SitesBLAST
Comparing WP_011799906.1 NCBI__GCF_000015505.1:WP_011799906.1 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 15 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)
26% identity, 39% coverage: 9:222/552 of query aligns to 33:255/583 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
O42885 Putative inorganic phosphate transporter C8E4.01c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 40% coverage: 10:230/552 of query aligns to 40:277/572 of O42885
Sites not aligning to the query:
- 12 modified: Phosphoserine
- 14 modified: Phosphoserine
- 292 modified: Phosphoserine
- 296 modified: Phosphoserine
Q09852 Putative inorganic phosphate transporter C23D3.12 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
22% identity, 57% coverage: 10:324/552 of query aligns to 38:423/559 of Q09852
- S297 (vs. gap) modified: Phosphoserine
- S299 (vs. gap) modified: Phosphoserine
8fvzA Pipt y150a
26% identity, 56% coverage: 14:322/552 of query aligns to 2:318/433 of 8fvzA
Sites not aligning to the query:
P25297 Inorganic phosphate transporter PHO84 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 6 papers)
22% identity, 39% coverage: 4:219/552 of query aligns to 52:277/587 of P25297
- C145 (≠ S100) 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 (≠ V115) mutation to C: Reduces phosphate binding, transport and signaling activities.
- R168 (= R125) 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 (= G129) mutation to C: Abolishes transport and signaling activities.
- G174 (≠ A131) mutation to C: Abolishes transport and signaling activities.
- G176 (= G133) mutation to C: Abolishes transport and signaling activities.
- D178 (≠ E135) 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 (= Y136) 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 (vs. gap) 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 (vs. gap) 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 (≠ S205) 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.
Sites not aligning to the query:
- 6 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
- 298 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); K→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 mutation Missing: Increases transport activity. Has no significant effect on membrane localization under low phosphate conditions. Results in severely delayed internalization after phosphate addition.
- 335 C→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.
- 358 D→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.; D→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.
- 392 V→C: Reduces transport and signaling activities.
- 399 C→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.
- 408 V→C: Reduces signaling activity and enhances transport activity.
- 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.
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)
25% identity, 36% coverage: 26:224/552 of query aligns to 52:229/444 of Q8NLB7
- D54 (≠ E28) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- D57 (= D31) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- R103 (≠ M83) mutation to A: Loss of transport activity.
Sites not aligning to the query:
- 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.
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
28% identity, 43% coverage: 78:316/552 of query aligns to 63:310/446 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 (≠ G255) mutation to A: Loss of transport activity.
- Q251 (= Q256) mutation to A: Loss of transport activity.
- N256 (vs. gap) mutation to A: Loss of transport activity.
Sites not aligning to the query:
- 22 D→N: Affects symport activity. May function as an uniporter.
- 357 W→A: Loss of transport activity.
P36035 Carboxylic acid transporter protein homolog from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
25% identity, 28% coverage: 69:221/552 of query aligns to 187:325/616 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)
6rw3A The molecular basis for sugar import in malaria parasites. (see paper)
26% identity, 52% coverage: 53:341/552 of query aligns to 51:343/437 of 6rw3A
Sites not aligning to the query:
Q9Z2I6 Synaptic vesicle glycoprotein 2C; Synaptic vesicle protein 2C from Rattus norvegicus (Rat) (see 3 papers)
27% identity, 26% coverage: 73:218/552 of query aligns to 204:346/727 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)
27% identity, 26% coverage: 73:218/552 of query aligns to 204:346/727 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.
O08966 Solute carrier family 22 member 1; Organic cation transporter 1; mOCT1 from Mus musculus (Mouse) (see paper)
28% identity, 31% coverage: 72:244/552 of query aligns to 162:313/556 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.
Q9LT15 Sugar transport protein 10; AtSTP10; D-glucose-H(+) symport protein STP10; D-glucose-proton symporter STP10; Hexose transporter 10 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
28% identity, 28% coverage: 74:230/552 of query aligns to 95:239/514 of Q9LT15
- E162 (= E145) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
- Q177 (= Q160) binding beta-D-glucose; mutation to A: Reduces affinity for glucose 37-fold.
- I184 (≠ L167) mutation to A: Reduces affinity for glucose 3-fold.
Sites not aligning to the query:
- 39 F→A: Reduces affinity for glucose 8-fold.
- 43 L→A: Reduces affinity for glucose 150-fold and turns STP10 into a low affinity transporter.
- 77 modified: Disulfide link with 449; C→A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
- 295 binding beta-D-glucose
- 296 binding beta-D-glucose
- 301 binding beta-D-glucose
- 332 binding beta-D-glucose
- 344 D→N: Abolishes glucose transport activity; when associated with Q-162.
- 410 binding beta-D-glucose
- 449 modified: Disulfide link with 77; C→A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
7aaqA Sugar/h+ symporter stp10 in outward occluded conformation (see paper)
28% identity, 28% coverage: 74:230/552 of query aligns to 75:219/487 of 7aaqA
Sites not aligning to the query:
Q12300 High glucose sensor RGT2; Low-affinity glucose receptor RGT2; Low-affinity transporter-like sensor RGT2; Restores glucose transport protein 2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
24% identity, 45% coverage: 72:322/552 of query aligns to 158:432/763 of Q12300
- R231 (= R152) mutation to K: In RGT2-1; constitutively signaling glucose receptor.
Sites not aligning to the query:
- 684:690 SIISDST→AIIADAA: In Rgt2(4SA); Abolishes Yck-dependent phosphorylation, interaction with MTH1 and STD1, and glucose signaling, but does not affect protein stability.
Query Sequence
>WP_011799906.1 NCBI__GCF_000015505.1:WP_011799906.1
MATTVDKSVMTAEQRKVIFASSLGTVFEWYDFYLYGSLAAIIAKQFFSGLDAGSAFIFAL
LAFAAGFIVRPFGALVFGRLGDMIGRKYTFLVTIVIMGLSTFIVGLLPSYASIGVAAPVI
LIALRMLQGLALGGEYGGAAVYVAEHAPEGRRGAYTSWIQTTATMGLFLSLLVILGVRTA
VGEVAFADWGWRVPFVVSILLLAVSVYIRLSMNESPAFQKMKAEGRTSKAPLSESFGQWK
NLKIVILALVGLTAGQAVVWYSGQFYSLFFLTQALKVDGPTANILVAYSLLLATPFFVVF
GTLSDKIGRKPIIMAGCLLAALTYFPVFTALTKAANPDLAEAQARNQVVVTADPKECSFQ
FNPTGTAKFTSSCDIAKQVLAGASVSYENVAGPAGTVASIKIGQNAIPSYTAKGLSADEA
RKKDVEFKKLIGDDLKAAGYPSKADPAKMDKVMVTAILFYLVLLVTMVYGPIAAMLVEMF
PTRIRYTSMSLPYHIGNGWFGGLLPTTAFAIVAQTGNMYNGLWYPIIIAGVTFVVGTLFV
KETKDYDIYAND
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