SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing BWI76_RS08745 FitnessBrowser__Koxy:BWI76_RS08745 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)

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)
45% identity, 95% coverage: 3:438/459 of query aligns to 5:437/457 of P15993

query
sites
P15993

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Y103 (≠ M101) 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)
43% identity, 98% coverage: 3:451/459 of query aligns to 13:458/458 of P24207

query
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P24207

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R26 (= R16) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
P54 (= P44) 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 (= F77) mutation to L: No effect on phenylalanine transport activity.
F90 (≠ Y80) mutation to L: 65% of wild-type phenylalanine transport activity.
Y92 (≠ R82) mutation to L: 41% of wild-type phenylalanine transport activity.
Y94 (= Y84) mutation to L: 69% of wild-type phenylalanine transport activity.
W95 (≠ L85) mutation to L: 10% of wild-type phenylalanine transport activity.
F98 (≠ L88) mutation to L: No effect on phenylalanine transport activity.
F101 (= F91) mutation to L: 38% of wild-type phenylalanine transport activity.
W105 (= W95) mutation to L: 39% of wild-type phenylalanine transport activity.
Y107 (= Y97) mutation to L: No effect on phenylalanine transport activity.
W108 (≠ T98) mutation to L: 71% of wild-type phenylalanine transport activity.
F111 (≠ M101) 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 (≠ D108) mutation E->G,L,V,N: Loss of activity.
K168 (= K158) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
E226 (= E218) mutation E->A,Q,K,R,W: Loss of activity.
R252 (= R244) mutation R->D,E,F,W,P: Loss of activity.
P341 (= P333) 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.
P442 (≠ L435) mutation to A: 46% of wild-type phenylalanine transport activity.; mutation to G: 52% of wild-type phenylalanine transport activity.; mutation to L: 43% of wild-type phenylalanine transport activity.

P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
35% identity, 98% coverage: 3:451/459 of query aligns to 2:450/469 of P46349

query
sites
P46349

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V

P

P

W

V

M

Q

T

A

V

I

V

V

V

A

M
x
G

G

T

V

F

A
x
F

L

S

L

Y

A

I

A

A

V

V

L

M

N

N

Y

Y

L

F

M

S

P

P

E

D

Q

T

V

V

F

F

V

L

L

F

I

L

A

V

S

N

L

S

A

S

A

G

F

A

A

I

T

A

V

L

W

L

V

V

W

Y

V

L

M

V

I

I

L

A

L

V

A

S

H

Q

F

L

A

K

M

M

R

R

R

K

G

K

L

L

S

E

A

K

E

T

E

N

R

P

G

E

N

A

I

L

A

K

F

I

P

K

V

M

P

W

L

L

W

F

P

P

V

F

A

L

P

T

L

Y

L

L

T

T

L

I

F

A

M

I

G

C

L
x
G

V

I

I

L

A

V

V

S

L

M

G

A

M

F

V

I

E

D

E

S

T

M

R

R

I

D

A

E

L

L

I

L

A

L

G

T

L

G

V

V

W

I

L

T

G

G

L

I

L

V

T

L

A

I

V

S

W

Y

F

L

A

V

-

F

R

R

V

K

R

R

K

K

G33 (= G34) mutation to D: Lack of activity.
G42 (= G43) mutation to S: Lack of activity.
G301 (≠ D303) mutation to V: Lack of activity.
G338 (≠ M340) mutation to E: Lack of activity.
F341 (≠ A343) mutation to S: Lack of activity.
G414 (≠ L416) mutation to R: Lack of activity.

P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
35% identity, 93% coverage: 2:426/459 of query aligns to 6:438/489 of P25737

query
sites
P25737

Q

K

Q

T

N

E

K

A

P

P

H

G

L

L

L

R

R

R

G

E

L

L

N

K

A

A

R

R

H

H

I

L

R

T

F

M

I

I

A

A

L

I

G

G

S

G

A

S

I

I

G

G

T

T

G

G

L

L

F

F

Y

V

G

A

S

S

A

G

S

A

A

T

I

I

K

S

A

Q

A

A

G

G

P

P

A

G

-

G

V

A

L

L

A

S

Y

Y

L

M

I

L

G

I

G

G

A

L

A

M

V

V

F

Y

I

F

V

L

M

M

R

T

A

S

L

L

G

G

E

E

M

L

A

A

V

A

R

Y

N

M

P

P

V

V

S

S

G

G

S

S

F

F

S

A

S

T

Y

Y

A

G

R

Q

Q

N

Y

Y

L

V

G

E

P

E

L

G

A

F

G

G

F

F

I

A

T

L

G

G

W

W

T

N

Y
|
Y

T

W

F

Y

E

N

M
x
W

V

A

I

V

V

T

A

I

L

A

A

V

D

D

V

L

T

V

A

A

F

A

G

Q

I

L

Y

V

M

M

G

S

L

W

W

W

Y

F

P

P

D

D

V

T

P

P

R

G

W

W

I

I

W

W

V

S

L

A

S

L

I

F

I

L

F

G

F

V

I

I

G

F

A

L

M

L

N

N

L

Y

C

I

S

S

V

V

R

R

V

G

F

F

G

G

E

E

M

A

E

E

F

Y

W

W

L

F

S

S

L

L

I

I

K
|
K

V

V

V

T

A

T

I

V

I

I

A

V

M

F

I

I

V

I

A

V

G

G

G

V

S

L

I

M

I

I

F

I

F

G

G

I

F

F

G

K

N

G

A

A

F

Q

P

P

A

A

T

-

G

G

L

W

E

S

N

N

L

-

W

W

S

T

H

I

G

G

G

E

F

-

A

A

P

P

-

F

-

A

N

G

G

G

W

F

E

A

G

A

I

M

I

I

A

G

S

V

L

A

G

M

I

I

V

V

M

G

F
|
F

A

S

F

F

G

Q

G

G

V

T

E
|
E

I

L

I

I

G

G

V

I

T

A

A

A

A

G

E
|
E

A

S

K

E

N

D

P

P

Q

A

K

K

V

N

I

I

P

P

Q

R

A

A

I

V

N

R

T

Q

I

V

P

F

L

W

R

R

I

I

V

L

L

L

F

F

Y

Y

V

V

C

F

T

A

L

I

A

L

I

I

L

I

M

S

A

L

I

I

F

I

P

P

W

Y

-

T

-

D

-

P

-

S

-

L

-

R

N

N

S
x
D

F

V

G

K

E
x
D

R

I

G

S

-

V

S

S

P

P

F

F

V

T

L

L

I

V

F

F

D

Q

G

H

L

A

G

G

I

L

P

L

A

S

A

A

T

A

I

V

L

M

N

N

I

A

I

V

V

I

I

L

S

T

A

A

S

V

I

L

S

S

A

A

I

G

N

N

S

S

D

G

I

M

F

Y

G

A

A

S

G

T

R

R

M

M

M

L

Y

Y

G

T

M

L

A

A

K

C

E

D

G

G

L

K

A

A

P

P

K

R

S

I

F

F

Q

A

R

K

I

L

A

S

S

R

N

G

G

G

V

V

P

P

-

R

-

N

-

A

-

L

W

Y

M

A

T

T

V

T

V

V

V

I

M

A

G

G

V

L

A

C

L

F

L

L

A

T

A

S

V

M

V

F

L

G

N

N

Y

-

L

-

M

-

P

-

E

Q

Q

T

V

V

F

Y

V

L

L

W

I

L

A

L

S

N

L

T

A

S

A

G

F

M

A

T

T

G

V

F

W

I

V

A

W

W

V

L

M

G

I

I

L

A

L

I

A

S

H

H

F

Y

A

R

M

F

R

R

G

G

-

Y

-

V

L

L

S

Q

A

G

E

H

E

D

R

I

G

N

N

D

I

L

A

P

F

Y

P

R

V

S

P

G

L

F

W

F

P

P

V

L

A

G

P

P

L

I

L

F

T

A

L

-

F

F

M

I

G

L

L

C

V

L

I

I

A

I

V

T

L

L

G

G

M

Q

V

N

E

Y

E
|
E

Y102 (= Y97) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
W106 (≠ M101) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
K163 (= K158) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
F216 (= F212) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
E222 (= E218) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
E230 (= E226) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
D275 (≠ S264) 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 (≠ E267) 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.
E438 (= E426) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
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.

P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
30% identity, 95% coverage: 8:445/459 of query aligns to 83:541/590 of P04817

