SitesBLAST

T27 (= T27) mutation T->A,S: Retains 60% of wild-type activity.; mutation to N: Retains 20% of wild-type activity.
E98 (= E98) mutation to A: Retains 80% of wild-type activity.
K156 (= K156) mutation K->A,Q: Retains less than 10% of wild-type activity.; mutation to R: Retains 40% of wild-type activity.
F212 (= F212) mutation F->A,Q: Loss of activity.; mutation to Y: No change in activity.
E218 (= E218) 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)
45% identity, 95% coverage: 2:445/467 of query aligns to 14:452/458 of P24207

query
sites
P24207

Q

N

Q

Q

A

E

Q

P

G

T

L

L

K

H

R

R

G

G

L

L

S

H

A

N

R
|
R

H

H

I

I

R

Q

F

L

M

I

A

A

L

L

G

G

S

G

A

A

I

I

G

G

T

T

G

G

L

L

F

F

Y

L

G

G

S

I

A

G

S

P

A

A

I

I

Q

Q

M

M

A

A

G

G

P
|
P

A

A

V

V

L

L

A

G

Y

Y

L

G

I

V

G

A

G

G

A

I

V

A

F

F

M

L

V

I

M

M

R

R

A

Q

L

L

G

G

E

E

M

M

A

V

V

V

H

E

N

E

P

P

V

V

A

S

G

G

S

S

F
|
F

G

A

H

H

Y
x
F

A

A

T
x
Y

T

K

Y
|
Y

L
x
W

G

G

P

P

M
x
F

A

A

G

G

F
|
F

I

L

L

S

G

G

W
|
W

T

N

Y
|
Y

A
x
W

F

V

E

M

M
x
F

V

V

I

L

V

V

A

G

I

M

A

A

D
x
E

V

L

T

T

A

A

F

A

G

G

I

I

Y

Y

M

M

G

Q

F

Y

W

W

F

F

P

P

E

D

V

V

A

P

R

T

W

W

I

I

W

W

V

A

L

A

G

A

I

F

V

F

F

I

L

I

I

I

G

N

G

A

L

V

N

N

L

L

C

V

N

N

V

V

K

R

V

L

F

Y

G

G

E

E

M

T

E

E

F

F

W

W

L

F

S

A

L

L

L

I

K
|
K

V

V

G

L

A

A

I

I

V

I

A

G

M

M

I

I

L

G

A

F

G

G

L

L

G

W

I

L

M

L

A

-

F

-

G

-

F

F

S

S

Q

G

V

H

G

G

T

-

G

G

H

E

A

K

V

A

G

S

M

I

S

D

N

N

L

L

F

W

D

R

H

Y

G

G

F

F

M

F

P

A

N

T

G

G

V

W

G

N

G

G

L

L

I

I

A

L

S

S

F

L

A

A

V

V

V

I

M

M

F

F

A

S

F

F

G

G

I

L

E
|
E

I

L

I

I

G

G

V

I

T

T

A

A

G

A

E

E

A

A

K

R

D

D

P

P

Q

E

R

K

V

S

I

I

P

P

K

K

A

A

I

V

N

N

A

Q

V

V

P

V

L

Y

R
|
R

I

I

L

L

F

F

Y

Y

V

I

L

G

T

S

L

L

F

V

V

V

L

L

M

L

C

A

L

L

Y

Y

P

P

W

W

P

V

Q

E

I

V

G

K

S

S

Q

N

G

S

S

S

P

P

F

F

V

V

Q

M

I

I

F

F

S

H

N

N

L

L

G

D

I

S

G

N

S

V

A

V

A

A

A

S

V

A

L

L

N

N

V

F

V

V

V

I

I

L

S

V

A

A

A

S

I

L

S

S

A

V

I

Y

N

N

S

S

D

G

I

V

F

Y

G

S

A

N

G

S

R

R

M

M

M

L

Y

F

G

G

L

L

A

S

Q

V

Q

Q

G

G

H

N

A

A

P

P

R

K

G

F

F

L

S

T

K

R

L

V

S

S

K

R

H

R

G

G

V

V

P
|
P

W

I

M

N

T

S

V

L

V

M

V

L

M

S

G

G

A

A

A

I

L

T

L

S

I

L

G

V

V

V

L

L

L

I

N

N

Y

Y

L

L

I

L

P

P

E

Q

N

K

V

A

F

F

L

G

L

L

I

L

A

M

S

A

I

L

A

V

T

V

F

A

A

T

T

L

V

L

W

L

V

N

W

W

L

I

M

M

I

I

L

C

L

L

T

A

Q

H

V

L

A

R

M

F

R

R

R

A

S

A

M

M

S

-

R

R

E

R

Q

Q

V

G

A

R

Q

E

L

T

K

Q

F

F

P

K

V

A

P

L

F

L

W

Y

P

P

Y

F

G

G

P

N

A

Y

M

L

A

C

I

I

A

A

F

F

M

L

V

G

F

M

I

I

F

L

G

L

V

L

L

M

G

C

Y

T

F

M

P

D

D

D

T

M

Q

R

A

L

A

S

L

A

I

I

V

L

G

L

V
x
P

I

V

W

W

V

I

V

V

F

F

L

L

V

F

A

M

S

A

Y

F

R26 (= R14) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
P54 (= P42) 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 (= F75) mutation to L: No effect on phenylalanine transport activity.
F90 (≠ Y78) mutation to L: 65% of wild-type phenylalanine transport activity.
Y92 (≠ T80) mutation to L: 41% of wild-type phenylalanine transport activity.
Y94 (= Y82) mutation to L: 69% of wild-type phenylalanine transport activity.
W95 (≠ L83) mutation to L: 10% of wild-type phenylalanine transport activity.
F98 (≠ M86) mutation to L: No effect on phenylalanine transport activity.
F101 (= F89) mutation to L: 38% of wild-type phenylalanine transport activity.
W105 (= W93) mutation to L: 39% of wild-type phenylalanine transport activity.
Y107 (= Y95) mutation to L: No effect on phenylalanine transport activity.
W108 (≠ A96) mutation to L: 71% of wild-type phenylalanine transport activity.
F111 (≠ M99) 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 (≠ D106) mutation E->G,L,V,N: Loss of activity.
K168 (= K156) 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 (≠ V435) 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)
45% identity, 96% coverage: 2:450/467 of query aligns to 6:449/457 of P15993

