SitesBLAST
Comparing WP_013403835.1 NCBI__GCF_000166355.1:WP_013403835.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
41% identity, 96% coverage: 16:433/436 of query aligns to 9:430/433 of 6f2wA
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
39% identity, 98% coverage: 7:433/436 of query aligns to 8:436/438 of O34739
- C94 (≠ F93) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ V140) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ L167) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ T288) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- C415 (≠ S412) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
P82251 b(0,+)-type amino acid transporter 1; b(0,+)AT1; Glycoprotein-associated amino acid transporter b0,+AT1; Solute carrier family 7 member 9 from Homo sapiens (Human) (see 11 papers)
26% identity, 98% coverage: 7:433/436 of query aligns to 26:458/487 of P82251
- V40 (= V21) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ VIGSG 24:28) binding L-arginine
- I44 (= I25) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ K32) to F: in CSNU; uncertain significance
- P52 (≠ A33) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ L51) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y80) to H: in CSNU; uncertain significance
- G105 (= G86) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W95) to R: in CSNU; uncertain significance
- I120 (≠ Y101) to L: in CSNU; uncertain significance
- T123 (≠ A104) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (vs. gap) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ L121) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ N147) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ V159) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G172) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (= L194) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (= A195) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (≠ S198) to D: in CSNU; decreased amino acid transport activity
- W230 (= W201) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (= D204) binding L-arginine; mutation to A: Complete loss of amino acid transport activity.
- W235 (= W206) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ S208) mutation to A: Reduces amino acid transport activity.
- G259 (= G230) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ L232) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ A257) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ A293) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ G296) to E: in CSNU; uncertain significance
- V330 (≠ A302) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M303) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (≠ T305) to Q: in CSNU; decreased amino acid transport activity; dbSNP:rs769576205; to W: in CSNU; severe loss of amino acid transport activity; dbSNP:rs121908484
- A354 (≠ S328) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ M353) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ T356) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (= W357) mutation to A: Complete loss of amino acid transport activity.
- Y386 (= Y360) mutation to A: Loss of amino acid transport activity.
- K401 (= K378) to E: in CSNU; uncertain significance; dbSNP:rs760264924
- L426 (≠ V402) to P: in CSNU; uncertain significance
Sites not aligning to the query:
- 482 P → L: in CSNU; severe loss of amino acid transport activity; no effect on localization to the apical membrane; dbSNP:rs146815072; mutation P->A,G,S,V: No effect on amino acid transport activity.; mutation P->F,I,M,W: Decreased amino acid transport activity.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
26% identity, 96% coverage: 17:433/436 of query aligns to 7:429/458 of 6li9B
Q9UPY5 Cystine/glutamate transporter; Amino acid transport system xc-; Calcium channel blocker resistance protein CCBR1; Solute carrier family 7 member 11; xCT from Homo sapiens (Human) (see 4 papers)
24% identity, 98% coverage: 2:430/436 of query aligns to 35:468/501 of Q9UPY5
- C86 (≠ G53) mutation to S: Does not affect L-cystine transport activity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- R135 (≠ T102) binding L-glutamate; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ Q125) modified: Interchain (with C-210 in SLC3A2); mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- Q191 (= Q154) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ L160) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435.
- K198 (= K161) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ W201) binding L-glutamate
- F254 (≠ N211) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ I228) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- C327 (≠ I285) mutation to A: Does not affect L-glutamate transport activity. Does not affect location at cell membrane Does not affect expression level.; mutation to L: Loss of L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Loss of inhibitio nof L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid. Decrease L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to T: Does not affect L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.
- F336 (≠ L294) mutation to A: Decreases L-cystine transport activity about 50%. Increases sensitivity to erastin-induced ferroptosis. Significantly decreases the L-cystine transport activity.; mutation to Y: Does not affect L-cystine transport activity.
- R396 (≠ T356) mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.; mutation to N: Loss of L-cystine transport activity.
- C414 (≠ N377) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- C435 (≠ G397) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
8xpuB Overall structure of the lat1-4f2hc bound with jph203 (see paper)
28% identity, 99% coverage: 5:436/436 of query aligns to 1:439/464 of 8xpuB
- binding Nanvuranlat: I20 (≠ V24), G22 (= G26), G24 (= G28), S101 (≠ I105), I104 (≠ A108), V105 (≠ L109), F209 (≠ W201), A210 (= A202), Y211 (= Y203), G212 (≠ D204), Y216 (≠ S208), I354 (≠ T349), N361 (≠ T356)
8x0wB Overall structure of the lat1-4f2hc bound with leu
28% identity, 99% coverage: 5:436/436 of query aligns to 1:439/464 of 8x0wB
8idaB Overall structure of the lat1-4f2hc bound with tyrosine
28% identity, 99% coverage: 5:436/436 of query aligns to 1:439/464 of 8idaB
7dsqB Overall structure of the lat1-4f2hc bound with 3,5-diiodo-l-tyrosine (see paper)
28% identity, 99% coverage: 5:436/436 of query aligns to 1:439/464 of 7dsqB
7dsnB Overall structure of the lat1-4f2hc bound with jx-119 (see paper)
28% identity, 99% coverage: 5:436/436 of query aligns to 1:439/464 of 7dsnB
- binding (2~{S})-2-azanyl-7-[[2-(1,3-benzoxazol-2-yl)phenyl]methoxy]-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: T19 (≠ M23), I20 (≠ V24), G22 (= G26), S23 (= S27), G24 (= G28), I97 (≠ Y101), I104 (≠ A108), F209 (≠ W201), A210 (= A202), G212 (≠ D204), I354 (≠ T349), N361 (≠ T356)
- binding cholesterol hemisuccinate: F109 (= F113), Y145 (≠ I145), K148 (= K148), V153 (≠ L153), Q326 (≠ R321)
Sites not aligning to the query:
7dslB Overall structure of the lat1-4f2hc bound with jx-078 (see paper)
28% identity, 99% coverage: 5:436/436 of query aligns to 1:439/464 of 7dslB