query
sites
P04817

H

E

L

V

L

K

R

R

G

E

L

L

N

K

A

Q

R

R

H

H

I

I

R

G

F

M

I

I

A

A

L

L

G

G

S

G

A

T

I

I

G

G

T

T

G

G

L

L

F

F

Y

I

G

G

S

L

A

S

S

T

A
x
P

I

L

K

T

A

N

A

A

G

G

P

P

-

V

A

G

V

A

L

L

L

I

A

S

Y

Y

L

L

I

F

G

M

G

G

A

S

A

L

V

A

F

Y

I

S

V

V

M

T

R

Q

A

S

L

L

G

G

E

E

M

M

A

A

V

T

R

F

N

I

P
|
P

V
|
V

S

T

G

S

S
|
S

F

F

S

T

S

V

Y

F

A

S

R

Q

Q

R

Y

F

L

L

G

S

P

P

L

A

A

F

G

G

F

A

I

A

T

N

G

G

W

Y

T

M

Y
|
Y

T

W

F

F

E

S

M

W

V

A

I

I

V

T

A

F

L

A

A

L

D

E

V

L

T

S

A

V

F

V

G

G

I

Q

Y

V

M

I

G

Q

L

F

W

W

Y

T

P

Y

D

K

V

V

P

P

R

L

W

A

I

A

W

W

V

I

L

S

S

I

I

F

I

W

F

V

F

I

I

I

G

T

A

I

M

M

N

N

L

L

C

F

S

P

V

V

R

K

V

Y

F

Y

G

G

E

E

M

F

E

E

F

F

W

W

L

V

S

A

L

S

I

I

K

K

V

V

V

L

A

A

I

I

A

G

M

F

I

L

V

I

A

Y

G

C

G

F

S

C

I

M

I

V

F

-

F

C

G

G

F

A

G

G

N

V

A

T

F

G

P

P

A

V

T

-

G

G

L

F

E

R

N

Y

L

W

W

R

S

N

H

P

G

G

G

A

F

W

A

G

P

P

N

G

-

I

-

S

-

K

-

D

-

K

-

N

-

E

-

G

-

R

-

F

-

L

G

G

W

W

E

-

G

-

I

-

I

V

A

S

S

S

L

L

G

I

I

N

V

A

M

A

F

F

A

T

F

F

G

Q

G

G

V

T

E

E

I

L

I

V

G

G

V

I

T

T

A

A

A
x
G

E

E

A

A

K

A

N

N

P
|
P

Q

R

K

K

V

S

I

V

P

P

Q

R

A

A

I

I

N

K

T

K

I

V

P

V

L

F

R

R

I

I

V

L

L

T

F

F

Y

Y

V

I

C

G

T

S

L

L

A

L

I

F

L

I

M

G

A

L

I

L

F

V

P

P

W

Y

N

N

-

D

-

P

-

K

-

L

-

T

-

Q

-

S

S
x
T

F
x
S

G
x
Y

E

V

R

S

G

T

S

S

P

P

F

F

V

I

L

I

I

A

F

I

D

E

G

N

L

S

G

G

I

T

P

K

A

V

A

L

A

P

T

H

I

I

L

F

N

N

I

A

I

V

V

I

I

L

S

T

A

T

S

I

I

I

S

S

A

A

I

A

N

N

S

S

D

N

I

I

F

Y

G

V

A

G

G

S

R

R

M

I

M

L

Y

F

G

G

M

L

A

S

K

K

E

N

G

K

L

L

A

A

P

P

K

K

S

F

F

L

Q

S

R

R

I

T

A

T

S

K

N

G

G

G

V

V

P

P

W

Y

M

I

T

A

V

V

V

F

V

V

M

T

G

A

V

A

A

F

L

G

L

A

A

L

A

A

V

Y

V

M

L

E

N

T

Y

S

L

T

M

G

P

G

E

D

Q

K

V

V

F

F

V

E

L
x
W

I

L

A

L

S

N

L

I

A

T

A

G

F

V

A

A

T

G

V
x
F

W

F

V

A

W

W

V

L

M

F

I

I

L

S

L

I

A

S

H

H

F

I

A

R

M

F

R

M

R

Q

G

A

L

L

S

K

A

Y

E

R

-

G

-

I

E

S

R

R

G

D

N

E

I

L

A

P

F

F

P

K

V

A

P

K

L

L

W

M

P

P

V

G

A

L

P

A

L

Y

T

A

L

A

L

T

F

F

M

M

G

T

L

I

V

I

I

I

A

I

V

I

L

Q

G

G

M

F

V

T

-

A

-

F

-

A

-

P

E

K

E

F

T

N

R

G

I

V

A

S

L

F

I

A

A

A

G

A

L

Y

V

I

W

S

L

I

G

F

L

L

L

F

T

L

A

A

V

V

W

W

P113 (≠ A38) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
P148 (= P72) mutation to L: In CAN1-337; confers citrulline transport activity in GAP1-deleted cells and leads to sensitivity to L-glutamic acid alpha-hydroxamate, alpha-aminoisobutyrate, 3-chloro-L-alanine, L-ethionine, L-allylglycine, and D-histidine, but not sensitivity to L-aspartic acid alpha-hydroxamate or p-fluoro-L-phenylalanine.
V149 (= V73) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
S152 (= S76) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
Y173 (= Y97) mutation to D: In CAN1-306; confers citrulline transport activity in GAP1-deleted cells.; mutation to H: In CAN1-327; confers citrulline transport activity in GAP1-deleted cells.
G308 (≠ A225) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
P313 (= P230) mutation to S: In CAN1-329; confers citrulline transport activity in GAP1-deleted cells and leads to sensitivity to L-glutamic acid alpha-hydroxamate, alpha-aminoisobutyrate, 3-chloro-L-alanine, L-ethionine, L-allylglycine, and D-histidine, L-aspartic acid alpha-hydroxamate and p-fluoro-L-phenylalanine.
TS 354:355 (≠ SF 264:265) mutation Missing: In CAN1-318; confers citrulline transport activity in GAP1-deleted cells.
Y356 (≠ G266) mutation to H: In CAN1-340; confers citrulline transport activity in GAP1-deleted cells.; mutation to N: In CAN1-339; confers citrulline transport activity in GAP1-deleted cells.
W451 (≠ L361) mutation to C: In CAN1-328; confers citrulline transport activity in GAP1-deleted cells.; mutation to L: In CAN1-316; confers citrulline transport activity in GAP1-deleted cells.; mutation to S: In CAN1-335; confers citrulline transport activity in GAP1-deleted cells.
F461 (≠ V371) mutation to S: In CAN1-307; confers citrulline transport activity in GAP1-deleted cells.

Q9URZ4 Cationic amino acid transporter 1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 87% coverage: 4:403/459 of query aligns to 75:488/587 of Q9URZ4

query
sites
Q9URZ4

Q

E

N

D

K

G

P

T

H

A

L

L

L

K

R

R

G

S

L

L

N

K

A

S

R

R

H

H

I

M

R

Q

F

M

I

I

A

S

L

I

G

G

S

G

A

A

I

I

G

G

T

T

G

G

L

L

F

Y

Y

V

G

G

S

S

A

G

S

S

A

S

I

L

K

A

A

D

A

G

G

G

P

P

A

A

-

S

V

V

L

I

A

N

Y

Y

L

S

I

L

G

I

G

G

A

I

A

M

V

M

F

F

I

F

V

I

M

V

R

Y

A

A

L

L

G

G

E

E

M

M

A

A

V

V

R

A

N

Y

P

P

V

V

S

A

G

G

S

G

F

F

S

N

S

T

Y

Y

A

A

R

T

Q

R

Y

F

L

I

G

D

P

P

L

A

A

W

G

G

F

F

I

A

T

V

G

S

W

W

T

N

Y

Y

T

F

F

I

E

N

M

Y

V

F

I

V

V

T

A

F

L

P

A

L

D

E

V

L

T

T

A

T

F

C

G

A

I

I

Y

T

M

F

G

R

L

Y

W

W

Y

-

P

T

D

D

V

I

P

N

R

S

W

A

I

A

W

W

V

I

L

S

S

I

I

F

I

L

F

V

I

I

G

I

A

I

M

V

N

N

L

L

C

F

S

G

V

V

R

R

V

A

F

Y

G

G

E

E

M

V

E

E

F

F

W

I

L

L

S

S

L

T

I

V

K

K

V

V

A

A

I

T

I

F

A

G

M

F

I

I

V

I

A

L

G

A

G

I

S

I

I

I

I

N

F

C

F

G

G

G

F

V

G

P

N

T

A

D

F

H

P

R

A

G

T

Y

G

I

L

G

E

G

N

S

L

I

W

I

S

K

H

H

G

K

G

P

F

F

A

R

P

-

N

H

G

G

W

F

E

K

G

G

I

F

I

C

A

S

S

V

L

F

G

T

I

T

V

A

M

A

F

F

A

S

F

F

G

S

G

G

V

T

E

E

I

V

I

I

G

G

V

L

T

A

A

A

E

E

A

V

K

D

N

N

P

P

Q

Q

K

K

V

A

I

L

P

P

Q

H

A

A

I

V

N

K

T

Q

I

V

P

F

L

W

R

R

I

I

V

A

L

I

F

F

Y

Y

V

V

C

V

T

S

L

L

-

I

-

L

-

I

A

G

I

L

L

L

M

I

A

S

I

P

F

D

P

D

W

P

N

N

S

L

F

M

G

G

E

N

R

G

G

S

-

T

-

S

-

V

S

S

P

P

F

F

V

V

L

L

I

A

F

I

D

K

G

E

L

A

G

N

I

I

P

K

A

G

A

L

A

P

T

S

I

V

L

F

N

N

I

A

I

V

V

I

I

I

S

I

A

S

S

V

I

V

S

S

A

V

I

T

N

N

S

S

D

S

I

T

F

Y

G

T

A

A

G

G

R

R

M

T

M

L

Y

H

G

G

M

M

A

A

K

N

E

L

G

K

L

Q

A

A

P

P

K

S

S

F

F

F

Q

K

R

Y

I

T

A

D

S

R

N

L

G

G

V

R

P

P

W

L

M

L

T

A

V

M

V

I

V

V

M

V

G

L

V

L

-

F

-

G

-

F

A

A

L

Y

L

I

A

N

A

E

V

A

V

D

L

K

N

N

-

G

Y

N

L

D

M

V

P

S

E

D

Q

T

V

V

F

F

V

N

L

W

I

L

A

L

S

A

L

L

A

S

A

G

F

L

A

S

T

N

V

F

W

F

V

T

W

W

V

G

M

S

I

I

L

C

L

L

A

C

H

H

F

I

A

I

M

F

R

R

-

L

-

A

-

F

-

K

R

Q

G

G

L

H

S

S

A

L

E

K

E

E

R

L

G

G

N

F

I

V

A

S

F

-

P

P

V

M

P

G

L

I

W

W

Sites not aligning to the query:

