SitesBLAST
Comparing PfGW456L13_3775 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3775 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 15 hits to proteins with known functional sites (download)
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
67% identity, 93% coverage: 1:430/461 of query aligns to 1:432/439 of P0AAF1
- C62 (= C60) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (= K66) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (= E75) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (= Y76) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (= K80) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (= Y88) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y90) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (= W199) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E205) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (= C208) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (= C283) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ I284) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (= W290) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (= K299) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (= Y306) mutation to L: Excretion activity decreases more than uptake activity.
- W422 (≠ Y420) mutation to L: Uptake activity decreases more than excretion activity.
- Y425 (≠ F423) mutation to F: Moderate decrease in both uptake and excretion activities.; mutation to L: Strong decrease in both uptake and excretion activities.
Sites not aligning to the query:
- 433 mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
36% identity, 93% coverage: 4:432/461 of query aligns to 3:429/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
36% identity, 93% coverage: 4:432/461 of query aligns to 7:433/445 of P60061
- I23 (≠ M20) binding ; binding
- S26 (= S23) binding
- Y93 (= Y90) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ S93) binding ; binding
- C97 (≠ L94) binding
- N101 (= N98) binding ; 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 (≠ I101) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (= W199) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A200) binding
- I205 (≠ L202) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (= W290) binding ; 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 (≠ A354) binding ; 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)
36% identity, 93% coverage: 4:432/461 of query aligns to 7:433/445 of P60063
- N22 (= N19) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ M20) binding
- GSG 25:27 (= GSG 22:24) Helix-breaking GSG motif TM1
- S26 (= S23) binding ; mutation to K: 5% Agm antiport.
- G27 (= G24) binding
- Y74 (≠ G71) 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 (= Y84) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y90) 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 (≠ S93) binding
- C97 (≠ L94) binding
- N101 (= N98) binding
- W202 (= W199) Periplasmic (proximal) gate; binding
- I205 (≠ L202) binding
- GVESA 206:210 (≠ GLESA 203:207) Helix-breaking GVESA motif TM6
- E208 (= E205) mutation E->A,D: 5-10% Agm antiport.
- W293 (= W290) binding
- F337 (≠ L334) mutation to A: Severely decreased antiport.
- S357 (≠ A354) binding
- Y365 (= Y362) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
3l1lA Structure of arg-bound escherichia coli adic (see paper)
35% identity, 93% coverage: 4:432/461 of query aligns to 1:416/423 of 3l1lA
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
33% identity, 97% coverage: 1:449/461 of query aligns to 1:444/444 of P0AAE8
- C12 (≠ L12) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (≠ L41) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (= W43) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (= Y55) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y57 (≠ F57) mutation to L: Strong decrease in cadaverine uptake.
- Y73 (= Y73) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 9-fold increase in Km for cadaverine for cadaverine uptake and 10-fold increase in Km for cadaverine for cadaverine excretion.
- E76 (≠ T77) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y90) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 10-fold increase in Km for cadaverine for cadaverine uptake and 5-fold increase in Km for cadaverine for cadaverine excretion.
- Y90 (≠ G91) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (= Y108) mutation to L: Strong decrease in cadaverine uptake.
- C125 (≠ T126) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (= Y175) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (≠ W186) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ T197) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E205) mutation to Q: Strong decrease in both cadaverine excretion and cadaverine uptake. 22-fold increase in Km for cadaverine for cadaverine uptake and 6-fold increase in Km for cadaverine for cadaverine excretion.
- Y235 (= Y236) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 23-fold increase in Km for cadaverine for cadaverine uptake and 7-fold increase in Km for cadaverine for cadaverine excretion.
- Y246 (≠ V247) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (= C283) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ S300) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (≠ T304) mutation to N: Strong decrease in both cadaverine excretion and cadaverine uptake. 24-fold increase in Km for cadaverine for cadaverine uptake and 9-fold increase in Km for cadaverine for cadaverine excretion.
- Y310 (≠ F311) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y366 (= Y362) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- Y368 (≠ L364) mutation to L: Strong decrease in cadaverine uptake.
- C370 (≠ M366) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
- E377 (≠ Q373) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C389 (≠ T386) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C394 (≠ L391) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C397 (≠ S397) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E408 (≠ M410) mutation to Q: Moderate decrease in cadaverine uptake.