query
sites
P15993

Q

Q

Q

H

A

G

Q

E

G

Q

L

L

K

K

R

R

G

G

L

L

S

K

A

N

R

R

H

H

I

I

R

Q

F

L

M

I

A

A

L

L

G

G

S

G

A

A

I

I

G

G

T

T

G

G

L

L

F

F

Y

L

G

G

S

S

A

A

S

S

A

V

I

I

Q

Q

M

S

A

A

G

G

P

P

A

G

V

I

L

I

L

L

A

G

Y

Y

L

A

I

I

G

A

G

G

A

F

A

I

V

A

F

F

M

L

V

I

M

M

R

R

A

Q

L

L

G

G

E

E

M

M

A

V

V

V

H

E

N

E

P

P

V

V

A

A

G

G

S

S

F

F

G

S

H

H

Y

F

A

A

T

Y

T

K

Y

Y

L

W

G

G

P

S

M

F

A

A

G

G

F

F

I

A

L

S

G

G

W

W

T

N

Y

Y

A

W

F

V

E

L

M
x
Y

V

V

I

L

V

V

A

A

I

M

A

A

D

E

V

L

T

T

A

A

F

V

G

G

I

K

Y

Y

M

I

G

Q

F

F

W

W

F

Y

P

P

E

E

V

I

A

P

R

T

W

W

I

V

W

S

V

A

L

A

G

V

I

F

V

F

F

V

L

V

I

I

G

N

G

A

L

I

N

N

L

L

C

T

N

N

V

V

K

K

V

V

F

F

G

G

E

E

M

M

E

E

F

F

W

W

L

F

S

A

L

I

K

K

V

V

G

I

A

A

I

V

V

V

A

A

M

M

I

I

L

I

A

F

G

G

L

G

G

W

I

L

M

L

A

-

F

-

G

-

F

F

S

S

Q

G

V

N

G

G

T

-

G

G

H

P

A

Q

V

A

G

T

M

V

S

S

N

N

L

L

F

W

D

D

H

Q

G

G

F

F

M

L

P

P

N

H

G

G

V

F

G

T

G

G

L

L

I

V

A

M

S

M

F

M

A

A

V

I

M

M

F

F

A

S

F

F

G

G

I

L

E

E

I

L

I

V

G

G

V

I

T

T

A

A

G

A

E

E

A

A

K

D

D

N

P

P

Q

E

R

Q

V

S

I

I

P

P

K

K

A

A

I

T

N

N

A

Q

V

V

P

I

L

Y

R

R

I

I

L

L

L

I

F

F

Y

Y

V

I

L

G

T

S

L

L

F

A

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V

L

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M

L

C

S

L

L

Y

M

P

P

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W

P

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R

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A

Q

D

G

T

S

S

P

P

F

F

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V

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L

I

I

F

F

S

H

N

E

L

L

G

G

I

D

G

T

S

F

A

V

A

A

A

N

V

A

L

L

N

N

V

I

V

V

I

L

S

T

A

A

I

L

S

S

A

V

I

Y

N

N

S

S

D

C

I

V

F

Y

G

C

A

N

G

S

R

R

M

M

M

L

Y

F

G

G

L

L

A

A

Q

Q

G

G

H

N

A

A

P

P

R

K

G

A

F

L

S

A

K

S

L

V

S

D

K

K

H

R

G

G

V

V

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P

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V

M

N

T

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V

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V

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S

G

A

A

L

A

V

L

T

L

A

I

L

G

C

V

V

L

L

L

I

N

N

Y

Y

L

L

I

A

P

P

E

E

N

S

V

A

F

F

L

G

L

L

I

L

A

M

S

A

I

L

A

V

T

V

F

S

A

A

T

L

V

V

W

I

V

N

W

W

L

A

M

M

I

I

L

S

L

L

T

A

Q

H

V

M

A

K

M

F

R

R

S

A

M

-

S

K

R

Q

E

E

Q

Q

V

G

A

V

Q

V

L

T

K

R

F

F

P

P

V

A

P

L

F

L

W

Y

P

P

Y

L

G

G

P

N

A

W

M

I

A

C

I

L

A

L

F

F

M

M

V

A

F

A

I

V

F

L

G

V

V

I

L

M

G

L

Y

M

F

T

P

P

D

G

T

M

Q

A

A

I

A

S

L

V

I

Y

V

L

G

I

V

P

I

V

W

W

V

L

V

I

F

V

L

L

V

G

A

I

S

G

Y

Y

L

L

L

F

W

K

C

E

K

K

Y103 (≠ M99) 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)
36% identity, 99% coverage: 1:461/467 of query aligns to 1:462/469 of P46349

