SitesBLAST

T27 (= T34) mutation T->A,S: Retains 60% of wild-type activity.; mutation to N: Retains 20% of wild-type activity.
E98 (≠ S105) mutation to A: Retains 80% of wild-type activity.
K156 (= K163) mutation K->A,Q: Retains less than 10% of wild-type activity.; mutation to R: Retains 40% of wild-type activity.
F212 (= F218) mutation F->A,Q: Loss of activity.; mutation to Y: No change in activity.
E218 (= E224) mutation E->A,Q: Loss of activity.; mutation to D: Retains 70% of wild-type activity.

P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
38% identity, 93% coverage: 9:459/484 of query aligns to 14:458/458 of P24207

query
sites
P24207

T

N

E

Q

Q

E

P

P

A

T

L

L

Q

H

R

R

T

G

L

L

S

H

N

N

R
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R

H

H

I

I

Q

Q

L

L

M

I

A

A

M

L

G

G

A

A

I

I

G

G

T

T

G

G

L

L

F

F

M

L

G

G

S

I

G

G

K

P

I

A

I

I

A

Q

L

M

S

A

G

G

T
x
P

S

A

I

V

I

L

L

L

I

G

Y

Y

M

G

I

V

I

A

G

G

L

I

F

I

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A

Y

F

F

L

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I

M

M

R

R

A

Q

M

L

G

G

E

E

M

M

L

V

S

E

N

E

L

P

N

V

F

S

K

G

T

S

F
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F

A

A

D

H

F
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F

A

A

G
x
Y

A

K

Y
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Y

L
x
W

G

G

P

P

R
x
F

A

A

A

G

F
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F

F

L

L

S

G

G

W
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W

S

N

Y
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Y

W
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W

L

V

S

M

W
x
F

S

V

V

L

A

V

V

G

I

M

G

A

D
x
E

A

L

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T

V

A

G

G

G

I

F

Y

F

M

Q

Q

Y

Y

W

W

F

F

P

P

D

D

V

V

P

P

A

T

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W

I

I

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W

A

A

I

A

G

A

M

F

L

F

M

I

T

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L

I

F

N

A

A

L

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N

N

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L

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N

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V

R

R

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L

F

Y

G

G

E

E

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E

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F

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W

F

F

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A

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K
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K

I

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A

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M

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G

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G

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L

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A

-

S

-

F

F

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S

S

G

P

H

S

G

G

G

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E

T

K

A

A

S

S

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I

N

D

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N

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D

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Y

Q

G

A

G

A

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F

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A

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G

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F

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G

G

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A

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G

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E
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E

L

L

I

I

G

G

T

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A

T

A

A

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T

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R

N

D

P

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E

E

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K

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A

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R

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D

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N

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F

V

V

V

I

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A

A

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A

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S

S

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A

Y

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N

S

S

G

G

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V

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Y

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S

R

R

M

M

L

L

F

F

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G

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L

A

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Q

D

G

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N

A

A

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P

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F

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G

L

A

L

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L

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L

L

L

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L

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F

Y

I

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P

E

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-

M

-

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A

A

F

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M

T

A

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L

S

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A

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F

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R

E

R

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G

A

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K

E

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T

A

Q

Y

F

K

K

-

A

-

L

M

Y

P

P

G

F

G

G

V

-

P

-

M

-

A

N

W

Y

F

L

S

C

L

I

A

A

F

F

L

L

G

G

F

M

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I

L

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C

L

L

L

L

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A

C

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R

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D

D

D

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R

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P

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W

W

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W

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L

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-

T

T

D

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K

K

R26 (= R21) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
P54 (≠ T49) 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 (= F82) mutation to L: No effect on phenylalanine transport activity.
F90 (= F85) mutation to L: 65% of wild-type phenylalanine transport activity.
Y92 (≠ G87) mutation to L: 41% of wild-type phenylalanine transport activity.
Y94 (= Y89) mutation to L: 69% of wild-type phenylalanine transport activity.
W95 (≠ L90) mutation to L: 10% of wild-type phenylalanine transport activity.
F98 (≠ R93) mutation to L: No effect on phenylalanine transport activity.
F101 (= F96) mutation to L: 38% of wild-type phenylalanine transport activity.
W105 (= W100) mutation to L: 39% of wild-type phenylalanine transport activity.
Y107 (= Y102) mutation to L: No effect on phenylalanine transport activity.
W108 (= W103) mutation to L: 71% of wild-type phenylalanine transport activity.
F111 (≠ W106) 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 (≠ D113) mutation E->G,L,V,N: Loss of activity.
K168 (= K163) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
E226 (= E224) mutation E->A,Q,K,R,W: Loss of activity.
R252 (= R250) mutation R->D,E,F,W,P: Loss of activity.
P341 (= P339) 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 (= P442) 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.

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)
37% identity, 93% coverage: 6:456/484 of query aligns to 3:448/457 of P15993

query
sites
P15993

S

E

G

G

L

Q

T

Q

E

H

Q

G

P

E

A

Q

L

L

Q

K

R

R

T

G

L

L

S

K

N

N

R

R

H

H

I

I

Q

Q

L

L

M

I

A

A

M

L

G

G

A

A

I

I

G

G

T

T

G

G

L

L

F

F

M

L

G

G

S

S

G

A

K

S

I

V

I

I

A

Q

L

S

S

A

G

G

T

P

S

G

I

I

L

L

I

G

Y

Y

M

A

I

I

I

A

G

G

L

F

F

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A

Y

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F

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I

M

M

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R

A

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M

L

G

G

E

E

M

M

L

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E

N

E

L

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N

V

F

A

K

G

T

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F

F

A

S

D

H

F

F

A

A

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Y

A

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Y

Y

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G

G

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S

R

F

A

A

A

G

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F

F

A

L

S

G

G

W

W

S

N

Y

Y

W

W

L

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S

L

W
x
Y

S

V

V

L

A

V

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A

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M

G

A

D

E

A

L

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T

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A

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G

G

G

K

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Y

F

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Y

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A

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L

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S

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A

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S

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D

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Q

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F

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G

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L

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A

A

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G

L

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-

P

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-

A

N

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W

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L

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L

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K

D

E

Y103 (≠ W106) 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%.

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, 81% coverage: 10:403/484 of query aligns to 4:393/469 of P46349

query
sites
P46349

E

S

Q

Q

P

S

A

G

L

L

Q

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R

K

T

E

L

L

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A

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G

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L

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G
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G

S

S

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G

K

S

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G
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G

T

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G

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G

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A

A

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Y

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M

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A

L

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N

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G

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G

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K

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F

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E

L

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N

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P

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K

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A

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A

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N

F

F

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A

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A

L

S

S

S

C

A

L

N

N

S

S

G
|
G

V

L

F

Y

S

T

S

S

R

R

M

M

L

L

F

Y

G

S

L

L

A

A

N

E

Q

R

D

N

N

E

A

A

P

P

G

R

I

R

F

F

R

M

R

K

L

L

S

S

G

K

N

K

S

G

V

V

P

P

L

V

L

Q

S

A

L

I

A

V

F

A

T
x
G

T

T

L

F

L
x
F

M

S

L

Y

V

I

G

A

V

V

L

V

L

M

L

N

F

Y

I

F

V

S

P

P

E

D

V

-

M

-

T

T

A

V

F

F

T

L

I

F

V

L

S

V

T

N

V

S

S

S

A

G

I

A

L

I

V

A

I

L

F

L

T

V

W

Y

S

L

T

V

I

I

L

A

A

V

S

S

Y

Q

I

L

A

K

Y

M

R

R

K

K

R

L

P

E

E

K

L

T

H

N

A

P

K

E

S

A

G33 (= G39) mutation to D: Lack of activity.
G42 (= G48) mutation to S: Lack of activity.
G301 (= G309) mutation to V: Lack of activity.
G338 (≠ T346) mutation to E: Lack of activity.
F341 (≠ L349) mutation to S: Lack of activity.

