SitesBLAST
Comparing 7026739 FitnessBrowser__ANA3:7026739 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)
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
74% identity, 99% coverage: 5:437/439 of query aligns to 6:435/439 of P0AAF1
- C62 (= C61) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (= K67) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (= E76) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (= Y77) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (≠ R81) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (= Y89) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y91) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (= W200) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E206) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (= C209) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (= C284) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ T285) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (= W291) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (= K300) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (≠ F307) mutation to L: Excretion activity decreases more than uptake activity.
- W422 (= W421) mutation to L: Uptake activity decreases more than excretion activity.
- Y425 (= Y424) mutation to F: Moderate decrease in both uptake and excretion activities.; mutation to L: Strong decrease in both uptake and excretion activities.
- E433 (= E435) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
36% identity, 93% coverage: 4:411/439 of query aligns to 6:411/445 of P60061
- I23 (≠ M21) binding ; binding
- S26 (= S24) binding
- Y93 (= Y91) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ S94) binding ; binding
- C97 (≠ L95) binding
- N101 (= N99) 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 (≠ I102) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (= W200) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A201) binding
- I205 (≠ L203) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (= W291) 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 (≠ A355) 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: 4:411/439 of query aligns to 6:411/445 of P60063
- N22 (= N20) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ M21) binding
- GSG 25:27 (= GSG 23:25) Helix-breaking GSG motif TM1
- S26 (= S24) binding ; mutation to K: 5% Agm antiport.
- G27 (= G25) binding
- Y74 (≠ G72) 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 (≠ F85) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y91) 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 (≠ S94) binding
- C97 (≠ L95) binding
- N101 (= N99) binding
- W202 (= W200) Periplasmic (proximal) gate; binding
- I205 (≠ L203) binding
- GVESA 206:210 (≠ GLESA 204:208) Helix-breaking GVESA motif TM6
- E208 (= E206) mutation E->A,D: 5-10% Agm antiport.
- W293 (= W291) binding
- F337 (≠ L335) mutation to A: Severely decreased antiport.
- S357 (≠ A355) binding
- Y365 (= Y363) 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)
36% identity, 93% coverage: 4:411/439 of query aligns to 2:407/437 of 5j4nA
3l1lA Structure of arg-bound escherichia coli adic (see paper)
35% identity, 93% coverage: 5:411/439 of query aligns to 1:394/423 of 3l1lA
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
32% identity, 91% coverage: 3:402/439 of query aligns to 2:401/444 of P0AAE8
- C12 (≠ L13) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (≠ L42) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (= W44) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (= Y56) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y57 (≠ F58) mutation to L: Strong decrease in cadaverine uptake.
- Y73 (= Y74) 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 (vs. gap) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y91) 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 (≠ A92) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (= Y109) mutation to L: Strong decrease in cadaverine uptake.
- C125 (≠ T127) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (= Y176) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (≠ F187) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ T198) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E206) 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 (= Y237) 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 (≠ V248) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (= C284) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ A301) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (≠ E305) 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 (≠ F312) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y366 (= Y363) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- Y368 (≠ L365) mutation to L: Strong decrease in cadaverine uptake.
- C370 (≠ M367) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
- E377 (≠ K375) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C389 (≠ I390) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C394 (≠ A395) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C397 (≠ S398) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
Sites not aligning to the query:
- 408 E→Q: Moderate decrease in cadaverine uptake.
- 423 Y→L: Strong decrease in both cadaverine excretion and cadaverine uptake.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
23% identity, 95% coverage: 9:424/439 of query aligns to 6:424/433 of 6f2wA
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
26% identity, 85% coverage: 6:378/439 of query aligns to 10:378/438 of O34739
- C94 (≠ A87) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ A134) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ G162) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ S287) 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.
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
30% identity, 31% coverage: 180:316/439 of query aligns to 206:341/456 of 5oqtA
Sites not aligning to the query:
- binding alanine: 38, 40, 41, 42
- binding : 24, 26, 28, 29, 32, 176, 177, 184, 188, 192
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
30% identity, 31% coverage: 180:316/439 of query aligns to 208:343/458 of 6f34A
Sites not aligning to the query:
- binding arginine: 40, 42, 43, 44, 115, 116, 119
- binding cholesterol: 201, 202
- binding : 28, 30, 31, 34, 178, 179, 186, 187, 190, 194
Q9UHI5 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; hLAT2; Solute carrier family 7 member 8 from Homo sapiens (Human) (see 3 papers)
26% identity, 76% coverage: 6:339/439 of query aligns to 38:381/535 of Q9UHI5
- I53 (≠ M21) binding
- Y93 (≠ F58) mutation to A: Nearly complete reduction of glycine, L-alanine, and L-glutamine uptake. Minimal effect on the transport of L-isoleucine, L-histidine and L-tryptophan.
