SitesBLAST
Comparing WP_083492049.1 NCBI__GCF_001431535.1:WP_083492049.1 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)
5ochC The crystal structure of human abcb8 in an outward-facing state
39% identity, 52% coverage: 293:619/623 of query aligns to 206:530/537 of 5ochC
Q9LVM1 ABC transporter B family member 25, mitochondrial; ABC transporter ABCB.25; AtABCB25; ABC transporter of the mitochondrion 3; AtATM3; Iron-sulfur clusters transporter ATM3; Protein STARIK 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 92% coverage: 44:618/623 of query aligns to 145:714/728 of Q9LVM1
- R612 (= R513) mutation to K: Resistant to sirtinol and reduced chlorophyll content.
5ochE The crystal structure of human abcb8 in an outward-facing state
34% identity, 71% coverage: 177:619/623 of query aligns to 134:571/576 of 5ochE
- binding adenosine-5'-diphosphate: Y341 (= Y386), C343 (≠ D388), G370 (= G414), G372 (= G416), K373 (= K417), T374 (= T418), T375 (= T419)
- binding cholesterol hemisuccinate: P163 (= P207), F238 (≠ W283), S242 (vs. gap), N243 (vs. gap), F246 (vs. gap), M285 (≠ L330), L288 (= L333), V295 (= V340)
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)
34% identity, 71% coverage: 177:619/623 of query aligns to 274:711/735 of Q9NUT2
- 507:514 (vs. 411:418, 63% identical) binding
- GK 512:513 (= GK 416:417) mutation to AR: Renders the protein unstable.
- K513 (= K417) mutation to A: Abolish binding to ATP.
- A690 (≠ S598) 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
P21439 Phosphatidylcholine translocator ABCB4; ATP-binding cassette sub-family B member 4; Multidrug resistance protein 3; P-glycoprotein 3; EC 7.6.2.1 from Homo sapiens (Human) (see 22 papers)
33% identity, 58% coverage: 259:621/623 of query aligns to 276:634/1286 of P21439
- A286 (≠ N273) to V: in PFIC3 and GBD1; does not alter plasma membrane location; inhibits efflux activity for PC; dbSNP:rs765478923
- S320 (vs. gap) to F: in ICP3, GBD1 and PFIC3; uncertain significance; does not alter plasma membrane location; does not inhibit efflux activity for PC; dbSNP:rs72552778
- I367 (≠ L350) to V: in dbSNP:rs1168923653
- Y403 (= Y386) to H: in PFIC3; does not alter cytoplasmic and cell membrane location; inhibits efflux activity for PC and cholesterol; dbSNP:rs121918443
- R406 (vs. gap) binding ; to Q: found in patients with cholangitis; uncertain significance; dbSNP:rs763807769
- GCGKST 432:437 (≠ GAGKTT 414:419) binding
- K435 (= K417) mutation to M: Inhibits efflux activity for PC and cholesterol, but does not alter glycosylation and surface expression in the presence of taurocholate.
- E450 (= E432) to G: in dbSNP:rs1189003716
- D459 (= D441) to H: in PFIC3; retained in the reticulum endoplasmic; greatly reduced expression
- Q477 (= Q459) binding
- P479 (≠ F461) to L: in PFIC3; greatly reduced expression; alters efflux activity for PC; dbSNP:rs748657435
- L481 (≠ R463) to R: in PFIC3; does not alter cytoplasmic and cell membrane location; inhibits efflux activity for PC and cholesterol
- A511 (= A495) to T: in PFIC3 and GBD1; dbSNP:rs1257887155
- E528 (≠ R512) to D: in GBD1; uncertain significance; moderate decrease of phosphatidylcholine transporter activity; does not alter plasma membrane location; dbSNP:rs8187797
- G535 (= G522) to D: in PFIC3; reduced phosphatidylcholine transporter activity; does not alter plasma membrane location
- G536 (= G523) binding ; to R: in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location
- I541 (= I528) to F: in PFIC3 and GBD1; dbSNP:rs66904256
- A546 (= A533) to D: in ICP3; disruption of protein trafficking with subsequent lack of functional protein at the cell surface; dbSNP:rs121918441
- E558 (= E545) mutation to Q: Loss of floppase activity. Strongly reduce the ATPase activity.