29 modified: Phosphoserine
30 modified: Phosphoserine
37 modified: Phosphoserine

P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
29% identity, 86% coverage: 9:401/459 of query aligns to 86:493/602 of P19145

query
sites
P19145

L

L

L

K

R

H

G

H

L

L

N

K

A

N

R

R

H

H

I

L

R

Q

F

M

I

I

A

A

L

I

G

G

S

G

A

A

I

I

G

G

T

T

G

G

L

L

F

L

Y

V

G

G

S

S

A

G

S

T

A

A

I

L

K

R

A

T

A

G

G

G

P

P

A

A

V

S

L

L

-

I

A

G

Y

W

L

G

I

S

G

T

G

G

A

T

A

M

V

I

F

Y

I

A

V

M

M

V

R

M

A

A

L

L

G

G

E

E

M

L

A

A

V

V

R

I

N

F

P

P

V

I

S

S

G

G

S

G

F

F

S

T

Y

Y

A

A

R

T

Q

R

Y

F

L

I

G

D

P

E

L

S

A

F

G

G

F

Y

I

A

T

N

G

N

W

F

T

N

Y

Y

T

M

F

L

E

Q

M

W

V

L

I

V

V

V

A

L

L

P

A

L

D

E

V

I

T

V

A

S

F

A

G

S

I

I

Y

T

M

V

G

N

L

F

W

W

Y

G

P

T

D

D

V

-

P

P

R

K

W

Y

I

R

W

D

V

G

L

F

S

V

I

A

I

L

F

F

F

W

I

L

G

A

A

I

-

V

-

I

M

I

N

N

L

M

C

F

S

G

V

V

R

K

V

G

F

Y

G

G

E

E

M

A

E

E

F

F

W

V

L

F

S

S

L

F

I

I

K

K

V

V

V

I

A

T

I

V

A

G

M

F

I

I

V

I

A

L

G

G

G

-

S

-

I

I

F

L

F

N

G

C

F

G

G

G

N

G

A

P

F

T

P

G

A

G

T

Y

G

I

L

G

E

G

N

K

L

Y

W

W

S

H

H

D

-

P

G

G

G

A

F

F

A

A

P

G

N

D

-

T

-

P

-

G

-

A

G

K

W

F

E

K

G

G

I

V

I

C

A

S

S

V

L

F

G

V

I

T

V

A

M

A

F

F

A

S

F

F

G
x
A

G

G

V

S

E

E

I

L

I

V

G

G

V

L

T

A

A

A

A

S

E

E

A

S

K

V

N

E

P

P

Q

R

K

K

V

S

I

V

P

P

Q

K

A

A

I

A

N

K

T

Q

I

V

P

F

L

W

R

R

I

I

V

T

L

L

F

F

Y

Y

V

I

C

L

T

S

L

L

A

L

I

M

L

I

M

G

A

L

I

L

F

V

P

P

W

Y

N

N

-

D

-

K

-

S

-

L

-

I

-

G

-

A

-

S

S

S

F

V

G

D

E

A

R

A

G

A

S

S

P

P

F

F

V

V

L

I

I

A

F

I

D

K

G

T

L

H

G

G

I

I

P

K

A

G

A

L

A

P

T

S

I

V

L

V

N

N

I

V

V

I

I

L

S

I

A

A

S

V

I

L

S

S

A

V

I

G

N

N

S

S

D

A

I

I

F

Y

G

A

A

C

G

S

R

R

M

T

M

M

Y

V

G

A

M

L

A

A

K

E

E

Q

G

R

L

F

A

L

P

P

K

E

S

I

F

F

Q

S

R

Y

I

V

A

D

S

R

N

K

G

G

V

R

P

P

W

L

M

V

T

G

V

I

V

A

V

V

M

T

G

S

V

A

A

F

L

G

L

L

A

I

A

A

V

F

V

V

L

A

N

A

Y

S

L

K

M

K

P

E

E

G

Q

E

V

V

F

F

V

N

L

W

I

L

A

L

S

A

L

L

A

S

A

G

F

L

A

S

T

S

V

L

W

F

V

T

W

W

V

G

M

G

I

I

L

C

L

I

A

C

H

H

F

I

A

R

M

F

R

R

R

K

G

A

L

L

S

A

A

A

E

Q

E

G

R

R

G

G

-

L

-

D

N

E

I

L

A

S

F

F

P

K

V

S

P

P

A297 (≠ G215) mutation to V: Impairs basic amino-acids transport and regulation by these amino-acids.

Sites not aligning to the query:

76 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

P48813 High-affinity glutamine permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
24% identity, 91% coverage: 2:417/459 of query aligns to 138:570/663 of P48813

query
sites
P48813

Q

Q

Q

E

Q

Q

N

K

K

Q

P

E

H

N

L

L

L

K

R

K

G

S

L

I

N

K

A

P

R

R

H

H

I

T

R

V

F

M

I

M

A

S

L

L

G

G

S

T

A

G

I

I

G

G

T

T

G

G

L

L

F

L

Y

V

G

G

S

N

A

S

S

K

A

V

I

L

K

N

A

N

A

A

G

G

P

P

A

G

-

G

V

L

L

I

A

G

Y

Y

L

A

I

I

G

M

G

G

A

S

A

C

V

V

F

Y

I

C

V

I

M

I

R

Q

A

A

L

C

G

G

E

E

M

L

A

A

V

V

-

I

R

Y

N

S

P

D

V

L

S

I

G

G

S

G

F

F

S

N

S

T

Y

Y

A

P

R

L

Q

F

Y

L

L

V

G

D

P

P

L

A

A

L

G

G

F

F

I

S

T

V

G

A

W

W

T

L

Y

F

T

C

F

L

E

Q

M

W

V

L

I

C

V

V

A

C

L

P

A

L

D

E

V

L

T

V

A

T

F

A

G

S

I

M

Y

T

M

I

G

K

L

Y

W

W

Y

T

P

T

D

S

V

V

P

N

R

P

W

D

I

V

W

F

V

V

L

V

S

I

I

F

I

Y

F

V

F

L

I

I

G

V

A

V

M

I

N

N

L

V

C

F

S

G

V

A

R

K

V

G

F

Y

G

A

E

E

M

A

E

D

F

F

W

F

L

F

S

N

L

C

I

C

K

K

V

I

V

L

A

M

I

I

I

V

A

G

M

F

I

F

V

I

A

L

G

A

G

-

S

I

I

I

F

D

F

C

G

G

F

G

G

A

N

G

A

T

F

D

P

G

A

Y

T

I

G

G

L

S

E

K

N

Y

L

W

W

R

S

D

H

P

G

G

G

A

F

F

A

R

P

G

N

D

G

T

-

P

-

I

-

Q

-

R

W

F

E

K

G

G

I

V

A

A

S

T

L

F

G

V

I

T

V

A

M

A

F

F

A

A

F

F

G

G

G

M

V

S

E

E

I

Q

I

L

G

A

V

M

T

T

A

A

A

S

E

E

A

Q

K

S

N

N

P

P

Q

R

K

K

V

A

I

I

P

P

Q

S

A

A

I

A

N

K

T

K

I

M

P

I

L

Y

R

R

I

I

V

L

L

F

F

V

Y

F

V

L

C

A

T

S

L

L

A

T

I

L

L

V

M

G

A

F

I

L

F

V

P

P

W

Y

N

T

S

S

F

D

-

Q

-

L

-

G

-

A

-

G

-

S

G

A

E

T

R

K

G

A

S

S

P

P

F

Y

V

V

L

I

I

A

F

V

D

S

G

S

L

H

G

G

I

V

P

R

A

V

A

P

T

H

I

F

L

I

N

N

I

A

I

V

V

I

I

L

S

L

A

S

S

V

I

L

S

S

A

V

I

A

N

N

S

G

D

A

I

F

F

Y

G

T

A

S

G

S

R

R

M

I

M

L

Y

M

G

S

M

L

A

A

K

K

E

Q

G

G

L

N

A

A

P

P

K

K

S

C

F

F

Q

D

R

Y

I

I

A

D

S

R

N

E

G

G

V

R

P

P

W

A

M

A

T

A

V

M

V

L

V

V

M

S

G

A

V

L

A

F

L

G

L

V

A

I

A

A

V

F

V

C

L

A

N

S

Y

S

L

K

M

K

P

E

E

E

Q

D

V

V

F

F

V

T

L

W

I

L

A

L

S

A

L

I

A

S

A

G

F

L

A

S

T

Q

V

L

W

F

V

T

W

W

V

I

M

T

I

I

L

C

L

L

A

S

H

H

F

I

A

R

M

F

R

R

G

A

L

M

S

K

A

V

E

Q

E

G

R

R

-

S

-

L

G

G

N

E

I

V

A

G

F

Y

P

K

-

S

-

Q

V

V

P

G

L

V

W

W

P

G

V

S

A

A

P

Y

L

A

L

V

T

L

L

M

F

V

M

L

G

A

L

L

V

I

Sites not aligning to the query:

132 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Q03770 SPS-sensor component SSY1; Amino-acid permease homolog SSY1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
24% identity, 91% coverage: 6:422/459 of query aligns to 274:771/852 of Q03770

