SitesBLAST
Comparing Ga0059261_3276 FitnessBrowser__Korea:Ga0059261_3276 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
39% identity, 86% coverage: 79:590/595 of query aligns to 183:698/715 of Q9JI39
- G497 (= G393) mutation to A: Decreases ATP binding about 50%.
- K498 (= K394) mutation to R: Decreases ATP binding about 50%.
- C547 (≠ A443) modified: S-glutathionyl cysteine; mutation to A: Does not affect ABCB10 glutathionylation.
- G602 (= G495) mutation to D: Affects ATP hydrolysis but not binding.; mutation to V: Affects ATP hydrolysis but not binding.
- E624 (= E517) mutation to Q: Affects ATP hydrolysis but not binding.
- C675 (≠ V568) 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)
39% identity, 86% coverage: 78:590/595 of query aligns to 217:733/738 of Q9NRK6
- C224 (≠ V85) 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 (≠ Q332) to T: in a breast cancer sample; somatic mutation
- K533 (= K394) mutation to E: Increases hemoglobin biosynthetic process.
- D545 (= D406) to N: in dbSNP:rs35698797
- C582 (≠ A443) 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 (= S493) mutation to R: Does not rescue hemoglobin and heme biosynthetic process.
- Q638 (= Q496) mutation to H: Does not rescue hemoglobin and heme biosynthetic process.
- D658 (= D516) mutation to A: Does not rescue hemoglobin and heme biosynthetic process.
- E659 (= E517) mutation to A: Does not rescue hemoglobin and heme biosynthetic process.
Sites not aligning to the query:
- 150 A → S: in dbSNP:rs4148756
- 215 C→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.
4ayxA Structure of the human mitochondrial abc transporter, abcb10 (rod form b) (see paper)
39% identity, 84% coverage: 78:579/595 of query aligns to 64:568/571 of 4ayxA
Sites not aligning to the query:
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)
39% identity, 87% coverage: 79:595/595 of query aligns to 198:715/735 of Q9NUT2
- 507:514 (vs. 388:395, 63% identical) binding
- GK 512:513 (= GK 393:394) mutation to AR: Renders the protein unstable.
- K513 (= K394) mutation to A: Abolish binding to ATP.
- A690 (≠ T570) 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
39% identity, 87% coverage: 79:594/595 of query aligns to 58:574/576 of 5ochE
- binding adenosine-5'-diphosphate: Y341 (= Y362), C343 (≠ T364), G370 (= G391), G372 (= G393), K373 (= K394), T374 (≠ S395), T375 (= T396)
- binding cholesterol hemisuccinate: P163 (= P184), F238 (≠ M259), S242 (≠ V263), N243 (≠ I264), F246 (≠ L267), M285 (≠ F306), L288 (= L309), V295 (≠ L316)
7y48B Cryo-em structure of biliverdin-bound mitochondrial abc transporter abcb10 from biortus
38% identity, 84% coverage: 78:579/595 of query aligns to 63:564/567 of 7y48B
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)
36% identity, 87% coverage: 76:590/595 of query aligns to 225:741/766 of Q9NP78
- K545 (= K394) mutation to A: Loss of peptide transport activity; whena ssociated with A-699.
- H699 (= H548) 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.
7vfiA Cryo-em structure of the mouse tapl (9mer-peptide bound) (see paper)
37% identity, 81% coverage: 108:590/595 of query aligns to 89:569/570 of 7vfiA
Sites not aligning to the query:
7v5cA Cryo-em structure of the mouse abcb9 (adp.Bef3-bound) (see paper)
37% identity, 81% coverage: 108:590/595 of query aligns to 90:570/572 of 7v5cA
- binding adenosine-5'-diphosphate: Y342 (= Y362), T344 (= T364), S372 (≠ A392), K374 (= K394), S375 (= S395), S376 (≠ T396), S473 (= S493), Q476 (= Q496)
- binding beryllium trifluoride ion: S370 (= S390), K374 (= K394), Q416 (= Q436), H528 (= H548)
- binding magnesium ion: S375 (= S395), Q416 (= Q436)
4aywA Structure of the human mitochondrial abc transporter, abcb10 (plate form) (see paper)
38% identity, 84% coverage: 78:575/595 of query aligns to 64:560/560 of 4aywA
Sites not aligning to the query:
7ehlA Cryo-em structure of human abcb8 transporter in nucleotide binding state (see paper)
38% identity, 85% coverage: 79:586/595 of query aligns to 62:558/563 of 7ehlA
- binding phosphoaminophosphonic acid-adenylate ester: Y334 (= Y362), G365 (= G393), K366 (= K394), T367 (≠ S395), T368 (= T396)
- binding cholesterol: R139 (= R156), L157 (≠ I175), L168 (≠ I186), G172 (≠ I190), G260 (≠ V279), L273 (≠ I292), F276 (= F295), Q284 (≠ T303), R285 (≠ G304)
