SitesBLAST
Comparing CCNA_03383 FitnessBrowser__Caulo:CCNA_03383 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)
5ochE The crystal structure of human abcb8 in an outward-facing state
42% identity, 80% coverage: 117:611/617 of query aligns to 75:570/576 of 5ochE
- binding adenosine-5'-diphosphate: Y341 (= Y383), C343 (≠ G385), G370 (= G412), G372 (= G414), K373 (= K415), T374 (≠ S416), T375 (= T417)
- binding cholesterol hemisuccinate: P163 (= P205), F238 (≠ T281), S242 (≠ I285), N243 (≠ T286), F246 (= F289), M285 (≠ I327), L288 (= L330), V295 (= V337)
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)
38% identity, 90% coverage: 62:616/617 of query aligns to 177:738/738 of Q9NRK6
- C215 (≠ F97) 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 (≠ V106) 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 (≠ A353) to T: in a breast cancer sample; somatic mutation
- K533 (= K415) mutation to E: Increases hemoglobin biosynthetic process.
- D545 (= D427) to N: in dbSNP:rs35698797
- C582 (≠ G464) 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 (= S514) mutation to R: Does not rescue hemoglobin and heme biosynthetic process.
- Q638 (= Q517) mutation to H: Does not rescue hemoglobin and heme biosynthetic process.
- D658 (= D537) mutation to A: Does not rescue hemoglobin and heme biosynthetic process.
- E659 (= E538) 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, 87% coverage: 62:600/617 of query aligns to 24:568/571 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)
42% identity, 80% coverage: 117:611/617 of query aligns to 215:710/735 of Q9NUT2
- 507:514 (vs. 409:416, 63% identical) binding
- GK 512:513 (= GK 414:415) mutation to AR: Renders the protein unstable.
- K513 (= K415) mutation to A: Abolish binding to ATP.
- A690 (≠ Q591) 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
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)
38% identity, 96% coverage: 17:611/617 of query aligns to 97:698/715 of Q9JI39
- G497 (= G414) mutation to A: Decreases ATP binding about 50%.
- K498 (= K415) mutation to R: Decreases ATP binding about 50%.
- C547 (≠ G464) modified: S-glutathionyl cysteine; mutation to A: Does not affect ABCB10 glutathionylation.
- G602 (= G516) mutation to D: Affects ATP hydrolysis but not binding.; mutation to V: Affects ATP hydrolysis but not binding.
- E624 (= E538) mutation to Q: Affects ATP hydrolysis but not binding.
- C675 (≠ V589) mutation to A: Prevents ABCB10 glutathionylation.
Sites not aligning to the query:
- 1:82 modified: transit peptide, Mitochondrion
7y48B Cryo-em structure of biliverdin-bound mitochondrial abc transporter abcb10 from biortus
38% identity, 87% coverage: 62:600/617 of query aligns to 23:564/567 of 7y48B
7ehlA Cryo-em structure of human abcb8 transporter in nucleotide binding state (see paper)
42% identity, 80% coverage: 117:611/617 of query aligns to 79:562/563 of 7ehlA
- binding phosphoaminophosphonic acid-adenylate ester: Y334 (= Y383), G365 (= G414), K366 (= K415), T367 (≠ S416), T368 (= T417)
- binding cholesterol: R139 (= R177), L157 (≠ K195), L168 (≠ I207), G172 (≠ M211), G260 (= G299), L273 (= L313), F276 (= F316), Q284 (≠ A324), R285 (≠ G325)
4aywA Structure of the human mitochondrial abc transporter, abcb10 (plate form) (see paper)
38% identity, 87% coverage: 62:596/617 of query aligns to 24:560/560 of 4aywA
Sites not aligning to the query:
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)
34% identity, 99% coverage: 1:611/617 of query aligns to 136:741/766 of Q9NP78
- LL 136:137 (≠ MM 1:2) mutation to AA: No effect on lysosomal localization.
- K545 (= K415) mutation to A: Loss of peptide transport activity; whena ssociated with A-699.
