SitesBLAST
Comparing CA265_RS22865 FitnessBrowser__Pedo557:CA265_RS22865 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)
7t55A Cryo-em structure of pcat1 in the inward-facing wide conformation under atp turnover condition (see paper)
32% identity, 85% coverage: 79:574/583 of query aligns to 215:713/715 of 7t55A
Sites not aligning to the query:
- binding : 14, 46, 47, 48, 52, 63, 64, 65, 66, 75, 83, 91, 93
4s0fA Crystal structure of the peptidase-containing abc transporter pcat1 e648q mutant complexed with atpgs in an occluded conformation (see paper)
32% identity, 85% coverage: 79:574/583 of query aligns to 65:563/565 of 4s0fA
8fhkC Heterodimeric abc transporter bmrcd in the occluded conformation bound to atp: bmrcd_oc-atp (see paper)
31% identity, 82% coverage: 100:576/583 of query aligns to 96:573/574 of 8fhkC
- binding adenosine-5'-triphosphate: Y344 (≠ H346), S346 (≠ T348), N351 (≠ A353), T371 (≠ S373), G372 (= G374), G374 (= G376), K375 (= K377), T377 (= T379), A472 (≠ K474), L473 (≠ V475), S474 (= S476), Q477 (≠ E479)
7m33C The structure of bacillus subtilis bmrcd in the inward-facing conformation bound to hoechst-33342 and atp (see paper)
31% identity, 82% coverage: 100:575/583 of query aligns to 97:572/573 of 7m33C
- binding adenosine-5'-triphosphate: Y345 (≠ H346), S347 (≠ T348), T372 (≠ S373), G373 (= G374), S374 (= S375), G375 (= G376), K376 (= K377), T377 (≠ S378), T378 (= T379), Y387 (= Y388), Q499 (≠ E500)
- binding 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bi-benzimidazole: F133 (≠ K132), E245 (≠ G251), F292 (≠ Q294), E296 (≠ N298)
Sites not aligning to the query:
8t1pC Heterodimeric abc transporter bmrcd in the occluded conformation bound to adpvi: bmrcd_oc-adpvi (see paper)
31% identity, 82% coverage: 100:576/583 of query aligns to 96:573/574 of 8t1pC
- binding adp orthovanadate: A472 (≠ K474), L473 (≠ V475), S474 (= S476), G475 (= G477), G476 (= G478), Q477 (≠ E479)
- binding adenosine-5'-triphosphate: Y344 (≠ H346), S346 (≠ T348), N351 (≠ A353), T371 (≠ S373), G372 (= G374), S373 (= S375), G374 (= G376), K375 (= K377), T376 (≠ S378), T377 (= T379), Q417 (= Q419), H529 (= H533)
- binding magnesium ion: T376 (≠ S378), Q417 (= Q419)
2onjA Structure of the multidrug abc transporter sav1866 from s. Aureus in complex with amp-pnp (see paper)
30% identity, 98% coverage: 5:575/583 of query aligns to 6:576/578 of 2onjA
- binding phosphoaminophosphonic acid-adenylate ester: Y349 (≠ H346), I356 (≠ A353), S376 (= S373), G377 (= G374), G378 (≠ S375), G379 (= G376), K380 (= K377), S381 (= S378), T382 (= T379), Q422 (= Q419), K477 (= K474), S479 (= S476), G480 (= G477), E503 (= E500), H534 (= H533)
2hydA Multidrug abc transporter sav1866 (see paper)
30% identity, 98% coverage: 5:575/583 of query aligns to 6:576/578 of 2hydA
7v5cA Cryo-em structure of the mouse abcb9 (adp.Bef3-bound) (see paper)
27% identity, 98% coverage: 4:576/583 of query aligns to 6:571/572 of 7v5cA
- binding adenosine-5'-diphosphate: Y342 (≠ H346), T344 (= T348), S372 (= S375), K374 (= K377), S375 (= S378), S376 (≠ T379), S473 (= S476), Q476 (≠ E479)
- binding beryllium trifluoride ion: S370 (= S373), K374 (= K377), Q416 (= Q419), H528 (= H533)
- binding magnesium ion: S375 (= S378), Q416 (= Q419)
7vfiA Cryo-em structure of the mouse tapl (9mer-peptide bound) (see paper)
27% identity, 98% coverage: 4:576/583 of query aligns to 5:570/570 of 7vfiA
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)
30% identity, 97% coverage: 15:578/583 of query aligns to 32:582/582 of P60752
- C88 (≠ F83) mutation to S: Does not affect ATPase activity.
