SitesBLAST
Comparing WP_109967879.1 NCBI__GCF_003173355.1:WP_109967879.1 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)
7sgrE Structure of hemolysin a secretion system hlyb/d complex (see paper)
30% identity, 95% coverage: 33:621/622 of query aligns to 127:686/700 of 7sgrE
8dckA Structure of hemolysin a secretion system hlyb/d complex, atp-bound (see paper)
30% identity, 94% coverage: 39:621/622 of query aligns to 128:681/691 of 8dckA
- binding adenosine-5'-triphosphate: Y466 (= Y407), I473 (≠ L414), S493 (≠ T433), G494 (= G434), S495 (≠ A435), G496 (= G436), K497 (= K437), S498 (≠ T438), T499 (= T439), Q539 (= Q479), A593 (≠ S533), G594 (≠ K534), S596 (= S536), G598 (= G538), Q599 (= Q539), Q620 (≠ E560), H651 (= H591)
- binding magnesium ion: S498 (≠ T438), Q539 (= Q479)
6quzD Structure of atpgs-bound outward-facing tm287/288 in complex with sybody sb_tm35 (see paper)
29% identity, 93% coverage: 46:621/622 of query aligns to 14:561/574 of 6quzD
- binding phosphothiophosphoric acid-adenylate ester: Y347 (= Y407), V353 (= V413), G374 (= G434), S375 (≠ A435), G376 (= G436), K377 (= K437), T378 (= T438), T379 (= T439), Q419 (= Q479), D474 (≠ K534), L475 (= L535), S476 (= S536), G478 (= G538), Q479 (= Q539), H531 (= H591)
- binding magnesium ion: T378 (= T438), Q419 (= Q479)
6qv0B Structure of atp-bound outward-facing tm287/288 in complex with sybody sb_tm35 (see paper)
29% identity, 93% coverage: 46:621/622 of query aligns to 10:557/570 of 6qv0B
- binding adenosine-5'-triphosphate: Y343 (= Y407), V349 (= V413), T369 (= T433), S371 (≠ A435), G372 (= G436), K373 (= K437), T374 (= T438), T375 (= T439), Q415 (= Q479), D470 (≠ K534), S472 (= S536), G474 (= G538), Q475 (= Q539), H527 (= H591)
- binding magnesium ion: T374 (= T438), Q415 (= Q479)
2onjA Structure of the multidrug abc transporter sav1866 from s. Aureus in complex with amp-pnp (see paper)
30% identity, 93% coverage: 43:621/622 of query aligns to 5:564/578 of 2onjA
- binding phosphoaminophosphonic acid-adenylate ester: Y349 (= Y407), I356 (≠ V413), S376 (≠ T433), G377 (= G434), G378 (≠ A435), G379 (= G436), K380 (= K437), S381 (≠ T438), T382 (= T439), Q422 (= Q479), K477 (= K534), S479 (= S536), G480 (= G537), E503 (= E560), H534 (= H591)
2hydA Multidrug abc transporter sav1866 (see paper)
30% identity, 93% coverage: 43:621/622 of query aligns to 5:564/578 of 2hydA
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; EC 7.6.2.- from Mus musculus (Mouse) (see 2 papers)
33% identity, 76% coverage: 149:620/622 of query aligns to 211:684/715 of Q9JI39
- G497 (= G436) mutation to A: Decreases ATP binding about 50%.
- K498 (= K437) mutation to R: Decreases ATP binding about 50%.
- C547 (≠ D486) modified: S-glutathionyl cysteine; mutation to A: Does not affect ABCB10 glutathionylation.
- G602 (= G538) mutation to D: Affects ATP hydrolysis but not binding.; mutation to V: Affects ATP hydrolysis but not binding.
- E624 (= E560) mutation to Q: Affects ATP hydrolysis but not binding.
- C675 (≠ H611) 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; EC 7.6.2.- from Homo sapiens (Human) (see 7 papers)
30% identity, 96% coverage: 27:621/622 of query aligns to 139:720/738 of Q9NRK6
- A150 (≠ R38) to S: in dbSNP:rs4148756
- C215 (≠ H99) 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 (≠ I118) mutation to L: Does not affect ATPase activity; when associated with S-215 and G-582. Activated by Zn (II) mesoporphyrin; when associated with S-215 and G-582.
- N229 (≠ V124) mutation to A: Does not affect ATPase activity in the absence or presence of biliverdin. No increased ATPase activity in the presence of biliverdin; when associated with A-398. Increased ATPase activity in the absence of biliverdin compared to WT; when associated with A-407. No increased ATPase activity in the presence of biliverdin; when associated with A-407. No increased ATPase activity in the presence of biliverdin; when associated with A-398 and A-407.