query
sites
P46349

M

M

Q

N

Q

Q

A

S

Q

Q

-

S

G

G

L

L

K

K

R

K

G

E

L

L

S

K

A

T

R

R

H

H

I

M

R

T

F

M

M

I

A

S

L

I

G

A

S

G

A

V

I

I

G

G

T

A

G

G

L

L

F

F

Y

V

G
|
G

S

S

A

G

S

S

A

V

I

I

Q

H

M

S

A

T

G
|
G

P

P

A

G

V

A

L

V

A

S

Y

Y

L

A

I

L

G

A

G

G

A

L

V

V

F

I

M

F

V

I

M

M

R

R

A

M

L

L

G

G

E

E

M

M

A

S

V

A

H

V

N

N

P

P

V

T

A

S

G

G

S

S

F

F

G

S

H

Q

Y

Y

A

A

T

H

T

D

Y

A

L

I

G

G

P

P

M

W

A

A

G

G

F

F

I

T

L

I

G

G

W

W

T

L

Y

Y

A

W

F

F

E

F

M

W

V

V

I

I

V

V

-

I

A

A

I

I

A

E

D

A

V

I

T

A

A

G

F

A

G

G

I

I

Y

-

M

I

G

Q

F

Y

W

W

F

F

P

H

E

D

V

I

A

P

R

L

W

W

I

L

W

T

V

S

L

L

G

I

I

L

V

T

F

I

L

V

I

L

G

T

G

L

L

T

N

N

L

V

C

Y

N

S

V

V

K

K

V

S

F

F

G

G

E

E

M

F

E

E

F

Y

W

W

L

F

S

S

L

L

L

I

K

K

V

V

G

V

A

T

I

I

V

I

A

A

M

F

I

L

L

I

A

V

G

G

L

F

G

A

I

F

M

I

A

-

F

F

G

G

F

F

S

A

Q

P

V

-

G

-

T

G

G

S

H

E

A

P

V

V

G

G

M

F

S

S

N

N

L

L

F

T

D

G

H

K

G

G

F

F

M

F

P

P

N

E

G

G

V

I

G

S

L

V

I

L

A

L

S

G

F

I

A

V

V

V

M

I

F

F

A

S

F

F

G

M

G

G

I

T

E

E

I

I

I

V

G

A

V

I

T

A

A

A

G

G

E

E

A

T

K

S

D

N

P

P

Q

I

R

E

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S

I

V

P

T

K

K

A

A

I

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R

A

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V

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R

R

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L

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F

F

Y

Y

V

V

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T

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L

I

F

A

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I

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M

V

C

A

L

L

Y

L

P

P

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W

P

N

Q

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A

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N

S

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L

G

E

S

S

P

P

F

F

V

V

Q

A

I

V

F

L

S

E

N

H

L

I

G

G

I

V

G

P

S

A

A

A

A

Q

V

I

L

M

N

N

V

F

V

I

V

V

I

L

S

T

A

A

A

V

I

L

S

S

A

C

I

L

N

N

S

S

D
x
G

I

L

F

Y

G

T

A

T

G

S

R

R

M

M

M

L

Y

Y

G

S

L

L

A

A

Q

E

Q

R

G

N

H

E

A

A

P

P

R

R

G

R

F

F

S

M

K

K

L

L

S

S

K

K

H

K

G

G

V

V

P

P

W

V

M

Q

T

A

V

I

V

V

V

A

M
x
G

G

T

A

F

A
x
F

L

S

L

Y

I

I

G

A

V

V

L

V

L

M

N

N

Y

Y

L

F

I

S

P

P

E

D

N

T

V

V

F

F

L

L

L

F

I

L

A

V

S

N

I

S

A

S

T

G

F

A

A

I

T

A

V

L

W

L

V

V

W

Y

L

L

M

V

I

I

L

A

L

V

T

S

Q

Q

V

L

A

K

M

M

R

R

R

K

S

K

M

L

S

E

R

K

E

T

Q

N

V

P

A

E

Q

A

L

L

K

K

F

I

P

K

V

M

-

W

-

L

-

F

P

P

F

F

W

L

P

T

Y

Y

G

L

P

T

A

I

M

I

A

A

I

I

A

C

F
x
G

M

I

V

L

F

V

I

S

F

M

G

A

V

F

L

I

G

D

Y

S

F

M

P

R

D

D

T

-

Q

-

A

E

A

L

L

L

I

L

V

T

G

G

V

V

I

I

W

T

V

G

V

I

F

V

L

L

V

I

A

-

S

S

Y

Y

L

L

L

V

W

F

C

R

K

K

P

R

R

K

A

V

G

S

Q

E

-

K

-

A

G

A

Q

N

P

P

V

V

A

T

E

Q

G33 (= G32) mutation to D: Lack of activity.
G42 (= G41) 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 (≠ F413) 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)
36% identity, 89% coverage: 2:417/467 of query aligns to 8:431/489 of P25737

