SitesBLAST
Comparing AO356_29245 FitnessBrowser__pseudo5_N2C3_1:AO356_29245 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)
Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
31% identity, 89% coverage: 16:413/447 of query aligns to 39:411/444 of Q8NLB7
- D54 (= D33) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- D57 (= D36) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- R103 (= R82) mutation to A: Loss of transport activity.
- W309 (= W311) mutation to V: Loss of transport activity.
- D312 (= D314) mutation to A: Loss of transport activity.
- R313 (≠ K315) mutation to A: Loss of transport activity.
- I317 (≠ K319) mutation I->H,Y: Loss of transport activity.
- R386 (= R388) mutation to A: Loss of transport activity.
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 96% coverage: 2:428/447 of query aligns to 10:434/448 of Q51955
- D41 (= D33) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- D44 (= D36) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- G85 (= G77) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (= D81) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G84) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to C: No change in 4-HBA transport and chemotaxis.; mutation G->L,V: Abolishes 4-HBA transport and chemotaxis.; mutation to Q: Decrease in 4-HBA transport and strong decrease in chemotaxis.
- R124 (= R116) mutation to A: Abolishes 4-HBA transport.
- E144 (= E136) mutation to A: Strong decrease in 4-HBA transport.
- H183 (≠ Q175) mutation to A: Decrease in 4-HBA transport and chemotaxis.
- D323 (= D314) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- H328 (≠ K319) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to R: Decrease in 4-HBA transport and loss of chemotaxis.
- R386 (= R376) mutation to A: Strong decrease in 4-HBA transport.
- R398 (= R388) mutation to A: Abolishes 4-HBA transport.
Sites not aligning to the query:
- 444 H→A: No change in 4-HBA transport and chemotaxis.
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
28% identity, 94% coverage: 22:442/447 of query aligns to 23:443/452 of Q5EXK5
- D82 (= D81) mutation to A: Loss of activity.
- V311 (≠ W311) mutation to W: Loss of activity.
- D314 (= D314) mutation to A: Loss of activity.
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, 92% coverage: 26:438/447 of query aligns to 20:398/403 of P77589
- E27 (≠ D33) mutation to A: Lack of 3HPP transport activity.; mutation to D: Slight decrease in 3HPP transport activity.
- D75 (= D81) mutation D->A,E: Lack of 3HPP transport activity.
- A272 (≠ W311) mutation to H: 30% increase in 3HPP transport activity.
- K276 (= K315) mutation to D: Lack of 3HPP transport activity.
Q02563 Synaptic vesicle glycoprotein 2A; Synaptic vesicle protein 2; Synaptic vesicle protein 2A from Rattus norvegicus (Rat) (see 2 papers)
28% identity, 46% coverage: 17:221/447 of query aligns to 163:380/742 of Q02563
- DMCLS 196:200 (≠ DMNID 50:54) mutation Missing: No change in uptake of C.botulinum neurotoxin type D (BoNT/D, botD) or C.botulinum neurotoxin type E (BoNT/E).
- 321:331 (vs. gap) mutation Missing: No change in uptake of BoNT/D or BoNT/E.
Sites not aligning to the query:
- 498 N→Q: No change in uptake of BoNT/E or C.botulinum neurotoxin type A (BoNT/A, botA) by mouse SV2A/SV2B knockout neurons; SV2A apparent molecular weight decreases. No change in uptake of BoNT/E; when associated with Q-548. No change in uptake of BoNT/D.
- 548 N→Q: No change in uptake of BoNT/E or BoNT/A by mouse SV2A/SV2B knockout neurons; SV2A apparent molecular weight decreases. No change in uptake of BoNT/E; when associated with Q-498. No change in uptake of BoNT/D.
- 570:573 RLVN→TLVQ: Restores apparent molecular weight to wild-type, does not restore uptake of BoNT/E.
- 573 N→Q: BoNT/E not taken up by mouse SV2A/SV2B knockout neurons, decreased uptake of BoNT/A; SV2A apparent molecular weight decreases. No change in uptake of BoNT/D.
Q9Z2I6 Synaptic vesicle glycoprotein 2C; Synaptic vesicle protein 2C from Rattus norvegicus (Rat) (see 3 papers)
28% identity, 46% coverage: 17:221/447 of query aligns to 149:366/727 of Q9Z2I6
Sites not aligning to the query:
- 1:57 Interaction with SYT1
- 529:566 (Microbial infection) C.botulinum neurotoxin type A-binding
- 559 N→A: Loss of one glycosylation site. No effect on C.botulinum neurotoxin type A (BoNT/A, botA) binding, but reduces the uptake of BoNT/A.
