SitesBLAST
Comparing WP_013091679.1 NCBI__GCF_000092885.1:WP_013091679.1 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)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
51% identity, 97% coverage: 9:481/488 of query aligns to 3:456/456 of 5oqtA
- binding alanine: I38 (= I44), G40 (= G46), T41 (≠ A47), G42 (= G48), F226 (= F251), A227 (= A252), I229 (= I254)
- binding : E24 (≠ T30), G26 (= G32), F28 (≠ T34), D29 (≠ S35), M32 (≠ A38), A176 (= A193), R177 (= R194), A184 (= A201), A188 (≠ T205), L192 (≠ A209), Q294 (≠ L319), V297 (≠ F322)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
51% identity, 97% coverage: 9:481/488 of query aligns to 5:458/458 of 6f34A
- binding arginine: I40 (= I44), G42 (= G46), T43 (≠ A47), G44 (= G48), E115 (= E119), Y116 (= Y120), A119 (≠ G123), F228 (= F251), A229 (= A252), I231 (= I254), V314 (= V337)
- binding cholesterol: W201 (≠ F216), Y202 (≠ F217)
- binding : G28 (= G32), F30 (≠ T34), D31 (≠ S35), M34 (≠ A38), A178 (= A193), R179 (= R194), A186 (= A201), I187 (≠ V202), A190 (≠ T205), L194 (≠ A209), Q296 (≠ L319), V299 (≠ F322)
P30825 High affinity cationic amino acid transporter 1; CAT-1; CAT1; Ecotropic retroviral leukemia receptor homolog; Ecotropic retrovirus receptor homolog; Solute carrier family 7 member 1; System Y+ basic amino acid transporter from Homo sapiens (Human) (see paper)
35% identity, 84% coverage: 7:418/488 of query aligns to 13:431/629 of P30825
- N226 (= N230) modified: carbohydrate, N-linked (GlcNAc...) asparagine
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
26% identity, 94% coverage: 18:478/488 of query aligns to 2:433/445 of P60061
- I23 (= I44) binding agmatine; binding L-arginine
- S26 (≠ A47) binding L-arginine
- Y93 (≠ A109) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ I112) binding agmatine; binding L-arginine
- C97 (≠ G113) binding agmatine
- N101 (≠ E119) binding agmatine; mutation to A: Vmax for Arg-Agm exchange 1% of wild-type, KM increases 3-fold.; mutation to D: Nearly wild-type Arg-Agm exchange.
- M104 (= M122) binding agmatine; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F251) binding L-arginine; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A252) binding agmatine
- I205 (= I254) binding agmatine; binding L-arginine; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ L334) binding agmatine; mutation W->C,H,L: Loss of Arg-Agm exchange.; mutation W->F,Y: Less than 20% Arg-Agm exchange activity. Vmax 15% of wild-type rate.
- S357 (≠ V399) binding L-arginine; mutation to A: 20% decreased affinity for Arg, 40% decrease affinity for Agm.
P60063 Arginine/agmatine antiporter from Escherichia coli O157:H7 (see 3 papers)
26% identity, 94% coverage: 18:478/488 of query aligns to 2:433/445 of P60063
- N22 (≠ A43) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (= I44) binding L-arginine
- GSG 25:27 (≠ GAG 46:48) Helix-breaking GSG motif TM1
- S26 (≠ A47) binding L-arginine; mutation to K: 5% Agm antiport.
- G27 (= G48) binding L-arginine
- Y74 (= Y97) mutation to A: 50% antiport activity at pH 6.0, 10-fold higher than wild-type antiport activity at pH 7.5, i.e. loss of pH-dependence of substrate transport. No change in binding of Arg or Agm.; mutation Y->C,H,L,M,Q,S: Loss of pH-dependence of substrate transport.; mutation to F: Approximately wild-type antiport.
- Y87 (vs. gap) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (≠ A109) mutation to A: Reduced binding affinity for Arg, no binding to Agm. 25% Agm antiport.; mutation to K: Almost no binding to both Arg and Agm. 5% Agm antiport.