- H589 (= H576) to T: in GBD1; requires 2 nucleotide substitutions
- R590 (= R577) to Q: found in patients with gallbladder and cholestasis; uncertain significance; dbSNP:rs45575636
Sites not aligning to the query:
- 34 modified: Phosphothreonine; T → M: in GBD1; reduces efflux activity for PC in a phosphorylation-dependent manner; dbSNP:rs142794414; T→D: Does not inhibit efflux activity for PC.
- 44 T→A: Reduces efflux activity for PC. Does not alter apical membrane location.
- 47 R → G: in GBD1; partly retained intracellularly; reduces efflux activity for PC in a phosphorylation-dependent manner; R → Q: found in patients with cholangitis; uncertain significance; dbSNP:rs372685632
- 49 S→A: Reduces efflux activity for PC. Does not alter apical membrane location.
- 68 G → R: in PFIC3; retained in the reticulum endoplasmic; greatly reduced expression; dbSNP:rs1343667900
- 73 L → V: in PFIC3 and GBD1; dbSNP:rs8187788
- 87 natural variant: D -> E
- 95 P → S: in dbSNP:rs377268767
- 175 T → A: found in patients with gallbladder and cholestasis; uncertain significance; dbSNP:rs58238559
- 201 T → M: in PFIC3; greatly reduced expression; alters efflux activity for PC; dbSNP:rs753318087
- 238 L → V: in dbSNP:rs45596335
- 263 I → V: in dbSNP:rs45547936
- 651 T → N: in dbSNP:rs45476795
- 652 R → G: in dbSNP:rs2230028
- 726 P → L: in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location; dbSNP:rs141677867
- 742 natural variant: G -> S
- 764 I → L: in a heterozygous patient with risperidone-induced cholestasis
- 775 T → M: found in patients with cholangitis; uncertain significance; dbSNP:rs148052192
- 788 R → Q: in GBD1; benign; dbSNP:rs8187801
- 934 A → T: found in patients with gallbladder and cholestasis; uncertain significance; dbSNP:rs61730509
- 953 A→D: Accumulates predominantly in intracellular compartments with only a small fraction at the plasma membrane and inhibits partially the efflux activity for PC.
- 964 V → T: found in patients with cholangitis; uncertain significance; requires 2 nucleotide substitutions
- 978 S → P: in PFIC3; alters efflux activity for PC; dbSNP:rs1051861187
- 985 V→M: Significantly reduces phosphatidylcholine floppase activity; when associated with Q-989 and V-990.
- 989 H→Q: Significantly reduces phosphatidylcholine floppase activity; when associated with M-985 and V-990.
- 990 A→V: Significantly reduces phosphatidylcholine floppase activity; when associated with M-985 and Q-989.
- 1046 binding
- 1071:1077 binding
- 1075 K→M: Inhibits efflux activity for PC and cholesterol, but does not alter glycosylation and surface expression in the presence of taurocholate.
- 1082 L → Q: in a heterozygous patient with amoxicillin/clavulanic acid-induced cholestasis; dbSNP:rs1214110864
- 1124 binding
- 1125 E → K: in PFIC3; alters efflux activity for PC
- 1168 P → S: in GBD1; reduced phosphatidylcholine transporter activity; does not alter plasma membrane location; dbSNP:rs121918442
- 1183 S → L: in GBD1; severely reduced phosphatidylcholine transporter activity; does not alter plasma membrane location
- 1184:1186 binding
- 1185 G → S: in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location
7n5aA Structure of atatm3 in the closed conformation (see paper)
30% identity, 60% coverage: 247:618/623 of query aligns to 223:587/589 of 7n5aA
7n59A Structure of atatm3 in the inward-facing conformation with gssg bound (see paper)
30% identity, 60% coverage: 247:618/623 of query aligns to 224:588/590 of 7n59A
Sites not aligning to the query:
P40416 Iron-sulfur clusters transporter ATM1, mitochondrial; EC 7.-.-.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
32% identity, 59% coverage: 249:618/623 of query aligns to 308:674/690 of P40416
- NSGQ 343:346 (≠ GTLL 284:287) binding
- K475 (= K417) mutation to M: Loss of function; significant decrease in ATP-binding; no homodimerization.; mutation Missing: Decreases ATP hydrolysis. Decreases transporter activity.