Sites not aligning to the query:

414 G→R: Lack of activity.

P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
36% identity, 87% coverage: 9:428/484 of query aligns to 8:430/489 of P25737

query
sites
P25737

T

T

E

E

Q

A

P

P

A

G

L

L

Q

R

R

R

T

E

L

L

S

K

N

A

R

R

H

H

I

L

Q

T

L

M

M

I

A

A

M

I

G

G

A

S

I

I

G

G

T

T

G

G

L

L

F

F

M

V

G

A

S

S

G

G

K

A

I

T

I

I

A

S

L

Q

S

A

G

G

-

P

T

G

S

G

I

A

I

L

L

L

I

S

Y

Y

M

M

I

L

I

I

G

G

L

L

F

M

V

V

Y

Y

F

F

V

L

M

M

R

T

A

S

M

L

G

G

E

E

M

L

L

A

S

Y

N

M

L

P

N

V

F

S

K

G

T

S

F

F

A

A

D

T

F

Y

A

G

G

Q

A

N

Y

Y

L

V

G

E

P

E

R

G

A

F

A

G

F

F

F

A

L

L

G

G

W

W

S

N

Y
|
Y

W

W

L

Y

S

N

W
|
W

S

A

V

V

A

T

V

I

I

A

G

V

D

D

A

L

V

V

V

A

G

Q

G

L

F

V

F

M

Q

S

Y

W

W

W

F

F

P

P

D

D

V

T

P

P

A

G

W

W

I

I

P

W

A

S

I

A

G

L

M

F

L

L

M

G

T

V

L

I

F

F

A

L

L

L

N

N

V

Y

L

I

T

S

V

V

R

R

L

G

F

F

G

G

E

E

I

A

E

E

F

Y

W

W

F

F

A

S

I

L

I

I

K
|
K

I

V

I

T

A

T

V

V

V

I

T

V

L

F

I

I

G

I

V

V

S

G

L

V

V

L

L

M

I

I

A

I

S

G

S

I

F

F

V

K

S

G

P

A

S

Q

G

-

V

-

T

P

A

A

S

G

L

W

N

S

H

N

L

W

L

T

D

I

K

G

Q

E

A

A

A

P

F

F

P

A

N

G

G

G

L

-

F

F

G

A

F

A

F

M

A

I

G

G

F

V

Q

A

M

M

A

I

I

V

-

G

F
|
F

S

S

F

F

A

Q

G

G

T

T

E
|
E

L

L

I

I

G

G

T

I

A

A

A

G

E
|
E

T

S

R

E

N

D

P

P

E

A

K

K

T

N

L

I

P

P

K

R

A

A

I

V

N

R

S

Q

I

V

P

F

L

W

R

R

I

I

I

L

L

L

F

F

Y

Y

V

V

L

F

A

A

L

I

A

L

C

I

I

I

I

S

A

L

V

I

T

I

S

P

W

Y

Q

T

Q

D

V

P

S

S

-

L

-

R

-

N

-
x
D

-

V

-

K

-
x
D

P

I

S

S

K

V

S

S

P

P

F

F

V

T

E

L

L

V

F

F

L

Q

V

H

A

A

G

G

F

L

P

L

A

S

A

A

G

A

I

V

V

M

N

N

F

A

V

V

V

I

L

L

T

T

S

A

A

V

A

L

S

S

S

A

A

G

N

N

S

S

G

G

V

M

F

Y

S

A

S

S

S

T

R

R

M

M

L

L

F

Y

G

T

L

L

A

A

N

C

Q

D

D

G

N

K

A

A

P

P

G

R

I

I

F

F

R

A

R

K

L

L

S

S

G

R

N

G

S

G

V

V

P

P

L

R

L

N

S

A

L

L

A

Y

F

A

T

T

L

V

L

-

M

-

L

I

V

A

G

G

V

L

L

C

L

F

L

L

F

T

I

S

V

M

P

F

E

G

V

N

M

Q

T

T

A

V

F

Y

T

L

I

W

V

L

S

L

T

N

V

T

S

S

A

G

I

M

L

T

V

G

I

F

F

I

T

A

W

W

S

L

T

G

I

I

L

A

A

I

S

S

Y

H

I

Y

A

R

Y

F

R

R

K

R

K

G

R

Y

P

V

E

-

L

L

H

Q

A

G

K

H

S

D

A

I

Y

N

K

D

M

L

P

P

-

Y

-

R

-

S

G

G

G

F

V

F

P

P

M

L

A

G

W

-

F

-

S

-

L

-

A

P

F

I

L

F

G

A

F

F

V

I

L

L

C

C

L

L

L

I

Y102 (= Y102) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
W106 (= W106) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
K163 (= K163) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
F216 (= F218) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
E222 (= E224) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
E230 (= E232) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
D275 (vs. gap) 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 (vs. gap) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-275.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
438 E→A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
443 D→A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
446 D→A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.

Q9URZ4 Cationic amino acid transporter 1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 87% coverage: 10:429/484 of query aligns to 76:503/587 of Q9URZ4

query
sites
Q9URZ4

E

D

Q

G

P

T

A

A

L

L

Q

K

R

R

T

S

L

L

S

K

N

S

R

R

H

H

I

M

Q

Q

L

M

M

I

A

S

M

I

G

G

A

A

I

I

G

G

T

T

G

G

L

L

F

Y

M

V

G

G

S

S

G

G

K

S

I

S

I

L

A

A

L

D

S

G

G

G

-

P

T

A

S

S

I

V

I

I

L

I

I

N

Y

Y

M

S

I

L

I

I

G

G

L

I

F

M

V

M

Y

F

F

F

V

I

M

V

R

Y

A

A

M

L

G

G

E

E

M

M

L

A

L

V

S

A

N

Y

L

P

N

V

F

A

K

G

T

G

F

F

A

N

D

T

F

Y

A

A

G

T

A

R

Y

F

L

I

G

D

P

P

R

A

A

W

A

G

F

F

F

A

L

V

G

S

W

W

S

N

Y

Y

W

F

L

I

S

N

W

Y

S

F

V

V

A

T

V

F

I

P

G

L

D

E

A

L

V

T

V

C

G

A

G

I

F

T

F

F

Q

R

Y

Y

W

W

F

T

P

D

-

I

D

N

V

S

P

A

A

A

W

W

I

I

P

S

A

I

I

-

G

-

M

F

L

L

M

V

T

V

L

I

F

I

A

I

L

V

N

N

V

L

L

F

T

G

V

V

R

R

L

A

F

Y

G

G

E

E

I

V

E

E

F

F

W

I

F

L

A

S

I

T

I

V

K

K

I

V

A

A

V

T

V

F

T

G

L

F

I

I

G

I

V

L

S

A

L

I

V

I

L

I

I

N

A

C

S

G

F

V

V

-

S

-

P

P

S

T

G

D

V

H

T

R

A

G

S

Y

L

I

N

G

H

G

L

S

L

I

D

I

K

K

Q

H

A

K

A

P

F

F

P

R

N

H

G

G

L

F

F

K

G

G

F

F

F

C

A

S

G

V

F

F

Q

T

M

T

A

A

I

A

F

F

S

S

F

F

A

S

G

G

T

T

E

E

L

V

I

I

G

G

T

L

A

A

E

E

T

V

R

D

N

N

P

P

E

Q

K

K

T

A

L

L

P

P

K

H

A

A

I

V

N

K

S

Q

I

V

P

F

L

W

R

R

I

I

I

A

L

I

F

F

Y

Y

V

V

L

V

A

S

L

L

A

I

C

L

I

I

I

G

A

L

V

L

T

I

S

S

W

P

Q

D

V

P

-

N

-

L

-

M

-

G

-

N

-

G

S

S

P

T

S

S

K

V

S

S

P

P

F

F

V

V

E

L

L

A

F

I

L

K

V

E

A

A

G

N

F

I

P

K

A

G

A

L

A

P

G

S

I

V

V

F

N

N

F

A

V

V

V

I

L

I

T

I

S

S

A

V

S

S

S

V

A

T

N

N

S

S

G

S

V

T

F

Y

S

T

S

A

S

G

R

R

M

T

L

L

F

H

G

G

L

M

A

A

N

N

Q

L

D

K

N

Q

A

A

P

P

G

S

I

F

F

F

R

K

R

Y

L

T

S

D

G

R

N

L

S

G

V

R

P

P

L

L

S

A

L

M

A

-

F

-

T

-

L

I

L

V

M

V

L

L

V

L

G

F

V

G

L

F

L

A

F

Y

I

I

V

N

P

E

E

A

V

D

M

K

T

N

A

G

F

N

T

D

I

V

V

S

S

D

T

T

V

V

-

F

-

N

-

W

-

L

-

A

-

L

S

S

A

G

I

L

L

S

V

N

I

F

F

F

T

T

W

W

S

G

T

S

I

I

L

C

A

L

S

C

Y

H

I

I

A

I

Y

F

R

R

-

L

-

A

-

F

K

K

R

Q

P

G

E

H

L

S

H

L

A

K

K

E

S

L

A

G

Y

F

K

V

M

S

P

P

G

M

G

G

V

I

P

-

M

-

A

-

W

W

F

G

S

S

L

C

A

I

F

G

L

L

G

F

F

F

-

N

V

I

L

L

C

C

L

L

L

M

A

A

Sites not aligning to the query:

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

P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
29% identity, 87% coverage: 6:427/484 of query aligns to 76:512/590 of P04817

query
sites
P04817

S

E

G

G

L

E

T

V

E

Q

Q

N

P

A

A

E

L

V

Q

K

R

R

T

E

L

L

S

K

N

Q

R

R

H

H

I

I

Q

G

L

M

M

I

A

A

M

L

G

G

A

T

I

I

G

G

T

T

G

G

L

L

F

F

M

I

G

G

S

L

G

S

K

T

I
x
P

I

L

A

T

L

N

S

A

G

G

T

P

S

V

I

G

I

A

L

L

I

I

-

S

Y

Y

M

L

I

F

I

M

G

G

L

S

F

L

V

A

Y

Y

F

S

V

V

M

T

R

Q

A

S

M

L

G

G

E

E

M

M

L

A

L

T

S

F

N

I

L
x
P

N
x
V

F

T

K

S

T
x
S

F

F

A

T

D

V

F

F

A

S

G

Q

A

R

Y

F

L

L

G

S

P

P

R

A

A

F

A

G

F

A

L

N

G

G

W

Y

S

M

Y
|
Y

W

W

L

F

S

S

W

W

S

A

V

I

A

T

V

F

I

A

G

L

D

E

A

L

V

S

V

V

G

G

G

Q

F

V

F

I

Q

Q

Y

F

W

W

F

T

P

Y

D

K

V

V

P

P

-

L

-

A

A

A

W

W

I

I

P

S

A

I

I

F

G

W

M

V

L

I

M

I

T

T

L

I

F

-

A

-

L

M

N

N

V

L

L

F

T

P

V

V

R

K

L

Y

F

Y

G

G

E

E

I

F

E

E

F

F

W

W

F

V

A

A

I

S

I

I

K

K

I

V

I

L

A

A

V

I

T

G

L

F

I

L

G

I

V

Y

S

C

L

F

V

C

L

M

I

V

A

C

S

G

S

A

F

G

V

V

S

T

-

G

P

P

S

V

G

G

V

F

T

R

A

Y

S

W

L

R

N

N

-

P

-

G

-

A

-

W

-

G

-

P

H

G

L

I

D

S

K

K

Q

D

A

K

A

N

F

-

P

-

N

E

G

G

L

R

F

F

-

L

G

G

F

W

F

V

A

S

G

S

F

L

Q

I

M

N

A

A

I

A

F

F

S

T

F

F

A

Q

G

G

T

T

E

E

L

L

I

V

G

G

T

I

A

T

A

A

A
x
G

E

E

T

A

R

A

N

N

P
|
P

E

R

K

K

T

S

L

V

P

P

K

R

A

A

I

I

N

K

S

K

I

V

P

V

L

F

R

R

I

I

I

L

L

T

F

F

Y

Y

V

I

L

G

A

S

L

L

A

L

C

F

I

I

I

G

A

L

V

L

T

V

S

P

W

Y

-

N

-

D

-

P

-

K

-

L

-

T

Q

Q

Q

S

V
x
T

S
|
S

-
x
Y

P

V

S

S

K

T

S

S

P

P

F

F

V

I

E

I

L

A

F

I

L

E

V

N

A

S

G

G

F

T

P

K

A

V

A

L

A

P

G

H

I

I

V

F

N

N

F

A

V

V

V

I

L

L

T

T

S

T

A

I

S

S

S

A

A

A

N

N

S

S

G

N

V

I

F

Y

S

V

S

G

S

S

R

R

M

I

L

L

F

F

G

G

L

L

A

S

N

K

Q

N

D

K

N

L

A

A

P

P

G

K

I

F

F

L

R

S

R

R

L

T

S

T

G

K

N

G

S

G

V

V

P

P

L

Y

L

I

S

A

L

V

A

F

F

V

T

T

T

A

L

A

L

F

M

G

L

A

V

L

G

A

V

Y

L

M

L

-

F

-

I

-

V

-

P

-

E

E

V

T

M

S

T

T

A

G

-

G

-

D

-

K

-

V

F

F

T

E

I
x
W

V

L

S

L

T

N

V

I

S

T

A

G

I

V

L

A

V

G

I
x
F

F

F

T

A

W

W

S

L

T

F

I

I

L

S

A

I

S

S

Y

H

I

I

A

R

Y

F

R

M

K

Q

-

A

-

L

-

K

-

Y

-

R

-

G

-

I

K

S

R

R

P

D

E

E

L

L

H

P

A

F

K

K

S

-

A

A

Y

K

K

L

M

M

P

P

G

G

G

-

V

-

P

-

M

L

A

A

W

Y

F

Y

S

A

L

A

A

T

F

F

L

M

G

T

F

I

V

I

L

I

C

I

L

I

P113 (≠ I43) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
P148 (≠ L77) 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 (≠ N78) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
S152 (≠ T81) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
Y173 (= Y102) 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 (≠ A231) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
P313 (= P236) 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 (≠ VS 271:272) mutation Missing: In CAN1-318; confers citrulline transport activity in GAP1-deleted cells.
Y356 (vs. gap) 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 (≠ I369) 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 (≠ I379) mutation to S: In CAN1-307; confers citrulline transport activity in GAP1-deleted cells.

P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
30% identity, 80% coverage: 8:394/484 of query aligns to 80:476/602 of P19145

query
sites
P19145

L

I

T

T

E

A

Q

Q

P

T

A

P

L

L

Q

K

R

H

T

H

L

L

S

K

N

N

R

R

H

H

I

L

Q

Q

L

M

M

I

A

A

M

I

G

G

A

A

I

I

G

G

T

T

G

G

L

L

F

L

M

V

G

G

S

S

G

G

K

T

I

A

I

L

A

R

L

T

S

G

G

G

T

P

S

A

I

S

I

L

L

L

I

I

-

G

Y

W

M

G

I

S

I

T

G

G

L

T

F

M

V

I

Y

Y

F

A

V

M

M

V

R

M

A

A

M

L

G

G

E

E

M

L

L

A

L

V

S

I

N

F

L

P

N

I

F

S

K

G

T

G

F

F

A

T

D

T

F

Y

A

A

G

T

A

R

Y

F

L

I

G

D

P

E

R

S

A

F

A

G

F

Y

F

A

L

N

G

N

W

F

S

N

Y

Y

W

M

L

L

S

Q

W

W

S

L

V

V

A

V

V

L

I

P

G

L

D

E

A

I

V

V

V

S

V

A

G

S

G

I

F

T

F

V

Q

N

Y

F

W

W

F

G

P

T

D

D

V

-

P

P

A

K

W

Y

I

R

P

D

A

G

I

F

G

V

M

A

L

L

-

F

-

W

M

L

T

A

L

I

F

V

A

I

L

I

N

N

V

M

L

F

T

G

V

V

R

K

L

G

F

Y

G

G

E

E

I

A

E

E

F

F

W

V

F

F

A

S

I

F

I

I

K

K

I

V

I

I

A

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V

T

G

L

F

I

I

G

I

V

L

S

G

L

I

V

I

L

L

I

N

A

C

S

G

F

G

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S

T

P

G

S

G

G

Y

V

I

T

G

A

G

S

K

L

Y

N

W

H

H

L

-

D

-

K

D

Q

P

A

G

A

A

F

F

-

A

-

G

-

D

-

T

P

P

N

G

G

A

L

K

F

F

-

K

G

G

F

V

F

C

A

S

G

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F

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M

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A

A

I

A

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A
|
A

G

G

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S

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L

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G

T

L

A

A

A

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E

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S

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P

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K

A

A

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A

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R

R

I

I

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F

Y

Y

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S

L

L

A

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C

M

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I

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A

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Y

Q

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Q

D

-

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-

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-

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-

S

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S

D

P

A

S

A

K

A

S

S

P

P

F

F

V

V

E

I

L

A

F

I

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K

V

T

A

H

G

G

F

I

P

K

A

G

A

L

A

P

G

S

I

V

V

V

N

N

F

V

V

V

V

I

L

L

T

I

S

A

A

V

A

L

S

S

S

V

A

G

N

N

S

S

G

A

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I

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Y

S

A

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C

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S

R

R

M

T

L

M

F

V

G

A

L

L

A

A

N

E

Q

Q

D

R

N

F

A

L

P

P

G

E

I

I

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F

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R

Y

L

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S

D

G

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N

K

S

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P

L

L

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S

G

L

I

A

A

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S

L

A

L

F

M

G

L

L

V

I

G

A

V

-

L

-

L

F

L

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F

A

I

A

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P

K

E

K

V

E

M

G

T

E

A

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F

F

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I

W

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S

L

T

A

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L

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S

A

G

I

L

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S

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L

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F

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T

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W

S

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T

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I

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H

I

I

A

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Y

F

R

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K

K

A297 (= A221) 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)
27% identity, 80% coverage: 10:394/484 of query aligns to 141:535/663 of P48813