- F398 (≠ T301) mutation to A: No increased ATPase activity in the presence of biliverdin. No increased ATPase activity in the presence of biliverdin; when associated with A-229. No increased ATPase activity in the presence of biliverdin; when associated with A-407. No increased ATPase activity in the presence of biliverdin; when associated with A-229 and A-407.
- T402 (≠ Q305) binding biliverdin IXalpha
- N407 (= N310) mutation to A: Increased ATPase activity in the absence of biliverdin compared to WT. No increased ATPase activity in the presence of biliverdin. Increased ATPase activity in the absence of biliverdin compared to WT; when associated with A-229. No increased ATPase activity in the presence of biliverdin; when associated with A-229. No increased ATPase activity in the presence of biliverdin; when associated with A-398. No increased ATPase activity in the presence of biliverdin; when associated with A-229 and A-398.
- R471 (≠ M374) to T: in a breast cancer sample; somatic mutation
- K533 (= K437) mutation to E: Increases hemoglobin biosynthetic process.
- S534 (≠ T438) binding Mg(2+)
- D545 (≠ R449) to N: in dbSNP:rs35698797
- C582 (≠ D486) 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 (= S536) mutation to R: Does not rescue hemoglobin and heme biosynthetic process.
- Q638 (= Q539) mutation to H: Does not rescue hemoglobin and heme biosynthetic process.
- D658 (= D559) binding Mg(2+); mutation to A: Does not rescue hemoglobin and heme biosynthetic process.
- E659 (= E560) mutation to A: Does not rescue hemoglobin and heme biosynthetic process.
4ayxA Structure of the human mitochondrial abc transporter, abcb10 (rod form b) (see paper)
32% identity, 76% coverage: 149:621/622 of query aligns to 93:567/571 of 4ayxA
Sites not aligning to the query:
9csiA Lipid A export ATP-binding/permease protein MsbA (see paper)
32% identity, 76% coverage: 148:621/622 of query aligns to 92:559/569 of 9csiA
- binding 3,3'-[(1,4-dioxobutane-1,4-diyl)bis(azanediyl)]bis[(4-butylbenzene-1-sulfonamido)benzoic acid]: M253 (≠ F308), M257 (≠ V312), T283 (≠ A339), A285 (≠ Y341), G286 (≠ P342)
- binding phosphoaminophosphonic acid-adenylate ester: Y344 (= Y407), D346 (≠ P409), T348 (= T411), S370 (≠ T433), G371 (= G434), G373 (= G436), K374 (= K437), T375 (= T438), S376 (≠ T439), Q416 (= Q479)
- binding magnesium ion: T375 (= T438), Q416 (= Q479)
Sites not aligning to the query:
8gk7A Msba bound to cerastecin c (see paper)
32% identity, 76% coverage: 148:621/622 of query aligns to 87:554/564 of 8gk7A
- binding phosphoaminophosphonic acid-adenylate ester: Y339 (= Y407), T343 (= T411), S365 (≠ T433), G366 (= G434), G368 (= G436), K369 (= K437), T370 (= T438), N467 (≠ K534), L468 (= L535), S469 (= S536), G470 (= G537), G471 (= G538)
- binding 2-[(4-butylbenzene-1-sulfonyl)amino]-5-[(3-{4-[(4-butylbenzene-1-sulfonyl)amino]-3-carboxyanilino}-3-oxopropyl)carbamoyl]benzoic acid: M248 (≠ F308), M252 (≠ V312), I277 (≠ L338), T278 (≠ A339), A280 (≠ Y341), G281 (≠ P342), S284 (≠ T345)
Sites not aligning to the query:
7metA A. Baumannii msba in complex with tbt1 decoupler (see paper)
31% identity, 76% coverage: 148:621/622 of query aligns to 86:553/564 of 7metA
Sites not aligning to the query:
5ochE The crystal structure of human abcb8 in an outward-facing state
31% identity, 80% coverage: 114:612/622 of query aligns to 34:549/576 of 5ochE
- binding adenosine-5'-diphosphate: Y341 (= Y407), C343 (vs. gap), G370 (= G434), G372 (= G436), K373 (= K437), T374 (= T438), T375 (= T439)
- binding cholesterol hemisuccinate: P163 (= P226), F238 (= F297), S242 (≠ V304), N243 (≠ Q305), F246 (= F308), M285 (≠ I348), L288 (vs. gap), V295 (≠ M354)
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)
31% identity, 76% coverage: 150:620/622 of query aligns to 227:697/735 of Q9NUT2
- 507:514 (vs. 431:438, 75% identical) binding ATP
- GK 512:513 (= GK 436:437) mutation to AR: Renders the protein unstable.