- E598 (= E545) mutation to A: Loss of function; slight decrease in ATP-binding.
Sites not aligning to the query:
- 216 R→Q: Decreases ATP hydrolysis. Decreases transporter activity.
- 280:284 binding
- 666:690 mutation Missing: Impairs protein stability.
7pslA S. Cerevisiae atm1 in msp1d1 nanodiscs in nucleotide-free state (see paper)
32% identity, 59% coverage: 249:618/623 of query aligns to 217:583/600 of 7pslA
Sites not aligning to the query:
4myhB Structure of the glutathione bound mitochondrial abc transporter, atm1 (see paper)
32% identity, 59% coverage: 249:618/623 of query aligns to 211:577/598 of 4myhB
Sites not aligning to the query:
7psnA S. Cerevisiae atm1 in msp1e3d1 nanodiscs with bound amp-pnp and mg2+ (see paper)
32% identity, 59% coverage: 249:618/623 of query aligns to 217:583/585 of 7psnA
- binding phosphoaminophosphonic acid-adenylate ester: Y354 (= Y386), H355 (vs. gap), R358 (≠ A389), G381 (= G414), K384 (= K417), S385 (≠ T418), T386 (= T419), Q426 (= Q459), M481 (≠ D519), I482 (≠ L520), S483 (= S521), E486 (≠ Q524), H540 (= H576)
- binding magnesium ion: S385 (≠ T418), Q426 (= Q459)
Sites not aligning to the query:
7psmA S. Cerevisiae atm1 in msp1d1 nanodiscs with bound amp-pnp and mg2+ (see paper)
32% identity, 59% coverage: 249:618/623 of query aligns to 217:583/585 of 7psmA
- binding phosphoaminophosphonic acid-adenylate ester: Y354 (= Y386), R358 (≠ A389), S380 (≠ N413), G381 (= G414), G383 (= G416), K384 (= K417), T386 (= T419), Q426 (= Q459), M481 (≠ D519), I482 (≠ L520), S483 (= S521)
Sites not aligning to the query:
7ehlA Cryo-em structure of human abcb8 transporter in nucleotide binding state (see paper)
40% identity, 53% coverage: 290:619/623 of query aligns to 254:563/563 of 7ehlA
Sites not aligning to the query:
7ph3A Amp-pnp bound nanodisc reconstituted msba with nanobodies, spin- labeled at position a60c (see paper)
28% identity, 83% coverage: 103:618/623 of query aligns to 70:577/577 of 7ph3A
- binding phosphoaminophosphonic acid-adenylate ester: Y349 (= Y386), S376 (≠ N413), G377 (= G414), G379 (= G416), K380 (= K417), S381 (≠ T418), T382 (= T419), Q422 (= Q459), L478 (≠ D519), S480 (= S521), G482 (= G523), Q483 (= Q524), H535 (= H576)
- binding magnesium ion: S381 (≠ T418), Q422 (= Q459)
7mewA E. Coli msba in complex with g247 (see paper)
28% identity, 83% coverage: 103:618/623 of query aligns to 65:572/572 of 7mewA
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)
28% identity, 83% coverage: 103:618/623 of query aligns to 72:579/582 of P60752
- C88 (≠ A119) mutation to S: Does not affect ATPase activity.
- E208 (= E244) 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 (vs. gap) mutation to A: Does not reduce substrate binding or nucleotide binding, but decreases ATP-dependent extrusion of substrates.