query
sites
Q03770

K

K

P

Y

H

H

L

I

L

Q

R

R

G

K

L

L

N

K

A

V

R

R

H

H

I

I

R

Q

F

M

I

L

A

S

L

I

G

G

S

A

A

C

I

F

G

S

T

V

G

G

L

L

F

F

Y

L

G

T

S

S

A

G

S

K

A

A

I

F

K

S

A

I

A

A

G

G

P

P

-

F

A

G

V

T

L

L

A

G

Y

F

L

G

I

L

G

T

G

G

A

S

A

I

V

I

F

L

I

A

V

T

M

M

R

L

A

S

L

F

G

T

E

E

M

L

A

S

V

T

R

L

N

I

P

P

V

V

S

S

G

S

S

G

F

F

S

S

S

G

Y

L

A

A

R

S

Q

R

Y

F

L

V

G

E

P

D

L

A

A

F

G

G

F

F

I

A

T

L

G

G

W

W

T

T

Y

Y

T

W

F

I

E

S

M

C

V

M

I

L

V

A

A

L

L

P

A

A

D

Q

V

V

T

S

A

S

F

S

G
x
T

I

F

Y

Y

M

L

G

S

L

Y

W

Y

Y

N

P

N

-

V

D

N

V

I

P

S

R

K

W

G

I

V

W

T

V

A

L

G

S

F

I

I

I

T

F

L

F

F

I

S

G

A

-

F

-

S

-

I

A

V

M

V

N

N

L

L

C

L

S

D

V

V

R

S

V

I

F

M

G

G

E

E

M

I

E

V

F

Y

W

V

L

A

S

G

L

I

I

S

K

K

V

V

V

I

A

I

I

A

I

I

A

L

M

M

I

V

-

F

-

T

-

M

-

I

-

L

-

N

V

A

A

G

G

H

G

G

S

N

I

D

I

I

F

H

F

E

G

G

F

V

G

G

N

F

A

R

F

Y

-

W

-

D

P

S

A

S

T

K

G

S

L

V

E

R

N

N

L

L

W

-

S

T

H

Y

G

G

G

L

F

Y

A

R

P

P

N

T

-

F

-

D

-

L

-

A

-

D

-

A

-

G

-

E

-

G

G

S

W

K

E

K

G

G

I

I

I

S

A

G

S

P

L

K

G

G

-

R

-

F

-

L

-

A

-

T

-

A

-

S

-

V

-

M

-

L

I

I

V

S

M

T

F

F

A

A

F

F

G

S

G

G

V

V

E

E

I

M

I

T

G

F

V

L

T

A

A

S

A

G

E

E

A

A

K

I

N

N

P

P

Q

R

K

K

V

T

I

I

P

P

Q

S

A

A

I

T

N

K

-

R

-

T

-

F

T

S

I

I

P

V

L

L

R

I

I

S

V

Y

L

V

F

F

Y

L

V

I

C

F

T

S

L

V

A

G

I

I

-

N

-

I

-

Y

-

S

-

G

-

D

-

P

-

R

L

L

M

L

A

S

I

Y

F

F

P

P

W

G

N

I

S

S

F

E

G

K

E

R

-

Y

-

E

-

A

-

I

-

K

-

G

-

T

-

G

-

M

-

D

-

W

-

R

-

L

-

R

-

T

-

N

-

C

R

R

G

G

-

G

-

I

-

D

-

Y

-

R

-

Q

-

I

-

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-

V

-

G

-

T

-

G

-

Y

-

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S

S

P

P

F

W

V

V

L

V

I

A

F

L

D

Q

G

N

L

F

G

G

I

L

P

C

A

T

A

F

A

A

T

S

I

A

L

F

N

N

I

A

I

I

V

L

I

I

S

F

A

F

S

T

I

A

S

T

A

A

I

G

N

I

S

S

D

S

I

L

F

F

G

S

A

C

G

S

R

R

M

T

M

L

Y

Y

G

A

M

M

A

S

K

V

E

Q

G

R

L

K

A

A

P

P

K

P

S

V

F

F

Q

E

R

I

I

C

A

S

S

K

N

R

G

G

V

V

P

P

W

Y

M

V

T

S

V

V

V

I

V

F

M

S

G

S

V

L

-

F

A

S

L

V

L

I

A

A

A

Y

V

I

V

A

L

V

N

D

Y

Q

L

T

M

A

P

I

E

E

Q

N

V

-

F

F

V

D

L

V

I

L

A

A

S

N

L

V

A

S

F

A

A

S

T

T

V

S

W

I

V

I

W

W

V

M

M

G

I

L

L

N

L

L

A

S

-

F

-

L

-

R

-

F

H

Y

F

Y

A

A

M

L

R

K

R

Q

G

R

L

K

S

D

A

I

E

I

E

S

R

R

G

N

N

D

I

S

A

S

F

Y

P

P

V

Y

-

K

-

S

P

P

L

F

W

Q

P

P

V

Y

A

L

P

A

L

I

L

Y

T

G

L

L

L

V

F

G

M

C

G

S

L

L

V

F

I

V

A

I

V

F

L

M

G

G

T382 (≠ G113) mutation T->H,L: Constitutively active, up-regulates amino acid permease transcription in response to subthreshold concentrations of amino acids.; mutation to K: In SSY1-102; constitutively active, up-regulates amino acid permease transcription in the absence of amino-acids.; mutation to R: Constitutively active, up-regulates amino acid permease transcription in the absence of amino acids.

6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
26% identity, 91% coverage: 37:455/459 of query aligns to 52:457/458 of 6f34A

query
sites
6f34A

S

A

A

A

I

A

K

E

A

H

A

A

G

G

P

P

A

A

V

L

L

V

L

L

A

S

Y

F

L

I

I

L

G

S

G

G

A

L

A

A

V

C

F

V

I

F

V

A

M

A

R

L

A

C

L

Y

G

A

E

E

M

F

A

A

V

S

R

T

N

V

P

P

V

V

S

S

G

G

S

S

F

A

S

Y

S

T

Y

Y

A

S

R

Y

Q

A

Y

T

L

F

G

G

P

E

L

L

A

I

G

A

F

W

I

I

T

L

G

G

W

W

T

D

Y

L

T

I

F

L

E
|
E

M
x
Y

V

G

I

V

V
x
A

A

S

L

S

A

A

D

V

V

A

T

V

A

G

F

W

-

S

G

G

I

Y

Y

F

M

Q

G

G

L

L

W

L

Y

S

P

G

D

E

V

L

P

P

R

K

W

A

I

L

W

T

V

S

L

A

S

Y

I

D

I

P

F

A

F

K

I

G

G

T

A

F

M

I

N

D

L

L

C

P

S

A

V

I

R

I

V

I

F

V

G

L

E

F

M

I

E

T

F

F

W

L

L

L

S

N

L

L

-

G

-

A

-

K

-

S

I
x
A

K
x
R

V

F

V

N

A

A

I

V

I

I

A

V

M
x
A

I
|
I

V

K

A

V

G
x
A

G

V

S

V

I

L

I
x
L

F

F

F

L

G

A

F

V

G

G

N

V

A
x
W

F
x
Y

P

-

A

-

T

V

G

K

L

P

E

E

N

N

L

-

W

W

S

T

H

P

G

-

F

F

A

M

P

P

N

Y

G

G

W

F

E

S

G

G

I

V

I

A

A

T

S

G

L

A

G

A

I

T

V

V

M

F

F
|
F

A
|
A

F

Y

G
x
I

G

G

V

F

E

D

I

A

I

V

G

S

V

T

T

A

A

A

A

E

E

E

A

V

K

R

N

N

P

P

Q

Q

K

R

V

D

I

M

P

P

Q

I

A

G

I

I

N

I

T

V

I

S

P

L

L

L

R

V

I

C

V

T

L

L

F

L

Y

Y

V

I

C

A

T

V

L

S

A

L

I

V

L

L

M

T

A

G

I

I

F

V

P

P

W

Y

N

E

S

Q

F

L

G

N

E

V

R

K

G

-

S

N

P

P

F

V

V

A

L

F

I

A

F

L

D

N

G

Y

L

I

G

H

I
x
Q

P

D

A

W

A
x
V

A

A

T

G

I

F

L

I

N

S

I

L

I

G

V

A

I

I

S

A

A

G

S

I

I

T

S

T

A
x
V

I

L

N

L

S

V

D

S

I

M

F

Y

G

G

A

Q

G

T

R

R

M

L

M

F

Y

Y

G

A

M

I

A

S

K

R

E

D

G

G

L

L

A

L

P

P

K

K

S

V

F

F

Q

A

R

R

I

I

A

S

-

P

S

T

N

R

G

Q

V

V

P

P

W

Y

M

V

T

N

V

T

V

W

V

L

M

T

G

G

-

A

V

V

A

A

L

V

L

F

A

A

A

G

V

I

-

P

L

L

N

N

Y

K

L

L

M

A

P

E

E

-

Q

-

V

-

F

L

V

T

L

N

I

I

A

G

S

T

L

L

A

F

A

A

F

F

A

I

T

T

V

V

W

S

V

I

W

G

V

V

M

L

I

V

L

L

L

-

A

-

H

-

F

-

A

-

M

-

R

R

R

K

G

T

L

Q

S

P

A

D

E

L

E

K

R

R

G

-

N

-

I

-

A

A

F

F

P

R

V

V

P

P

L

F

W

V

P

P

V

V

A

V

P

P

L

I

L

L

T

A

L

V

L

L

F

F

M

C

G

G

L

Y

V

L

I

-

A

-

V

V

L

L

G

Q

M

L

V

P

E

A

E

M

T

T

R

W

I

I

A

G

L

F

I

V

A

S

G

-

L

-

V

-

W

W

L

L

G

L

L

I

L

G

T

L

A

V

V

I

W

Y

F

F

A

I

R

Y

V

G

R

R

K

K

N

H

A

S

V

E

L

L

binding arginine: E115 (= E100), Y116 (≠ M101), A119 (≠ V104), F228 (= F212), A229 (= A213), I231 (≠ G215), V314 (≠ A299)
binding cholesterol: W201 (≠ A180), Y202 (≠ F181)
binding : A178 (≠ I157), R179 (≠ K158), A186 (≠ M165), I187 (= I166), A190 (≠ G169), L194 (≠ I173), Q296 (≠ I281), V299 (≠ A284)

Sites not aligning to the query:

binding arginine: 40, 42, 43, 44
binding : 28, 30, 31, 34

5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
26% identity, 91% coverage: 37:455/459 of query aligns to 50:455/456 of 5oqtA