query
sites
P48813

E

K

Q

Q

P

E

A

N

L

L

Q

K

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K

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L

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A

G

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N

G

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G

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G

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I

L

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G

Y

Y

M

A

I

I

I

M

G

G

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F

C

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V

Y

Y

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M

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Q

A

A

M

C

G

G

E

E

M

L

-

A

-

V

L

I

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Y

S

S

N

D

L

L

-

I

-

G

N

G

F

F

K

N

T

T

F

Y

A

P

D

L

F

F

A

-

G

-

A

-

Y

L

L

V

G

D

P

P

R

A

A

L

A

G

F

F

F

S

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G

A

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W

W

S

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C

A

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C

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L

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E

A

L

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V

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V

A

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G

M

F

T

F

I

Q

K

Y

Y

W

W

F

T

P

T

D

S

V

V

P

N

A

P

W

D

I

V

P

F

A

V

I

V

G

I

M

F

L

Y

M

V

T

L

L

I

F

V

A

V

L

I

N

N

V

V

L

F

T

G

V

A

R

K

L

G

F

Y

G

A

E

E

I

A

E

D

F

F

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F

F

F

A

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I

C

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K

I

I

I

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A

M

V

I

V

V

T

G

L

F

I

F

G

-

V

I

S

L

L

A

V

I

L

I

I

I

A

D

S

C

S

G

F

G

V

A

S

G

P

T

S

D

G

G

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Y

T

I

A

G

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S

L

-

N

K

H

Y

L

W

L

R

D

D

K

P

-

G

-

A

-

F

Q

R

A

G

A

D

F

T

P

P

N

I

G

Q

L

R

F

F

-

K

G

G

F

V

A

A

G

T

F

F

Q

V

M

T

A

A

I

A

F

F

S

A

F

F

A

G

G

M

T

S

E

E

L

Q

I

L

G

A

T

M

A

T

A

A

A

S

E

E

T

Q

R

S

N

N

P

P

E

R

K

K

T

A

L

I

P

P

K

S

A

A

I

A

N

K

S

K

I

M

P

I

L

Y

R

R

I

I

I

L

L

F

F

V

Y

F

V

L

L

A

A

S

L

L

A

T

C

L

I

V

-

G

-

F

-

L

I

V

A

P

V

Y

T

T

S

S

W

D

Q

Q

Q

L

V

L

-

G

-

A

-

G

S

S

P

A

S

T

K

K

-

A

S

S

P

P

F

Y

V

V

E

I

L

A

F

V

L

S

V

S

A

H

G

G

F

V

P

R

A

V

A

P

G

H

I

F

V

I

N

N

F

A

V

V

V

I

L

L

T

L

S

S

A

V

A

L

S

S

S

V

A

A

N

N

S

G

G

A

V

F

F

Y

S

T

S

S

R

R

M

I

L

L

F

M

G

S

L

L

A

A

N

K

Q

Q

D

G

N

N

A

A

P

P

G

K

I

C

F

F

R

D

R

Y

L

I

S

D

G

R

N

E

S

G

V

R

P

P

L

A

S

A

L

M

A

L

F

V

T

S

T

A

L

L

L

F

M

G

L

V

V

I

G

A

V

F

L

C

L

A

L

S

F

S

I

K

V

K

P

E

E

E

V

-

M

-

T

D

A

V

F

F

T

T

I

W

V

L

S

L

T

A

V

I

S

S

A

G

I

L

L

S

V

Q

I

L

F

F

T

T

W

W

S

I

T

T

I

I

L

C

A

L

S

S

Y

H

I

I

A

R

Y

F

R

R

K

R

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)
22% identity, 87% coverage: 6:428/484 of query aligns to 269:765/852 of Q03770

query
sites
Q03770

S

S

G

R

L

A

T

T

E

R

Q

K

P

Y

A

H

L

I

Q

Q

R

R

T

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L

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S

K

N

V

R

R

H

H

I

I

Q

Q

L

M

M

L

A

S

M

I

G

G

G

A

A

C

I

F

G

S

T

V

G

G

L

L

F

F

M

L

G

T

S

S

G

G

K

K

I

A

I

F

A

S

L

I

S

A

G

G

T

P

-

F

S

G

I

T

I

L

L

L

I

G

Y

F

M

G

I

L

I

T

G

G

L

S

F

I

V

I

Y

L

F

A

V

T

M

M

R

L

A

S

M

F

G

T

E

E

M

L

L

S

L

T

S

L

N

I

L

P

N

V

F

S

K

S

T

G

F

F

A

S

D

G

F

L

A

A

G

S

A

R

Y

F

L

V

G

E

P

D

R

A

A

F

A

G

F

F

F

A

L

L

G

G

W

W

S

T

Y

Y

W

W

L

I

S

S

W

C

S

M

V

L

A

A

V

L

I

P

G

A

D

-

A

Q

V

V

V

S

G

S

G
x
T

F

F

F

Y

Q

L

Y

S

W

Y

F

Y

P

N

D

N

V

V

P

N

A

I

W

S

I

K

P

G

A

V

I

T

G

A

M

G

L

F

M

I

T

T

L

L

F

F

A

S

-

A

-

F

-

S

-

I

-

V

L

V

N

N

V

L

L

L

T

D

V

V

R

S

L

I

F

M

G

G

E

E

I

I

E

V

F

Y

W

V

F

A

A

G

I

I

I

S

K

K

I

V

I

I

A

I

V

A

V

I

T

L

L

M

I

V

G

F

V

T

S

M

L

I

V

I

L

L

I

N

A

A

S

G

S

H

-

G

-

N

-

D

-

I

-

H

-

E

-

G

-

V

-

G

-

F

-

R

-

Y

-

W

-

D

-

S

-

K

-

S

-

V

-

R

-

N

-

L

-

T

-

Y

-

G

F

L

V

Y

S

R

P

P

S

T

G

F

V

D

T

L

A

A

S

D

L

A

N

G

H

E

L

G

L

S

D

K

K

K

Q

G

A

I

A

S

F

G

P

P

N

K

G

G

L

R

F

F

G

L

F

A

F

T

A

A

G

S

F

V

Q

M

M

L

-

I

A

S

I

T

F

F

S

A

F

F

A

S

G

G

T

V

E

E

L

M

I

T

G

F

T

L

A

A

A

S

A

G

E

E

T

A

R

I

N

N

P

P

E

R

K

K

T

T

L

I

P

P

K

S

A

A

I

T

N

K

S

R

I

T

P

F

L

S

R

I

I

V

I

L

L

I

F

S

Y

Y

V

V

L

F

A

L

L

I

-

F

-

S

-

V

-

G

-

I

-

N

-

I

-

Y

-

S

-

G

-

D

-

P

-

R

-

L

-

S

-

Y

-

F

-

P

-

G

-

I

-

S

-

E

-

K

-

R

-

Y

A

E

C

A

I

I

A

K

V

G

T

T

-

G

-

M

-

D

-

W

-

R

-

L

-

R

-

T

-

N

-

C

-

R

-

G

-

I

S

D

W

Y

Q

R

Q

Q

V

I

S

S

P

V

S

G

-

T

-

G

-

Y

K

S

S

S

P

P

F

W

V

V

E

V

L

A

F

L

L

Q

V

N

A

F

G

G

F

L

P

C

A

T

A

F

A

A

G

S

I

A

V

F

N

N

F

A

V

I

V

L

L

I

T

F

S

F

A

T

A

A

S

T

S

A

A

G

N

I

S

S

G

S

V

L

F

F

S

S

S

C

S

S

R

R

M

T

L

L

F

Y

G

A

L

M

A

S

N

V

Q

Q

D

R

N

K

A

A

P

P

G

P

I

V

F

F

R

E

R

I

L

C

S

S

G

K

N

R

S

G

V

V

P

P

L

Y

L

V

S

S

L

V

A

I

F

F

T

S

L

L

L

F

M

S

L

V

V

I

G

A

V

Y

L

I

L

A

L

-

F

-

I

V

V

D

P

Q

E

T

V

A

M

I

T

E

A

N

F

F

T

D

I

V

V

L

S

A

T

N

V

V

S

S

A

S

I

A

L

S

V

T

I

S

F

I

T

I

W

W

S

M

T

G

I

L

L

N

A

L

S

S

Y

F

I

L

A

R

Y

F

R

Y

-

Y

-

A

-

L

K

K

K

Q

R

R

P

K

E

D

L

I

H

I

A

S

K

R

S

N

A

D

Y

S

K

S

M

Y

P

P

G

Y

G

K

V

S

P

P

M

F

A

Q

W

P

F

Y

S

-

L

L

A

A

F

I

L

Y

G

G

F

L

V

V

L

G

C

C

L

S

L

L

T382 (≠ G119) 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.

P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
22% identity, 77% coverage: 23:397/484 of query aligns to 15:385/445 of P60061

