sample; somatic mutation
- K533 (= K418) mutation to E: Increases hemoglobin biosynthetic process.
- D545 (≠ V430) to N: in dbSNP:rs35698797
- C582 (≠ T467) mutation to G: Does not affect ATPase activity; when associated with S-215 and L-224. Activated by Zn (II) mesoporphyrin; when associated with S-215 and L-224.
- S635 (= S517) mutation to R: Does not rescue hemoglobin and heme biosynthetic process.
- Q638 (= Q520) mutation to H: Does not rescue hemoglobin and heme biosynthetic process.
- D658 (= D540) mutation to A: Does not rescue hemoglobin and heme biosynthetic process.
- E659 (= E541) mutation to A: Does not rescue hemoglobin and heme biosynthetic process.
Sites not aligning to the query:
- 150 A → S: in dbSNP:rs4148756
4ayxA Structure of the human mitochondrial abc transporter, abcb10 (rod form b) (see paper)
36% identity, 91% coverage: 38:601/620 of query aligns to 9:566/571 of 4ayxA
2onjA Structure of the multidrug abc transporter sav1866 from s. Aureus in complex with amp-pnp (see paper)
32% identity, 93% coverage: 39:616/620 of query aligns to 8:578/578 of 2onjA
- binding phosphoaminophosphonic acid-adenylate ester: Y349 (= Y374), I356 (≠ V394), S376 (= S414), G377 (= G415), G378 (≠ A416), G379 (= G417), K380 (= K418), S381 (= S419), T382 (= T420), Q422 (= Q460), K477 (≠ R515), S479 (= S517), G480 (= G518), E503 (= E541), H534 (= H572)
2hydA Multidrug abc transporter sav1866 (see paper)
32% identity, 93% coverage: 39:616/620 of query aligns to 8:578/578 of 2hydA
7y48B Cryo-em structure of biliverdin-bound mitochondrial abc transporter abcb10 from biortus
35% identity, 91% coverage: 38:601/620 of query aligns to 8:562/567 of 7y48B
4aywA Structure of the human mitochondrial abc transporter, abcb10 (plate form) (see paper)
35% identity, 91% coverage: 38:599/620 of query aligns to 9:560/560 of 4aywA
7ehlA Cryo-em structure of human abcb8 transporter in nucleotide binding state (see paper)
37% identity, 85% coverage: 82:610/620 of query aligns to 56:558/563 of 7ehlA
- binding phosphoaminophosphonic acid-adenylate ester: Y334 (= Y374), G365 (= G417), K366 (= K418), T367 (≠ S419), T368 (= T420)
- binding cholesterol: R139 (= R168), L157 (= L187), L168 (≠ V198), G172 (≠ I202), G260 (= G290), L273 (= L304), F276 (= F307), Q284 (≠ A315), R285 (≠ G316)
5ochC The crystal structure of human abcb8 in an outward-facing state
36% identity, 87% coverage: 75:616/620 of query aligns to 39:531/537 of 5ochC
Q0WML0 ABC transporter B family member 27; ABC transporter ABCB.27; AtABCB27; Aluminum tolerance-related ATP-binding cassette transporter; Antigen peptide transporter-like 2; Transporter associated with antigen processing-like protein 2; AtTAP2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
37% identity, 83% coverage: 105:620/620 of query aligns to 137:640/644 of Q0WML0
- E261 (= E229) mutation to K: In als1-1; loss of aluminum tolerance.
