SitesBLAST
Comparing CCNA_03226 FitnessBrowser__Caulo:CCNA_03226 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)
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
33% identity, 93% coverage: 22:430/438 of query aligns to 14:420/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
33% identity, 93% coverage: 22:430/438 of query aligns to 18:424/445 of P60061
- I23 (≠ M27) binding ; binding
- S26 (= S30) binding
- Y93 (= Y97) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ S100) binding ; binding
- C97 (≠ V101) binding
- N101 (= N105) 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 (≠ I108) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (= W208) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A209) binding
- I205 (≠ L211) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (= W299) 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 (= S363) 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)
33% identity, 93% coverage: 22:430/438 of query aligns to 18:424/445 of P60063
- N22 (= N26) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ M27) binding
- GSG 25:27 (= GSG 29:31) Helix-breaking GSG motif TM1
- S26 (= S30) binding ; mutation to K: 5% Agm antiport.
- G27 (= G31) binding
- Y74 (≠ F78) 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 (≠ F91) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y97) 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 (≠ S100) binding
- C97 (≠ V101) binding
- N101 (= N105) binding
- W202 (= W208) Periplasmic (proximal) gate; binding
- I205 (≠ L211) binding
- GVESA 206:210 (≠ GVETA 212:216) Helix-breaking GVESA motif TM6
- E208 (= E214) mutation E->A,D: 5-10% Agm antiport.
- W293 (= W299) binding
- F337 (≠ L343) mutation to A: Severely decreased antiport.
- S357 (= S363) binding
- Y365 (= Y371) 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)
33% identity, 93% coverage: 22:430/438 of query aligns to 12:407/423 of 3l1lA
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
30% identity, 98% coverage: 6:433/438 of query aligns to 1:428/439 of P0AAF1
- C62 (≠ A68) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (vs. gap) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (= E82) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (≠ E83) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (≠ R87) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (≠ W95) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y97) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (= W208) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E214) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (≠ T217) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (≠ A292) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ L293) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (= W299) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (≠ A308) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (≠ V315) mutation to L: Excretion activity decreases more than uptake activity.
- W422 (≠ A427) mutation to L: Uptake activity decreases more than excretion activity.
- Y425 (= Y430) 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.
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
34% identity, 85% coverage: 11:383/438 of query aligns to 4:378/444 of P0AAE8
- C12 (= C19) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (≠ I48) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (= W50) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (= Y62) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y57 (≠ F64) mutation to L: Strong decrease in cadaverine uptake.
- Y73 (= Y80) 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 (= E83) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y97) 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 (≠ W98) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (= Y115) mutation to L: Strong decrease in cadaverine uptake.
- C125 (≠ T134) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (≠ A184) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (≠ S195) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ T206) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E214) 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 (= Y245) 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 (≠ T256) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (≠ A292) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ A309) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (≠ E313) 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 (≠ F320) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y366 (= Y371) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- Y368 (≠ F373) mutation to L: Strong decrease in cadaverine uptake.
- C370 (≠ S375) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
- E377 (≠ Q382) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
Sites not aligning to the query:
- 389 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 394 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 397 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 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)
26% identity, 95% coverage: 22:435/438 of query aligns to 12:429/433 of 6f2wA
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)
28% identity, 92% coverage: 5:406/438 of query aligns to 22:423/487 of P82251
- V40 (= V24) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ MIGSG 27:31) binding
- I44 (= I28) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ L35) to F: in CSNU; uncertain significance
- P52 (= P36) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (vs. gap) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y80) to H: in CSNU; uncertain significance
- G105 (= G86) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W95) to R: in CSNU; uncertain significance
- I120 (≠ V101) to L: in CSNU; uncertain significance
- T123 (≠ A104) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (= V122) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ A124) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ A149) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ V161) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G172) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ A201) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (= A202) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (≠ L205) to D: in CSNU; decreased amino acid transport activity
- W230 (= W208) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ L211) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ V213) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ T215) mutation to A: Reduces amino acid transport activity.
- G259 (= G237) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ A239) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (= S264) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ S300) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ Q303) to E: in CSNU; uncertain significance
- V330 (≠ A309) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M310) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R312) 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 (= A332) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ T357) mutation to A: Markedly reduces amino acid transport activity.
- A382 (= A360) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ L361) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ T364) mutation to A: Loss of amino acid transport activity.
- K401 (≠ Q384) to E: in CSNU; uncertain significance; dbSNP:rs760264924
Sites not aligning to the query:
- 426 L → P: in CSNU; uncertain significance
- 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.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
26% identity, 86% coverage: 11:386/438 of query aligns to 9:380/438 of O34739
- C94 (≠ V93) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ T142) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ A169) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A295) 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.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
28% identity, 90% coverage: 14:406/438 of query aligns to 1:394/458 of 6li9B
7nf6B Ovine b0,+at-rbat heterodimer (see paper)
29% identity, 79% coverage: 14:360/438 of query aligns to 2:354/455 of 7nf6B
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, 82% coverage: 11:369/438 of query aligns to 37:398/535 of Q9UHI5
- I53 (≠ M27) binding
- Y93 (≠ F64) 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 (= N105) 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 (≠ I123) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ A143) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (≠ W208) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ L211) 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 (≠ P267) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity; dbSNP:rs142951280
- N395 (≠ S366) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (≠ T367) mutation to A: Strongly reduces L-leucine uptake activity.