query
sites
P25737

Q

T

Q

E

A

A

Q

P

G

G

L

L

K

R

R

R

G

E

L

L

S

K

A

A

R

R

H

H

I

L

R

T

F

M

M

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

Q

S

M

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

M

F

V

L

M

M

R

T

A

S

L

L

G

G

E

E

M

L

A

A

V

A

H

Y

N

M

P

P

V

V

A

S

G

G

S

S

F

F

G

A

H

T

Y

Y

A

G

T

Q

T

N

Y

Y

L

V

G

E

P

E

M

G

A

F

G

G

F

F

I

A

L

L

G

G

W

W

T

N

Y
|
Y

A

W

F

Y

E

N

M
x
W

V

A

I

V

V

T

A

I

I

A

A

V

D

D

V

L

T

V

A

A

F

A

G

Q

I

L

Y

V

M

M

G

S

F

W

W

W

F

F

P

P

E

D

V

T

A

P

R

G

W

W

I

I

W

W

-

S

-

A

-

L

V

F

L

L

G

G

I

V

V

I

F

F

L

L

I

-

G

-

L

L

N

N

L

Y

C

I

N

S

V

V

K

R

V

G

F

F

G

G

E

E

M

A

E

E

F

Y

W

W

L

F

S

S

L

L

L

I

K
|
K

V

V

G

T

A

T

I

V

V

I

A

V

M

F

I

I

L

I

A

V

G

G

L

V

G

-

I

L

M

M

A

I

F

I

G

G

F

I

S

F

Q

K

V

-

G

-

T

G

G

A

H

Q

A

P

V

A

G

G

M

W

S

S

N

N

L

W

F

T

D

I

H

G

G

E

G

A

F

P

M

F

P

A

N

G

G

G

V

F

G

A

L

M

I

I

A

G

S

V

F

A

A

M

V

I

V

V

M

G

F
|
F

A

S

F

F

G

Q

G

G

I

T

E
|
E

I

L

I

I

G

G

V

I

T

A

A

A

G

G

E
|
E

A

S

K

E

D

D

P

P

Q

A

R

K

V

N

I

I

P

P

K

R

A

A

I

V

N

R

A

Q

V

V

P

F

L

W

R

R

I

I

L

L

F

F

Y

Y

V

V

L

F

T

A

L

I

F

L

V

I

L

I

M

S

C

L

L

I

Y

I

P

P

W

Y

-

T

-

D

P

P

Q

S

I

L

G

L

S

R

Q

N

G
x
D

-

V

-

K

-
x
D

-

I

-

S

-

V

S

S

P

P

F

F

V

T

Q

L

I

V

F

F

S

Q

N

H

L

A

G

G

I

L

G

L

S

S

A

A

V

V

L

M

N

N

V

A

V

V

V

I

I

L

S

T

A

A

A

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

L

L

A

A

Q

C

Q

D

G

G

H

K

A

A

P

P

R

R

G

I

F

F

S

A

K

K

L

L

S

S

K

R

H

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

A

L

A

C

L

F

L

L

I

T

G

S

V

M

L

F

L

G

N

N

Y

-

L

-

I

-

P

-

E

Q

N

T

V

V

F

Y

L

L

L

W

I

L

A

L

S

N

I

T

A

S

T

G

F

M

A

T

T

G

V

F

W

I

V

A

W

W

L

L

M

G

I

I

L

A

L

I

T

S

Q

H

V

Y

A

R

M

F

R

R

S

G

-

Y

-

V

M

L

S

Q

R

G

E

H

Q

D

V

I

A

N

Q

D

L

L

K

P

F

Y

P

R

V

S

P

G

F

F

W

F

P

P

Y

L

G

G

P

P

A

I

M

F

A

A

I

F

A

I

F

L

M

C

V

L

F

I

I

I

Y102 (= Y95) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
W106 (≠ M99) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
K163 (= K156) 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 (≠ G269) 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.

P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
31% identity, 85% coverage: 3:399/467 of query aligns to 80:489/590 of P04817