query
sites
P60061

I

V

Q

T

L

L

M

M

A

V

M

S

G

G

G

N

A
x
I

I

M

G

G

T
x
S

G

G

L

V

F

F

M

L

G

L

S

P

G

A

K

N

I

L

I

A

A

S

L

T

S

G

G

G

T

I

S

A

I

I

I

Y

-

G

L

W

I

L

Y

V

M

T

I

I

G

G

L

-

F

-

V

-

Y

-

F

-

V

-

M

-

R

-

A

A

M

L

G

G

-

L

E

S

M

M

L

V

L

Y

S

A

N

K

L

M

N

S

F

F

K

L

T

D

F

P

A

S

D

P

F

-

A

G

G

G

A

S

Y

Y

L

A

G

Y

P

A

R

R

A

R

A

C

F

F

-

G

-

P

F

F

L

L

G

G

W

Y

S

Q

-

T

-

N

-

V

-

L

Y
|
Y

W

W

L

L

S
x
A

W
x
C

S

W

V

I

A

G

V
x
N

I

I

G

A

D
x
M

A

V

V

V

V

I

V

G

G

V

G

G

F

Y

F

L

Q

S

Y

Y

W

F

F

F

P

P

D

I

V

L

P

K

A

D

-

P

-

L

-

V

-

L

W

T

I

I

P

T

A

C

I

V

G

V

M

V

L

L

M

W

T

I

L

F

F

V

A

L

L

L

N

N

V

I

L

V

T

G

V

P

R

K

L

M

F

I

G

T

E

R

I

V

E

Q

F

-

W

-

F

-

A

A

I

V

I

A

K

T

I

V

I

L

A

A

V

L

V

I

T

P

L

I

I

V

G

G

V

I

S

A

L

V

-

F

-

G

-

W

-

F

-

W

-

F

-

R

-

G

-

E

V

T

L

Y

I

M

A

A

S

A

S

W

F

N

V

V

S

S

P

G

S

L

G

G

V

T

T

F

A

G

S

A

L

I

N

Q

H

S

L

T

L

L

D

N

K

-

Q

-

A

-

F

-

P

-

N

-

G

-

L

-

F

-

G

-

F

-

A

-

G

-

F

-

Q

-

M

V

A

T

I

L

F
x
W

S
|
S

F

F

A
x
I

G

G

T

V

E

E

L

S

I

A

G

S

T

V

A

A

A

G

E

V

T

V

R

K

N

N

P

P

E

K

K

R

T

N

L

V

P

P

K

I

A

A

I

T

N

I

S

G

I

G

P

V

L

L

R

I

I

A

L

V

F

C

Y

Y

V

V

L

L

A

S

L

T

A

T

C

A

I

I

I

M

A

G

V

M

T

I

S

P

W

N

Q

A

V

L

S

R

P

V

S

S

K

A

S

S

P

P

F

F

V

G

E

D

L

A

F

A

L

R

V

M

A

A

G

L

F

G

P

D

A

T

A

A

A

G

G

A

I

I

V

V

N

S

F

F

V

C

V

A

L

A

T

A

S

G

A

C

A

L

S

G

S

S

A

L

N

G

S

G

G
x
W

V

T

F

L

S

L

S

A

S

G

R

Q

M

T

L

A

F

K

G

A

L

A

A

A

N

D

Q

D

D

G

N

L

A

F

P

P

G

P

I

I

F

F

R

A

R

R

L

V

S

N

G

K

N

A

S

G

V

T

P

P

L

V

L

A

S

G

L

L

A

I

F

I

T

V

T

G

L

I

L

L

M

M

L

T

V

I

G

-

V

F

L

Q

L

L

L

S

F

S

I

I

V

S

P

P

E

N

V

A

M

T

T

K

A

E

F

F

T

G

I

L

V

V

S

S

T

S

V

V

S
|
S

A

V

I

I

L

F

V

T

I

L

F

V

T

P

W

Y

-

L

-

Y

-

T

-

C

-

A

S

A

T

L

I

L

L

L

A

L

S

G

Y

H

I

G

A

H

Y

F

R

G

K

K

K

A

R

R

P

P

I23 (≠ A31) binding agmatine; binding L-arginine
S26 (≠ T34) binding L-arginine
Y93 (= Y102) mutation to L: Greatly decreased Arg uptake into liposomes.
A96 (≠ S105) binding agmatine; binding L-arginine
C97 (≠ W106) binding agmatine
N101 (≠ V110) binding agmatine; 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 (≠ D113) binding agmatine; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
W202 (≠ F218) binding L-arginine; mutation to L: Halves Arg uptake into liposomes.
S203 (= S219) binding agmatine
I205 (≠ A221) binding agmatine; binding L-arginine; mutation to A: About wild-type affinity for Arg and Agm.
W293 (≠ G309) binding agmatine; 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 (= S374) binding L-arginine; 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)
22% identity, 77% coverage: 23:397/484 of query aligns to 15:385/445 of P60063

query
sites
P60063

I

V

Q

T

L

L

M

M

A

V

M

S

G

G

G
x
N

A
x
I

I

M

G
|
G

T
x
S

G
|
G

L

V

F

F

M

L

G

L

S

P

G

A

K

N

I

L

I

A

A

S

L

T

S

G

G

G

T

I

S

A

I

I

I

Y

-

G

L

W

I

L

Y

V

M

T

I

I

G

G

L

-

F

-

V

-

Y

-

F

-

V

-

M

-

R

-

A

A

M

L

G

G

-

L

E

S

M

M

L

V

L

Y

S

A

N

K

L

M

N

S

F

F

K

L

T

D

F

P

A

S

D

P

F

-

A

G

G

G

A

S

Y
|
Y

L

A

G

Y

P

A

R

R

A

R

A

C

F

F

-

G

-

P

F

F

L

L

G

G

W
x
Y

S

Q

-

T

-

N

-

V

-

L

Y
|
Y

W

W

L

L

S
x
A

W
x
C

S

W

V

I

A

G

V
x
N

I

I

G

A

D

M

A

V

V

V

V

I

V

G

G

V

G

G

F

Y

F

L

Q

S

Y

Y

W

F

F

F

P

P

D

I

V

L

P

K

A

D

-

P

-

L

-

V

-

L

W

T

I

I

P

T

A

C

I

V

G

V

M

V

L

L

M

W

T

I

L

F

F

V

A

L

L

L

N

N

V

I

L

V

T

G

V

P

R

K

L

M

F

I

G

T

E

R

I

V

E

Q

F

-

W

-

F

-

A

A

I

V

I

A

K

T

I

V

I

L

A

A

V

L

V

I

T

P

L

I

I

V

G

G

V

I

S

A

L

V

-

F

-

G

-

W

-

F

-

W

-

F

-

R

-

G

-

E

V

T

L

Y

I

M

A

A

S

A

S

W

F

N

V

V

S

S

P

G

S

L

G

G

V

T

T

F

A

G

S

A

L

I

N

Q

H

S

L

T

L

L

D

N

K

-

Q

-

A

-

F

-

P

-

N

-

G

-

L

-

F

-

G

-

F

-

A

-

G

-

F

-

Q

-

M

V

A

T

I

L

F
x
W

S

S

F

F

A
x
I

G
|
G

T
x
V

E
|
E

L
x
S

I
x
A

G

S

T

V

A

A

A

G

E

V

T

V

R

K

N

N

P

P

E

K

K

R

T

N

L

V

P

P

K

I

A

A

I

T

N

I

S

G

I

G

P

V

L

L

R

I

I

A

L

V

F

C

Y

Y

V

V

L

L

A

S

L

T

A

T

C

A

I

I

I

M

A

G

V

M

T

I

S

P

W

N

Q

A

V

L

S

R

P

V

S

S

K

A

S

S

P

P

F

F

V

G

E

D

L

A

F

A

L

R

V

M

A

A

G

L

F

G

P

D

A

T

A

A

A

G

G

A

I

I

V

V

N

S

F

F

V

C

V

A

L

A

T

A

S

G

A

C

A

L

S

G

S

S

A

L

N

G

S

G

G
x
W

V

T

F

L

S

L

S

A

S

G

R

Q

M

T

L

A

F

K

G

A

L

A

A

A

N

D

Q

D

D

G

N

L

A

F

P

P

G

P

I

I

F

F

R

A

R

R

L

V

S

N

G

K

N

A

S

G

V

T

P

P

L

V

L

A

S

G

L

L

A

I

F

I

T

V

T

G

L

I

L

L

M

M

L

T

V

I

G

-

V
x
F

L

Q

L

L

L

S

F

S

I

I

V

S

P

P

E

N

V

A

M

T

T

K

A

E

F

F

T

G

I

L

V

V

S

S

T

S

V

V

S
|
S

A

V

I

I

L

F

V

T

I

L

F

V

T

P

W
x
Y

-

L

-

Y

-

T

-

C

-

A

S

A

T

L

I

L

L

L

A

L

S

G

Y

H

I

G

A

H

Y

F

R

G

K

K

K

A

R

R

P

P

N22 (≠ G30) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
I23 (≠ A31) binding L-arginine
GSG 25:27 (≠ GTG 33:35) Helix-breaking GSG motif TM1
S26 (≠ T34) binding L-arginine; mutation to K: 5% Agm antiport.
G27 (= G35) binding L-arginine
Y74 (= Y89) 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 (≠ W100) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
Y93 (= Y102) 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 (≠ S105) binding L-arginine
C97 (≠ W106) binding L-arginine
N101 (≠ V110) binding L-arginine
W202 (≠ F218) Periplasmic (proximal) gate; binding L-arginine
I205 (≠ A221) binding L-arginine
GVESA 206:210 (≠ GTELI 222:226) Helix-breaking GVESA motif TM6
E208 (= E224) mutation E->A,D: 5-10% Agm antiport.
W293 (≠ G309) binding L-arginine
F337 (≠ V354) mutation to A: Severely decreased antiport.
S357 (= S374) binding L-arginine
Y365 (≠ W382) 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)
22% identity, 77% coverage: 23:397/484 of query aligns to 11:381/437 of 5j4nA