- H699 (= H569) 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
7v5cA Cryo-em structure of the mouse abcb9 (adp.Bef3-bound) (see paper)
35% identity, 90% coverage: 57:611/617 of query aligns to 18:570/572 of 7v5cA
- binding adenosine-5'-diphosphate: Y342 (= Y383), T344 (≠ G385), S372 (≠ A413), K374 (= K415), S375 (= S416), S376 (≠ T417), S473 (= S514), Q476 (= Q517)
- binding beryllium trifluoride ion: S370 (= S411), K374 (= K415), Q416 (= Q457), H528 (= H569)
- binding magnesium ion: S375 (= S416), Q416 (= Q457)
7vfiA Cryo-em structure of the mouse tapl (9mer-peptide bound) (see paper)
35% identity, 90% coverage: 57:611/617 of query aligns to 17:569/570 of 7vfiA
5ochC The crystal structure of human abcb8 in an outward-facing state
40% identity, 80% coverage: 117:611/617 of query aligns to 69:529/537 of 5ochC
2onjA Structure of the multidrug abc transporter sav1866 from s. Aureus in complex with amp-pnp (see paper)
36% identity, 82% coverage: 105:611/617 of query aligns to 59:576/578 of 2onjA
- binding phosphoaminophosphonic acid-adenylate ester: Y349 (= Y383), I356 (≠ A391), S376 (= S411), G377 (= G412), G378 (≠ A413), G379 (= G414), K380 (= K415), S381 (= S416), T382 (= T417), Q422 (= Q457), K477 (≠ T512), S479 (= S514), G480 (= G515), E503 (= E538), H534 (= H569)
2hydA Multidrug abc transporter sav1866 (see paper)
36% identity, 82% coverage: 105:611/617 of query aligns to 59:576/578 of 2hydA
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)
39% identity, 82% coverage: 108:612/617 of query aligns to 131:635/644 of Q0WML0
- E261 (= E238) mutation to K: In als1-1; loss of aluminum tolerance.
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)
37% identity, 85% coverage: 87:611/617 of query aligns to 56:586/589 of 3wmgA
Sites not aligning to the query:
P60752 ATP-dependent lipid A-core flippase; Lipid A export ATP-binding/permease protein MsbA; Lipid flippase; EC 7.5.2.6 from Escherichia coli (strain K12) (see 7 papers)
33% identity, 92% coverage: 45:613/617 of query aligns to 16:581/582 of P60752
- C88 (≠ F117) mutation to S: Does not affect ATPase activity.
- E208 (≠ G237) mutation to A: Does not reduce substrate binding or nucleotide binding, but decreases ATP-dependent extrusion of substrates. Inhibits formation of outward-facing conformation.; mutation to C: Exhibits ATPase activity. Forms intermolecular cross-links.; mutation to Q: Improves basal ATPase activity and increases transport activity.
- K212 (≠ D241) mutation to A: Does not reduce substrate binding or nucleotide binding, but decreases ATP-dependent extrusion of substrates.
- A270 (≠ G299) mutation to T: Temperature-sensitive. Loss of lipid export to the outer membrane. Significantly decreases ATPase activity at 42 degrees Celsius but not at 30 degrees Celsius.
- C315 (≠ M344) mutation to S: Does not affect ATPase activity.
- E506 (= E538) mutation to Q: Lacks cell viability and does not support growth. Can still bind ATP and slowly hydrolyze ATP, but becomes locked into a closed dimer conformation.
- L511 (= L543) mutation to P: Loss of ATPase activity; ATP is still bound.
- D512 (= D544) mutation to G: Loss of ATPase activity; ATP is still bound.
- H537 (= H569) mutation to A: Lacks cell viability and does not support growth. Can still bind ATP and slowly hydrolyze ATP, but becomes locked into a closed dimer conformation.