6quzD Structure of atpgs-bound outward-facing tm287/288 in complex with sybody sb_tm35 (see paper)
31% identity, 93% coverage: 38:614/620 of query aligns to 13:573/574 of 6quzD
- binding phosphothiophosphoric acid-adenylate ester: Y347 (= Y374), V353 (= V394), G374 (= G415), S375 (≠ A416), G376 (= G417), K377 (= K418), T378 (≠ S419), T379 (= T420), Q419 (= Q460), D474 (≠ R515), L475 (= L516), S476 (= S517), G478 (= G519), Q479 (= Q520), H531 (= H572)
- binding magnesium ion: T378 (≠ S419), Q419 (= Q460)
6qv0B Structure of atp-bound outward-facing tm287/288 in complex with sybody sb_tm35 (see paper)
31% identity, 93% coverage: 38:614/620 of query aligns to 9:569/570 of 6qv0B
- binding adenosine-5'-triphosphate: Y343 (= Y374), V349 (= V394), T369 (≠ S414), S371 (≠ A416), G372 (= G417), K373 (= K418), T374 (≠ S419), T375 (= T420), Q415 (= Q460), D470 (≠ R515), S472 (= S517), G474 (= G519), Q475 (= Q520), H527 (= H572)
- binding magnesium ion: T374 (≠ S419), Q415 (= Q460)
7metA A. Baumannii msba in complex with tbt1 decoupler (see paper)
33% identity, 92% coverage: 39:610/620 of query aligns to 8:561/564 of 7metA
Q9NP78 ABC-type oligopeptide transporter ABCB9; ATP-binding cassette sub-family B member 9; ATP-binding cassette transporter 9; ABC transporter 9 protein; hABCB9; TAP-like protein; TAPL; EC 7.4.2.6 from Homo sapiens (Human) (see 4 papers)
31% identity, 98% coverage: 8:616/620 of query aligns to 151:743/766 of Q9NP78
- K545 (= K418) mutation to A: Loss of peptide transport activity; whena ssociated with A-699.
- H699 (= H572) mutation to A: Loss of peptide transport activity; whena ssociated with A-545.
Sites not aligning to the query:
- 17 Intramolecular salt bridge with Arg-57. Essential for the release from the ER; D→N: Loss of lysosomal localization. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect dimerization. Does not affect peptide transport activity. Decreases interaction with YIF1B.; D→R: Loss of lysosomal localization. Does not affect lysosomal localization; when associated with D-57. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with D-57. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with D-100.
- 45 Important for the second trafficking step from the Golgi to the endosomal and lysosomal compartments; D→K: Loss of lysosomal localization; when assosiated with K-49. Loss of lysosomal localization; when assosiated with K-49 and D-100. Does not affect peptide transport activity; when assosiated with K-49 and D-100.; D→N: Decreases lysosomal localization; when associated with N-49.
- 49 Important for the second trafficking step from the Golgi to the endosomal and lysosomal compartments; D→K: Loss of lysosomal localization; when assosiated with K-45. Loss of lysosomal localization; when assosiated with K-45 and D-100. Does not affect peptide transport activity; when assosiated with K-45 and D-100.; D→N: Decreases lysosomal localization; when associated with N-45.
- 57 Intramolecular salt bridge with Asp-17. Essential for the release from the ER; R→A: Decreases lysosomal localization. Loss of lysosomal localization; when associated with A-100.; R→D: Loss of lysosomal localization. Does not affect lysosomal localization; when associated with R-17. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with R-17.
- 100 K→A: Decreases lysosomal localization. Loss of lysosomal localization; when associated with A-57.; K→D: Decreases lysosomal localization. Loss of lysosomal localization; when assosiated with R-17. Loss of lysosomal localization; when assosiated with K-45 and K-49. Does not affect peptide transport activity; when assosiated with K-45 and K-49. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with R-17.
- 121 V → M: in dbSNP:rs3803002
- 136:137 LL→AA: No effect on lysosomal localization.