query
sites
5j4nA

I

V

Q

T

L

L

M

M

A

V

M

S

G

G

G

N

A
x
I

I

M

G

G

T

S

G

G

L

V

F

F

M

L

G

L

S

P

G

A

K

N

I

L

I

A

A

S

L

T

S

G

G

G

T

I

S

A

I

I

I

Y

-

G

L

W

I

L

Y

V

M

T

I

I

G

G

L

-

F

-

V

-

Y

-

F

-

V

-

M

-

R

-

A

A

M

L

G

G

-

L

E

S

M

M

L

V

L

Y

S

A

N

K

L

M

N

S

F

F

K

L

T

D

F

P

A

S

D

P

F

-

A

G

G

G

A

S

Y

Y

L

A

G

Y

P

A

R

R

A

R

A

C

F

F

-

G

-

P

F

F

L

L

G

G

W

Y

S

Q

-

T

-

N

-

V

-

L

Y

Y

W

W

L

L

S
x
A

W
x
C

S

W

V

I

A
x
G

V
x
N

I

I

G

A

D
x
M

A

V

V

V

V

I

V

G

G

V

G

G

F

Y

F

L

Q

S

Y

Y

W

F

F

F

P

P

D

I

V

L

P

K

A

D

-

P

-

L

-

V

-

L

W

T

I

I

P

T

A

C

I

V

G

V

M

V

L

L

M

W

T

I

L

F

F

V

A

L

L

L

N

N

V

I

L

V

T

G

V

P

R

K

L

M

F

I

G

T

E

R

I

V

E

Q

F

-

W

-

F

-

A

A

I

V

I

A

K

T

I

V

I

L

A

A

V

L

V

I

T

P

L

I

I

V

G

G

V

I

S

A

L

V

-

F

-

G

-

W

-

F

-

W

-

F

-

R

-

G

-

E

V

T

L

Y

I

M

A

A

S

A

S

W

F

N

V

V

S

S

P

G

S

L

G

G

V

T

T

F

A

G

S

A

L

I

N

Q

H

S

L

T

L

L

D

N

K

-

Q

-

A

-

F

-

P

-

N

-

G

-

L

-

F

-

G

-

F

-

A

-

G

-

F

-

Q

-

M

V

A

T

I

L

F

W

S

S

F

F

A

I

G

G

T

V

E

E

L

S

I

A

G

S

T

V

A

A

A

G

E

V

T

V

R

K

N

N

P

P

E

K

K

R

T

N

L

V

P

P

K

I

A

A

I

T

N

I

S

G

I

G

P

V

L

L

R

I

I

A

L

V

F

C

Y

Y

V

V

L

L

A

S

L

T

A

T

C

A

I

I

I

M

A

G

V

M

T

I

S

P

W

N

Q

A

V

L

S

R

P

V

S

S

K

A

S

S

P

P

F

F

V

G

E

D

L

A

F

A

L

R

V

M

A

A

G

L

F

G

P

D

A

T

A

A

A

G

G

A

I

I

V

V

N

S

F

F

V

C

V

A

L

A

T

A

S

G

A

C

A

L

S

G

S

S

A

L

N

G

S

G

G
x
W

V

T

F

L

S

L

S

A

S

G

R

Q

M

T

L

A

F

K

G

A

L

A

A

A

N

D

Q

D

D

G

N

L

A

F

P

P

G

P

I

I

F

F

R

A

R

R

L

V

S

N

G

K

N

A

S

G

V

T

P

P

L

V

L

A

S

G

L

L

A

I

F

I

T

V

T

G

L

I

L

L

M

M

L

T

V

I

G

-

V

F

L

Q

L

L

L

S

F

S

I

I

V

S

P

P

E

N

V

A

M

T

T

K

A

E

F

F

T

G

I

L

V

V

S

S

T

S

V

V

S

S

A

V

I

I

L

F

V

T

I

L

F

V

T

P

W

Y

-

L

-

Y

-

T

-

C

-

A

S

A

T

L

I

L

L

L

A

L

S

G

Y

H

I

G

A

H

Y

F

R

G

K

K

K

A

R

R

P

P

binding agmatine: I19 (≠ A31), A92 (≠ S105), C93 (≠ W106), G96 (≠ A109), N97 (≠ V110), M100 (≠ D113), W289 (≠ G309)

3l1lA Structure of arg-bound escherichia coli adic (see paper)
22% identity, 77% coverage: 23:397/484 of query aligns to 9:368/423 of 3l1lA

query
sites
3l1lA

I

V

Q

T

L

L

M

M

A

V

M

S

G

G

G

A

A
x
I

I

M

G

G

T
x
S

G
|
G

L

V

F

F

M

L

G

L

S

P

G

A

K

N

I

L

I

A

A

S

L

T

S

G

G

G

T

I

S

A

I

I

I

Y

-

G

L

W

I

L

Y

V

M

T

I

I

G

G

L

-

F

-

V

-

Y

-

F

-

V

-

M

-

R

-

A

A

M

L

G

G

-

L

E

S

M

M

L

V

L

Y

S

A

N

K

L

M

N

S

F

F

K

L

T

D

F

P

A

S

D

P

F

-

A

G

G

G

A

S

Y

Y

L

A

G

Y

P

A

R

R

A

R

A

C

F

F

-

G

-

P

F

F

L

L

G

G

W

Y

S

Q

-

T

-

N

-

V

-

L

Y

Y

W

W

L

L

S

A

W

C

S

W

V

I

A
x
G

V
x
N

I

I

G

A

D

M

A

V

V

V

V

I

V

G

G

V

G

G

F

Y

F

L

Q

S

Y

Y

W

F

F

F

P

P

D

I

V

L

P

K

A

D

-

P

W

W

I

V

P

L

A

T

I

I

G

T

M

C

L

V

M

V

T

V

L

L

F

W

A

I

-

F

-

V

-

L

L

L

N

N

V

I

L

V

T

G

V

P

R

K

L

M

F

I

G

T

E

R

I

V

E

Q

F

-

W

-

F

-

A

A

I

V

I

A

K

T

I

V

I

L

A

A

V

L

V

I

T

P

L

I

I

V

G

G

V

I

S

A

L

V

V

F

-

G

-

W

-

F

-

W

L

F

I

R

A

G

S

E

S

T

F

Y

V

M

S

A

P

-

S

-

G

A

V

I

T

Q

A

S

S

T

L

L

N

N

H

-

L

-

D

-

K

-

Q

-

A

-

F

-

P

-

N

-

G

-

L

-

F

-

G

-

F

-

A

-

G

-

F

-

Q

-

M

V

A

T

I

L

F
x
W

S
|
S

F

F

A
x
I

G

G

T

V

E

E

L

S

I

A

G

S

T

V

A

A

A

G

E

V

T

V

R

K

N

N

P

P

E

K

K

R

T

N

L

V

P

P

K

I

A

A

I

T

N

I

S

G

I

G

P

V

L

L

R

I

I

A

L

V

F

C

Y

Y

V

V

L

L

A

S

L

T

A

T

C

A

I

I

I

M

A

G

V

M

T

I

S

P

W

N

Q

A

V

L

S

R

P

V

S

S

K

A

S

S

P

P

F

F

V

G

E

D

L

A

F

A

L

R

V

M

A

A

G

L

F

G

P

D

A

T

A

A

A

G

G

A

I

I

V

V

N

S

F

F

V

C

V

A

L

A

T

A

S

G

A

C

A

L

S

G

S

S

A

L

N

G

S

G

G
x
W

V

T

F

L

S

L

S

A

S

G

R

Q

M

T

L

A

F

K

G

A

L

A

A

A

N

D

Q

D

D

G

N

L

A

F

P

P

G

P

I

I

F

F

R

A

R

R

L

V

S

N

G

K

N

A

S

G

V

T

P

P

L

V

L

A

S

G

L

L

A

I

F

I

T

V

T

G

L

I

L

L

M

M

L

T

V

I

G

-

V

F

L

Q

L

L

L

S

F

S

I

I

V

S

P

P

E

N

V

A

M

T

T

K

A

E

F

F

T

G

I

L

V

V

S

S

T

S

V

V

S

S

A

V

I

I

L

F

V

T

I

L

F

V

T

P

W

Y

-

L

-

Y

-

T

-

C

-

A

S

A

T

L

I

L

L

L

A

L

S

G

Y

H

I

G

A

H

Y

F

R

G

K

K

K

A

R

R

P

P

binding arginine: I17 (≠ A31), S20 (≠ T34), G21 (= G35), G94 (≠ A109), N95 (≠ V110), W185 (≠ F218), S186 (= S219), I188 (≠ A221), W276 (≠ G309)

P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
22% identity, 50% coverage: 5:244/484 of query aligns to 6:242/461 of P76037

query
sites
P76037

P

P

S

L

G

N

L

I

T

A

E

A

Q

Q

P

P

A

G

-

K

-

T

-

R

L

L

Q

R

R

K

T

S

L

L

S

K

N

L

R

W

H

Q

I

V

Q

V

L

M

M

M

A

G

M

L

G

A

G

Y

A

L

I

T

G

P

T

M

G

T

L

V

F

F

M

D

G

T

S

F

G

G

K

I

I

V

I

S

A

G

L

I

S

S

G

D

T

G

S

H

I

V

I

P

L

A

I

S

Y

Y

M

L

I

L

I

A

G

L

L

A

F

G

V

V

Y

L

F

F

V

T

M

A

R

I

A

S

M

Y

G

G

E

K

M

L

L

V

L

R

S

Q

N

F

L

P

N

E

F

A

K

G

T

S

F

A

A

Y

D

T

F

Y

A

A

G

Q

A

K

Y

S

L

I

G

N

P

P

R

H

A

V

A

G

F

F

F

M

L

V

G

G

W

W

S

S

Y

S

W

L

L

L

S

D

W
x
Y

S

L

V

F

A

L

V

P

I

M

G

I

D

N

A

V

V

L

V

A

G

K

G

I

F

Y

F

L

Q

S

Y

A

W

L

F

F

P

P

D

E

V

V

P

P

A

P

W

W

I

V

P

W

A

V

I

V

G

T

M

F

L

V

M

A

T

I

L

L

F

T

A

A

L

A

N

N

V

L

L

K

T

S

V

V

R

N

L

L

F

V

G

A

E

N

I

F

E

N

F

T

W

L

F

F

A

V

I

L

I

V

K

Q

I

I

I

S

A

I

V

M

V

V

T

V

L

F

I

I

G

-

V

-

S

-

L

-

V

F

L

L

I

V

A

V

S

Q

S

G

F

L

V

H

S

K

P

G

S

E

G

G

V

V

T

G

A

T

-

V

-

W

S

S

L

L

N

Q

H

P

L

F

L

I

D

S

K

E

Q

N

A

A

A

H

F

-

P

-

N

-

G

-

L

L

F

I

G

P

F

I

A

T

G

G

F

A

Q

T

M

I

A

V

I

C

F

F

S

S

F

F

A

L

G

G

T

F

E

D

L

A

I

V

G

T

T

T

A

L

A

S

A

E

E

E

T

T

R

P

N

D

P

A

E

A

K

R

T

V

L

I

P

P

K

K

A

A

I

I

Y110 (≠ W106) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.