- E208 (≠ T203) 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 (≠ R207) mutation to A: Does not reduce substrate binding or nucleotide binding, but decreases ATP-dependent extrusion of substrates.
- A270 (≠ L268) 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 (≠ L310) mutation to S: Does not affect ATPase activity.
- E506 (= E500) 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 (= L505) mutation to P: Loss of ATPase activity; ATP is still bound.
- D512 (= D506) mutation to G: Loss of ATPase activity; ATP is still bound.
- H537 (= H533) 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.
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)
27% identity, 98% coverage: 4:576/583 of query aligns to 177:742/766 of Q9NP78
- K545 (= K377) mutation to A: Loss of peptide transport activity; whena ssociated with A-699.
- H699 (= H533) 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.
6bppA E. Coli msba in complex with lps and inhibitor g092 (see paper)
30% identity, 96% coverage: 15:575/583 of query aligns to 29:576/576 of 6bppA
- binding (2E)-3-{6-[(1S)-1-(3-amino-2,6-dichlorophenyl)ethoxy]-4-cyclopropylquinolin-3-yl}prop-2-enoic acid: L168 (≠ Y166), A172 (≠ I170), V175 (≠ I173), S176 (= S174), I179 (≠ S177), A256 (≠ R258), M288 (≠ F287), L291 (= L289), M292 (≠ F290), K296 (≠ Q294)
6bplA E. Coli msba in complex with lps and inhibitor g907 (see paper)
30% identity, 96% coverage: 15:575/583 of query aligns to 29:576/576 of 6bplA
- binding (2E)-3-{6-[(1S)-1-(2-chloro-6-cyclopropylphenyl)ethoxy]-4-cyclopropylquinolin-3-yl}prop-2-enoic acid: F154 (≠ I149), L168 (≠ Y166), V175 (≠ I173), S176 (= S174), I179 (≠ S177), A256 (≠ R258), M288 (≠ F287), L291 (= L289), M292 (≠ F290), L295 (= L293), K296 (≠ Q294)
7mewA E. Coli msba in complex with g247 (see paper)
30% identity, 96% coverage: 15:575/583 of query aligns to 25:572/572 of 7mewA
7ph3A Amp-pnp bound nanodisc reconstituted msba with nanobodies, spin- labeled at position a60c (see paper)
30% identity, 96% coverage: 15:575/583 of query aligns to 30:577/577 of 7ph3A
- binding phosphoaminophosphonic acid-adenylate ester: Y349 (≠ H346), S376 (= S373), G377 (= G374), G379 (= G376), K380 (= K377), S381 (= S378), T382 (= T379), Q422 (= Q419), L478 (≠ K474), S480 (= S476), G482 (= G478), Q483 (≠ E479), H535 (= H533)
- binding magnesium ion: S381 (= S378), Q422 (= Q419)
7bcwA Structure of msba in salipro with adp vanadate (see paper)
30% identity, 96% coverage: 15:575/583 of query aligns to 27:574/574 of 7bcwA
- binding adenosine-5'-diphosphate: Y346 (≠ H346), G374 (= G374), S375 (= S375), K377 (= K377), S378 (= S378), T379 (= T379), L475 (≠ K474), S477 (= S476), Q480 (≠ E479)
- binding magnesium ion: S378 (= S378), Q419 (= Q419)
- binding vanadate ion: S373 (= S373), K377 (= K377), S477 (= S476), A505 (≠ S504), H532 (= H533)
8dmmA Structure of the vanadate-trapped msba bound to kdl (see paper)