- A270 (≠ I302) 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 (≠ L347) mutation to S: Does not affect ATPase activity.
- E506 (= E545) 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 (= L550) mutation to P: Loss of ATPase activity; ATP is still bound.
- D512 (= D551) mutation to G: Loss of ATPase activity; ATP is still bound.
- H537 (= H576) 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.
2onjA Structure of the multidrug abc transporter sav1866 from s. Aureus in complex with amp-pnp (see paper)
33% identity, 55% coverage: 274:618/623 of query aligns to 236:576/578 of 2onjA
- binding phosphoaminophosphonic acid-adenylate ester: Y349 (= Y386), I356 (≠ A393), S376 (≠ N413), G377 (= G414), G378 (≠ A415), G379 (= G416), K380 (= K417), S381 (≠ T418), T382 (= T419), Q422 (= Q459), K477 (≠ D519), S479 (= S521), G480 (= G522), E503 (= E545), H534 (= H576)
2hydA Multidrug abc transporter sav1866 (see paper)
33% identity, 55% coverage: 274:618/623 of query aligns to 236:576/578 of 2hydA
8dmmA Structure of the vanadate-trapped msba bound to kdl (see paper)
28% identity, 83% coverage: 103:618/623 of query aligns to 68:575/576 of 8dmmA
- binding adp orthovanadate: Y347 (= Y386), R350 (≠ A389), S374 (≠ N413), G375 (= G414), S376 (≠ A415), G377 (= G416), K378 (= K417), S379 (≠ T418), T380 (= T419), Q420 (= Q459), L476 (≠ D519), S478 (= S521), G479 (= G522), G480 (= G523), H533 (= H576)
- 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 (≠ R114), Y83 (= Y118), R184 (≠ N223), R234 (≠ F270), K239 (≠ A275), I246 (≠ F282), I250 (≠ L286)
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
6bppA E. Coli msba in complex with lps and inhibitor g092 (see paper)
28% identity, 83% coverage: 103:618/623 of query aligns to 69:576/576 of 6bppA
- binding (2E)-3-{6-[(1S)-1-(3-amino-2,6-dichlorophenyl)ethoxy]-4-cyclopropylquinolin-3-yl}prop-2-enoic acid: L168 (≠ A202), A172 (≠ V206), V175 (≠ F209), S176 (≠ H214), I179 (≠ A217), A256 (≠ G291), M288 (≠ F323), L291 (= L326), M292 (≠ R327), K296 (≠ E331)
Query Sequence
>WP_083492049.1 NCBI__GCF_001431535.1:WP_083492049.1
MPASRSSSAPGQSNPSLRERVGAMRNLPPFLRQIWQTSPWLASASLGLRIIRALLPVAML
YVGKLIIDSAVLLSQHDAGFPPFGEALSSGLLTPLLTLLALEFGLAIASDLLGRIVSYAD
SLLSELFTNVTSVRLMEHAASLDLEDFEDPELQDKLDRARRQTMGRMNLMSQLFGQVQDA
ITVASLAVGLLVYAPWLIVLLALALVPAFIGESHFNAAGYSLNFQWTPERRQLDYLRQVG
ASVETAKEVKIFNLHRFLIDRYRLLADRFFHANRALARKRAFWGTLLAALGTLGYYTAYA
YIAWRTVRGDFSIGDLTFLAGSFLRLRQLLEGLLIGFSQVASQALYLDDLFSFFQITPEI
HTRPDAIPVPRPIRQGFVFDNVGFRYPDAETWAVRHLDFQLHAGEVLALVGENGAGKTTL
VKLLARLYDPDEGRILLDGRDLRDYDLDDLRANMGVIFQDFVRYNLTAGENIGVGQVDAL
DDAQRIRDAARRGMAEEVIQALPGGYQQVIGRRFKQGVDLSGGQWQKIAIARAYMRQAQV
MILDEPTAALDARAEYEVFQRFRELSEQRTAVLISHRFSSVRMADRILVLADGRIEASGS
HAQLMAEGGRYAELFELQAAGYR
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