SitesBLAST
Comparing WP_035703060.1 NCBI__GCF_000691145.1:WP_035703060.1 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)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
50% identity, 99% coverage: 3:456/460 of query aligns to 2:457/458 of 6f34A
- binding arginine: I40 (≠ V39), G42 (= G41), T43 (= T42), G44 (= G43), E115 (≠ V114), Y116 (= Y115), A119 (≠ T118), F228 (= F228), A229 (= A229), I231 (≠ L231), V314 (= V314)
- binding cholesterol: W201 (≠ F201), Y202 (= Y202)
- binding : G28 (= G27), F30 (≠ L29), D31 (= D30), M34 (≠ L33), A178 (≠ K178), R179 (≠ K179), A186 (≠ F186), I187 (≠ V187), A190 (≠ G190), L194 (= L194), Q296 (= Q296), V299 (= V299)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
50% identity, 98% coverage: 4:456/460 of query aligns to 1:455/456 of 5oqtA
- binding alanine: I38 (≠ V39), G40 (= G41), T41 (= T42), G42 (= G43), F226 (= F228), A227 (= A229), I229 (≠ L231)
- binding : E24 (≠ T25), G26 (= G27), F28 (≠ L29), D29 (= D30), M32 (≠ L33), A176 (≠ K178), R177 (≠ K179), A184 (≠ F186), A188 (≠ G190), L192 (= L194), Q294 (= Q296), V297 (= V299)
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)
36% identity, 87% coverage: 2:399/460 of query aligns to 11:436/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
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)
25% identity, 96% coverage: 5:446/460 of query aligns to 6:451/487 of P82251
- V40 (≠ I36) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ VIGTG 39:43) binding L-arginine
- I44 (= I40) 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 (= A65) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y94) to H: in CSNU; uncertain significance
- G105 (= G100) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W109) to R: in CSNU; uncertain significance
- I120 (≠ Y115) to L: in CSNU; uncertain significance
- T123 (= T118) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ F145) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ A147) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ T174) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ F186) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G199) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ V226) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ F227) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (vs. gap) to D: in CSNU; decreased amino acid transport activity
- W230 (vs. gap) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ L231) binding L-arginine; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F233) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ A235) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S257) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ L259) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ T284) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ N319) mutation to S: Does not affect amino acid transport activity.
- A324 (= A322) to E: in CSNU; uncertain significance
- V330 (≠ A328) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M329) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R331) 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 (≠ S351) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ N376) mutation to A: Markedly reduces amino acid transport activity.
- A382 (= A379) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ L380) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ F383) mutation to A: Loss of amino acid transport activity.
- K401 (= K398) to E: in CSNU; uncertain significance; dbSNP:rs760264924
- L426 (= L425) 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.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
23% identity, 89% coverage: 15:425/460 of query aligns to 6:433/489 of P25737
- Y102 (≠ L111) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (vs. gap) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K179) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F228) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ D234) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E242) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ N282) 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 (≠ E285) 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.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 438 E→A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 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.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
25% identity, 89% coverage: 36:446/460 of query aligns to 11:422/458 of 6li9B
Q88CZ8 L-histidine transporter HutT from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
24% identity, 88% coverage: 17:423/460 of query aligns to 2:417/467 of Q88CZ8
- T27 (= T42) mutation T->A,S: Retains 60% of wild-type activity.; mutation to N: Retains 20% of wild-type activity.
- E98 (≠ M116) mutation to A: Retains 80% of wild-type activity.
- K156 (= K188) mutation K->A,Q: Retains less than 10% of wild-type activity.; mutation to R: Retains 40% of wild-type activity.
- F212 (= F228) mutation F->A,Q: Loss of activity.; mutation to Y: No change in activity.
- E218 (≠ D234) mutation E->A,Q: Loss of activity.; mutation to D: Retains 70% of wild-type 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)
23% identity, 93% coverage: 16:441/460 of query aligns to 5:439/457 of P15993
- Y103 (= Y115) 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, 89% coverage: 16:424/460 of query aligns to 2:404/438 of O34739
- C94 (≠ M107) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ A167) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ L194) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ V314) 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.