query
sites
P04817

Q

Q

A

N

Q

A

G

E

L

V

K

K

R

R

G

E

L

L

S

K

A

Q

R

R

H

H

I

I

R

G

F

M

M

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

Q

T

M

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

M

S

V

V

M

T

R

Q

A

S

L

L

G

G

E

E

M

M

A

A

V

T

H

F

N

I

P
|
P

V
|
V

A

T

G

S

S
|
S

F

F

G

T

H

V

Y

F

A

S

T

Q

T

R

Y

F

L

L

G

S

P

P

M

A

A

F

G

G

F

A

I

A

L

N

G

G

W

Y

T

M

Y
|
Y

A

W

F

F

E

S

M

W

V

A

I

I

V

T

A

F

I

A

A

L

D

E

V

L

T

S

A

V

F

V

G

G

I

Q

Y

V

M

I

G

Q

F

F

W

W

F

T

P

Y

E

K

V

V

-

P

-

L

A

A

R

A

W

W

I

I

W

S

V

I

L

F

G

W

I

V

V

I

F

I

L

T

I

I

G

-

L

M

N

N

L

L

C

F

N

P

V

V

K

K

V

Y

F

Y

G

G

E

E

M

F

E

E

F

F

W

W

L

V

S

A

L

S

L

I

K

K

V

V

G

L

A

A

I

I

V

I

A

G

M

F

I

L

L

I

-

Y

-

C

-

F

-

C

-

M

-

V

A

C

G

G

L

A

G

G

I

V

M

T

A

G

-

P

F

V

G

G

F

F

S

R

Q

Y

V

W

G

R

T

N

G

P

H

G

A

A

V

W

G

G

-

P

-

G

-

I

M

I

S

S

N

K

L

D

F

K

D

N

H

E

G

G

G

R

F

F

M

L

P

-

N

-

G

-

V

-

G

-

G

G

L

W

I

V

A

S

S

S

F

L

A

I

V

N

V

A

M

A

F

F

A

T

F

F

G

Q

G

G

I

T

E

E

I

L

I

V

G

G

V

I

T

T

A

A

G
|
G

E

E

A

A

K

A

D

N

P
|
P

Q

R

R

K

V

S

I

V

P

P

K

R

A

A

I

I

N

K

A

K

V

V

P

V

L

F

R

R

I

I

L

L

L

T

F

F

Y

Y

V

I

L

G

T

S

L

L

F

L

V

F

L

I

M

G

C

L

L

L

Y

V

P

P

W

Y

-

N

-

D

P

P

Q

K

I

L

G

T

S

Q

-

S

-
x
T

-
x
S

-
x
Y

-

V

Q

S

G

T

S

S

P

P

F

F

V

I

Q

I

I

A

F

I

S

E

N

N

L

S

G

G

I

T

G

K

S

V

A

L

A

P

A

H

V

I

L

F

N

N

V

A

V

V

V

I

I

L

S

T

A

T

A

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

L

L

A

S

Q

K

Q

N

G

K

H

L

A

A

P

P

R

K

G

F

F

L

S

S

K

R

L

T

S

T

K

K

H

G

G

G

V

V

P

P

W

Y

M

I

T

A

V

V

V

F

V

V

M

T

G

A

A

A

A

F

L

G

L

A

I

L

G

A

V

Y

L

M

L

E

N

T

Y

S

L

T

I

G

P

G

E

D

N

K

V

V

F

F

L

E

L
x
W

I

L

A

L

S

N

I

I

A

T

T

G

F

V

A

A

T

G

V
x
F

W

F

V

A

W

W

L

L

M

F

I

I

L

S

L

I

T

S

Q

H

V

I

A

R

M

F

R

M

R

Q

S

A

M

L

S

K

R

Y

E

R

Q

G

V

I

A

S

Q

R

L

D

K

E

F

L

P

P

P113 (≠ A36) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
P148 (= P70) 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 (= V71) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
S152 (= S74) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
Y173 (= Y95) 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 (= G225) 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 (vs. gap) 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 (≠ 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, 89% coverage: 2:415/467 of query aligns to 75:498/587 of Q9URZ4

query
sites
Q9URZ4

Q

E

Q

D

A

G

Q

T

G

A

L

L

K

K

R

R

G

S

L

L

S

K

A

S

R

R

H

H

I

M

R

Q

F

M

M

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

Q

A

M

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

M

F

V

I

M

V

R

Y

A

A

L

L

G

G

E

E

M

M

A

A

V

V

H

A

N

Y

P

P

V

V

A

A

G

G

S

G

F

F

G

N

H

T

Y

Y

A

A

T

T

T

R

Y

F

L

I

G

D

P

P

M

A

A

W

G

G

F

F

I

A

L

V

G

S

W

W

T

N

Y

Y

A

F

F

I

E

N

M

Y

V

F

I

V

V

T

A

F

I

P

A

L

D

E

V

L

T

T

A

T

F

C

G

A

I

I

Y

T

M

F

G

R

F

Y

W

W

F

T

P

D

-

I

E

N

V

S

A

A

R

A

W

W

I

I

W

S

V

I

L

F

G

L

I

V

V

V

F

I

L

I

I

I

G

-

L

V

N

N

L

L

C

F

N

G

V

V

K

R

V

A

F

Y

G

G

E

E

M

V

E

E

F

F

W

I

L

L

S

S

L

T

L

V

K

K

V

V

G

V

A

A

I

T

V

F

A

G

M

F

I

I

L

I

A

L

G

A

L

I

G

I

I

I

M

N

A

C

F

G

G

G

F

V

S

P

Q

T

V

D

G

H

T

R

G

G

H

Y

A

I

V

G

G

G

M

-

S

-

N

S

L

I

F

I

D

K

H

H

G

K

G

P

F

F

M

R

P

-

N

H

G

G

V

F

G

K

G

G

L

F

I

C

A

S

S

V

F

F

A

T

V

T

V

A

M

A

F

F

A

S

F

F

G

S

G

G

I

T

E

E

I

V

I

I

G

G

V

L

T

A

A

A

G

A

E

E

A

V

K

D

D

N

P

P

Q

Q

R

K

V

A

I

L

P

P

K

H

A

A

I

V

N

K

A

Q

V

V

P

F

L

W

R

R

I

I

L

A

L

I

F

F

Y

Y

V

V

L

V

T

S

L

L

F

I

V

L

-

I

-

G

L

L

M

L

C

I

L

S

Y

P

P

D

W

D

P

P

Q

N

I

L

G

M

S

G

Q

N

G

G

-

S

-

T

-

S

-

V

S

S

P

P

F

F

V

V

Q

L

I

A

F

I

S

K

N

E

L

A

G

N

I

I

G

K

S

G

A

L

A

P

A

S

V

V

L

F

N

N

V

A

V

V

V

I

I

I

S

I

A

S

A

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

L

M

A

A

Q

N

Q

L

G

K

H

Q

A

A

P

P

R

S

G

F

F

F

S

K

K

Y

L

T

S

D

K

R

H

L

G

G

V

R

P

P

W

L

M

L

T

A

V

M

V

I

V

V

M

V

G

-

A

-

L

L

I

F

G

G

V

-

L

F

N

A

Y

Y

L

I

-

N

-

E

-

A

-

D

-

K

-

N

-

G

-

N

-

D

I

V

P

S

E

D

N

T

V

V

F

F

L

N

L

W

I

L

A

L

S

A

I

L

A

S

T

G

F

L

A

S

T

N

V

F

W

F

V

T

W

W

L

G

M

S

I

I

L

C

L

L

T

C

Q

H

V

I

A

I

M

F

R

R

R

L

S

A

M

F

S

K

R

K

E

Q

-

G

-

H

Q

S

V

L

A

K

Q

E

L

L

K

G

F

F

P

V

V

S

P

P

F

M

W

G

P

I

Y

W

G

G

P

S

A

C

M

I

A

G

I

L

A

F

F

F

M

N

V

I

Sites not aligning to the query:

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

P48813 High-affinity glutamine permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 83% coverage: 2:389/467 of query aligns to 140:538/663 of P48813

query
sites
P48813

Q

Q

Q

K

A

Q

Q

E

G

N

L

L

K

K

R

K

G

S

L

I

S

K

A

P

R

R

H

H

I

T

R

V

F

M

M

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

Q

N

M

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

M

C

V

I

M

I

R

Q

A

A

L

C

G

G

E

E

M

L

A

A

V

V

-

I

H

Y

N

S

P

D

V

L

A

I

G

G

S

G

F

F

G

N

H

T

Y

Y

A

P

T

L

T

F

Y

L

L

V

G

D

P

P

M

A

A

L

G

G

F

F

I

S

L

V

G

A

W

W

T

L

Y

F

A

C

F

L

E

Q

M

W

V

L

I

C

V

V

A

C

I

P

A

L

D

E

V

L

T

V

A

T

F

A

G

S

I

M

Y

T

M

I

G

K

F

Y

W

W

F

T

P

T

E

S

V

V

A

N

R

P

W

D

I

V

W

F

V

V

L

V

G

I

I

F

V

Y

F

V

L

L

I

I

G

V

L

I

N

N

L

V

C

F

N

G

V

A

K

K

V

G

F

Y

G

A

E

E

M

A

E

D

F

F

W

F

L

F

S

N

L

C

K

K

V

I

G

L

A

M

I

I

V

V

A

G

M

F

I

F

L

I

A

L

G

A

L

I

G

I

I

I

M

D

A

C

F

G

G

G

F

-

S

-

Q

-

V

A

G

G

T

T

G

D

H

G

A

Y

V

I

G

G

M

S

S

K

N

Y

L

W

F

R

D

D

H

P

G

G

G

A

F

F

M

R

P

G

N

D

G

T

-

P

-

I

-

Q

-

R

V

F

G

K

G

G

L

V

I

V

A

A

S

T

F

F

A

V

V

T

V

A

M

A

F

F

A

A

F

F

G

G

G

M

I

S

E

E

I

Q

I

L

G

A

V

M

T

T

A

A

G

S

E

E

A

Q

K

S

D

N

P

P

Q

R

R

K

V

A

I

I

P

P

K

S

A

A

I

A

N

K

A

K

V

M

P

I

L

Y

R

R

I

I

L

L

L

F

F

V

Y

F

V

L

L

A

T

S

L

L

F

T

V

L

L

V

M

G

C

F

L

L

Y

V

P

P

W

Y

P

T

Q

S

I

D

-

Q

-

L

-

G

-

A

-

G

-

S

G

A

S

T

Q

K

G

A

S

S

P

P

F

Y

V

V

Q

I

I

A

F

V

S

S

N

S

L

H

G

G

I

V

G

R

S

V

A

V

A

P

A

H

V

F

L

I

N

N

V

A

V

V

V

I

I

L

S

L

A

S

A

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

L

L

A

A

Q

K

Q

Q

G

G

H

N

A

A

P

P

R

K

G

C

F

F

S

D

K

Y

L

I

S

D

K

R

H

E

G

G

V

R

P

P

W

A

M

A

T

A

V

M

V

L

V

V

M

S

G

A

A

L

A

F

L

G

L

V

I

I

G

A

V

F

L

C

L

A

N

S

Y

S

L

K

I

K

P

E

E

E

N

D

V

V

F

F

L

T

L

W

I

L

A

L

S

A

I

I

A

S

T

G

F

L

A

S

T

Q

V

L

W

F

V

T

W

W

L

I

M

T

I

I

L

C

L

L

T

S

Q

H

V

I

A

R

M

F

R

R

S

A

M

M

S

K

Sites not aligning to the query:

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

P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
30% identity, 85% coverage: 7:401/467 of query aligns to 86:493/602 of P19145