Sites not aligning to the query:
- 402 T → M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity; dbSNP:rs758342760
- 418 R → C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity; dbSNP:rs146946494
- 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
6irtB Human lat1-4f2hc complex bound with bch (see paper)
25% identity, 77% coverage: 21:359/438 of query aligns to 7:353/457 of 6irtB
7dsqB Overall structure of the lat1-4f2hc bound with 3,5-diiodo-l-tyrosine (see paper)
25% identity, 77% coverage: 21:359/438 of query aligns to 14:360/464 of 7dsqB
Sites not aligning to the query:
7dsnB Overall structure of the lat1-4f2hc bound with jx-119 (see paper)
25% identity, 77% coverage: 21:359/438 of query aligns to 14:360/464 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 (≠ N26), I20 (≠ M27), G22 (= G29), S23 (= S30), G24 (= G31), I97 (≠ V101), I104 (= I108), F209 (≠ W208), A210 (= A209), G212 (≠ L211), I354 (≠ A353)
- binding cholesterol hemisuccinate: F109 (≠ A112), Y145 (≠ A147), K148 (≠ R150), V153 (≠ T155), Q326 (≠ N326)
Sites not aligning to the query:
7dslB Overall structure of the lat1-4f2hc bound with jx-078 (see paper)
25% identity, 77% coverage: 21:359/438 of query aligns to 14:360/464 of 7dslB
7dskB Overall structure of the lat1-4f2hc bound with jx-075 (see paper)
25% identity, 77% coverage: 21:359/438 of query aligns to 14:360/464 of 7dskB
- binding (2~{S})-2-azanyl-7-(naphthalen-1-ylmethoxy)-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: T19 (≠ N26), I20 (≠ M27), S23 (= S30), G24 (= G31), I97 (≠ V101), S100 (≠ A104), S101 (≠ N105), F209 (≠ W208), G212 (≠ L211), Y216 (≠ T215), V353 (≠ M352), I354 (≠ A353)
- binding cholesterol hemisuccinate: K148 (≠ R150), A149 (≠ S151), V153 (≠ T155), F157 (≠ T159), H324 (≠ S324)
Sites not aligning to the query:
Q01650 Large neutral amino acids transporter small subunit 1; 4F2 light chain; 4F2 LC; 4F2LC; CD98 light chain; Integral membrane protein E16; E16; L-type amino acid transporter 1; hLAT1; Solute carrier family 7 member 5; y+ system cationic amino acid transporter from Homo sapiens (Human) (see 3 papers)
26% identity, 82% coverage: 21:379/438 of query aligns to 57:413/507 of Q01650
- Y117 (≠ F78) mutation to A: Strongly decreased leucine transport activity.
- C164 (≠ A124) modified: Interchain (with C-210 in SLC3A2)
- D223 (≠ G182) to V: in dbSNP:rs17853937
- N230 (vs. gap) to K: in dbSNP:rs1060250
- A246 (= A202) mutation to V: Nearly abolishes leucine transport activity.
- F252 (≠ W208) mutation to A: Nearly abolishes leucine transport activity.
- W257 (≠ V213) mutation to A: Nearly abolishes leucine transport activity.
- N258 (≠ E214) mutation to A: Decreased leucine transport activity.; mutation to D: Nearly abolishes leucine transport activity.
- Y259 (≠ T215) mutation to A: Strongly decreased leucine transport activity.
- E303 (≠ A259) mutation to K: Decreased leucine transport activity.
- P375 (≠ S336) mutation to L: Nearly abolishes leucine transport activity.
Sites not aligning to the query:
- 483:507 mutation Missing: Nearly abolishes leucine transport activity.
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
26% identity, 80% coverage: 20:369/438 of query aligns to 6:358/457 of 7b00A
Sites not aligning to the query:
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
26% identity, 80% coverage: 20:369/438 of query aligns to 6:358/458 of 7cmiB
Query Sequence
>CCNA_03226 FitnessBrowser__Caulo:CCNA_03226
MGGAKMTAVRSKPLGVWMCAALVVGNMIGSGVFMLPASLAPYGWNAVIAWILTIGGSLCL
AYVFAKLAGAFPRAGGPFAYTEEAFGRAPGFLVAWSYWISVWVANAAIAIAAISYLSVFL
PVIAKVPALPALLTVAVVWTATAINCAGARSAGWTQVVTTVLKLVPLIAVAGLAVSVLLR
KGPAAITPFEPSALSGASITAAAALTLWALLGVETATIPADKVKDPARTIPRATLAGTAF
AGLVYLVVSSGVLLLTPTAVLQGSNAPFVDFVSYHGGGDFRLALAAFATISALGALNGWS
LIQGELPAAMAREGVFPAWFAKTSANGTPVRAHLVSSVLVTILVLMNYAKSMADAFTFMA
LLSTTSTLFAYLFCSLAVLRLQGQGRMDRSKALTLVAALGALYSVWTFSGAGWSVTLWGL
VLLAVGAPIYWLMRRAAR
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