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
24% identity, 86% coverage: 12:408/460 of query aligns to 8:399/461 of P76037
- Y110 (= Y115) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
7nf6B Ovine b0,+at-rbat heterodimer (see paper)
24% identity, 92% coverage: 26:446/460 of query aligns to 2:423/455 of 7nf6B
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
25% identity, 88% coverage: 24:426/460 of query aligns to 2:401/433 of 6f2wA
9h76A Bacterial lat transporter basc in complex with l-ala and nb53 (see paper)
25% identity, 85% coverage: 36:426/460 of query aligns to 12:399/430 of 9h76A
8xyjA Structure of y+lat1 bound with lys
25% identity, 88% coverage: 18:424/460 of query aligns to 1:404/459 of 8xyjA
8xxiA Structure of y+lat1 bound with leu
25% identity, 88% coverage: 18:424/460 of query aligns to 1:404/465 of 8xxiA
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, 85% coverage: 36:424/460 of query aligns to 56:443/503 of Q7YQK4
- C88 (≠ A67) 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 (= C77) 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 (≠ I141) mutation to S: No change to KM or Vmax for Phe.
- C172 (vs. gap) mutation to S: No change to KM or Vmax for Phe.
- C174 (vs. gap) mutation to S: No change to KM or Vmax for Phe.
- C183 (≠ L157) 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 (≠ V193) mutation to D: Decreased KM and Vmax for Trp. Increased KM and Vmax for Phe; when associated with L-234.
- W234 (= W208) 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 (≠ L311) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ G356) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (≠ T382) mutation to S: No significant effect on inhibition by HgCl(2).
- C439 (= C420) mutation to S: Prevents insertion into the plasma membrane and possibly protein folding.
Sites not aligning to the query:
- 454 C→S: No significant effect on inhibition by HgCl(2). Slightly increased KM but slightly decreased Vmax for Phe.
- 492 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe.
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
26% identity, 72% coverage: 26:356/460 of query aligns to 10:331/445 of P60061
- I23 (≠ V39) binding agmatine; binding L-arginine
- S26 (≠ T42) binding L-arginine
- Y93 (≠ G108) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ L111) binding agmatine; binding L-arginine
- C97 (≠ L112) binding agmatine
- N101 (≠ M116) 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 (≠ A119) binding agmatine; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F228) binding L-arginine; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A229) binding agmatine
- I205 (≠ L231) binding agmatine; binding L-arginine; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ N318) 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.
Sites not aligning to the query:
- 357 binding L-arginine; S→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, 72% coverage: 26:356/460 of query aligns to 10:331/445 of P60063
- N22 (≠ A38) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ V39) binding L-arginine
- GSG 25:27 (≠ GTG 41:43) Helix-breaking GSG motif TM1
- S26 (≠ T42) binding L-arginine; mutation to K: 5% Agm antiport.
- G27 (= G43) binding L-arginine
- Y74 (= Y92) 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 (≠ H105) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (≠ G108) 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 (≠ L111) binding L-arginine
- C97 (≠ L112) binding L-arginine
- N101 (≠ M116) binding L-arginine
- W202 (≠ F228) Periplasmic (proximal) gate; binding L-arginine
- I205 (≠ L231) binding L-arginine
- GVESA 206:210 (≠ GFDAI 232:236) Helix-breaking GVESA motif TM6
- E208 (≠ D234) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ N318) binding L-arginine
Sites not aligning to the query:
- 337 F→A: Severely decreased antiport.
- 357 binding L-arginine
- 365 Y→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, 72% coverage: 26:356/460 of query aligns to 6:327/437 of 5j4nA
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)
24% identity, 88% coverage: 22:425/460 of query aligns to 35:438/531 of Q9QXW9
- Y130 (= Y115) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ T118) 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 (= F228) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
Query Sequence
>WP_035703060.1 NCBI__GCF_000691145.1:WP_035703060.1
MRHILRKKHIHDLLEQSRQQKVKKTLGGLDLTLLGIGAVIGTGVMVLTGITAAKDAGPAV
IFSFAIAAIVCSLAALCYAEMASALPVFGSAYTYSYTTMGELVGHLMGWTLLSVYMLTAS
AVASGWSSYFNSLLEGFGISIPHQFLAGPEQGGYMNLPAIIIALLIAWILSRGTKESKKF
NNIMVFVKLGIIVLFIVVGGFYVEPANWQPFMPFGTEGIIAGAAAVFFAFLGFDAISASA
EEVKNPQRNLPIGIIGSLLICTIIYIVVCLVMTGMVHYTKLNVTEAMSYVLQSVHQHSVA
GIISVGAVIGLMAVIFANNYAATRIAFAMGRDGLLPKVFSKTNKSDTPVASIWVIGGMTA
VISGFIDLKDLSNLANIGALLTFAMVSLSVLILRKTHKQLERGFRVPFVPVLPIISMGCC
VFLMLNLPGRTWLYFGVWLIIGVVMYAAYSNKHSELAKSA
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