SitesBLAST
Comparing WP_017597434.1 NCBI__GCF_000341125.1:WP_017597434.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 12 hits to proteins with known functional sites (download)
Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see paper)
27% identity, 56% coverage: 67:309/433 of query aligns to 87:318/444 of Q8NLB7
- R103 (= R83) mutation to A: Loss of transport activity.
- W309 (= W300) mutation to V: Loss of transport activity.
- D312 (= D303) mutation to A: Loss of transport activity.
- R313 (= R304) mutation to A: Loss of transport activity.
- I317 (≠ A308) mutation I->H,Y: Loss of transport activity.
Sites not aligning to the query:
- 54 D→A: Loss of transport activity.; D→E: Retains 50% of its transport activity.
- 57 D→A: Loss of transport activity.; D→E: Retains 50% of its transport activity.
- 386 R→A: Loss of transport activity.
P36035 Carboxylic acid transporter protein homolog from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 36% coverage: 68:225/433 of query aligns to 186:330/616 of P36035
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 9 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
- 338 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
4gc0A The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to 6-bromo-6-deoxy-d-glucose (see paper)
22% identity, 70% coverage: 72:375/433 of query aligns to 66:407/475 of 4gc0A
4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
22% identity, 70% coverage: 72:375/433 of query aligns to 66:407/475 of 4gbzA
4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
22% identity, 70% coverage: 72:375/433 of query aligns to 66:407/475 of 4gbyA
P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
22% identity, 70% coverage: 72:375/433 of query aligns to 70:411/491 of P0AGF4
- G83 (= G85) mutation to A: Abolishes xylose transport.
- R133 (= R125) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E145) mutation to A: Abolishes xylose transport.
- R160 (≠ K152) mutation to A: Abolishes xylose transport.
- Q168 (= Q160) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- Q288 (≠ L265) mutation to A: Abolishes xylose transport.
- QQ 288:289 (≠ LQ 265:266) binding beta-D-xylose
- Q289 (= Q266) mutation to A: Strongly decreases xylose transport.
- N294 (≠ T271) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- Y298 (vs. gap) mutation to A: Abolishes xylose transport.
- N325 (≠ E291) mutation to A: No effect on xylose transport.
- G340 (= G306) mutation to A: Abolishes xylose transport.
- R341 (≠ T307) mutation R->A,W: Abolishes xylose transport.
- W392 (≠ R357) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- E397 (≠ Q361) mutation to A: Abolishes xylose transport.
- R404 (= R368) mutation to A: Strongly decreases xylose transport.
Sites not aligning to the query:
- 24 F→A: Decreases xylose transport.
- 415 binding beta-D-xylose
- 416 W→A: Strongly decreases xylose transport.
8bw7A Cryo-em structure of rat slc22a6 bound to alpha-ketoglutaric acid (see paper)
24% identity, 77% coverage: 38:372/433 of query aligns to 90:430/497 of 8bw7A
8bvtA Cryo-em structure of rat slc22a6 bound to probenecid (see paper)
23% identity, 77% coverage: 38:372/433 of query aligns to 99:443/508 of 8bvtA
Sites not aligning to the query:
8bvsA Cryo-em structure of rat slc22a6 bound to tenofovir (see paper)
23% identity, 77% coverage: 38:372/433 of query aligns to 90:434/502 of 8bvsA
O15244 Solute carrier family 22 member 2; Organic cation transporter 2; hOCT2 from Homo sapiens (Human) (see 8 papers)
22% identity, 73% coverage: 61:374/433 of query aligns to 154:469/555 of O15244
- M165 (≠ V75) to I: lower Vmax for MPP(+) transport; no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol; dbSNP:rs8177507
- Y169 (≠ H79) mutation to F: No change in TEA uptake.
- T201 (≠ A111) to M: in dbSNP:rs145450955
- Y241 (≠ A159) mutation to F: Slight decrease in TEA uptake. No change in tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-362. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-362 and F-377.
- Y257 (≠ D183) mutation to F: No change in TEA uptake.
