SitesBLAST
Comparing Echvi_1191 FitnessBrowser__Cola:Echvi_1191 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)
37% identity, 99% coverage: 6:592/595 of query aligns to 104:698/715 of Q9JI39
- G497 (= G394) mutation to A: Decreases ATP binding about 50%.
- K498 (= K395) mutation to R: Decreases ATP binding about 50%.
- C547 (≠ G444) modified: S-glutathionyl cysteine; mutation to A: Does not affect ABCB10 glutathionylation.
- G602 (= G496) mutation to D: Affects ATP hydrolysis but not binding.; mutation to V: Affects ATP hydrolysis but not binding.
- E624 (= E518) mutation to Q: Affects ATP hydrolysis but not binding.
- C675 (≠ V569) 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, 96% coverage: 23:592/595 of query aligns to 159:733/738 of Q9NRK6
- C215 (≠ A80) 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 (≠ V89) 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 (≠ E336) to T: in a breast cancer sample; somatic mutation
- K533 (= K395) mutation to E: Increases hemoglobin biosynthetic process.
- D545 (≠ T407) to N: in dbSNP:rs35698797
- C582 (≠ G444) 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 (= S494) mutation to R: Does not rescue hemoglobin and heme biosynthetic process.
- Q638 (= Q497) mutation to H: Does not rescue hemoglobin and heme biosynthetic process.
- D658 (= D517) mutation to A: Does not rescue hemoglobin and heme biosynthetic process.
- E659 (= E518) 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)
39% identity, 94% coverage: 23:583/595 of query aligns to 6:571/571 of 4ayxA
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)
40% identity, 95% coverage: 27:593/595 of query aligns to 60:635/644 of Q0WML0
- E261 (= E221) mutation to K: In als1-1; loss of aluminum tolerance.
7y48B Cryo-em structure of biliverdin-bound mitochondrial abc transporter abcb10 from biortus
39% identity, 94% coverage: 23:583/595 of query aligns to 5:567/567 of 7y48B
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, 94% coverage: 37:594/595 of query aligns to 19:588/589 of 3wmgA
Sites not aligning to the query:
4aywA Structure of the human mitochondrial abc transporter, abcb10 (plate form) (see paper)
38% identity, 93% coverage: 23:576/595 of query aligns to 6:560/560 of 4aywA
6a6mA Crystal structure of an outward-open nucleotide-bound state of the eukaryotic abc multidrug transporter cmabcb1 (see paper)
37% identity, 94% coverage: 37:594/595 of query aligns to 20:589/589 of 6a6mA
- binding phosphoaminophosphonic acid-adenylate ester: Y352 (= Y363), R355 (= R366), S380 (= S391), G383 (= G394), K384 (= K395), S385 (= S396), T386 (= T397), Q429 (= Q437)
- binding decyl-beta-d-maltopyranoside: G378 (= G389), G379 (≠ H390), G381 (= G392), L545 (= L551), Q558 (≠ K564), D559 (= D565), F579 (= F584), L583 (= L588)
- binding magnesium ion: S385 (= S396), Q429 (= Q437)
7vfiA Cryo-em structure of the mouse tapl (9mer-peptide bound) (see paper)
37% identity, 95% coverage: 27:592/595 of query aligns to 5:569/570 of 7vfiA
7v5cA Cryo-em structure of the mouse abcb9 (adp.Bef3-bound) (see paper)
37% identity, 95% coverage: 27:592/595 of query aligns to 6:570/572 of 7v5cA
- binding adenosine-5'-diphosphate: Y342 (= Y363), T344 (= T365), S372 (≠ A393), K374 (= K395), S375 (= S396), S376 (≠ T397), S473 (= S494), Q476 (= Q497)
- binding beryllium trifluoride ion: S370 (= S391), K374 (= K395), Q416 (= Q437), H528 (= H549)
- binding magnesium ion: S375 (= S396), Q416 (= Q437)
7fc9A Crystal structure of cmabcb1 in lipidic mesophase revealed by lcp-sfx (see paper)
37% identity, 93% coverage: 37:589/595 of query aligns to 20:584/584 of 7fc9A
- binding phosphoaminophosphonic acid-adenylate ester: Y352 (= Y363), R355 (= R366), S380 (= S391), G383 (= G394), K384 (= K395), S385 (= S396), T386 (= T397), Q429 (= Q437), H543 (= H549)
- binding magnesium ion: D127 (= D143), T188 (≠ S205), S192 (≠ Q209), E312 (≠ R329), S385 (= S396), Q429 (= Q437)
- binding zinc ion: E31 (≠ S48), E74 (≠ Q90), E119 (= E135), D127 (= D143), S192 (≠ Q209), E193 (≠ D210), N347 (≠ D358), H349 (≠ S360), H349 (≠ S360), E359 (≠ D370), D451 (≠ E459), E452 (≠ Q460), E510 (= E518), H543 (= H549)
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, 95% coverage: 27:592/595 of query aligns to 177:741/766 of Q9NP78
- K545 (= K395) mutation to A: Loss of peptide transport activity; whena ssociated with A-699.
- H699 (= H549) 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.
