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: D104 (≠ A137), Y341 (= Y374), C343 (≠ A388), S369 (= S414), G370 (= G415), G371 (≠ A416), G372 (= G417), K373 (= K418), T374 (≠ S419), T375 (= T420)
- binding magnesium ion: T374 (≠ S419), D496 (= D540), E497 (= E541)
- binding cholesterol hemisuccinate: P163 (= P196), F238 (≠ V275), S242 (= S279), N243 (≠ I280), F246 (≠ I283), Q282 (≠ A315), M285 (≠ V318), L288 (≠ I321), S289 (= S322), 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
- binding phosphomethylphosphonic acid adenylate ester: D111 (≠ A137), Y348 (= Y374), A350 (= A388), R351 (≠ Q389), I356 (≠ V394), S376 (= S414), G377 (= G415), S378 (≠ A416), G379 (= G417), K380 (= K418), S381 (= S419), T382 (= T420), Q422 (= Q460)
- binding glycine: R17 (≠ K46), Y81 (= Y107), R89 (= R115)
- binding magnesium ion: S381 (= S419), Q422 (= Q460), D505 (= D540)
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), V476 (= V514), K477 (≠ R515), S479 (= S517), G480 (= G518), G481 (= G519), E503 (= E541), A507 (= A545), 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
- binding adenosine-5'-diphosphate: Y349 (= Y374), I356 (≠ V394), S376 (= S414), G377 (= G415), G378 (≠ A416), G379 (= G417), K380 (= K418), S381 (= S419), T382 (= T420), Y391 (= Y429), L463 (≠ F501), V476 (= V514), K477 (≠ R515), S479 (= S517), Q482 (= Q520)
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