query
sites
5oqtA

S

A

A

A

I

A

K

E

A

H

A

A

G

G

P

P

A

A

V

L

L

V

L

L

A

S

Y

F

L

I

I

L

G

S

G

G

A

L

A

A

V

C

F

V

I

F

V

A

M

A

R

L

A

C

L

Y

G

A

E

E

M

F

A

A

V

S

R

T

N

V

P

P

V

V

S

S

G

G

S

S

F

A

S

Y

S

T

Y

Y

A

S

R

Y

Q

A

Y

T

L

F

G

G

P

E

L

L

A

I

G

A

F

W

I

I

T

L

G

G

W

W

T

D

Y

L

T

I

F

L

E

E

M

Y

V

G

I

V

V

A

A

S

L

S

A

A

D

V

V

A

T

V

A

G

F

W

-

S

G

G

I

Y

Y

F

M

Q

G

G

L

L

W

L

Y

S

P

G

D

E

V

L

P

P

R

K

W

A

I

L

W

T

V

S

L

A

S

Y

I

D

I

P

F

A

F

K

I

G

G

T

A

F

M

I

N

D

L

L

C

P

S

A

V

I

R

I

V

I

F

V

G

L

E

F

M

I

E

T

F

F

W

L

L

L

S

N

L

L

-

G

-

A

-

K

-

S

I
x
A

K
x
R

V

F

V

N

A

A

I

V

I

I

A

V

M
x
A

I

I

V

K

A

V

G
x
A

G

V

S

V

I

L

I
x
L

F

F

F

L

G

A

F

V

G

G

N

V

A

W

F

Y

P

-

A

-

T

V

G

K

L

P

E

E

N

N

L

-

W

W

S

T

H

P

G

-

F

F

A

M

P

P

N

Y

G

G

W

F

E

S

G

G

I

V

I

A

A

T

S

G

L

A

G

A

I

T

V

V

M

F

F
|
F

A
|
A

F

Y

G
x
I

G

G

V

F

E

D

I

A

I

V

G

S

V

T

T

A

A

A

A

E

E

E

A

V

K

R

N

N

P

P

Q

Q

K

R

V

D

I

M

P

P

Q

I

A

G

I

I

N

I

T

V

I

S

P

L

L

L

R

V

I

C

V

T

L

L

F

L

Y

Y

V

I

C

A

T

V

L

S

A

L

I

V

L

L

M

T

A

G

I

I

F

V

P

P

W

Y

N

E

S

Q

F

L

G

N

E

V

R

K

G

-

S

N

P

P

F

V

V

A

L

F

I

A

F

L

D

N

G

Y

L

I

G

H

I
x
Q

P

D

A

W

A
x
V

A

A

T

G

I

F

L

I

N

S

I

L

I

G

V

A

I

I

S

A

A

G

S

I

I

T

S

T

A

V

I

L

N

L

S

V

D

M

I

M

F

Y

G

G

A

Q

G

T

R

R

M

L

M

F

Y

Y

G

A

M

I

A

S

K

R

E

D

G

G

L

L

A

L

P

P

K

K

S

V

F

F

Q

A

R

R

I

I

A

S

-

P

S

T

N

R

G

Q

V

V

P

P

W

Y

M

V

T

N

V

T

V

W

V

L

M

T

G

G

-

A

V

V

A

A

L

V

L

F

A

A

A

G

V

I

-

P

L

L

N

N

Y

K

L

L

M

A

P

E

E

-

Q

-

V

-

F

L

V

T

L

N

I

I

A

G

S

T

L

L

A

F

A

A

F

F

A

I

T

T

V

V

W

S

V

I

W

G

V

V

M

L

I

V

L

L

L

-

A

-

H

-

F

-

A

-

M

-

R

R

R

K

G

T

L

Q

S

P

A

D

E

L

E

K

R

R

G

-

N

-

I

-

A

A

F

F

P

R

V

V

P

P

L

F

W

V

P

P

V

V

A

V

P

P

L

I

L

L

T

A

L

V

L

L

F

F

M

C

G

G

L

Y

V

L

I

-

A

-

V

V

L

L

G

Q

M

L

V

P

E

A

E

M

T

T

R

W

I

I

A

G

L

F

I

V

A

S

G

-

L

-

V

-

W

W

L

L

G

L

L

I

L

G

T

L

A

V

V

I

W

Y

F

F

A

I

R

Y

V

G

R

R

K

K

N

H

A

S

V

E

L

L

binding alanine: F226 (= F212), A227 (= A213), I229 (≠ G215)
binding : A176 (≠ I157), R177 (≠ K158), A184 (≠ M165), A188 (≠ G169), L192 (≠ I173), Q294 (≠ I281), V297 (≠ A284)

Sites not aligning to the query:

binding alanine: 38, 40, 41, 42
binding : 24, 26, 28, 29, 32

P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
24% identity, 88% coverage: 49:451/459 of query aligns to 58:447/461 of P76037

query
sites
P76037

A

S

Y

Y

L

L

I

L

G

A

G

L

A

A

A

G

V

V

F

L

I

F

V

T

M

A

R

I

A

S

L

Y

G

G

E

K

M

L

A

V

V

R

R

Q

N

F

P

P

V

E

S

A

G

G

S

S

F

A

S

Y

S

T

Y

Y

A

A

R

Q

Q

K

Y

S

L

I

G

N

P

P

L

H

A

V

G

G

F

F

I

M

T

V

G

G

W

W

T

S

Y

S

T

L

F

L

E

D

M
x
Y

V

L

I

F

V

L

A

P

L

M

A

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V

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A

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F

A

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K

I

I

Y

Y

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L

Y

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P

D

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V

V

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P

R

P

W

W

I

V

W

W

V

V

L

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T

I

F

I

V

F

A

F

I

I

L

G

T

A

A

M

A

N

N

L

L

C

K

S

S

V

V

R

N

V

L

F

V

G

A

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N

M

F

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N

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W

-

L

-

S

T

L

L

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A

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M

M

I

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G

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S

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F

I

I

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F

F

L

G

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F

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N

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A

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P

K

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G

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F

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I

G

P

I

I

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A

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I

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C

F

F

A

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F

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D

I

A

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G

T

V

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A

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P

N

D

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I

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I

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F

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V

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N

V

L

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-

I

-

L

-

L

F

A

N

H

H

F

F

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M

R

R

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G

G

L

M

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N

A

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L

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A

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L

L

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G

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V

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W

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L

L

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Y

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W

F

Y

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L

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I

A

R

R

R

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Y

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K

K

Y110 (≠ M101) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.

O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
23% identity, 85% coverage: 21:411/459 of query aligns to 20:397/438 of O34739

query
sites
O34739

I

L

A

V

L

I

G

G

S

T

A

I

I

I

G

G

T

S

G

G

L

V

F

F

Y

M

G

K

S

P

A

G

S

A

A

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I

L

K

A

A

Y

A

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G

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K

-

M

V

A

L

L

L

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L

G

G

A

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A

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L

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I

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x
C

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G

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W

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W

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K

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A

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L

C
|
C

S

V

V

I

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N

V

I

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I

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G

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K

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Y

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G

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I

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V

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x
C

I

I

F

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F

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W

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G

G

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D

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Q

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I

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S

I

I

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S

G

A
x
C

I

L

N

N

S

G

D

K

I

V

F

L

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A

F

G

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R

R

M

V

M

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Y

F

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A

M

M

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K

E

E

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G

K

L

Q

A

L

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P

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F

-

A

-

E

K

K

S

L

F

S

Q

H

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V

I

H

A

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S

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F

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P

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W

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I

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I

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Q

M

I

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A

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A

A

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L

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N

Y

-

L

-

M

-

P

P

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D

Q

K

V

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F

-

V

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L

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I

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S

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A

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A

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M

I

A

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A

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F

A

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M

L

R

R

R

K

G

R

L

A

S

K

A

G

E

E

E

K

R

R

G

-

N

-

I

-

A

A

F

Y

P

S

V

V

P

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L

L

W

Y

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P

L

I

L

L

T

A

L

I

C94 (≠ T93) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
C141 (= C142) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
C168 (≠ S171) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
C291 (≠ A299) 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.

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)
24% identity, 82% coverage: 3:378/459 of query aligns to 22:430/629 of P30825

query
sites
P30825

Q

S

Q

R

N

E

K

E

P

T

H

R

L

L

L

S

R

R

G

C

L

L

N

N

A

T

R

F

H

D

I

L

R

V

F

A

I

L

A

G

L

V

G

G

S

S

A

T

I

L

G

G

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A

G

G

L

V

F

Y

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V

Y

L

G

A

S

G

A

A

S

V

A

A

I

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K

E

A

N

A

A

G

G

P

P

A

A

V

I

L

V

L

I

A

S

Y

F

L

L

I

I

G

A

A

L

A

A

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F

V

I

L

V

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A

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L

Y

G

G

E

E

M

F

A

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V

A

R

R

N

V

P

P

V

K

S

T

G

G

S

S

F

A

S

Y

S

L

Y

Y

A

S

R

Y

Q

V

Y

T

L

V

G

G

P

E

L

L

A

W

G

A

F

F

I

I

T

T

G

G

W

W

T

N

Y

L

T

I

F

L

E

S

M

Y

V

I

I

I

-

G

-

T

-

S

V

V

A

A

L

R

A

A

D

W

V

S

T

A

A

T

F

F

G

D

I

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Y

L

M

I

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G

L

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W

P

Y

I

P

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D

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V

F

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R

R

W

T

I

H

W

M

V

T

L

L

S

N

I

A

-

P

-

G

-

V

-

L

-

A

-

E

-

N

-

P

-

D

I

I

F

F

F

A

I

V

G

I

A

I

M

I

N

L

L

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C

L

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L

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F

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L

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K

K

V

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I

C

I

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M

V

I

L

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A

L

G

G

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F

-

I

-

M

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K

G

G

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S

I

V

I

K

F

N

F

W

-

Q

-

L

-

T

-

E

G

D

F

F

G

G

N
|
N

A

T

F

S

P

G

A

R

T

L

G

C

L

L

E

N

N

N

L

D

W

T

S

K

H

E

G

G

-

K

-

P

-

G

-

V

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G

G

G

F

F

A

M

P

P

N

F

G

G

W

F

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S

G

G

I

V

I

L

A

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S

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L

A

G

A

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C

M

F

F

Y

A

A

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F

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G

G

V

F

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D

I

C

I

I

G

A

V

T

T

T

A

G

A

E

E

E

A

V

K

K

N

N

P

P

Q

Q

K

K

V

A

I

I

P

P

Q

V

A

G

I

I

N

V

T

A

I

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P

L

L

L

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I

I

C

V

F

L

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Y

Y

V

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C

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L

S

A

A

I

A

L

L

M

T

A

L

I

M

F

M

P

P

W

Y

N

F

S

C

F

L

G

-

E

D

R

N

G

N

S

S

P

P

F

L

V

P

L

D

I

A

F

F

D

K

G

H

L

V

G

G

I

W

P

E

A

G

A

A

A

K

T

Y

I

A

L

V

N

A

I

V

I

G

V

S

I

L

S

C

A

A

S

L

I

S

S

A

A

S

I

L

N

L

S

G

D

S

I

M

F

F

G

P

A

M

G

P

R

R

M

V

M

I

Y

Y

G

A

M

M

A

A

K

E

E

D

G

G

L

L

A

L

P

F

K

K

S

F

F

L

Q

A

R

N

I

V

A

N

S

D

N

R

G

T

V

K

P

T

W

P

M

I

T

I

V

A

V

T

V

L

M

A

G

S

V

G

A

A

L

V

L

A

A

A

A

V

V

M

V

A

L

F

N

L

Y

F

L

D

M

L

P

K

E

D

Q

L

V

V

F

D

V

L

L

M

-

S

I

I

A

G

S

T

L

L

A

L

A

A

F

Y

A

S

T

L

V

V

W

A

V

A

W

C

V

V

M

L

I

V

L

L

N226 (= N179) modified: carbohydrate, N-linked (GlcNAc...) asparagine

6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
23% identity, 85% coverage: 21:412/459 of query aligns to 12:393/433 of 6f2wA