5ochC The crystal structure of human abcb8 in an outward-facing state
38% identity, 87% coverage: 79:594/595 of query aligns to 52:533/537 of 5ochC
7metA A. Baumannii msba in complex with tbt1 decoupler (see paper)
35% identity, 93% coverage: 35:586/595 of query aligns to 14:561/564 of 7metA
6a6mA Crystal structure of an outward-open nucleotide-bound state of the eukaryotic abc multidrug transporter cmabcb1 (see paper)
38% identity, 82% coverage: 102:591/595 of query aligns to 90:588/589 of 6a6mA
- binding phosphoaminophosphonic acid-adenylate ester: Y352 (= Y362), R355 (= R365), S380 (= S390), G383 (= G393), K384 (= K394), S385 (= S395), T386 (= T396), Q429 (= Q436)
- binding decyl-beta-d-maltopyranoside: G378 (= G388), G379 (≠ P389), G381 (= G391), L545 (= L550), Q558 (≠ D563), D559 (≠ E564), F579 (≠ L582), L583 (= L586)
- binding magnesium ion: S385 (= S395), Q429 (= Q436)
3wmgA Crystal structure of an inward-facing eukaryotic abc multidrug transporter g277v/a278v/a279v mutant in complex with an cyclic peptide inhibitor, acap (see paper)
38% identity, 82% coverage: 102:591/595 of query aligns to 89:587/589 of 3wmgA
Sites not aligning to the query:
7fc9A Crystal structure of cmabcb1 in lipidic mesophase revealed by lcp-sfx (see paper)
39% identity, 82% coverage: 102:586/595 of query aligns to 90:583/584 of 7fc9A
- binding phosphoaminophosphonic acid-adenylate ester: Y352 (= Y362), R355 (= R365), S380 (= S390), G383 (= G393), K384 (= K394), S385 (= S395), T386 (= T396), Q429 (= Q436), H543 (= H548)
- binding magnesium ion: D127 (= D139), T188 (≠ V197), S192 (≠ Q205), E312 (≠ R325), S385 (= S395), Q429 (= Q436)
- binding zinc ion: E119 (= E131), D127 (= D139), S192 (≠ Q205), E193 (≠ D206), N347 (= N357), H349 (≠ T359), H349 (≠ T359), E359 (≠ S369), D451 (≠ E458), E452 (= E459), E510 (= E517), H543 (= H548)
Sites not aligning to the query:
6qexA Nanodisc reconstituted human abcb1 in complex with uic2 fab and taxol (see paper)
35% identity, 90% coverage: 57:590/595 of query aligns to 66:598/1182 of 6qexA
Sites not aligning to the query:
- binding cholesterol: 15, 18, 36, 43, 745, 749, 751, 755, 757, 761, 762, 765, 769, 772, 775, 854, 857, 861, 864, 865
- binding taxol: 38, 631, 852, 859, 889, 892, 896
7a6fA Nanodisc reconstituted human abcb1 in complex with mrk16 fab and zosuquidar (see paper)
35% identity, 88% coverage: 66:590/595 of query aligns to 59:580/1164 of 7a6fA
Sites not aligning to the query:
- binding cholesterol: 607, 615, 618, 646, 727, 731, 744, 747, 748
- binding Zosuquidar: 34, 34, 613, 764, 767, 838, 841, 874, 878, 879
7a6eA Nanodisc reconstituted human abcb1 in complex with mrk16 fab and tariquidar (see paper)
35% identity, 88% coverage: 66:590/595 of query aligns to 59:580/1164 of 7a6eA
- binding cholesterol: Y68 (= Y75), I72 (≠ L79), T153 (≠ G163), T160 (≠ V170), L167 (≠ A177), V168 (≠ Y178), A171 (≠ I181), I172 (≠ G182), A259 (≠ T269), W266 (= W276), Y267 (≠ D277)
- binding tariquidar: W183 (≠ L193), F254 (≠ I264), I257 (≠ L267), Y258 (≠ F268), Y261 (≠ I271), F287 (≠ I297), Q298 (≠ A308)
Sites not aligning to the query:
- binding cholesterol: 43, 645, 727, 731, 732, 736, 843, 846
- binding tariquidar: 34, 41, 613, 616, 763, 837, 841, 866, 867, 871, 874, 878
7a6cA Nanodisc reconstituted human abcb1 in complex with mrk16 fab and elacridar (see paper)
35% identity, 88% coverage: 66:590/595 of query aligns to 59:580/1164 of 7a6cA
Sites not aligning to the query:
- binding cholesterol: 644, 727, 728, 757, 846, 847, 880
- binding elacridar: 38, 616, 620, 658, 841, 874, 882
Query Sequence
>Ga0059261_3276 FitnessBrowser__Korea:Ga0059261_3276
MAEPASKPETSPTPRKLSSLRIVWRHTSRYPLQLGLAIVALILAAGATLWIPRTFKEVVD
KGFGADADPSRIGAYFQGLLLVVVVLAFATAMRFYFVSWLGERTVADLRAAVHRNLLRLP
PKWFEENRPSEIASRLTADTAVVEQIVGTTVSVALRNLLIAIGGTVYLFVLAPKIAAYLI
IGIPVIVLPIMWLGGRVRRFSRTSQDRVADIGAIASETLGAMRIVQAFGQERREGERFQT
AVDAGFATARKRFATRALMTALVIFALFTAITLIMWDAVYGVAEGRISGGSITAFVITAG
LVTGAFGALTEVYGDLLRASGAASRLAELLAQEPDIAAPANPVPLPVPPLGAIDFKNVTF
RYPTRPEVSALHQFTLSVAPGETVAVVGPSGAGKSTLFQLVQRFYDPEGGEIRVDGIPVR
SADPGEVRARMAMVPQETVIFAATARDNLRYGRWDATEEQIWQAAEAANAAEFLRELPQG
LETFLGEDGARLSGGQRQRLAIARALLRDAPILLLDEATSALDAESERLVQDALEHLMQG
RTTLVIAHRLATVRAAKRIIVMDEGRIVETGTHAELVAKGGLYAKLASLQFNDAP
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