30% identity, 96% coverage: 15:575/583 of query aligns to 28:575/576 of 8dmmA
- binding adp orthovanadate: Y347 (≠ H346), R350 (≠ A349), S374 (= S373), G375 (= G374), S376 (= S375), G377 (= G376), K378 (= K377), S379 (= S378), T380 (= T379), Q420 (= Q419), L476 (≠ K474), S478 (= S476), G479 (= G477), G480 (= G478), H533 (= H533)
- binding (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-[(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-carboxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-5-[[(3~{R})-3-dodecanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanyltetradecanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-4-[(3~{R})-3-tetradecanoyloxytetradecanoyl]oxy-oxan-2-yl]methoxy]-5-oxidanyl-oxan-4-yl]oxy-4,5-bis(oxidanyl)oxane-2-carboxylic acid: Y79 (≠ R74), Y83 (= Y82), R184 (≠ K183), R234 (≠ E236), K239 (= K241), I246 (≠ V249), I250 (≠ T253)
Sites not aligning to the query:
- binding (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-[(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-carboxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-5-[[(3~{R})-3-dodecanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanyltetradecanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-4-[(3~{R})-3-tetradecanoyloxytetradecanoyl]oxy-oxan-2-yl]methoxy]-5-oxidanyl-oxan-4-yl]oxy-4,5-bis(oxidanyl)oxane-2-carboxylic acid: 25
7ph2A Nanodisc reconstituted msba in complex with nanobodies, spin-labeled at position a60c (see paper)
30% identity, 96% coverage: 15:575/583 of query aligns to 21:568/569 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 (≠ I24), L37 (= L31), F277 (= F284), A282 (vs. gap), R285 (≠ G291)
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)
32% identity, 82% coverage: 102:581/583 of query aligns to 354:832/842 of Q9DC29
- L356 (= L104) mutation to P: Results in retention of the protein in the Golgi apparatus.
- G579 (vs. gap) 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.
7pslA S. Cerevisiae atm1 in msp1d1 nanodiscs in nucleotide-free state (see paper)
34% identity, 76% coverage: 135:575/583 of query aligns to 131:583/600 of 7pslA
Sites not aligning to the query:
Query Sequence
>CA265_RS22865 FitnessBrowser__Pedo557:CA265_RS22865
MGLLLNYLKHHKWIVALALLLAGINIGFSLLDPYITGRILDRFINKKDSLTYNQYLWGSL
GLIGLAIGAAMVSRIAKNFQDYFTSVIVQKVGAKMYADGLQHSLKLPYQIFEDQRSGETL
GILQKVRLDSEKFITSFISILFVSLIGMIFVIVYSVSVSYKVTLVYFSAIPIISFVSWFL
SRKIKTIQRSIVGETTALAGSTTESLRNIELVKSLGLADQEIDRLNKTTYKILGLELKKV
KYVRSMSFVQGTTVNLVRSTMVLVLLLLIFDNTISAGQYFSFLFYSFFLFGPLQELGNVI
LTWREAEVSLGNFKKILSTPVDKKPENPTSIAKIKDLTFNNVGFKHLTANRNALDNISFK
THHGQTIAFVGPSGSGKSTLVKLLVGLYPAKDGEILYNGIPSNDIDLDALREKIGFVTQD
TQLFSGTIRENLLFVNPNATDEECYKVLNQAACQTLLARADKGLDSLIGEGGVKVSGGEK
QRLSIARALLRQPDILVFDEATSSLDSITEEEITKTIRSVSDLTDHITILIAHRLSTIKH
ADKIYVLEKGNIIEEGRHEELIAQNGLYQAMWRQQIGERVVEA
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