- A96 (≠ I112) binding L-arginine
- C97 (≠ G113) binding L-arginine
- N101 (≠ E119) binding L-arginine
- W202 (≠ F251) Periplasmic (proximal) gate; binding L-arginine
- I205 (= I254) binding L-arginine
- GVESA 206:210 (≠ GFDAV 255:259) Helix-breaking GVESA motif TM6
- E208 (≠ D257) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ L334) binding L-arginine
- F337 (vs. gap) mutation to A: Severely decreased antiport.
- S357 (≠ V399) binding L-arginine
- Y365 (≠ F407) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
26% identity, 92% coverage: 28:478/488 of query aligns to 3:429/437 of 5j4nA
3l1lA Structure of arg-bound escherichia coli adic (see paper)
25% identity, 92% coverage: 28:478/488 of query aligns to 1:416/423 of 3l1lA
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
24% identity, 91% coverage: 15:458/488 of query aligns to 1:442/489 of P25737
- M1 (≠ I15) modified: Initiator methionine, Removed
- Y102 (≠ L116) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y120) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K203) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F251) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ D257) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E265) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ G313) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-278.
- D278 (≠ T316) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-275.
- E438 (≠ V454) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
Sites not aligning to the query:
- 443 D→A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 446 D→A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
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)
23% identity, 97% coverage: 1:471/488 of query aligns to 1:452/487 of P82251
- V40 (≠ I41) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ IIGAG 44:48) binding L-arginine
- I44 (= I45) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (vs. gap) to F: in CSNU; uncertain significance
- P52 (vs. gap) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ I70) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y99) to H: in CSNU; uncertain significance
- G105 (= G105) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W114) to R: in CSNU; uncertain significance
- I120 (≠ E119) to L: in CSNU; uncertain significance
- T123 (≠ M122) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (= V142) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ I144) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ T189) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (= A201) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G214) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ R244) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ G245) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (≠ V248) to D: in CSNU; decreased amino acid transport activity
- W230 (≠ F251) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ I254) binding L-arginine; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F256) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ A258) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S280) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ V282) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ P307) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ T335) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ Q345) to E: in CSNU; uncertain significance
- V330 (≠ T351) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M352) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (≠ Q354) 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 (≠ S375) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (= S400) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ T403) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ L404) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ F407) mutation to A: Loss of amino acid transport activity.
- K401 (≠ A422) to E: in CSNU; uncertain significance; dbSNP:rs760264924
- L426 (vs. gap) 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.
P15993 Aromatic amino acid transport protein AroP; Aromatic amino acid:H(+) symporter AroP; General aromatic amino acid permease; General aromatic transport system from Escherichia coli (strain K12) (see paper)
25% identity, 88% coverage: 22:448/488 of query aligns to 6:413/457 of P15993
- Y103 (= Y120) Key residue for tryptophan transport; mutation to F: Decreases tryptophan transport to less than 50% of wild-type levels and reduces the ability of tryptophan to inhibit phenylalanine transport from 95 to 62%.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
25% identity, 86% coverage: 23:441/488 of query aligns to 4:397/438 of O34739
- C94 (≠ I112) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ A179) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ A209) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ V337) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
Sites not aligning to the query:
- 415 C→S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
23% identity, 78% coverage: 73:455/488 of query aligns to 43:401/455 of 7p9uB
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)
23% identity, 78% coverage: 73:455/488 of query aligns to 87:445/501 of Q9UPY5
- R135 (≠ Y120) binding L-glutamate; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ I144) 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 (≠ N196) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ V202) 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 (= K203) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (vs. gap) binding L-glutamate
- F254 (≠ T261) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ L278) 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 (vs. gap) 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 (≠ Y343) 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 (≠ T403) 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 (≠ D421) 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 (= C444) 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.
Sites not aligning to the query:
- 86 C→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.