query
sites
6f2wA

I

V

A

V

L

V

G

G

S

T

A
x
V

I

I

G
|
G

T
x
A

G
|
G

L

I

F

F

Y

F

G

K

S

P

A

T

S

A

A

V

I

Y

K

G

A

A

G

G

-

A

P

P

A

G

V

L

-

G

L

L

A

A

Y

W

L

F

I

V

G

A

G

G

A

I

V

T

F

I

I

A

V

G

M

G

R

L

A

T

L

V

G

A

E

E

M

I

A

G

V

T

R

I

N

Y

P

P

V

Q

S

T

G

G

S

G

F

M

S

M

S

I

Y

Y

A

L

R

E

Q

K

Y

V

L

Y

G

G

P

R

L

W

A

L

G

G

F

F

I

L

T

V

G

G

W

W

T

A

Y

-

T

-

F

-

E

Q

M

M

V

V

I

I

V

Y

A

Y

L

P

A

A

D

N

V

I

T

A

A

A

F

L

G

A

I

I

Y

I

M

F

G

A

L

T

W

Q

Y

F

P

V

D

N

-

L

-

F

-

A

-

L

-

S

-

D

-

S

-

T

-

I

V

V

P

P

R

T

W

A

I

I

W

-

V

-

L

L

S

T

I

S

I

I

F

F

F

L

I

M

G

G

A

-

M

V

N

N

L

F

C

L

S

G

V

T

R

K

V

Y

F

S

G

G

E

W

M

I

E

Q

F

T

W

L

L

A

S

T

L

I

I

L

K

K

V

L

V

I

A

P

I

L

I

V

A

V

M

I

I

I

V

V

A

A

G

G

G

-

S

-

I

-

F

-

G

-

F

-

G

-

N

L

A

L

F

Y

P

P

A

G

T

G

G

G

L

V

E

I

N

R

L

L

-

V

-

P

-

F

-

S

-

V

W

E

S

T

H

H

G

P

G

V

F

L

A

T

P

S

N

F

G

G

W

-

E

S

G

A

I

L

I

I

A

A

S

T

L

L

G

-

I

-

V

-

M

-

F
|
F

A
|
A

F

Y

G
x
D

G

G

V

W

E

I

I

N

I

V

G

G

V

T

T

L

A

A

A

G

E

E

A

M

K

K

N

N

P

P

Q

G

K

K

V

M

I

L

P

P

Q

K

A

V

I

I

N

I

T

G

I

G

P

L

L

S

R

I

I

V

V

M

L

A

F

V

Y

Y

V

L

C

L

T

T

L

N

A

I

I

A

L

Y

M

L

A

F

I

V

F

L

P

D

W

S

N

S

S

Q

F

L

G

A

E

G

R

T

G

D

S

T

P

P

F

A

V

A

L

L

I

V

-

A

-

S

-

H

-

L

F

F

D

E

G

G

L

I

G

G

I

-

P

-

A

-

A

S

T

K

I

L

L

V

N

T

I

I

I

G

V

I

I

L

S

I

A

S

S

V

I

F

S

G

A

G

I

I

N

N

S

G

D

Y

I

I

F

I

G

S

A

G

G

L

R

R

M

V

M

P

Y

Y

G

A

M

L

A

A

K

T

E

Q

G

K

L

M

A

L

P

P

K

F

S

S

-

D

-

W

F

F

Q

A

R

R

I

I

A

N

S

-

N

-

G

-

V

-

P

P

W

K

M

T

T

N

V

L

V

P

V

I

M

N

G

G

V

G

A

L

L

V

L

M

A

L

A

G

V

I

V

A

L

I

N

V

Y

M

L

I

M

L

P

T

E

G

Q

Q

V

-

F

F

V

N

L

Q

I

L

A

T

S

D

L

L

A

I

A

V

F

F

A

V

T

I

V

W

W

F

V

F

W

I

V

T

M

L

I

T

L

F

L

I

A

A

H

V

F

I

A

I

M

L

R

R

R

K

G

T

L

Q

S

P

A

D

E

I

E

E

R

R

G

-

N

-

I

-

A

P

F

Y

P

R

V

V

P

P

L

F

W

Y

P

P

V

V

A

I

P

P

L

L

L

I

T

A

L

I

binding alpha-aminoisobutyric acid: V17 (≠ A26), G19 (= G28), A20 (≠ T29), G21 (= G30), F199 (= F212), A200 (= A213), D202 (≠ G215)

5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
23% identity, 83% coverage: 24:405/459 of query aligns to 17:398/437 of 5j4nA

query
sites
5j4nA

G

G

S

N

A
x
I

I

M

G

G

T

S

G

G

L

V

F

F

Y

L

G

L

S

P

A

A

S

N

A

L

I

A

K

S

A

T

A

G

G

G

P

I

A

A

V

I

L

Y

-

G

-

W

L

L

A

V

Y

T

L

I

I

I

G

G

G

A

A

L

A

G

V

L

F

S

I

M

V

V

M

Y

R

-

A

-

L

-

G

A

E

K

M

M

A

S

V

F

R

L

N

D

P

P

V

S

S

P

G

G

S

G

F

S

S

Y

S

A

Y

Y

A

A

R

R

Q

R

Y

C

L

F

G

G

P

P

L

F

A

L

G

G

F

Y

I

Q

T

T

G

N

W

V

T

L

Y

Y

T

W

F

L

E
x
A

M
x
C

V

W

I

I

V
x
G

A
x
N

L

I

A

A

D
x
M

V

V

T

V

A

I

F

G

G

V

I

G

Y

Y

M

L

G

S

L

Y

W

F

Y

F

P

P

D

I

V

L

P

K

R

D

-

P

-

L

-

V

-

L

-

T

-

I

-

T

-

C

-

V

-

L

W

W

I

I

W

F

V

V

L

L

S

-

I

-

F

-

I

-

G

-

A

-

M

L

N

N

L

I

C

V

S

G

V

P

R

K

V

M

F

I

G

T

E

R

M

V

E

Q

F

A

W

V

L

A

S

T

L

V

I

L

K

A

V

L

V

I

A

P

I

I

I

V

A

G

M

I

I

A

V

V

A

F

G

G

G

-

S

-

I

-

I

W

F

F

F

W

G

F

F

R

G

G

N

E

A

T

F

Y

P

M

A

A

T

A

G

-

L

-

E

-

N

-

L

-

W

W

S

N

H

V

G

S

G

G

F

L

A

G

P

T

N

F

G

G

W

-

E

-

G

A

I

I

I

Q

A

S

S

T

L

L

G

N

I

V

V

T

M

L

F

W

A

S

F

F

G

I

G

G

V

V

E

E

I

S

I

A

G

S

V

V

T

A

A

A

A

G

E

V

A

V

K

K

N

N

P

P

Q

K

K

R

V

N

I

V

P

P

Q

I

A

A

I

T

N

I

T

G

I

G

P

V

L

L

R

I

I

A

V

A

L

V

F

C

Y

Y

V

V

C

L

T

S

L

T

A

T

I

A

L

I

M

M

A

G

I

M

F

I

P

P

W

N

N

A

S

A

F

L

G

R

E

V

R

S

G

A

S

S

P

P

F

F

V

G

L

D

I

A

F

A

D

R

-

M

G

A

L

L

G

G

I

D

P

T

A

A

A

G

A

A

T

-

I

I

L

V

N

S

I

F

I

C

V

A

I

A

S

A

A

G

S

C

I

L

S

G

A

S

I

L

N

G

S

G

D
x
W

I

T

F

L

G

L

A

A

G

G

R

Q

M

T

M

A

Y

K

G

A

M

A

A

A

K

D

E

D

G

G

L

L

A

F

P

P

K

P

S

I

F

F

Q

A

R

R

I

V

A

N

S

K

N

A

G

G

V

T

P

P

W

V

M

A

T

G

V

L

V

I

M

V

G

G

V

I

A

-

L

L

L

M

A

T

A

I

V

F

V

Q

L

L

N

S

Y

S

L

I

M

S

P

P

E

N

-

A

-

T

Q

K

V

E

F

F

V

G

L

L

I

V

A

S

S

S

L

V

A

S

A

V

F

I

A

F

T

T

V

L

W

V

V

P

W

Y

V

L

M

Y

I

T

L

C

L

A

A

A

H

L

F

L

A

L

M

L

R

G

R

H

G

G

L

H

S

F

A

G

E

K

E

A

R

R

-

P

-

A

-

Y

-

L

-

A

-

V

G

T

N

T

I

I

A

A

F

F

P

L

V

Y

P

C

L

I

W

W

P

A

V

V

binding agmatine: I19 (≠ A26), A92 (≠ E100), C93 (≠ M101), G96 (≠ V104), N97 (≠ A105), M100 (≠ D108), W289 (≠ D303)