query
sites
P19145

L

L

K

K

R

H

G

H

L

L

S

K

A

N

R

R

H

H

I

L

R

Q

F

M

M

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

Q

R

M

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

M

A

V

M

M

V

R

M

A

A

L

L

G

G

E

E

M

L

A

A

V

V

H

I

N

F

P

P

V

I

A

S

G

G

S

G

F

F

G

T

H

T

Y

Y

A

A

T

T

T

R

Y

F

L

I

G

D

P

E

M

S

A

F

G

G

F

Y

I

A

L

N

G

N

W

F

T

N

Y

Y

A

M

F

L

E

Q

M

W

V

L

I

V

V

V

A

L

I

P

A

L

D

E

V

I

T

V

A

S

F

A

G

S

I

I

Y

T

M

V

G

N

F

F

W

W

F

G

P

T

E

D

V

P

A

K

R

Y

W

R

I

D

W

G

V

F

L

V

G

A

I

L

V

F

F

W

L

L

-

A

I

I

G

V

G

I

L

I

N

N

L

M

C

F

N

G

V

V

K

K

V

G

F

Y

G

G

E

E

M

A

E

E

F

F

W

V

L

F

S

S

L

F

L

I

K

K

V

V

G

I

A

T

I

V

V

V

A

G

M

F

I

I

L

I

A

-

G

-

L

L

G

G

I

I

M

I

A

-

F

L

G

N

F

C

S

G

Q

G

V

G

G

P

T

T

G

G

H

G

A

Y

V

I

G

G

M

G

S

K

N

Y

L

W

F

H

D

D

H

P

G

G

G

A

F

F

M

A

P

G

N

D

G

T

V

P

G

G

-

A

-

K

-

F

-

K

G

G

L

V

I

C

A

S

S

V

F

F

A

V

V

T

V

A

M

A

F

F

A

S

F

F

G
x
A

G

G

I

S

E

E

I

L

I

V

G

G

V

L

T

A

A

A

G

S

E

E

A

S

K

V

D

E

P

P

Q

R

R

K

V

S

I

V

P

P

K

K

A

A

I

A

N

K

A

Q

V

V

P

F

L

W

R

R

I

I

L

T

L

L

F

F

Y

Y

V

I

L

L

T

S

L

L

F

L

V

M

L

I

M

G

C

L

L

L

Y

V

P

P

W

Y

P

N

Q

D

-

K

-

S

-

L

-

I

-

G

-

A

-

S

I

V

G

D

S

A

Q

A

G

A

S

S

P

P

F

F

V

V

Q

I

I

A

F

I

S

K

N

T

L

H

G

G

I

I

G

K

S

G

A

L

A

P

A

S

V

V

L

V

N

N

V

V

V

I

I

L

S

I

A

A

A

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

L

L

A

A

Q

E

Q

Q

G

R

H

F

A

L

P

P

R

E

G

I

F

F

S

S

K

Y

L

V

S

D

K

R

H

K

G

G

V

R

P

P

W

L

M

V

T

G

V

I

V

A

V

V

M

T

G

S

A

A

A

F

L

G

L

L

I

I

G

A

V

F

L

V

L

A

N

A

Y

S

L

K

I

K

P

E

E

G

N

E

V

V

F

F

L

N

L

W

I

L

A

L

S

A

I

L

A

S

T

G

F

L

A

S

T

S

V

L

W

F

V

T

W

W

L

G

M

G

I

I

L

C

L

I

T

C

Q

H

V

I

A

R

M

F

R

R

R

K

S

A

M

L

S

A

R

A

E

Q

-

G

-

R

Q

G

V

L

A

D

Q

E

L

L

K

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)

Q03770 SPS-sensor component SSY1; Amino-acid permease homolog SSY1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
23% identity, 85% coverage: 7:405/467 of query aligns to 277:754/852 of Q03770

query
sites
Q03770

L

I

K

Q

R

R

G

K

L

L

S

K

A

V

R

R

H

H

I

I

R

Q

F

M

M

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

Q

S

M

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

M

A

V

T

M

M

R

L

A

S

L

F

G

T

E

E

M

L

A

S

V

T

H

L

N

I

P

P

V

V

A

S

G

S

S

G

F

F

G

S

H

G

Y

L

A

A

T

S

T

R

Y

F

L

V

G

E

P

D

M

A

A

F

G

G

F

F

I

A

L

L

G

G

W

W

T

T

Y

Y

A

W

F

I

E

S

M

C

V

M

I

L

V

A

A

L

I

P

A

A

D

Q

V

V

T

S

A

S

F

S

G
x
T

I

F

Y

Y

M

L

G

S

F

Y

W

Y

F

N

P

N

-

V

E

N

V

I

A

S

R

K

W

G

I

V

W

-

V

T

L

A

G

G

I

F

V

I

F

T

L

L

I

F

G

S

G

A

-

F

-

S

-

I

-

V

L

V

N

N

L

L

C

L

N

D

V

V

K

S

V

I

F

M

G

G

E

E

M

I

E

V

F

Y

W

V

L

A

S

G

L

I

L

S

K

K

V

V

G

I

A

I

I

A

V

I

A

L

M

M

I

V

L

F

A

T

-

M

-

I

-

L

-

N

-

A

-

G

-

H

-

G

-

N

-

D

-

I

-

H

-

E

G

G

L

V

G

G

I

F

M

R

A

Y

F

W

G

D

F

S

S

S

Q

K

V

S

G

V

T

R

G

N

H

L

A

T

V

Y

G

G

M

L

S

Y

-

R

-

P

-

T

-

F

N

D

L

L

F

A

D

D

H

A

G

G

G

E

F

G

M

S

P

K

N

K

G

G

V

I

G

S

G

G

L

P

I

K

A

G

S

R

F

F

-

L

-

A

-

T

A

A

V

S

V

V

M

M

-

L

-

I

-

S

-

T

F

F

A

A

F

F

G

S

G

G

I

V

E

E

I

M

I

T

G

F

V

L

T

A

A

S

G

G

E

E

A

A

K

I

D

N

P

P

Q

R

R

K

V

T

I

I

P

P

K

S

A

A

I

T

N

K

A

R

V

T

P

F

L

S

R

I

I

V

L

L

L

I

F

S

Y

Y

V

V

L

F

T

L

L

I

F

F

V

S

-

V

-

G

-

I

-

N

-

I

-

Y

-

S

-

G

-

D

-

P

-

R

L

L

M

L

C

S

L

Y

Y

F

P

P

-

G

-

I

-

S

-

E

-

K

-

R

-

Y

-

E

-

A

-

I

-

K

-

G

-

T

-

G

-

M

-

D

-

W

-

R

-

L

-

R

-

T

-

N

-

C

-

R

-

G

-

I

-

D

W

Y

P

R

Q

Q

I

I

G

S

-

V

-

G

-

T

S

G

Q

Y

G

S

S

S

P

P

F

W

V

V

Q

V

I

A

F

L

S

Q

N

N

L

F

G

G

I

L

G

C

S

T

A

F

A

A

A

S

V

A

L

F

N

N

V

A

V

I

V

L

I

I

S

F

A

F

A

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

L

M

A

S

Q

V

Q

Q

G

R

H

K

A

A

P

P

R

P

G

V

F

F

S

E

K

I

L

C

S

S

K

K

H

R

G

G

V

V

P

P

W

Y

M

V

T

S

V

V

V

I

V

F

M

S

G

S

A

L

A

F

L

S

L

V

I

I

G

A

-

Y

V

I

L

A

L

V

N

D

Y

Q

L

T

I

A

P

I

E

E

N

N

V

-

F

F

L

D

L

V

I

L

A

A

S

N

I

V

A

S

T

S

F

A

A

S

T

T

V

S

W

I

V

I

W

W

L

M

M

G

I

L

L

N

L

L

T

S

-

F

-

L

-

R

-

F

-

Y

Q

A

V

L

A

K

M

Q

R

R

R

K

S

D

M

I

S

I

R

S

E

R

Q

N

V

D

A

S

Q

S

L

Y

K

P

F

Y

P

K

V

S

P

P

F

F

W

Q

P

P

Y

Y

T382 (≠ G111) 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.

