SitesBLAST
Comparing WP_035703024.1 NCBI__GCF_000691145.1:WP_035703024.1 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 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)
26% identity, 82% coverage: 4:447/539 of query aligns to 21:451/456 of 5oqtA
- binding alanine: I38 (≠ S20), G40 (≠ I22), T41 (≠ G23), G42 (≠ S24), F226 (= F214), A227 (= A215), I229 (≠ N217)
- binding : E24 (≠ R7), G26 (= G9), F28 (= F11), D29 (≠ A12), M32 (= M14), A176 (≠ T162), R177 (≠ F163), A184 (≠ V170), A188 (≠ L174), L192 (≠ A178), Q294 (≠ I289), V297 (≠ L292)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
26% identity, 82% coverage: 4:447/539 of query aligns to 23:453/458 of 6f34A
- binding arginine: I40 (≠ S20), G42 (≠ I22), T43 (≠ G23), G44 (≠ S24), E115 (≠ N92), Y116 (≠ W93), A119 (≠ I96), F228 (= F214), A229 (= A215), I231 (≠ N217), V314 (≠ T307)
- binding cholesterol: W201 (≠ H185), Y202 (≠ S186)
- binding : G28 (= G9), F30 (= F11), D31 (≠ A12), M34 (= M14), A178 (≠ T162), R179 (≠ F163), A186 (≠ V170), I187 (= I171), A190 (≠ L174), L194 (≠ A178), Q296 (≠ I289), V299 (≠ L292)
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
25% identity, 81% coverage: 14:447/539 of query aligns to 10:430/433 of 6f2wA
9h76A Bacterial lat transporter basc in complex with l-ala and nb53 (see paper)
25% identity, 81% coverage: 14:447/539 of query aligns to 8:428/430 of 9h76A
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
26% identity, 72% coverage: 4:390/539 of query aligns to 8:384/469 of P46349
- G33 (= G29) mutation to D: Lack of activity.
- G42 (= G38) mutation to S: Lack of activity.
- G301 (= G308) mutation to V: Lack of activity.
- G338 (≠ N349) mutation to E: Lack of activity.
- F341 (≠ V352) mutation to S: Lack of activity.
Sites not aligning to the query:
- 414 G→R: Lack of activity.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
25% identity, 64% coverage: 4:347/539 of query aligns to 13:350/489 of P25737
- Y102 (≠ N92) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ I96) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K168) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F214) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ Q220) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E228) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ G270) 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 (≠ H273) 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.
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)
25% identity, 72% coverage: 3:389/539 of query aligns to 27:431/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q88CZ8 L-histidine transporter HutT from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
25% identity, 63% coverage: 4:342/539 of query aligns to 7:333/467 of Q88CZ8
- T27 (≠ S24) mutation T->A,S: Retains 60% of wild-type activity.; mutation to N: Retains 20% of wild-type activity.
- E98 (≠ A95) mutation to A: Retains 80% of wild-type activity.
- K156 (= K168) mutation K->A,Q: Retains less than 10% of wild-type activity.; mutation to R: Retains 40% of wild-type activity.
- F212 (= F214) mutation F->A,Q: Loss of activity.; mutation to Y: No change in activity.
- E218 (≠ Q220) mutation E->A,Q: Loss of activity.; mutation to D: Retains 70% of wild-type activity.
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, 83% coverage: 4:450/539 of query aligns to 42:480/503 of Q7YQK4
- C88 (≠ G48) 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 (≠ S58) 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 (≠ K128) mutation to S: No change to KM or Vmax for Phe.
- C172 (≠ S140) mutation to S: No change to KM or Vmax for Phe.
- C174 (≠ L142) mutation to S: No change to KM or Vmax for Phe.
- C183 (≠ Y151) 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 (vs. gap) mutation to D: Decreased KM and Vmax for Trp. Increased KM and Vmax for Phe; when associated with L-234.
- W234 (= W200) 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 (≠ A300) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ L350) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (vs. gap) mutation to S: No significant effect on inhibition by HgCl(2).
- C439 (≠ S416) mutation to S: Prevents insertion into the plasma membrane and possibly protein folding.
- C454 (≠ T427) 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.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
25% identity, 83% coverage: 2:447/539 of query aligns to 6:435/438 of O34739
- C94 (≠ A91) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ M137) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ K168) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ S303) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- C415 (≠ T427) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
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, 76% coverage: 2:411/539 of query aligns to 9:405/457 of P15993
- Y103 (≠ I96) 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%.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
23% identity, 74% coverage: 4:404/539 of query aligns to 19:408/458 of P24207
- R26 (≠ F11) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P39) mutation to A: 50% of wild-type phenylalanine transport activity.; mutation to G: No change in phenylalanine transport activity.; mutation to L: 26% of wild-type phenylalanine transport activity.