6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
23% identity, 43% coverage: 203:408/484 of query aligns to 213:408/458 of 6f34A

query
sites
6f34A

P

P

N

Y

G

G

L

F

F

S

G

G

F

V

F

A

A

T

G

G

F

A

Q

A

M

T

A

V

I

F

F
|
F

S
x
A

F

Y

A
x
I

G

G

T

F

E

D

L

A

I

V

G

S

T

T

A

A

A

E

E

E

T

V

R

R

N

N

P

P

E

Q

K

R

T

D

L

M

P

P

K

I

A

G

I

I

N

I

S

V

I

S

P

L

L

L

R

V

I

C

I

T

L

L

F

L

Y

Y

V

I

L

A

A

V

L

S

A

L

C

V

I

L

I

T

A

G

V

I

T

V

S

P

W

Y

Q

E

Q

Q

V

L

S

N

P

-

S

V

K

K

S

N

P

P

-

V

-

A

-

F

-

A

-

L

-

N

F

Y

V

I

E

H

L
x
Q

F

D

L

W

V
|
V

A

A

G

G

F

F

-

I

-

S

-

L

P

G

A

A

A

I

A

A

G

G

I

I

V

T

N

T

F
x
V

V

L

L

V

T

S

S

-

A

-

S

-

A

-

N

-

S

-

G

-

V

M

F

Y

S

G

S

Q

S

T

R

R

M

L

L

F

F

Y

G

A

L

I

A

S

N

R

Q

D

D

G

N

L

A

L

P

P

G

K

I

V

F

F

R

A

R

R

L

I

S

S

-

P

G

T

N

R

S

Q

V

V

P

P

L

Y

L

V

S

N

L

T

A

W

F

L

T

T

-

G

-

A

T

A

L

V

L

A

M

V

L

F

V

A

G

G

V

I

L

I

L

P

L

L

F

N

I

K

V

L

P

A

E

E

V

-

M

-

T

-

A

-

F

-

T

-

I

-

V

-

S

-

T

-

V

L

S

T

A

N

I

I

L

G

V

T

I

L

F

F

T

A

W

F

S

I

T

T

I

V

L

S

A

I

S

G

Y

V

I

L

A

V

Y

L

R

R

K

K

K

T

R

Q

P

P

E

D

L

L

H

-

A

-

K

K

S

R

A

A

Y

F

K

R

M

V

P

P

binding arginine: F228 (= F218), A229 (≠ S219), I231 (≠ A221), V314 (≠ F296)
binding : Q296 (≠ L281), V299 (= V284)

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

5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
23% identity, 43% coverage: 203:408/484 of query aligns to 211:406/456 of 5oqtA

query
sites
5oqtA

P

P

N

Y

G

G

L

F

F

S

G

G

F

V

F

A

A

T

G

G

F

A

Q

A

M

T

A

V

I

F

F
|
F

S
x
A

F

Y

A
x
I

G

G

T

F

E

D

L

A

I

V

G

S

T

T

A

A

A

E

E

E

T

V

R

R

N

N

P

P

E

Q

K

R

T

D

L

M

P

P

K

I

A

G

I

I

N

I

S

V

I

S

P

L

L

L

R

V

I

C

I

T

L

L

F

L

Y

Y

V

I

L

A

A

V

L

S

A

L

C

V

I

L

I

T

A

G

V

I

T

V

S

P

W

Y

Q

E

Q

Q

V

L

S

N

P

-

S

V

K

K

S

N

P

P

-

V

-

A

-

F

-

A

-

L

-

N

F

Y

V

I

E

H

L
x
Q

F

D

L

W

V
|
V

A

A

G

G

F

F

-

I

-

S

-

L

P

G

A

A

A

I

A

A

G

G

I

I

V

T

N

T

F

V

V

L

L

V

T

M

S

-

A

-

S

-

A

-

N

-

S

-

G

-

V

M

F

Y

S

G

S

Q

S

T

R

R

M

L

L

F

F

Y

G

A

L

I

A

S

N

R

Q

D

D

G

N

L

A

L

P

P

G

K

I

V

F

F

R

A

R

R

L

I

S

S

-

P

G

T

N

R

S

Q

V

V

P

P

L

Y

L

V

S

N

L

T

A

W

F

L

T

T

-

G

-

A

T

A

L

V

L

A

M

V

L

F

V

A

G

G

V

I

L

I

L

P

L

L

F

N

I

K

V

L

P

A

E

E

V

-

M

-

T

-

A

-

F

-

T

-

I

-

V

-

S

-

T

-

V

L

S

T

A

N

I

I

L

G

V

T

I

L

F

F

T

A

W

F

S

I

T

T

I

V

L

S

A

I

S

G

Y

V

I

L

A

V

Y

L

R

R

K

K

K

T

R

Q

P

P

E

D

L

L

H

-

A

-

K

K

S

R

A

A

Y

F

K

R

M

V

P

P

binding alanine: F226 (= F218), A227 (≠ S219), I229 (≠ A221)
binding : Q294 (≠ L281), V297 (= V284)

Sites not aligning to the query:

binding alanine: 38, 40, 41, 42
binding : 24, 26, 28, 29, 32, 176, 177, 184, 188, 192

O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
20% identity, 83% coverage: 9:408/484 of query aligns to 3:387/438 of O34739

query
sites
O34739

T

T

E

E

Q

D

P

N

A

G

L

L

Q

K

R

K

T

E

L

I

S

G

N

L

R

L

H

F

I

A

Q

L

L

T

M

L

A

V

M

I

G

G

G

T

A

I

I

I

G

G

T

S

G

G

L

V

F

F

M

M

G

K

S

P

G

G

K

A

I

V

I

L

A

A

L

Y

S

S

G

G

T

D

S

S

I

K

I

M

L

A

I

L

Y

F

M

A

-

W

-

L

-

G

I

I

I

L

G

T

L

L

F

A

V

G

Y

G

F

L

V

T

M

I

R

A

A

E

M

I

G

G

E

T

M

Q

L

I

L

P

S

K

N

T

L

G

N

G

F

L

K

Y

T

T

F

Y

A

L

D

E

F

-

A

-

G

-

A

E

Y

V

L

Y

G

G

P

E

R

F

A

W

A

G

F

F

F

L

L
x
C

G

G

W

W

S

V

Y

Q

W

I

L

I

S

I

W

Y

S

G

V

P

A

A

V

I

I

I

G

G

D

-

A

-

V

-

V

A

V

L

G

G

G

L

F

Y

F

F

Q

G

Y

S

W

L

F

M

P

A

D

N

V

L

P

F

A

G

W

W

-

G

-

S

-

G

-

L

I

S

P

K

A

V

I

I

G

G

M

I

L

I

M

A

T

V

L

L

F

F

-

L

-
x
C

A

V

L

I

N

N

V

I

L

I

T

G

V

T

R

K

L

Y

F

G

G

G

E

F

I

V

E

Q

F

T

W

L

F

T

A

T

I

I

I

G

K

K

I

L

I

I

A

P

V

I

V

A

T
x
C

L

I

I

I

G

V

V

F

S

G

L

L

V

-

L

-

I

-

A

-

S

-

F

W

V

K

S

G

P

D

S

Q

G

H

V

I

T

F

A

T

S

A

L

V

N

N

H

E

L

S

L

I

D

S

K

D

Q

M

A

-

F

-

P

-

N

-

G

-

L

-

F

-

G

N

F

F

F

G

A

A

G

A

F

I

Q

L

M

A

A

T

I

L

F

F

S

A

F

Y

A

D

G

G

T

W

E

I

L

L

I

L

G

A

T

A

A

L

A

G

E

E

T

M

R

K

N

N

P

P

E

E

K

K

T

L

L

L

P

P

K

R

A

A

I

M

N

T

S

G

I

G

P

L

L

L

R

I

I

V

I

T

L

A

F

I

Y

Y

V

I

L

F

A

I

L

N

A

F

C

A

I

L

A

H

V

I

T

L

S

S

W

A

Q

N

Q

E

V

I

S

V

P

T

S

L

K

G

S

E

P

N

F

A

V

T

E

S

L

T

F

A

L

A

V

T

A

M

G

L

F

F

P

G

A

S

A

I

A

G

G

G

-

K

I

L

V

I

N

S

F

V

V

G

V

I

L

I

T

V

S

S

A

I

A

F

S

G

S
x
C

A

L

N

N

S

G

G

K

V

V

F

L

S

S

S

F

S

P

R

R

M

V

L

S

F

F

G

A

L

M

A

A

N

E

Q

R

D

K

N

Q

A

L

P

P

G

-

I

F

F

A

R

E

R

K

L

L

S

S

G

H

N

V

S

H

-

P

-

S

-

F

-

R

V

T

P

P

L

W

L

I

S

A

L

I

A

S

F

F

T

Q

T

I

L

A

L

L

M

A

L

L

V

-

G

-

V

I

L

M

L

L

F

I

I

S

V

N

P

P

E

D

V

K

M

L

T

S

A

E

F

I

T

S

I

I

V

F

S

-

T

-

V

-

S

-

A

-

I

M

L

I

V

Y

I

I

F

F

T

Y

W

V

S

M

T

A

I

F

L

F

A

A

S

V

Y

F

I

I

A

L

Y

R

R

K

K

R

K

A

R

K

P

G

E

E

L

-

H

-

A

-

K

K

S

R

A

A

Y

Y

K

S

M

V

P

P

C94 (≠ L98) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
C141 (vs. gap) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
C168 (≠ T169) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
C291 (≠ S305) 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.

