SitesBLAST
Comparing WP_012385490.1 NCBI__GCF_000019845.1:WP_012385490.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 10 hits to proteins with known functional sites (download)
Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
28% identity, 45% coverage: 30:225/439 of query aligns to 56:233/444 of Q8NLB7
- D57 (= D31) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- R103 (= R83) mutation to A: 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.
- 309 W→V: Loss of transport activity.
- 312 D→A: Loss of transport activity.
- 313 R→A: Loss of transport activity.
- 317 mutation I->H,Y: Loss of transport activity.
- 386 R→A: Loss of transport activity.
Q9R0W2 Solute carrier family 22 member 2; Organic cation transporter 2; rOCT2 from Rattus norvegicus (Rat) (see paper)
22% identity, 77% coverage: 33:369/439 of query aligns to 126:466/555 of Q9R0W2
- C451 (≠ A354) 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.
8et9A Cryo-em structure of the organic cation transporter 2 in complex with 1-methyl-4-phenylpyridinium (see paper)
24% identity, 92% coverage: 31:433/439 of query aligns to 122:513/517 of 8et9A
Q9Y7Q9 Probable metabolite transporter C2H8.02 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
25% identity, 48% coverage: 14:222/439 of query aligns to 36:256/583 of Q9Y7Q9
Sites not aligning to the query:
- 267 modified: Phosphoserine
- 269 modified: Phosphoserine
- 289 modified: Phosphoserine
- 290 modified: Phosphoserine
- 292 modified: Phosphoserine
- 330 modified: Phosphoserine
8et8A Cryo-em structure of the organic cation transporter 1 in complex with verapamil (see paper)
29% identity, 37% coverage: 61:223/439 of query aligns to 152:293/532 of 8et8A
Sites not aligning to the query:
- binding (2S)-2-(3,4-dimethoxyphenyl)-5-{[2-(3,4-dimethoxyphenyl)ethyl](methyl)amino}-2-(propan-2-yl)pentanenitrile: 31, 35, 353, 360, 378, 381, 385, 449, 469
8et7A Cryo-em structure of the organic cation transporter 1 in complex with diphenhydramine (see paper)
29% identity, 37% coverage: 61:223/439 of query aligns to 152:293/532 of 8et7A
Sites not aligning to the query:
P77589 3-(3-hydroxy-phenyl)propionate transporter; 3HPP transporter; 3-(3-hydroxy-phenyl)propionate:H(+) symporter; 3HPP:H(+) symporter from Escherichia coli (strain K12) (see paper)
30% identity, 36% coverage: 73:231/439 of query aligns to 66:205/403 of P77589
- D75 (= D82) mutation D->A,E: Lack of 3HPP transport activity.
Sites not aligning to the query:
- 27 E→A: Lack of 3HPP transport activity.; E→D: Slight decrease in 3HPP transport activity.
- 272 A→H: 30% increase in 3HPP transport activity.
- 276 K→D: Lack of 3HPP transport activity.
P36035 Carboxylic acid transporter protein homolog from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
23% identity, 70% coverage: 70:375/439 of query aligns to 188:498/616 of P36035
- K338 (vs. gap) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 9 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Q63089 Solute carrier family 22 member 1; Organic cation transporter 1; rOCT1 from Rattus norvegicus (Rat) (see 4 papers)
28% identity, 31% coverage: 33:168/439 of query aligns to 126:250/556 of Q63089
- C155 (≠ T62) mutation to A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-179; S-322; A-358; A-418; S-437; A-470 and A-474.
- C179 (≠ T89) mutation to A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; S-322; A-358; A-418; S-437; A-470 and A-474.
- M212 (≠ I130) mutation to L: No change in TEA and MPP(+) uptake.
- V213 (≠ G131) mutation to G: Decreased TEA uptake. No change in MPP(+) uptake.
- S214 (≠ V132) mutation to G: Decreased TEA and MPP(+) uptake.
- K215 (≠ G133) mutation to Q: Loss of TEA and MPP(+) uptake activity.; mutation to R: Loss of TEA and MPP(+) uptake activity.
- G216 (= G134) mutation to A: Decreased TEA and MPP(+) uptake.
- S217 (≠ E135) mutation to G: No change in TEA and MPP(+) uptake.
- W218 (= W136) mutation to F: Decreased guanidine, histamine, serotonin and TEA uptake. No change in MPP(+) uptake. No change in TEA and MPP(+) affinity. Decreased TEA Vmax. No change in MPP(+) Vmax.; mutation to L: Decreased guanidine, histamine, serotonin, TEA and MPP(+) uptake. Decreased TEA affinity. No change in MPP(+) affinity. Decreased TEA and MPP(+) Vmax.; mutation to Y: Decreased guanidine, histamine, serotonin and TEA uptake. No change in MPP(+) uptake. Increased TEA and MPP(+) affinity. Decreased TEA and MPP(+) Vmax.
- V219 (vs. gap) mutation to L: No change in TEA and MPP(+) uptake.