- K513 (= K437) mutation to A: Abolish binding to ATP.
- A690 (≠ E613) 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
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)
32% identity, 76% coverage: 149:621/622 of query aligns to 151:622/644 of Q0WML0
- E261 (≠ D259) mutation to K: In als1-1; loss of aluminum tolerance.
7t55A Cryo-em structure of pcat1 in the inward-facing wide conformation under atp turnover condition (see paper)
28% identity, 96% coverage: 24:621/622 of query aligns to 129:702/715 of 7t55A
Sites not aligning to the query:
- binding : 14, 46, 47, 48, 52, 63, 64, 65, 66, 75, 83, 91, 93
8vowA Cryo-em structure of the abc transporter pcat1 cysteine-free core bound with mgatp and vi (see paper)
28% identity, 93% coverage: 43:621/622 of query aligns to 1:552/566 of 8vowA
- binding adenosine-5'-diphosphate: A464 (≠ S533), N465 (≠ K534), L466 (= L535), S467 (= S536)
- binding adenosine-5'-triphosphate: Y338 (= Y407), R341 (≠ D410), S364 (≠ T433), G365 (= G434), S366 (≠ A435), K368 (= K437), T369 (= T438), Q410 (= Q479)
8vozA ABC-type bacteriocin transporter (see paper)
28% identity, 93% coverage: 43:621/622 of query aligns to 7:558/571 of 8vozA
- binding 3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxypropyl hexadecanoate: I160 (≠ V221), N268 (≠ Q328)
- binding adenosine-5'-diphosphate: Y344 (= Y407), V350 (= V413), G371 (= G434), G373 (= G436), K374 (= K437), T375 (= T438), T376 (= T439), A470 (≠ S533), N471 (≠ K534)
- binding magnesium ion: T375 (= T438), Q416 (= Q479)
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)
28% identity, 95% coverage: 28:621/622 of query aligns to 165:729/766 of Q9NP78
- K545 (= K437) mutation to A: Loss of peptide transport activity; whena ssociated with A-699.
- H699 (= H591) 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.
Q9DC29 ATP-binding cassette sub-family B member 6; ABC-type heme transporter ABCB6; EC 7.6.2.5 from Mus musculus (Mouse) (see paper)
31% identity, 76% coverage: 150:621/622 of query aligns to 345:813/842 of Q9DC29
- L356 (≠ Y161) mutation to P: Results in retention of the protein in the Golgi apparatus.
- G579 (≠ L388) mutation to E: Results in retention of the protein in the Golgi apparatus.
Sites not aligning to the query:
- 170 S→G: Results in retention of the protein in the Golgi apparatus.
Query Sequence
>WP_109967879.1 NCBI__GCF_003173355.1:WP_109967879.1
MTSQSGPIGKIPLRGRLRLLRDSLTYVPPGKDGEFKYRDILYFTRYLIPLKYAIISSLIL
TFISSLLGTALPLSGKWIIDYIFMHQSIEPVLDRLSAHHLAFLVPFASQVFSSLPLLIGT
LAVVSIVKYLIGNELSLINYRINTEYGYRVKMAVFTHVMKYPVSFFKSTRSGYLLARISS
DTAGLSGISGSFLQNIITAGTSLCVTATVLSALSLPLTLFVIITVPVSVIISYWVVRFTR
SYSIRMRESGLQMAADGQDLFSSIDLIKTHAAEERELNRYMKRTLDNISLNIASMLFGQV
TGGVQMAFTNIVRLIVMLYGGSLVLSNQMSIGSYTAFLAMYPQLTGAISTFLQMPLNLQG
TALAAGRVKELLDMTTEYEHDDPKKTLLYPDIRTNGHIIVDCVSFSYDPDTPVLKDVSLE
IQPGDRIGLIGQTGAGKTTFINLLLKFYRPNQGKILIDDYDYADLNPAWIRNQIAVVSQD
LMLFHDTVMNNIRYSRPEADDEEVMRAAQSAGIHDEIIRLQNGYDTIVGERGSKLSGGQK
QRIAIARAFLRNAQIVILDEPTAHLDIETEELLIREFISVCSGRTMVVITHRESLLRLVD
RVYRLKKGKIHEEKRDASLISA
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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