6q81A Structure of p-glycoprotein(abcb1) in the post-hydrolytic state (see paper)
36% identity, 81% coverage: 120:619/620 of query aligns to 111:598/1182 of 6q81A
Sites not aligning to the query:
3g61A Structure of p-glycoprotein reveals a molecular basis for poly- specific drug binding (see paper)
36% identity, 81% coverage: 120:619/620 of query aligns to 111:598/1182 of 3g61A
- binding (4S,11S,18S)-4,11,18-tri(propan-2-yl)-6,13,20-triselena-3,10,17,22,23,24-hexaazatetracyclo[17.2.1.1~5,8~.1~12,15~]tetracosa-1(21),5(24),7,12(23),14,19(22)-hexaene-2,9,16-trione: L268 (= L278), Y271 (≠ L281), F300 (= F309), F307 (≠ G316)
Sites not aligning to the query:
- binding (4S,11S,18S)-4,11,18-tri(propan-2-yl)-6,13,20-triselena-3,10,17,22,23,24-hexaazatetracyclo[17.2.1.1~5,8~.1~12,15~]tetracosa-1(21),5(24),7,12(23),14,19(22)-hexaene-2,9,16-trione: 39, 635, 639, 860, 885, 889, 889
3g60A Structure of p-glycoprotein reveals a molecular basis for poly- specific drug binding (see paper)
36% identity, 81% coverage: 120:619/620 of query aligns to 111:598/1182 of 3g60A
- binding (4R,11R,18R)-4,11,18-tri(propan-2-yl)-6,13,20-triselena-3,10,17,22,23,24-hexaazatetracyclo[17.2.1.1~5,8~.1~12,15~]tetracosa-1(21),5(24),7,12(23),14,19(22)-hexaene-2,9,16-trione: Y271 (≠ L281), F300 (= F309), I304 (≠ M313), F307 (≠ G316)
Sites not aligning to the query:
- binding (4R,11R,18R)-4,11,18-tri(propan-2-yl)-6,13,20-triselena-3,10,17,22,23,24-hexaazatetracyclo[17.2.1.1~5,8~.1~12,15~]tetracosa-1(21),5(24),7,12(23),14,19(22)-hexaene-2,9,16-trione: 632, 635, 639, 860, 886, 889, 892
7v5cA Cryo-em structure of the mouse abcb9 (adp.Bef3-bound) (see paper)
31% identity, 95% coverage: 31:616/620 of query aligns to 1:572/572 of 7v5cA
- binding adenosine-5'-diphosphate: Y342 (= Y374), T344 (≠ A388), S372 (≠ A416), K374 (= K418), S375 (= S419), S376 (≠ T420), S473 (= S517), Q476 (= Q520)
- binding beryllium trifluoride ion: S370 (= S414), K374 (= K418), Q416 (= Q460), H528 (= H572)
- binding magnesium ion: S375 (= S419), Q416 (= Q460)
Query Sequence
>5210659 FitnessBrowser__PV4:5210659
MSQPLSSASHDAASGPKRSAPQPKRPGAKQAVLPWIGGFLRPYRGKVIAAIVFLFIGSLA
WLSLGQGVRLMVDEGFLRENGERLNEIILLVIGITALSSSAIFCRFYLMTWLGERVSADI
RLKVYDHLLKLSPGFYARLRTGEVISRFTADATLLQSVVGSSLSMALRASVTVVGGLVMM
AITSLKLTALVLLAVPLVLGPIFFFGRKVRELSRKSQDRVGDLGAYVDESLHEIHTVQAY
CHEDRDRQLFSERVEAVMEAARGRIKYRAILISLVMFLSILAIALITWVGAKDVMSEAIT
PGELSAFMFYAVMVAGAVATISEVIGEIQRAAGATERLIELVETPIDIPLAPKPVSLPAK
VRGELSLEQVRFSYPVQASADSAEEMEAQAGVEVIRGLSLHIAPGERVALVGASGAGKST
LFELLQRFYVLDSGVIALDGIDIASLRPQDLRQQYALVPQESVIFATSVLENVRYGRPDA
SLEEVQAACVAARADEFIADFSEGYQTYLGERGVRLSGGQKQRIAIARAILADRPVLLLD
EATSALDAVSEQKVKQALDVLMQGRTTLIIAHRLATVLNADRILVMDKGELIASGTHGEL
MQSNSLYREFASLQLLSEEA
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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