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)
23% identity, 87% coverage: 21:419/459 of query aligns to 38:427/487 of P82251

query
sites
P82251

I

I

A

I

L
x
V

G

G

S

T

A
x
I

I
|
I

G
|
G

T
x
S

G
|
G

L

I

F

F

Y

V

G
x
S

S
x
P

A

K

S

S

A

V

I

L

-

S

-

N

-

T

K

E

A

A

A

V

G

G

P

P

A

C

V

L

L

I

A

W

Y
x
A

L

A

I

C

G

G

G

V

A

L

A

A

V

T

F

L

-

G

-

A

I

L

V

C

M

F

R

A

A

E

L

L

G

G

E

T

M

M

A

I

V

T

R

K

N

-

P

-

V

-

S

S

G

G

S

G

F

E

S

Y

S

P

Y
|
Y

A

L

R

M

Q

E

Y

A

L

Y

G
|
G

P

P

L

I

A

P

G

A

F

Y

I

L

T

F

G

S

W
|
W

T

A

-

S

-

L

-

I

-

V

-
x
I

-

K

-

P

Y
x
T

T

S

F

F

E

A

M

I

V

I

I

C

V

L

A

S

L

F

A

S

D

E

V

Y

T

V

A

C

F

A

G

P

I

F

Y

Y

M
x
V

G

G

L
x
C

W

K

Y

P

P

P

D

Q

V

I

P

V

R

V

W

K

I

C

W

L

V

A

L

A

S

A

I

A

I

I

F

L

F

F

I

I

G

S

A

T

M

V

N

N

L

S

C

L

S

S

V
|
V

R

R

V

L

F

G

G

S

E

Y

M

V

E

Q

F

N

W

I

L

F

S

T

L
x
A

I

A

K

K

V

L

V

V

A

I

I

V

I

A

A

I

M

I

I

I

V

I

A

S

G
|
G

G

-

S

-

I

L

I

V

F

L

G

A

F

Q

G

G

N

N

A

T

F

-

P

-

A

-

T

-

G

-

L

-

E

K

N

N

L

F

W

-

S

-

H

-

G

-

F

-

A

-

P

D

N

N

G

S

W

F

E

E

G

G

I

A

I

Q

A

L

S

S

L

V

G

G

I

A

V

I

M

S

F
x
L

A
|
A

F

F

-

Y

-
x
N

-

G

-

L

-
x
W

-

A

-

Y

G
x
D

G

G

V
x
W

E

N

I
x
Q

I

L

G

N

V

Y

T

I

A

T

A

E

E

E

A

L

K

R

N

N

P

P

Q

Y

K

R

V

N

I

L

P

P

Q

L

A

A

I

I

N

I

T

-

I

-

P

-

L

I

R
x
G

I

I

V
x
P

L

L

F

V

Y

T

V

A

C

C

T

Y

L

I

A

L

I

M

L

N

M

V

A

S

I

Y

F

F

P

T

W

V

N

M

S

T

F

A

G

T

E

E

-

L

R

Q

G
x
S

S

Q

P

A

F

V

V

A

L

V

I

T

F

F

D

G

G

D

L

R

G

V

I

L

P

Y

A

P

A

A

A

S

T

W

I

I

L

V

N

P

I

L

I

F

V

V

I

A

S

F

A

S

S

T

I

I

S

G

A

A

I

A

N

N

S

G

D

T

I
x
C

F

F

G

T

A
|
A

G

G

R

R

M

L

M

I

Y

Y

G
x
V

M
x
A

A

G

K
x
R

E

E

G

G

L

H

A

M

P

L

K

K

S

V

F

L

Q

S

R

Y

I

I

A

S

S

V

N

R

G

R

V

L

-

T

P

P

W

A

M

P

T
x
A

V

I

V

F

M

Y

G

G

V

I

A

-

L

-

A

-

V

I

V

A

L

T

N

I

Y

Y

L

I

M

I

P

P

E

G

Q

D

V

I

F

N

V

S

L

L

I

V

A

-

S

N

L

Y

A

F

A
x
S

F

F

A

A

T
x
A

V
x
W

W

L

V

F

W
x
Y

V

G

M

L

I

T

L

I

L

L

A

G

H

L

F

I

A

V

M

M

R

R

R

F

G

T

L

R

S
x
K

A

E

E

L

E

E

R

R

G

-

N

-

I

-

A

-

F

-

P

P

V

I

P

K

L

V

W

P

P

V

V

V

A

I

P

P

-

V

L

L

L

M

T

T

L

L

L

I

F

S

M

V

G

F

L

L

V

V

I
x
L

A

A

V40 (≠ L23) to M: in CSNU; uncertain significance
IIGSG 43:47 (≠ AIGTG 26:30) binding
I44 (= I27) to T: in CSNU; type I; dbSNP:rs121908485
S51 (≠ G34) to F: in CSNU; uncertain significance
P52 (≠ S35) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
A70 (≠ Y50) 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 (vs. gap) to L: in CSNU; uncertain significance
T123 (≠ Y97) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
V142 (≠ M116) to A: no effect on amino acid transport activity; dbSNP:rs12150889
C144 (≠ L118) modified: Interchain (with C-114 in SLC3A1)
V170 (= V144) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
A182 (≠ L156) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
G195 (= G169) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
L223 (≠ F212) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
A224 (= A213) 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 (≠ G215) binding ; mutation to A: Complete loss of amino acid transport activity.
W235 (≠ V217) mutation to A: Complete loss of amino acid transport activity.
Q237 (≠ I219) mutation to A: Reduces amino acid transport activity.
G259 (≠ R244) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
P261 (≠ V246) to L: in CSNU; types I and III; dbSNP:rs121908486
S286 (≠ G269) to F: in CSNU; uncertain significance; dbSNP:rs755135545
C321 (≠ I304) mutation to S: Does not affect amino acid transport activity.
A324 (= A307) to E: in CSNU; uncertain significance
V330 (≠ G313) to M: in CSNU; type III; dbSNP:rs201618022
A331 (≠ M314) to V: in CSNU; non-classic type I; dbSNP:rs768466784
R333 (≠ K316) 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 (≠ T336) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
S379 (≠ A367) mutation to A: Markedly reduces amino acid transport activity.
A382 (≠ T370) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
W383 (≠ V371) mutation to A: Complete loss of amino acid transport activity.
Y386 (≠ W374) mutation to A: Loss of amino acid transport activity.
K401 (≠ S389) to E: in CSNU; uncertain significance; dbSNP:rs760264924
L426 (≠ I418) 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.

P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
23% identity, 83% coverage: 24:405/459 of query aligns to 21:402/445 of P60061

query
sites
P60061

G

G

S

N

A
x
I

I

M

G

G

T
x
S

G

G

L

V

F

F

Y

L

G

L

S

P

A

A

S

N

A

L

I

A

K

S

A

T

A

G

G

G

P

I

A

A

V

I

L

Y

-

G

-

W

L

L

A

V

Y

T

L

I

I

I

G

G

G

A

A

L

A

G

V

L

F

S

I

M

V

V

M

Y

R

-

A

-

L

-

G

A

E

K

M

M

A

S

V

F

R

L

N

D

P

P

V

S

S

P

G

G

S

G

F

S

S

Y

S

A

Y

Y

A

A

R

R

Q

R

Y

C

L

F

G

G

P

P

L

F

A

L

G

G

F

Y

I

Q

T

T

G

N

W

V

T

L

Y
|
Y

T

W

F

L

E
x
A

M
x
C

V

W

I

I

V

G

A
x
N

L

I

A

A

D
x
M

V

V

T

V

A

I

F

G

G

V

I

G

Y

Y

M

L

G

S

L

Y

W

F

Y

F

P

P

D

I

V

L

P

K

R

D

-

P

-

L

-

V

-

L

-

T

-

I

-

T

-

C

-

V

-

L

W

W

I

I

W

F

V

V

L

L

S

-

I

-

F

-

I

-

G

-

A

-

M

L

N

N

L

I

C

V

S

G

V

P

R

K

V

M

F

I

G

T

E

R

M

V

E

Q

F

A

W

V

L

A

S

T

L

V

I

L

K

A

V

L

V

I

A

P

I

I

I

V

A

G

M

I

I

A

V

V

A

F

G

G

G

-

S

-

I

-

I

W

F

F

F

W

G

F

F

R

G

G

N

E

A

T

F

Y

P

M

A

A

T

A

G

-

L

-

E

-

N

-

L

-

W

W

S

N

H

V

G

S

G

G

F

L

A

G

P

T

N

F

G

G

W

-

E

-

G

A

I

I

I

Q

A

S

S

T

L

L

G

N

I

V

V

T

M

L

F
x
W

A
x
S

F

F

G
x
I

G

G

V

V

E

E

I

S

I

A

G

S

V

V

T

A

A

A

A

G

E

V

A

V

K

K

N

N

P

P

Q

K

K

R

V

N

I

V

P

P

Q

I

A

A

I

T

N

I

T

G

I

G

P

V

L

L

R

I

I

A

V

A

L

V

F

C

Y

Y

V

V

C

L

T

S

L

T

A

T

I

A

L

I

M

M

A

G

I

M

F

I

P

P

W

N

N

A

S

A

F

L

G

R

E

V

R

S

G

A

S

S

P

P

F

F

V

G

L

D

I

A

F

A

D

R

-

M

G

A

L

L

G

G

I

D

P

T

A

A

A

G

A

A

T

-

I

I

L

V

N

S

I

F

I

C

V

A

I

A

S

A

A

G

S

C

I

L

S

G

A

S

I

L

N

G

S

G

D
x
W

I

T

F

L

G

L

A

A

G

G

R

Q

M

T

M

A

Y

K

G

A

M

A

A

A

K

D

E

D

G

G

L

L

A

F

P

P

K

P

S

I

F

F

Q

A

R

R

I

V

A

N

S

K

N

A

G

G

V

T

P

P

W

V

M

A

T

G

V

L

V

I

M

V

G

G

V

I

A

-

L

L

L

M

A

T

A

I

V

F

V

Q

L

L

N

S

Y

S

L

I

M

S

P

P

E

N

-

A

-

T

Q

K

V

E

F

F

V

G

L

L

I

V

A

S

S

S

L

V

A
x
S

A

V

F

I

A

F

T

T

V

L

W

V

V

P

W

Y

V

L

M

Y

I

T

L

C

L

A

A

A

H

L

F

L

A

L

M

L

R

G

R

H

G

G

L

H

S

F

A

G

E

K

E

A

R

R

-

P

-

A

-

Y

-

L

-

A

-

V

G

T

N

T

I

I

A

A

F

F

P

L

V

Y

P

C

L

I

W

W

P

A

V

V

I23 (≠ A26) binding ; binding
S26 (≠ T29) binding
Y93 (= Y97) mutation to L: Greatly decreased Arg uptake into liposomes.
A96 (≠ E100) binding ; binding
C97 (≠ M101) binding
N101 (≠ A105) 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 (≠ D108) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
W202 (≠ F212) binding ; mutation to L: Halves Arg uptake into liposomes.
S203 (≠ A213) binding
I205 (≠ G215) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
W293 (≠ D303) 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 (≠ A366) 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)
23% identity, 83% coverage: 24:405/459 of query aligns to 21:402/445 of P60063