- S270 (= S197) to A: decreased Ki value for TBA inhibition of MPP(+); no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol; dbSNP:rs316019
- Y279 (≠ V207) mutation to F: No change in TEA uptake.
- Y280 (≠ R208) mutation to F: No change in TEA uptake.
- P284 (≠ E212) mutation to A: Decreased TEA and metformin uptake. Decreased tyrosine phosphorylation.
- PESPR 284:288 (≠ EESPV 212:216) Proline-rich sequence
- S286 (= S214) mutation to A: No change in TEA and metformin uptake. No change in tyrosine phosphorylation.
- P287 (= P215) mutation to A: Decreased TEA and metformin uptake. Decreased tyrosine phosphorylation.
- Y362 (≠ L265) mutation to F: Decreased TEA uptake and YES1-mediated tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-241. Strong decrease in TEA uptake; when associated with F-377. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-241 and F-377.
- Y377 (≠ L281) mutation to F: Slight decrease in TEA uptake. No change in tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-362. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-241 and F-362.
- R400 (= R304) to C: lower Vmax and reduced Ki value for TBA inhibition of MPP(+); lower transport efficiency (Vmax/Km) and clearance of cyclo(his-pro); no change in transport efficiency (Vmax/Km) and clearance of salsolinol; dbSNP:rs8177516
- K432 (≠ I337) to Q: lower Km value for MPP(+) and reduced Ki value for TBA inhibition of MPP; no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol; dbSNP:rs8177517
- Y458 (= Y363) mutation to F: No change in TEA uptake.
Sites not aligning to the query:
- 54 P → S: in dbSNP:rs8177504
- 73 Y→F: No change in TEA uptake.
- 92 Y→F: No change in TEA uptake.
- 128 Y→F: No change in TEA uptake.
- 544 Y→F: No change in TEA uptake.
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
22% identity, 68% coverage: 78:373/433 of query aligns to 63:376/446 of A0A0H2VG78
- R102 (= R125) mutation to A: Loss of transport activity.
- I105 (≠ Q128) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E145) mutation to A: Loss of transport activity.
- Q137 (= Q160) mutation to A: Loss of transport activity.
- Q250 (≠ G256) mutation to A: Loss of transport activity.
- Q251 (≠ G257) mutation to A: Loss of transport activity.
- N256 (≠ T262) mutation to A: Loss of transport activity.
- W357 (≠ R357) mutation to A: Loss of transport activity.
Sites not aligning to the query:
- 22 D→N: Affects symport activity. May function as an uniporter.
Q9R0W2 Solute carrier family 22 member 2; Organic cation transporter 2; rOCT2 from Rattus norvegicus (Rat) (see paper)
22% identity, 72% coverage: 65:374/433 of query aligns to 158:469/555 of Q9R0W2
- C451 (≠ A356) Involved in recognition of organic cations and participates in structural changes that occur during translocation of organic cations; mutation to M: Transport activity strongly reduced.
Query Sequence
>WP_017597434.1 NCBI__GCF_000341125.1:WP_017597434.1
MADRTSPTAARPARAAVAAFVGTTIEWFDFYVYATAAGLVFGTLFFPGDIDPMVGLMASF
ATFAVGFFARPLGGVVFGHFGDRLGRKSALVTTLLMMGVATFCVGLLPTYAQVGFVAPLL
LVVLRFVQGIAVGGEWGGAVLMAVESAPEERKTFYGSFAQLGNPAGALLATGSFGLITAW
DSDLLYTWGWRLPFLASCLLVLVGLVVRLKVEESPVFEAARENRAAEPEGPPLRETLRTS
WRAVLLGIGVLPVAVGGYYVVTTFLQAYGVTEAGISEQLILSGLTLAAFVELFATLATAW
LGDRFGTARIVTVGLAAVAVLALPQFLVLETGSAVLIVLMLCLMRVAMAAVYGPIARVLA
QMYPPRVRYTGISVSYQVAGALFGGLSPLACTALFALTGSILSVAVLLVVMALVSIACLS
RAPRHSDAETLPV
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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