- S220 (≠ G137) mutation to I: Decreased TEA and MPP(+) uptake.
- G221 (= G138) mutation to A: Decreased TEA and MPP(+) uptake.
- Y222 (≠ A139) mutation to F: No change in guanidine, histamine, serotonin, TEA and MPP(+) uptake. Increased TEA affinity. No change in MPP(+) affinity. Decreased TEA Vmax. No change in MPP(+) Vmax.; mutation to L: Decreased guanidine, serotonin, TEA and MPP(+) uptake. No change in histamine uptake. Increased TEA and MPP(+) affinity. Decreased TEA and MPP(+) Vmax.
- T223 (≠ V140) mutation to I: Decreased TEA uptake. No change in MPP(+) uptake.
- L224 (= L141) mutation to V: Decreased TEA and MPP(+) uptake.
- I225 (≠ L142) mutation to G: No change in TEA and MPP(+) uptake.
- T226 (≠ S143) mutation to A: Decreased TEA uptake. No change in MPP(+) uptake.
- E227 (≠ M144) mutation to D: Loss of TEA and MPP(+) uptake activity.; mutation to Q: Loss of TEA and MPP(+) uptake activity.
- F228 (≠ E145) mutation to I: No change in TEA and MPP(+) uptake.
- V229 (≠ S146) mutation to A: Decreased TEA and MPP(+) uptake.; mutation to L: Loss of TEA and MPP(+) uptake activity.
Sites not aligning to the query:
- 26 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-155; A-179; S-322; A-358; A-418; S-437; A-470 and A-474.
- 286 S→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-292; A-296; A-328 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-292; A-296; A-328 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-292; A-296; A-328 and A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-292; A-296; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-292; A-296; A-328 and A-550.
- 292 S→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-296; A-328 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-286; A-296; A-328 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-296; A-328 and A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-296; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-296; A-328 and A-550.
- 296 T→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-328; A-550. Significant increase of the ASP uptake by PKA activation. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-328; A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-328; A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-328 and A-550.
- 322 C→S: Reduces the activation by MMTS. Abolishes the activation by MMTs; when associated with M-451. Choline affinity is increased fivefold by MMTS. Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; A-358; A-418; S-437; A-470 and A-474. Choline affinity is increased four- to fivefold; when associated with M-451.
- 328 S→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-296 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-296 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-296; A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-296 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-296 and A-550.
- 358 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-418; S-437; A-470 and A-474.
- 418 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; S-437; A-470 and A-474.
- 437 C→S: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-470 and A-474.
- 451 C→M: Reduces the activation by MMTS. Abolishes the activation by MMTs; when associated with S-322. Abolishes the effect of MMTs on choline-induced currents. Choline affinity is not influenced by MMTS. Choline affinity is increased four- to fivefold; when associated with S-322.
- 470 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-437 and A-474.
- 474 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-437 and A-470.
- 475 D→E: Decreased MPP(+) uptake, no change in MPP(+) affinity. Decreased NMN uptake, increased NMN affinity. Decreased choline uptake, increased choline affinity.; D→N: Decreased MPP(+) uptake.; D→R: Decreased MPP(+) uptake.
- 550 T→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-296; A-328. Significant increase of the ASP uptake by PKA activation. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-296 and A-328. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-296; A-328. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-296 and A-328. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-296 and A-328.
O08966 Solute carrier family 22 member 1; Organic cation transporter 1; mOCT1 from Mus musculus (Mouse) (see paper)
25% identity, 48% coverage: 33:242/439 of query aligns to 126:313/556 of O08966
Sites not aligning to the query:
- 32 L→F: Increased trospium uptake. Increased trospium affinity. No change in fenoterol uptake.
- 36 Y→C: Decreased fenoterol uptake. Decreased fenoterol affinity. No change in trospium uptake. No change in terbutaline affinity.
Query Sequence
>WP_012385490.1 NCBI__GCF_000019845.1:WP_012385490.1
MVTDVSETASKRIERRAAIASVIGTTIEWYDFFIYGTAAALIFPKLYFGAGASEGLMESF
STIFVGFLSRPIGAALFGHIGDRVGRKATLVATLTLMGVATVLVGILPDRTSIGAWAGWG
LVVLRFFQGIGVGGEWGGAVLLSMESHQGDRRGFMASLPHIGVPLGLVVSVLAWSACSYW
SGGNLEDGAWRIPFLASGALLVFGLVVRLGVPETPDFVKAQREVRASMPPLIEAIKTQWR
SILLAALIRPGEQASFYMLSTFVVLYGSAQLGLGREFMLNAVLLGAVASCFMVPYFGHLG
DRIGRRRIYLTGAIVMTLFALPYFWLLDTRQPILVIVAILGLMAAHDMMYGPQAAYITES
FPAHIRYTGASLGYQSASIIAGGPAPLVSLWLFNTFGTGYAVGAFLALLGLVSACGAFFL
GREPLPEPARDQQLQPQEV
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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