SitesBLAST
Comparing WP_091521441.1 NCBI__GCF_900115115.1:WP_091521441.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 9 hits to proteins with known functional sites (download)
Q9Y7Q9 Probable metabolite transporter C2H8.02 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
25% identity, 42% coverage: 6:220/514 of query aligns to 35:256/583 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
Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
24% identity, 45% coverage: 27:258/514 of query aligns to 56:269/444 of Q8NLB7
- D57 (= D28) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- R103 (≠ L80) 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.
8fvzA Pipt y150a
23% identity, 60% coverage: 14:320/514 of query aligns to 5:319/433 of 8fvzA
Sites not aligning to the query:
P36035 Carboxylic acid transporter protein homolog from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 34% coverage: 47:223/514 of query aligns to 171:330/616 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)
Q09852 Putative inorganic phosphate transporter C23D3.12 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 32% coverage: 61:227/514 of query aligns to 95:268/559 of Q09852
Sites not aligning to the query:
- 297 modified: Phosphoserine
- 299 modified: Phosphoserine
P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
21% identity, 45% coverage: 3:235/514 of query aligns to 2:246/491 of P0AGF4
- F24 (≠ E25) mutation to A: Decreases xylose transport.
- G83 (≠ T86) mutation to A: Abolishes xylose transport.
- R133 (= R122) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E142) mutation to A: Abolishes xylose transport.
- R160 (= R149) mutation to A: Abolishes xylose transport.
- Q168 (= Q157) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
Sites not aligning to the query:
- 288 Q→A: Abolishes xylose transport.
- 288:289 binding beta-D-xylose
- 289 Q→A: Strongly decreases xylose transport.
- 294 binding beta-D-xylose; 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 beta-D-xylose; W→A: Abolishes xylose transport.
- 397 E→A: Abolishes xylose transport.
- 404 R→A: Strongly decreases xylose transport.
- 415 binding beta-D-xylose
- 416 W→A: Strongly decreases xylose transport.
O42885 Putative inorganic phosphate transporter C8E4.01c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 30% coverage: 69:223/514 of query aligns to 108:273/572 of O42885
Sites not aligning to the query:
- 12 modified: Phosphoserine
- 14 modified: Phosphoserine
- 292 modified: Phosphoserine
- 296 modified: Phosphoserine
P25297 Inorganic phosphate transporter PHO84 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 6 papers)
22% identity, 59% coverage: 15:316/514 of query aligns to 66:428/587 of P25297
- C145 (≠ A97) mutation to S: No significant effect on transport activity; when associated with S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
- F160 (= F112) mutation to C: Reduces phosphate binding, transport and signaling activities.
- R168 (= R122) mutation to A: Reduces transport activity. No significant effects on affinity for inorganic phosphate. No significant effects on growth rates.; mutation to C: Abolishes transport and signaling activities.; mutation to E: Reduces transport activity. Moderately reduces affinity for inorganic phosphate. No significant effects on growth rates.; mutation to Q: Reduces transport activity. Moderately reduces affinity for inorganic phosphate. Moderately reduces growth rates under low phosphate conditions. No significant effects on growth rates under high phosphate conditions.
- G172 (= G126) mutation to C: Abolishes transport and signaling activities.
- G174 (≠ A128) mutation to C: Abolishes transport and signaling activities.
- G176 (= G130) mutation to C: Abolishes transport and signaling activities.
- D178 (≠ E132) mutation D->E,N: Reduces transport activity. No significant effects on affinity for inorganic phosphate. No significant effects on signaling activities. No significant effects on growth rates.
- Y179 (= Y133) mutation to A: Significantly reduces transport activity. Causes pronounced increase in secreted phosphatase activity under high phosphate conditions. Reduces growth rates under low phosphate conditions. Slightly reduces signaling activity.; mutation to G: Abolishes transport activity. Causes pronounced increase in secreted phosphatase activity under high phosphate conditions. Reduces growth rates under low phosphate conditions. Abolishes signaling activity.; mutation Y->S,F: No significant effects on transport activity. No significant effects on growth rates under low phosphate conditions. Does not affect patterns of secreted phosphatase activities under low and high phosphate conditions. No significant effects on signaling activity.