Q9FFL1 Polyamine transporter RMV1; Protein RESISTANT TO METHYL VIOLOGEN 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
23% identity, 71% coverage: 69:411/484 of query aligns to 107:425/490 of Q9FFL1

query
sites
Q9FFL1

M

M

G

G

E

T

M

M

L

F

L

P

S

E

N

N

L

G

N

G

F

Y

K

V

T

V

F

W

A

V

D

T

F

L

A

A

G

-

A

-

Y

-

L

M

G

G

P

P

R

Y

A

W

A

G

F

F

F

Q

L

Q

G

G

W

W

S

V

Y

K

W

W

L

L

S

S

W

-

S

-

V

-

A

G

V

V

I

I

G

D

D

N

A

A

V

L

V

Y

V

P

G

I

G

L

F

F

F

L

Q

D

Y

Y

W

L

F

K

P

S

D

G

V

I

P

P

-

I

-

L

-

G

A

S

W

G

I

I

P

P

A

R

I

V

G

A

M

A

L

I

M

L

T

V

L

L

-

T

F

V

A

A

L

L

N

T

V

Y

L

L

T

N

V

Y

R

R

L

G

F

L

G

-

E

-

I

-

E

-

F

-

W

-

F

-

A

S

I

I

I

V

K

G

I

V

I

A

A

A

V

V

V

L

T

L

L

G

I

V

G

F

V

S

S

I

L

L

V

P

L

F

I

V

A

V

S

M

S

S

F

F

V

M

S

S

P

I

S

P

G

K

V

L

T

K

A

P

S

S

L

R

N

W

H

L

L

V

D

S

K

K

Q

K

-

M

-

K

-

G

-

V

-

N

-

W

A

S

A

L

F

Y

P

L

N

N

G

T

L

L

F

F

G

-

F

-

A

-

G

-

F

-

Q

-

M

-

A

-

I

-

F

W

S

N

F

L

A

N

G

Y

T

W

E

D

L

S

I

V

G

S

T

T

A

L

A

T

A

G

E

E

T

V

R

E

N

N

P

P

E

S

K

K

T

T

L

L

P

P

K

R

A

A

I

L

N

F

S

Y

I

A

P

L

L

L

R

L

I

V

L

F

F

S

Y

Y

V

I

L

F

A

P

L

V

A

L

C

T

I

G

I

T

A

G

V

A

T

I

S

A

W

L

Q

D

Q

Q

V

K

S

L

P

W

S

T

K

D

S

G

P

Y

F

F

V

A

E

D

L

I

F

G

L

K

V

V

A

I

G

G

F

-

P

-

A

-

G

G

I

V

V

W

N

L

F

G

V

W

L

I

T

Q

S

A

A

A

S

A

S

T

A

S

N

N

S

M

G

G

V

M

F

F

-

L

-

A

-

E

-

M

-

S

S

S

S

D

S

S

R

F

M

Q

L

L

F

L

G

G

L

M

A

A

N

E

Q

R

D

G

N

M

A

L

P

P

G

E

I

V

F

F

R

A

R

K

L

R

S

S

G

R

N

Y

S

R

V

T

P

P

L

W

L

V

S

G

L

I

A

L

F

F

T

S

T

A

L

S

L

G

M

V

L

I

V
x
I

G

L

V

S

L

W

L

L

L

S

F

F

I

-

V

-

P

Q

E

E

V

I

M

V

T

A

A

A

F

E

T

N

I

L

V

L

S

Y

T

C

V

F

S

G

A

M

I

V

L

L

V

E

I

F

F

I

T

T

W

-

S

-

T

-

I

-

L

-

A

-

S

-

Y

F

I

V

A

R

Y

L

R

R

K

M

K

K

R

Y

P

P

E

A

L

-

H

-

A

A

K

S

S

R

A

P

Y

F

K

K

M

I

P

P

G

V

G

G

V

V

I377 (≠ V352) mutation to F: Loss of sensitivity to paraquat.

9h76A Bacterial lat transporter basc in complex with l-ala and nb53 (see paper)
23% identity, 55% coverage: 141:408/484 of query aligns to 130:380/430 of 9h76A

query
sites
9h76A

L

L

F

M

A

G

L

V

N

N

V

F

L

L

T

G

V

T

R

K

L

Y

F

S

G

G

E

W

I

I

E

Q

F

T

W

L

F

A

A

T

I

I

I

L

K

K

I

L

I

I

A

P

V

L

V

V

T

-

L

-

I

-

G

-

V

-

S

-

L

-

V

V

L

I

I

I

A

V

S

A

S

G

F

L

V

L

S

Y

P

P

S

G

G

G

V

-

T

-

A

-

S

G

L

V

N

I

H

R

L

L

L

V

D

P

K

F

Q

S

A

V

A

E

F

T

P

H

N

P

G

V

L

L

F

T

G

S

F

F

F

G

A

S

G

A

F

L

Q

I

M

A

A

T

I

L

F

F

S

A

F

Y

A
x
D

G

G

T

W

E

I

L

N

I

V

G

G

T

T

A

L

A

A

A

G

E

E

T

M

R

K

N

N

P

P

E

G

K

K

T

M

L

L

P

P

K

K

A

V

I

I

N

I

S

G

I

G

P

L

L

S

R

I

I

V

I

M

L

A

F

V

Y

Y

V

L

L

L

A

T

L

N

A

I

C

A

I

Y

I

L

A

F

V

V

T

L

S

D

W

S

Q

S

Q

Q

V

L

S

A

P

G

S

T

K

D

S

T

P

P

-

A

F

L

V

V

E

A

L

S

F

H

L

L

V

F

A

E

G

G

F

I

P

-

A

-

A

G

A

S

G

K

I

L

V

V

N

T

F

I

V

G

V

I

L

L

T

I

S

S

A

V

A

F

S

G

A

I

N

N

S

G

G

Y

V

I

F

I

S

S

S

G

S

L

R

R

M

V

L

P

F

Y

G

A

L

L

A

A

N

T

Q

Q

D

K

N

M

A

L

P

P

G

-

I

-

F

F

R

S

R

D

L

W

S

F

G

A

N

R

S

I

V

N

P

P

L

K

L

T

S

N

L

L

A

P

F

I

T

N

T

G

L

G

L

L

M

V

L

M

V

L

G

G

V

I

L

A

L

I

L

V

F

M

I

I

V

L

P

T

E

G

V

Q

M

F

T

N

A

Q

F

L

T

T

I

-

V

-

S

-

T

-

V

-

S

-

A

D

I

L

L

I

V

V

I

F

F

V

T

I

W

W

S

F

T

F

I

I

L

T

A

L

S

T

Y

F

I

I

A

A

-

V

-

I

Y

L

R

R

K

K

K

T

R

Q

P

P

E

D

L

I

H

-

A

-

K

E

S

R

A

P

Y

Y

K

R

M

V

P

P

binding alanine: D200 (≠ A221)

Sites not aligning to the query:

binding alanine: 17, 18, 19

Query Sequence

>AO356_29455 FitnessBrowser__pseudo5_N2C3_1:AO356_29455
MKSIPSGLTEQPALQRTLSNRHIQLMAMGGAIGTGLFMGSGKIIALSGTSIILIYMIIGL
FVYFVMRAMGEMLLSNLNFKTFADFAGAYLGPRAAFFLGWSYWLSWSVAVIGDAVVVGGF
FQYWFPDVPAWIPAIGMLMTLFALNVLTVRLFGEIEFWFAIIKIIAVVTLIGVSLVLIAS
SFVSPSGVTASLNHLLDKQAAFPNGLFGFFAGFQMAIFSFAGTELIGTAAAETRNPEKTL
PKAINSIPLRIILFYVLALACIIAVTSWQQVSPSKSPFVELFLVAGFPAAAGIVNFVVLT
SAASSANSGVFSSSRMLFGLANQDNAPGIFRRLSGNSVPLLSLAFTTLLMLVGVLLLFIV
PEVMTAFTIVSTVSAILVIFTWSTILASYIAYRKKRPELHAKSAYKMPGGVPMAWFSLAF
LGFVLCLLALRPDTRIALLVMPGWFIWLAIAYQLTDARKPKSAPGNSEGNAPPPRNITQS
ANIP

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