- Y423 (≠ V426) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
P39277 L-methionine/branched-chain amino acid exporter YjeH from Escherichia coli (strain K12) (see paper)
24% identity, 62% coverage: 3:287/461 of query aligns to 4:283/418 of P39277
- T24 (≠ S23) mutation to Y: Strong decrease in methionine efflux.
- G25 (= G24) mutation to F: Strong decrease in methionine efflux.
- W195 (= W199) mutation to A: Strong decrease in methionine efflux.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
23% identity, 80% coverage: 8:374/461 of query aligns to 3:370/433 of 6f2wA
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
23% identity, 90% coverage: 6:419/461 of query aligns to 9:422/438 of O34739
- C94 (≠ T86) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ T133) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ L161) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ S286) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- C415 (≠ G412) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
27% identity, 54% coverage: 2:252/461 of query aligns to 22:281/458 of 6f34A
- binding arginine: I40 (≠ M20), G42 (= G22), T43 (≠ S23), G44 (= G24), E115 (≠ S93), Y116 (≠ L94), A119 (= A97), F228 (≠ W199), A229 (= A200), I231 (≠ L202)
- binding cholesterol: W201 (= W169), Y202 (≠ F170)
- binding : G28 (≠ S8), F30 (≠ G10), D31 (≠ Q11), M34 (= M14), A178 (≠ G145), R179 (= R146), A186 (≠ W153), I187 (≠ G154), A190 (= A157), L194 (= L161)
Sites not aligning to the query:
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
27% identity, 54% coverage: 2:252/461 of query aligns to 20:279/456 of 5oqtA
- binding alanine: I38 (≠ M20), G40 (= G22), T41 (≠ S23), G42 (= G24), F226 (≠ W199), A227 (= A200), I229 (≠ L202)
- binding : E24 (≠ K6), G26 (≠ S8), F28 (≠ G10), D29 (≠ Q11), M32 (= M14), A176 (≠ G145), R177 (= R146), A184 (≠ W153), A188 (= A157), L192 (= L161)
Sites not aligning to the query:
Q22397 Amino acid transporter protein 6 from Caenorhabditis elegans (see paper)
23% identity, 77% coverage: 19:373/461 of query aligns to 32:391/523 of Q22397
Sites not aligning to the query:
- 521:523 PDZ-binding motif; mutation Missing: Abolishes the interaction with nrfl-1.
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)
22% identity, 69% coverage: 38:353/461 of query aligns to 78:391/501 of Q9UPY5
- C86 (≠ T46) 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 (≠ L95) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ L117) 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 (≠ G148) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ G154) 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 (≠ V155) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ W199) binding
- F254 (≠ A209) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ L226) 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 (= C283) 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 (= F292) 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.
Sites not aligning to the query:
- 396 R→A: Loss of L-cystine transport activity.; R→K: Loss of L-cystine transport activity.; R→N: Loss of L-cystine transport activity.
- 414 C→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.
- 435 C→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.
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
22% identity, 69% coverage: 38:353/461 of query aligns to 34:347/453 of 7epzB
Sites not aligning to the query:
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
22% identity, 69% coverage: 38:353/461 of query aligns to 34:347/455 of 7p9uB
Query Sequence
>PfGW456L13_3775 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3775
MSVAKKMSVGQLTMLTAVNMLGSGIVLLPTKLAEVGAISILSWLITATGSLALAYAFARC
GMLSRKTGGMGGYAEYTFGKAGNYITNYTYGLSLLIANVAISITAVGYIQVLFGIELDSL
QVGLATIALLWITTFANFGGASITGRIGAVTVWGVIAPVVLVSTVGWFWFDSSVYAAGWN
PHDKGWFEAAGASVAITLWAFLGLESACANTDAVENPERNVPIAVLGGTLGAAVIYIVST
NVIFGIVGNEELAASTAPFGLVFAKMFTPMVGDIVMAAMVLACIGSLLGWQFTIAQVYKS
SADTGYFLPIFAKGNKAGTPIVGMLVLLAAQTALALLTISPDLSKQFDTLVNLAVVTNLV
PYILSMAALMTMQKVSNVPEGKALATNVIALIAAAYSYLALYSSGEQALMLGGVATIVGY
TLFGFVNNRLIRLEALNNSVPTQTVSAQHLTAEPVPVNNLN
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