Q496J9 Synaptic vesicle glycoprotein 2C from Homo sapiens (Human) (see 4 papers)
28% identity, 46% coverage: 17:221/447 of query aligns to 149:366/727 of Q496J9
Sites not aligning to the query:
- 519:563 (Microbial infection) C.botulinum neurotoxin type A-binding
- 534 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 559 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: No change in interaction with C.botulinum neurotoxin type A heavy chain (botA, BoNT/A HC). Decreased molecular weight probably due to glycosylation loss, decreased interaction with BoNT/A HC.; N→Q: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC. Greater reduction in weight; when associated with Q-565.
- 561 S→A: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC.
- 563 F→A: No longer interacts with BoNT/A HC.
- 565 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Decreased molecular weight probably due to glycosylation loss, no change in binding to BoNT/A heavy chain. Greater reduction in weight; when associated with Q-559.
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
26% identity, 43% coverage: 36:227/447 of query aligns to 22:213/446 of A0A0H2VG78
- D22 (= D36) mutation to N: Affects symport activity. May function as an uniporter.
- R102 (= R116) mutation to A: Loss of transport activity.
- I105 (≠ A119) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E136) mutation to A: Loss of transport activity.
- Q137 (≠ F151) mutation to A: Loss of transport activity.
Sites not aligning to the query:
- 250 Q→A: Loss of transport activity.
- 251 Q→A: Loss of transport activity.
- 256 N→A: Loss of transport activity.
- 357 W→A: Loss of transport activity.
O57379 Solute carrier family 22 member 6; Organic anion transporter 1; Renal organic anion transporter 1; ROAT1; fROAT1 from Pseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus) (see paper)
24% identity, 74% coverage: 68:398/447 of query aligns to 156:488/562 of O57379
- K394 (= K315) mutation to A: Reduced transport activity.
- R478 (= R388) mutation to D: Reduced transport activity.
Sites not aligning to the query:
- 34 H→I: Reduced transport activity.
P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
25% identity, 49% coverage: 34:252/447 of query aligns to 25:264/491 of P0AGF4
- G83 (= G84) mutation to A: Abolishes xylose transport.
- R133 (= R116) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E136) mutation to A: Abolishes xylose transport.
- R160 (= R143) mutation to A: Abolishes xylose transport.
- Q168 (vs. gap) binding ; mutation to A: Abolishes xylose transport.
Sites not aligning to the query:
- 24 F→A: Decreases xylose transport.
- 288 Q→A: Abolishes xylose transport.
- 288:289 binding
- 289 Q→A: Strongly decreases xylose transport.
- 294 binding ; N→A: Abolishes xylose transport.
- 298 Y→A: Abolishes xylose transport.
- 325 N→A: No effect on xylose transport.
- 340 G→A: Abolishes xylose transport.
- 341 mutation R->A,W: Abolishes xylose transport.
- 392 binding ; W→A: Abolishes xylose transport.
- 397 E→A: Abolishes xylose transport.
- 404 R→A: Strongly decreases xylose transport.
- 415 binding
- 416 W→A: Strongly decreases xylose transport.
4gc0A The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to 6-bromo-6-deoxy-d-glucose (see paper)
25% identity, 49% coverage: 34:252/447 of query aligns to 21:260/475 of 4gc0A
Sites not aligning to the query:
4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
25% identity, 49% coverage: 34:252/447 of query aligns to 21:260/475 of 4gbzA
Sites not aligning to the query:
4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
25% identity, 49% coverage: 34:252/447 of query aligns to 21:260/475 of 4gbyA
Sites not aligning to the query:
P25297 Inorganic phosphate transporter PHO84 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 76% coverage: 68:405/447 of query aligns to 114:509/587 of P25297
- K298 (≠ Q223) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Sites not aligning to the query:
- 6 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
8bw7A Cryo-em structure of rat slc22a6 bound to alpha-ketoglutaric acid (see paper)
23% identity, 74% coverage: 66:397/447 of query aligns to 124:447/497 of 8bw7A
Q8VC69 Solute carrier family 22 member 6; Kidney-specific transport protein; Novel kidney transcript; mNKT; Organic anion transporter 1; mOAT1; Renal organic anion transporter 1; mROAT1 from Mus musculus (Mouse) (see 2 papers)
23% identity, 74% coverage: 66:397/447 of query aligns to 136:469/545 of Q8VC69
- C183 (≠ S113) mutation to A: Decreased cell surface expression level and PAH transport activity. Complete loss of PAH transport activity; when associated with A-49; A-78; A-99; A-122; A-172; A-200; A-362; A-335; A-379; A-402; A-427 and A-434.