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
23% identity, 78% coverage: 73:455/488 of query aligns to 43:401/453 of 7epzB
Sites not aligning to the query:
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
23% identity, 81% coverage: 26:420/488 of query aligns to 17:389/461 of P76037
- Y110 (= Y120) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
Q7YQK4 Large neutral amino acids transporter small subunit 1; 4F2 light chain; 4F2 LC; 4F2LC; L-type amino acid transporter 1; LAT1; Solute carrier family 7 member 5 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
24% identity, 95% coverage: 9:472/488 of query aligns to 23:463/503 of Q7YQK4
- C88 (≠ G72) mutation to S: No significant effect on inhibition by HgCl(2). Decreased KM and Vmax for Phe. Similar affect on KM and Vmax for Phe; when associated with S-183.
- C98 (= C82) mutation to S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe. Slightly less decreased KM and Vmax for Phe; when associated with S-183.
- C160 (≠ I146) mutation to S: No change to KM or Vmax for Phe.
- C172 (≠ V158) mutation to S: No change to KM or Vmax for Phe.
- C174 (≠ L160) mutation to S: No change to KM or Vmax for Phe.
- C183 (≠ V169) mutation to S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe. Similar affect on KM and Vmax for Phe; when associated with S-88. Slightly less decreased KM and Vmax for Phe; when associated with S-98.
- G219 (≠ H222) mutation to D: Decreased KM and Vmax for Trp. Increased KM and Vmax for Phe; when associated with L-234.
- W234 (≠ F237) mutation to L: Decreased KM and Vmax for Trp. Increased KM but decreased Vmax for Phe. Increased KM and Vmax for Phe; when associated with D-219.
- C331 (≠ K327) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ G380) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (≠ A406) mutation to S: No significant effect on inhibition by HgCl(2).
- C439 (= C444) mutation to S: Prevents insertion into the plasma membrane and possibly protein folding.
- C454 (≠ L463) mutation to S: No significant effect on inhibition by HgCl(2). Slightly increased KM but slightly decreased Vmax for Phe.
Sites not aligning to the query:
- 492 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
23% identity, 90% coverage: 31:471/488 of query aligns to 1:423/458 of 6li9B
Q9QXW9 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; mLAT2; Solute carrier family 7 member 8 from Mus musculus (Mouse) (see paper)
23% identity, 92% coverage: 3:449/488 of query aligns to 2:438/531 of Q9QXW9
- Y130 (= Y120) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ G123) mutation to S: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake. Increases the export of both L-leucine and L-phenylalanine.
- F242 (= F251) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
25% identity, 85% coverage: 27:442/488 of query aligns to 1:393/433 of 6f2wA
8qeyA Structure of human asc1/cd98hc heteromeric amino acid transporter (see paper)
24% identity, 62% coverage: 69:372/488 of query aligns to 39:324/449 of 8qeyA
Sites not aligning to the query:
Query Sequence
>WP_013091679.1 NCBI__GCF_000092885.1:WP_013091679.1
MADTGYMARKSVAEIVASADVEEGRHLSKTLGATSITAMGIGAIIGAGIFVLTGTAAAQF
AGPAITLSFILGGIACAFVGLCYSELAAMLPVCGSSYTYTYATLGEIFAWIIGWDLILEY
AMGAATVAVGWSGYIVSLLRNVGIDIPPTLAAAPGTVVKLADGSTVTGVINLPAVVIIAI
LTTLLVLGTKESARLNNVMVAVKLTVVVAFIAIGLFFIKPEHWHPFIPANTGQFGSFGMS
GILRGSAVVFFAFIGFDAVSTAAQEARQPQRDMPIGILGSLVICTVLYILVAAVLTGLVP
YTELNVPDPIAKGVDTIGLTWFAILIKIGALTGLTTVILVLLYGQSRIFFTMSQDGLLPH
FFAKVHLRLHTPYLSQILIGSVVAIVAALTPIGVLGEMVSIGTLFAFVLVCGAVIYLRRS
DAEAARPFRAPGVPVVPVLGILFCLLLMVGLPLVTWLRLVVWLVIGMVIYLSYGRDHSVL
RHPERKRT
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