6a6mA Crystal structure of an outward-open nucleotide-bound state of the eukaryotic abc multidrug transporter cmabcb1 (see paper)
37% identity, 85% coverage: 87:611/617 of query aligns to 57:587/589 of 6a6mA
- binding phosphoaminophosphonic acid-adenylate ester: Y352 (= Y383), R355 (= R386), S380 (= S411), G383 (= G414), K384 (= K415), S385 (= S416), T386 (= T417), Q429 (= Q457)
- binding decyl-beta-d-maltopyranoside: G378 (= G409), G379 (≠ P410), G381 (= G412), L545 (= L571), Q558 (≠ E584), D559 (≠ E585), F579 (≠ L603), L583 (= L607)
- binding magnesium ion: S385 (= S416), Q429 (= Q457)
7fc9A Crystal structure of cmabcb1 in lipidic mesophase revealed by lcp-sfx (see paper)
37% identity, 84% coverage: 87:607/617 of query aligns to 57:583/584 of 7fc9A
- binding phosphoaminophosphonic acid-adenylate ester: Y352 (= Y383), R355 (= R386), S380 (= S411), G383 (= G414), K384 (= K415), S385 (= S416), T386 (= T417), Q429 (= Q457), H543 (= H569)
- binding magnesium ion: D127 (= D160), T188 (≠ V218), S192 (≠ Q226), E312 (vs. gap), S385 (= S416), Q429 (= Q457)
- binding zinc ion: E74 (≠ A104), E119 (= E152), D127 (= D160), S192 (≠ Q226), E193 (≠ D227), N347 (= N378), H349 (≠ V380), H349 (≠ V380), E359 (≠ P390), D451 (= D479), E452 (= E480), E510 (= E538), H543 (= H569)
Sites not aligning to the query:
7ph2A Nanodisc reconstituted msba in complex with nanobodies, spin-labeled at position a60c (see paper)
33% identity, 92% coverage: 45:612/617 of query aligns to 5:569/569 of 7ph2A
- binding (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-4-[(2~{R},3~{S},4~{S},5~{R},6~{R})-6-[(1~{S})-1,2-bis(oxidanyl)ethyl]-4-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-[(1~{S})-1,2-bis(oxidanyl)ethyl]-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-3,5-bis(oxidanyl)oxan-2-yl]oxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-4-[(3~{R})-3-nonanoyloxytetradecanoyl]oxy-5-[[(3~{R})-3-octanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{S},5~{S},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanylnonanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-oxan-2-yl]methoxy]-5-oxidanyl-oxane-2-carboxylic acid: D30 (≠ T70), L37 (≠ F77), F277 (vs. gap), A282 (= A320), R285 (≠ A323)
Query Sequence
>CCNA_03383 FitnessBrowser__Caulo:CCNA_03383
MMTDANSGDQKVEGRPGAGAELVQGMTEAGARRPRRKDIRPLAHLLPFVIAHKGDGLAAG
FFLLFSTAATLGLTYAFKNVIDHGFSKGQDAAINSAFVGLGAVALVLALATALRFFFITR
LGERVVADLRRKLYGHTLSLDQPYFLKTRTGEVLSRLTTDVALVEQLVGASISIALRNIL
NLIGGLTAMAVVSPKLAGFIVLMVPVILAPMFLVGRRVRKLTVTAQDRFADAVGYAGESL
DALETVQAFGRESASSGRFGAAVEAAYKASVRRITTRATMTAMVITLAFGGITLLLWTGA
RLVLAGEMTGGTLAQFAMLAVMAAGSIGALGEVWGDVQKASGAMDRISELLNAKPDIAAP
PQPKTLPVPGQGEIAFENVVFAYPGRPDLPALNGFDLRVKPGETVALVGPSGAGKSTVLR
LLLRFYDPQSGCILLDGVNLRDAEPAEVRARMALVAQDSPLFSGSAMDNIRFGRPDATDE
QVRAAADAAQATGFLSALPEGFDTPVGERAKTLSGGQRQRLAIARALVREAPILLLDEAT
SALDAESEQLVQQALATAMEGRTTLVIAHRLATVLKADRIVVMEEGRVVEQGAHAELFAK
GGLYARLARLQFGVEAA
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