- C434 (≠ L362) mutation to A: Decreased cell surface expression level and PAH transport activity. 80% decrease of PAH transport activity; when associated with A-49; A-122 and A-183. Complete loss of PAH transport activity; when associated with A-49; A-78; A-99; A-122; A-172; A-183; A-200; A-362; A-335; A-379; A-402 and A-427.
Sites not aligning to the query:
- 39 N→Q: Complete loss of PAH transport activity.
- 49 C→A: Decreased cell surface expression level and PAH transport activity. Complete loss of PAH transport activity; when associated with A-78; A-99; A-122; A-172; A-183; A-200; A-362; A-335; A-379; A-402; A-427 and A-434.
- 56 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 86 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 91 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 107 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 122 C→A: Decreased cell surface expression level and PAH transport activity. Complete loss of PAH transport activity; when associated with A-49; A-78; A-99; A-172; A-183; A-200; A-362; A-335; A-379; A-402; A-427 and A-434.
8bvsA Cryo-em structure of rat slc22a6 bound to tenofovir (see paper)
23% identity, 74% coverage: 66:397/447 of query aligns to 124:451/502 of 8bvsA
8bvtA Cryo-em structure of rat slc22a6 bound to probenecid (see paper)
23% identity, 74% coverage: 66:397/447 of query aligns to 133:460/508 of 8bvtA
Sites not aligning to the query:
Q9VCA2 Organic cation transporter protein from Drosophila melanogaster (Fruit fly) (see paper)
26% identity, 74% coverage: 66:397/447 of query aligns to 138:474/548 of Q9VCA2
Sites not aligning to the query:
- 97 modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q4U2R8 Solute carrier family 22 member 6; Organic anion transporter 1; hOAT1; PAH transporter; hPAHT; Renal organic anion transporter 1; hROAT1 from Homo sapiens (Human) (see 6 papers)
24% identity, 74% coverage: 66:397/447 of query aligns to 142:475/563 of Q4U2R8
- Y230 (= Y154) mutation to A: Loss of membrane protein expression and little uptake of cidofovir.
- K431 (≠ A354) mutation to A: Decrease in the level of membrane protein expression and 70 % loss of PAH uptake.
- F438 (≠ L361) mutation to A: Decrease in the level of membrane protein expression, 70 % loss of PAH uptake, increased affinity for cidofovir, lower Vmax for PAH, and lower Km and Vmax for cidofovir.
Sites not aligning to the query:
- 7 L → P: in dbSNP:rs1415632329
- 30 L→A: Complete loss of PAH transport activity.
- 36 T→A: Complete loss of PAH transport activity.
- 39 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Complete loss of PAH transport activity.
- 50 R → H: lower Vmax; increase in substrate affinity and increase in the affinity for the nucleoside phosphonate analogs cidofovir, adefovir and tenofovir; dbSNP:rs11568626
- 56 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 92 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 97 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 104 P → L: in dbSNP:rs11568627
- 113 modified: carbohydrate, N-linked (GlcNAc...) asparagine
Query Sequence
>AO356_29245 FitnessBrowser__pseudo5_N2C3_1:AO356_29245
MQPVNVYALAVDSTFNRFHGLILFWCVLILIIDGYDLAVVGAALPAIMKDMNIDPTSAGV
MAGAALFGTMLGAIFLGTLADRIGRPKMIAICVALFSIFTAAAGLTSDPISFSISRFVAG
LGIGGVLPICTAQMGEFSPLKLRTRLVTLVFAGYSVGGILVALTGKQLIESYGWQWVFYV
ALLPVLLIPLILKTMPESIGYLLKTGRQEELRAIARKIDPTLQIDENTVMVGNAAVLDKQ
QAPVRHLFKEGRGFSTVMIWAAFMTGLFMVYALNSWLTKLMAMAGFSLGSALNFVIVFNV
GAIVGAIGGGWLSDKLNIKHVLVGFYIVGAIALTVLGYTRSTTLLFPVVFVVGASTLGTQ
LLAYAYAGDFYPSTIRSTGVGFASGVGRIGAIVAPVLIGWLVSLNLPLEKNFMAISLAGL
IGAAAVTLINQSRADSTHVRKAAALTP
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