- F87 (≠ M72) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y75) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ Q77) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ S79) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ H80) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (= F83) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F86) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W90) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (≠ N92) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W93) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ I96) mutation to L: 60% of wild-type phenylalanine transport activity.; mutation to Y: Enables the transport of tryptophan to almost the same steady-state level as that of phenylalanine.
- E118 (= E103) mutation E->G,L,V,N: Loss of activity.
- K168 (= K168) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (≠ Q220) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (≠ V252) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P337) mutation to A: 5% of wild-type phenylalanine transport activity.; mutation P->G,Q,K,R: Loss of activity.; mutation to S: 3% of wild-type phenylalanine transport activity.; mutation to T: 17% of wild-type phenylalanine transport activity.
Sites not aligning to the query:
- 442 P→A: 46% of wild-type phenylalanine transport activity.; P→G: 52% of wild-type phenylalanine transport activity.; P→L: 43% of wild-type phenylalanine transport activity.
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
24% identity, 55% coverage: 44:342/539 of query aligns to 58:340/461 of P76037
- Y110 (vs. gap) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
8j8mB Overall structure of the lat1-4f2hc bound with tryptophan
24% identity, 83% coverage: 4:450/539 of query aligns to 3:441/463 of 8j8mB
8j8lB Overall structure of the lat1-4f2hc bound with l-dopa
24% identity, 83% coverage: 4:450/539 of query aligns to 3:441/463 of 8j8lB
8x0wB Overall structure of the lat1-4f2hc bound with leu
24% identity, 83% coverage: 4:450/539 of query aligns to 3:441/464 of 8x0wB
8idaB Overall structure of the lat1-4f2hc bound with tyrosine
24% identity, 83% coverage: 4:450/539 of query aligns to 3:441/464 of 8idaB
7dsqB Overall structure of the lat1-4f2hc bound with 3,5-diiodo-l-tyrosine (see paper)
24% identity, 83% coverage: 4:450/539 of query aligns to 3:441/464 of 7dsqB
7dsnB Overall structure of the lat1-4f2hc bound with jx-119 (see paper)
24% identity, 83% coverage: 4:450/539 of query aligns to 3:441/464 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 (≠ S20), I20 (= I21), G22 (= G23), S23 (= S24), G24 (= G25), I97 (≠ V99), I104 (≠ M111), F209 (= F214), A210 (= A215), G212 (≠ N217), I354 (≠ A373), N361 (≠ T380)
- binding cholesterol hemisuccinate: F109 (≠ W116), Y145 (≠ W152), K148 (= K159), V153 (≠ I164), Q326 (≠ I338)
Sites not aligning to the query:
7dslB Overall structure of the lat1-4f2hc bound with jx-078 (see paper)
24% identity, 83% coverage: 4:450/539 of query aligns to 3:441/464 of 7dslB
Query Sequence
>WP_035703024.1 NCBI__GCF_000691145.1:WP_035703024.1
MNHLHRRMGTFALMMVGLGSIIGSGWLFGAWRAAQIAGPAAILSWLIGMVVILFIALSYS
ELGSMFPEAGGMVKYTQYSHGSFIGFIAAWANWIAIVSVIPVEAVASVQYMSSWPWEWAK
WTSHLVTKGVLTTEGLMVASVLLVIYFLLNYWTVGLFSKANTFITIFKIVIPGLTIGALL
FVGFHSENFTSGTSIAPNGWASVLTAVATSGIVFAFNGFQSPINMAGEAKNPGRSIPIAI
VGSILIATVIYVLLQIAFIGAVDPSMIVNGWGHLNFNSPFADLAIALGINWLVLILYADA
FVSPSGTGITYTATTSRMIYGMEKNKYMPSVLGRLHPIYGVPRPAMFFNLGVSFIFLFLF
RGWGVLAEIISVATLISYLTGPVTVMTLRKTGTDLYRPLRIKGLSIIAPLGFVFASLTLY
WARWPLTGQVLFIILIGLPIYFYYQAKAKWKGFGRHFKAGAWMVVYLLVMMTISCLGSDK
FGGYNVIHYGWDMALIAVVALLFYMWALKSGFETEFLEDAKKINDELRAFQKEAASSKE
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