query
sites
P60063

G

G

S
x
N

A
x
I

I

M

G
|
G

T
x
S

G
|
G

L

V

F

F

Y

L

G

L

S

P

A

A

S

N

A

L

I

A

K

S

A

T

A

G

G

G

P

I

A

A

V

I

L

Y

-

G

-

W

L

L

A

V

Y

T

L

I

I

I

G

G

G

A

A

L

A

G

V

L

F

S

I

M

V

V

M

Y

R

-

A

-

L

-

G

A

E

K

M

M

A

S

V

F

R

L

N

D

P

P

V

S

S

P

G

G

S

G

F

S

S
x
Y

S

A

Y

Y

A

A

R

R

Q

R

Y

C

L

F

G

G

P

P

L

F

A

L

G

G

F
x
Y

I

Q

T

T

G

N

W

V

T

L

Y
|
Y

T

W

F

L

E
x
A

M
x
C

V

W

I

I

V

G

A
x
N

L

I

A

A

D

M

V

V

T

V

A

I

F

G

G

V

I

G

Y

Y

M

L

G

S

L

Y

W

F

Y

F

P

P

D

I

V

L

P

K

R

D

-

P

-

L

-

V

-

L

-

T

-

I

-

T

-

C

-

V

-

L

W

W

I

I

W

F

V

V

L

L

S

-

I

-

F

-

I

-

G

-

A

-

M

L

N

N

L

I

C

V

S

G

V

P

R

K

V

M

F

I

G

T

E

R

M

V

E

Q

F

A

W

V

L

A

S

T

L

V

I

L

K

A

V

L

V

I

A

P

I

I

I

V

A

G

M

I

I

A

V

V

A

F

G

G

G

-

S

-

I

-

I

W

F

F

F

W

G

F

F

R

G

G

N

E

A

T

F

Y

P

M

A

A

T

A

G

-

L

-

E

-

N

-

L

-

W

W

S

N

H

V

G

S

G

G

F

L

A

G

P

T

N

F

G

G

W

-

E

-

G

A

I

I

I

Q

A

S

S

T

L

L

G

N

I

V

V

T

M

L

F
x
W

A

S

F

F

G
x
I

G
|
G

V
|
V

E
|
E

I
x
S

I
x
A

G

S

V

V

T

A

A

A

A

G

E

V

A

V

K

K

N

N

P

P

Q

K

K

R

V

N

I

V

P

P

Q

I

A

A

I

T

N

I

T

G

I

G

P

V

L

L

R

I

I

A

V

A

L

V

F

C

Y

Y

V

V

C

L

T

S

L

T

A

T

I

A

L

I

M

M

A

G

I

M

F

I

P

P

W

N

N

A

S

A

F

L

G

R

E

V

R

S

G

A

S

S

P

P

F

F

V

G

L

D

I

A

F

A

D

R

-

M

G

A

L

L

G

G

I

D

P

T

A

A

A

G

A

A

T

-

I

I

L

V

N

S

I

F

I

C

V

A

I

A

S

A

A

G

S

C

I

L

S

G

A

S

I

L

N

G

S

G

D
x
W

I

T

F

L

G

L

A

A

G

G

R

Q

M

T

M

A

Y

K

G

A

M

A

A

A

K

D

E

D

G

G

L

L

A

F

P

P

K

P

S

I

F

F

Q

A

R

R

I

V

A

N

S

K

N

A

G

G

V

T

P

P

W

V

M

A

T

G

V

L

V

I

M

V

G

G

V

I

A

-

L

L

L

M

A

T

A

I

V
x
F

V

Q

L

L

N

S

Y

S

L

I

M

S

P

P

E

N

-

A

-

T

Q

K

V

E

F

F

V

G

L

L

I

V

A

S

S

S

L

V

A
x
S

A

V

F

I

A

F

T

T

V

L

W

V

V

P

W
x
Y

V

L

M

Y

I

T

L

C

L

A

A

A

H

L

F

L

A

L

M

L

R

G

R

H

G

G

L

H

S

F

A

G

E

K

E

A

R

R

-

P

-

A

-

Y

-

L

-

A

-

V

G

T

N

T

I

I

A

A

F

F

P

L

V

Y

P

C

L

I

W

W

P

A

V

V

N22 (≠ S25) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
I23 (≠ A26) binding
GSG 25:27 (≠ GTG 28:30) Helix-breaking GSG motif TM1
S26 (≠ T29) binding ; mutation to K: 5% Agm antiport.
G27 (= G30) binding
Y74 (≠ S78) 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 (≠ E100) binding
C97 (≠ M101) binding
N101 (≠ A105) binding
W202 (≠ F212) Periplasmic (proximal) gate; binding
I205 (≠ G215) binding
GVESA 206:210 (≠ GVEII 216:220) Helix-breaking GVESA motif TM6
E208 (= E218) mutation E->A,D: 5-10% Agm antiport.
W293 (≠ D303) binding
F337 (≠ V348) mutation to A: Severely decreased antiport.
S357 (≠ A366) binding
Y365 (≠ W374) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.

P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
24% identity, 63% coverage: 66:354/459 of query aligns to 59:340/444 of P0AAE8

query
sites
P0AAE8

E

R

M

L

A

A

V

T

R

K

N

N

P

P

V

Q

S

Q

G

G

S

G

F

P

S

I

S

A

Y
|
Y

A

A

R

G

Q
x
E

Y

-

L

I

G

S

P

P

L

A

A

F

G

G

F

F

I

Q

T

T

G

G

W

V

T

L

Y
|
Y

T
x
Y

F

H

E

A

M

N

V

W

I

I

V

G

A

N

L

L

A

A

-

I

D

G

V

I

T

T

A

A

F

V

G

S

I

-

Y
|
Y

M

L

G

S

L

T

W

F

Y

F

P

P

-

V

-

L

-

N

-

D

D

P

V

V

P

P

R

A

W

G

I

I

W

A

V
x
C

L

I

S

A

I

I

I

V

F

W

F

V

I

F

G

T

A

F

M

V

N

N

L

M

C

L

S

G

V

-

R

-

V

-

F

-

G

G

E

T

M

W

E

V

F

S

W

R

L

L

S

T

L

T

I

I

K

G

V

L

V

V

A

L

I

V

I

L

A

I

M

P

I

V

V

V

A

M

G

T

G

A

S

I

I

V

I

G

F

W

F

H

G

W

F

F

G

D

N

A

A

A

F

T

P
x
Y

A

A

T

A

G

N

L

W

E

N

N

T

L

A

W

D

S

T

H

T

G
x
D

G

G

F

H

A

A

P

-

N

-

G

-

W

-

E

-

G

-

I

I

A

K

S

S

L

I

G

L

I

L

V
x
C

M

L

F

W

A

A

F

F

G

V

G

G

V

V

E
|
E

I

S

I

A

G

A

V

V

T

S

A

T

A

G

E

M

A

V

K

K

N

N

P

P

Q

K

K

R

V

T

I

V

P

P

Q

L

A

A

I

T

N

M

T

L

I

G

P

T

L

G

R

L

I

A

V

G

L

I

F

V

Y
|
Y

V

I

C

A

T

A

L

T

A

Q

I

V

L

L

M

S

A

G

I

M

F
x
Y

P

P

W

S

N

S

S

V

F

M

G

A

E

A

R

S

G

G

S

A

P

P

F

F

V

A

L

I

I

S

F

A

D

S

G

T

L

I

G

L

I

G

P

N

A

W

A

A

T

P

I

L

L

V

N

S

I

A

I

F

V

T

I

A

S

F

A

A

S
x
C

I

L

S

T

A

S

I

L

N

G

S

S

D

W

I

M

F

M

G

L

A

V

G

G

R

Q

M

A

M

G

Y

V

G
x
R

M

A

A

A

K

N

E
x
D

G

G

L

N

A

F

P

P

K

K

S

V

F
x
Y

Q

G

R

E

I

V

A

D

S

S

N

N

G

G

V

I

P

P

W

K

M

K

T

G

V

L

M

A

G

A

V

V

A

K

L

M

L

T

A

A

A

L

V

M

V

I

L

L

N

I

Y

T

L

L

M

M

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 (≠ Q83) 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 (≠ T98) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
Y107 (= Y115) mutation to L: Strong decrease in cadaverine uptake.
C125 (≠ V129) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
Y174 (≠ P182) mutation to L: Moderate decrease in cadaverine uptake.
D185 (≠ G193) mutation to N: Moderate decrease in cadaverine uptake.
C196 (≠ V210) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
E204 (= E218) 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 (= Y249) 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 (≠ F260) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
C282 (≠ S296) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
R299 (≠ G313) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
D303 (≠ E317) 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 (≠ F324) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.

Sites not aligning to the query:

12 C→S: Does not affect cadaverine excretion and cadaverine uptake.
41 W→L: Moderate decrease in cadaverine uptake.
43 W→L: Strong decrease in cadaverine uptake.
55 Y→L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
57 Y→L: Strong decrease in cadaverine uptake.
366 Y→L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
368 Y→L: Strong decrease in cadaverine uptake.
370 C→S: Strong decrease in both cadaverine excretion and cadaverine uptake.
377 E→Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
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.

Query Sequence

>BWI76_RS08745 FitnessBrowser__Koxy:BWI76_RS08745
MQQQNKPHLLRGLNARHIRFIALGSAIGTGLFYGSASAIKAAGPAVLLAYLIGGAAVFIV
MRALGEMAVRNPVSGSFSSYARQYLGPLAGFITGWTYTFEMVIVALADVTAFGIYMGLWY
PDVPRWIWVLSIIFFIGAMNLCSVRVFGEMEFWLSLIKVVAIIAMIVAGGSIIFFGFGNA
FPATGLENLWSHGGFAPNGWEGIIASLGIVMFAFGGVEIIGVTAAEAKNPQKVIPQAINT
IPLRIVLFYVCTLAILMAIFPWNSFGERGSPFVLIFDGLGIPAAATILNIIVISASISAI
NSDIFGAGRMMYGMAKEGLAPKSFQRIASNGVPWMTVVVMGVALLAAVVLNYLMPEQVFV
LIASLAAFATVWVWVMILLAHFAMRRGLSAEERGNIAFPVPLWPVAPLLTLLFMGLVIAV
LGMVEETRIALIAGLVWLGLLTAVWFARVRKNAVLAVTE

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