- C237 (vs. gap) mutation to S: No significant effect on transport activity; when associated with S-145, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
- C241 (≠ T179) mutation to S: No significant effect on transport activity; when associated with S-145, S-237, S-245, S-263, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
- C245 (≠ F183) mutation to S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-263, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
- C263 (≠ S202) mutation to S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
- K298 (vs. gap) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); mutation to A: No significant effect on membrane localization under low phosphate conditions and internalization after phosphate addition. Strongly affects vacuolar sorting of the protein after internalization.
- 304:327 (vs. 223:229, 13% identical) mutation Missing: Increases transport activity. Has no significant effect on membrane localization under low phosphate conditions. Results in severely delayed internalization after phosphate addition.
- C335 (vs. gap) mutation to S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-399, S-434, S-455, S-474, S-510 and S-519.
- D358 (≠ G254) mutation to E: Abolishes transport activity. Causes pronounced increase in secreted phosphatase activity under high phosphate conditions. Moderately decreases signaling activities. Significantly reduces growth rates under low phosphate conditions. No significant effects on growth rates under high phosphate conditions.; mutation to N: Significantly reduces transport activity. No significant effects on affinity for inorganic phosphate. Causes pronounced increase in secreted phosphatase activity under high phosphate conditions. No significant effects on signaling activities. Significantly reduces growth rates under low phosphate conditions. No significant effects on growth rates under high phosphate conditions.
- V392 (≠ L283) mutation to C: Reduces transport and signaling activities.
- C399 (≠ G290) mutation to S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-434, S-455, S-474, S-510 and S-519.
- V408 (≠ L300) mutation to C: Reduces signaling activity and enhances transport activity.
Sites not aligning to the query:
- 6 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
- 434 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-455, S-474, S-510 and S-519.
- 455 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-474, S-510 and S-519.
- 473 E→K: No significant effects on transport activity. No significant effects on affinity for inorganic phosphate. No significant effects on growth rates.; E→Q: No significant effects on transport activity. Reduces affinity for inorganic phosphate. No significant effects on growth rates.
- 474 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-510 and S-519.
- 492 mutation K->A,Q: No significant effects on transport activity. Reduces affinity for inorganic phosphate. No significant effects on growth rates.; K→E: Reduces transport activity. Reduces affinity for inorganic phosphate. Significantly reduces growth rates under low phosphate conditions. No significant effects on growth rates under high phosphate conditions.
- 510 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-474 and S-519.
- 519 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-474 and S-510.
Q9Z2I6 Synaptic vesicle glycoprotein 2C; Synaptic vesicle protein 2C from Rattus norvegicus (Rat) (see 3 papers)
33% identity, 17% coverage: 70:156/514 of query aligns to 204:282/727 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.
Query Sequence
>WP_091521441.1 NCBI__GCF_900115115.1:WP_091521441.1
MNNTETKKSSIWSVIMASSMGTLIEWYDFYIFGSLAIVLSTKFFPSDNPTAAFLSTLATF
AAGFVVRPFGALFFGRLGDLIGRKYTFMVTLMLMGGATFVIGCVPSYESIGFVAPVIVLV
MRLLQGLALGGEYGGAATYVAEHAPKGQRGFWTSWIQTTATVGLFISLIVILITRSVMTE
EQFDLWGWRVPFWLSIVMVYISYLIRKNMSESPEFAKAKKEGKTSTNPLKESFGNRYNLK
FVLLALFGATMGQGVIWYTGQFYAMSYIKTVMFVDSNQVDGLLGIALLLGTPFFVFFGWL
SDKVGRKPILLAGMLIAIISYRPIYRAMYASTDTNLKTEMVDKRIASAEIKTTNAASDSI
YKVKKFYTDGTEYSETTTVHLKDGVANITEKGDVDKHVKKTMFITSSIKWKLVFLVFVQV
LFVTMVYGPIAAFLVEMFPVKIRYTSMSLPYHIGNGIFGGLLPAISTYFVANAEKTGHSE
FFLEGLWYPIIVGAISFVIGFIYINKKVTKYSDK
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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