- N134 (= N99) Important for substrate specificity; binding ; mutation to Q: Reduces L-leucine uptake activity. Abolishes L-tryptophan uptake.; mutation to S: The substrate specificity changed dramatically reducing L-glutamine, glycine and L-alanine uptake activity thus mimicking the selectivity of SLC7A5.
- C154 (≠ N117) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ V136) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (≠ I195) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ T198) Important for substrate specificity; binding ; mutation to S: Strong decrease in the uptake of large substrates L-tryptophan, L-glutamine, and L-histidine but increases the uptake of small neutral amino acids glycine and L-alanine.
- V302 (≠ F260) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
Sites not aligning to the query:
- 395 binding ; N→Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- 396 Y→A: Strongly reduces L-leucine uptake activity.
- 402 T → M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- 418 R → C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity
- 460 V → E: found in a patient with age-related hearing loss; strongly decreases L-alanine transport activity. Decreases L-tyrosine transport activity. Decreases cell membrane localization
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)
25% identity, 93% coverage: 6:413/439 of query aligns to 37:449/531 of Q9QXW9
- Y130 (≠ L96) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (= N99) 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 (≠ I195) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
25% identity, 83% coverage: 39:403/439 of query aligns to 34:393/455 of 7p9uB
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
25% identity, 83% coverage: 39:403/439 of query aligns to 34:393/453 of 7epzB
Sites not aligning to the query:
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)
25% identity, 83% coverage: 39:403/439 of query aligns to 78:437/501 of Q9UPY5
- C86 (≠ T47) 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 (≠ A98) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ V116) 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 (≠ T145) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ V151) 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 (≠ T152) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ W200) binding
- F254 (≠ A210) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ T230) 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 (= C284) 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 (= F293) 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 (≠ N359) 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 (≠ V379) 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 (≠ A401) 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.
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
26% identity, 75% coverage: 9:339/439 of query aligns to 1:341/457 of 7b00A
Sites not aligning to the query:
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
26% identity, 75% coverage: 9:339/439 of query aligns to 1:341/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
26% identity, 75% coverage: 9:339/439 of query aligns to 1:341/458 of 7cmhB
Sites not aligning to the query:
P39277 L-methionine/branched-chain amino acid exporter YjeH from Escherichia coli (strain K12) (see paper)
24% identity, 66% coverage: 1:288/439 of query aligns to 1:283/418 of P39277
- T24 (≠ S24) mutation to Y: Strong decrease in methionine efflux.
- G25 (= G25) mutation to F: Strong decrease in methionine efflux.
- W195 (= W200) mutation to A: Strong decrease in methionine efflux.
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)
23% identity, 45% coverage: 185:380/439 of query aligns to 248:437/629 of P30825
Sites not aligning to the query:
- 226 modified: carbohydrate, N-linked (GlcNAc...) asparagine
Query Sequence
>7026739 FitnessBrowser__ANA3:7026739
MSKSANKIGVVQLTIITIVNMMGSGIIMLPTQLAQVGTISILSWLVTAAGSTALAYAFAK
CGMFSKKSGGMGGYAEYAFGRSGNFMANYTYAVSLLIANVAIAISAVGYAAVLLEVNLSP
MAICLATIGVLWLATVANFGGARITGRVSSVTVWGIILPVIGVSLIGWFWFDIDLYKGAW
NPHDMPFFKALGGSIAMTLWAFLGLESACANSETVDNPEKNVPIAVMGGTLGAALIYIVS
TNVIAGIVPNADLANSNAPFGLAFAQMFNPVVGKIVMACAIISCTGSLLGWQFTIAQVFK
ASADEGFFPKVFSKVSKADAPIWGMTIIVSIQTLLSLMTISPSLSKQFEALVNLAVVTNI
VPYILSMAALGVMQKQLKVPANKARVANVIAVIGALYSFYALYSSGETAVMLGAIATFFG
WTIYGVISNKTPTAEIKAA
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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