5ochE The crystal structure of human abcb8 in an outward-facing state
38% identity, 90% coverage: 56:592/595 of query aligns to 35:570/576 of 5ochE
- binding adenosine-5'-diphosphate: Y341 (= Y363), C343 (≠ T365), G370 (= G392), G372 (= G394), K373 (= K395), T374 (≠ S396), T375 (= T397)
- binding cholesterol hemisuccinate: P163 (= P188), F238 (= F259), S242 (= S265), N243 (≠ F266), F246 (= F269), M285 (≠ I310), L288 (= L313), V295 (= V320)
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: 75:592/595 of query aligns to 193:710/735 of Q9NUT2
- 507:514 (vs. 389:396, 63% identical) binding
- GK 512:513 (= GK 394:395) mutation to AR: Renders the protein unstable.
- K513 (= K395) mutation to A: Abolish binding to ATP.
- A690 (≠ E571) 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
7o9wA Encequidar-bound human p-glycoprotein in complex with uic2-fab (see paper)
39% identity, 84% coverage: 92:592/595 of query aligns to 83:585/1169 of 7o9wA
- binding ~{N}-[2-[2-[4-[2-(6,7-dimethoxy-3,4-dihydro-1~{H}-isoquinolin-2-yl)ethyl]phenyl]-1,2,3,4-tetrazol-5-yl]-4,5-dimethoxy-phenyl]-4-oxidanylidene-2,3-dihydrochromene-2-carboxamide: W188 (≠ F197), F195 (≠ L204), F259 (≠ I268), I262 (≠ L271), Y266 (≠ I275), F292 (≠ Y302), F299 (vs. gap), Q303 (≠ G312)
Sites not aligning to the query:
- binding ~{N}-[2-[2-[4-[2-(6,7-dimethoxy-3,4-dihydro-1~{H}-isoquinolin-2-yl)ethyl]phenyl]-1,2,3,4-tetrazol-5-yl]-4,5-dimethoxy-phenyl]-4-oxidanylidene-2,3-dihydrochromene-2-carboxamide: 34, 38, 618, 625, 768, 839, 842, 846, 872, 876, 879, 883, 887
7a6fA Nanodisc reconstituted human abcb1 in complex with mrk16 fab and zosuquidar (see paper)
39% identity, 84% coverage: 92:592/595 of query aligns to 78:580/1164 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)
39% identity, 84% coverage: 92:592/595 of query aligns to 78:580/1164 of 7a6eA
- binding cholesterol: T153 (≠ A167), T160 (≠ V174), L167 (= L181), V168 (≠ F182), A171 (= A185), I172 (≠ T186), A259 (≠ G273), W266 (= W280), Y267 (= Y281)
- binding tariquidar: W183 (≠ F197), F254 (≠ I268), I257 (≠ L271), Y258 (≠ F272), Y261 (≠ I275), F287 (≠ Y302), Q298 (≠ G312)
Sites not aligning to the query:
- binding cholesterol: 43, 68, 72, 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)
39% identity, 84% coverage: 92:592/595 of query aligns to 78:580/1164 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
7a69A Nanodisc reconstituted human abcb1 in complex with mrk16 fab and vincristine (see paper)
39% identity, 84% coverage: 92:592/595 of query aligns to 78:580/1164 of 7a69A
Sites not aligning to the query:
- binding cholesterol: 67, 727, 731, 732, 843, 846, 846, 850
- binding vincristine: 37, 38, 763, 834, 837, 871, 874, 878
7ehlA Cryo-em structure of human abcb8 transporter in nucleotide binding state (see paper)
39% identity, 90% coverage: 56:592/595 of query aligns to 35:562/563 of 7ehlA
- binding phosphoaminophosphonic acid-adenylate ester: Y334 (= Y363), G365 (= G394), K366 (= K395), T367 (≠ S396), T368 (= T397)
- binding cholesterol: R139 (= R160), L157 (= L179), L168 (= L190), G172 (≠ A194), G260 (= G282), L273 (= L296), F276 (= F299), Q284 (≠ G307), R285 (≠ G308)
Query Sequence
>Echvi_1191 FitnessBrowser__Cola:Echvi_1191
MAKKKKALEEHEKRKLNKKNLSKLIGIFNFVLPYKGIFIVGLIFLLFSSLTLLAFPYVAG
KLIDVAQGKKWMFSNINTIALVLIGILFVQSVFSFFRVWLFALVSERSMRDIRLSLYSRL
VNLPMSFFDKRRTGELISRITSDVSLLQDTFSVTLAELFRQIITLLAGTVFLFVTTPRLT
LFMLATFPVLVIIAMVFGKFIRKLSKETQDELAAANVIVEETLQSISTVKSFAGEAYEAA
RYGKGLNKVVKVALKAAGFRGAFISFIIFALFGGIVAVMWYGAMMVSTGAMSIGDLVSFV
LYTTFIGGSIAGLGDIYGQVQKAIGSSERVLEILDESPEESLADYQEVSIKGNVSFSDVS
FNYPTRPEADVLKHINISIQSGEKIALAGHSGAGKSTIIQLLMKFYTINFGEITIDDKPI
QNWNLKQLRSNIGIVPQEVLLFGGSIRENIAYAKPEATEQEIIEAAKKANAWQFIGKFPE
GLDTLVGERGIKLSGGQRQRIAIARAILKNPSILILDEATSSLDAESEALVQEALDELMK
NRTTIVIAHRLATIRKVDRIYVMKDGEIVEEGSHDDLAVQKGGFYANLVKLQFAE
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