O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
22% identity, 90% coverage: 2:419/467 of query aligns to 3:405/438 of O34739

query
sites
O34739

Q

T

Q

E

A

D

Q

N

G

G

L

L

K

K

R

K

G

E

L

I

S

G

A

L

R

L

H

F

I

A

R

L

F

T

M

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

V

I

L

Q

A

M

Y

A

S

G

G

P

D

A

S

-

K

-

M

V

A

L

L

L

F

A

A

Y

W

L

L

I

L

G

G

A

I

A

L

V

T

F

L

M

A

V

G

M

G

R

L

A

T

L

I

G

A

E

E

M

I

A

G

V

T

H

Q

N

I

P

P

V

K

A

T

G

G

S

G

F

L

G

Y

H

T

Y

Y

A

L

T

E

Y

V

L

Y

G

G

P

E

M

F

A

W

G

G

F

F

I

L

L
x
C

G

G

W

W

T

V

Y

-

A

-

F

-

E

Q

M

I

V

I

I

I

V

Y

A

G

I

P

A

A

D

I

V

I

T

G

A

A

F

L

G

G

I

L

Y

Y

M

F

G

G

F

S

W

L

F

M

P

A

E

N

V

L

A

F

R

G

W

W

I

G

W

S

V

G

L

L

G

S

I

K

V

V

F

I

-

G

L

I

I

I

G

A

G

V

L

L

N

F

L

L

C
|
C

N

V

V

I

K

N

V

I

F

I

G

G

E

T

M

K

E

Y

-

G

F

F

W

V

L

Q

S

T

L

L

L

T

K

T

V

I

G

G

A

K

I

L

V

I

A

P

M

I

I

A

L
x
C

A

-

G

-

L

-

G

-

I

I

M

I

A

V

F

F

G

G

F

L

S

W

Q

K

V

-

G

G

T

D

G

Q

H

H

A

I

V

F

G

T

M

A

S

V

N

N

L

-

F

-

D

E

H

S

G

I

G

S

F

D

M

M

P

N

N

F

G

G

V

-

G

-

L

-

I

-

A

A

S

A

F

I

A

L

V

A

V

T

M

L

F

F

A

A

F

Y

G

D

G

G

I

W

E

I

I

L

G

A

V

A

T

L

A

G

G

G

E

E

A

M

K

K

D

N

P

P

Q

E

R

K

V

L

I

L

P

P

K

R

A

A

I

M

N

T

A

G

V

G

P

L

L

L

R

I

I

V

L

T

L

A

F

I

Y

Y

V

I

L

F

T

I

L

N

F

F

V

A

L

L

M

L

C

H

L

I

Y

L

P

S

W

A

P

N

Q

E

I

I

G

V

S

T

Q

L

G

G

S

E

P

N

F

A

V

T

Q

S

I

T

F

A

S

A

N

T

L

M

G

L

I

F

G

G

S

S

-

I

A

G

A

K

V

L

L

I

N

S

V

V

V

G

V

I

I

I

S

V

A

S

A

I

I

F

S

G

A
x
C

I

L

N

N

S

G

D

K

I

V

F

L

G

S

A

F

G

P

R

R

M

V

M

S

Y

F

G

A

L

M

A

A

Q

E

Q

R

G

K

H

Q

A

L

P

P

R

-

G

-

F

F

S

A

K

E

L

K

S

L

K

S

H

H

-

V

-

H

-

P

-

S

-

F

G

R

V

T

P

P

W

W

M

I

T

A

V

I

V

S

V

F

M

Q

G

I

A

A

A

L

L

A

L

L

I

I

G

M

V

M

L

L

L

I

N

S

Y

N

L

-

I

-

P

P

E

D

N

K

V

-

F

-

L

-

I

L

A

S

S

E

I

I

A

S

T

I

F

F

A

M

T

I

V

Y

W

I

V

F

W

Y

L

V

M

M

I

A

L

F

T

A

Q

V

V

F

A

I

M

L

R

R

R

K

S

R

M

A

S

K

R

G

E

E

Q

K

V

R

A

A

Q

-

L

-

K

-

F

Y

P

S

V

V

P

P

F

L

W

Y

P

P

Y

F

G

M

P

P

A

I

M

L

A

A

I

I

A

A

F

G

M

S

V

F

F

F

I

V

F

L

G

G

C94 (≠ L91) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
C141 (= C140) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
C168 (≠ L165) 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.

6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
23% identity, 81% coverage: 35:413/467 of query aligns to 52:420/458 of 6f34A

query
sites
6f34A

S

A

A

A

I

A

Q

E

M

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

M

F

V

A

M

A

R

L

A

C

L

Y

G

A

E

E

M

F

A

A

V

S

H

T

N

V

P

P

V

V

A

S

G

G

S

S

F

A

G

Y

H

T

Y

Y

A

S

T

Y

T

A

Y

T

L

F

G

G

P

E

M

L

A

I

G

A

F

W

I

I

L

L

G

G

W

W

T

D

Y

L

A

I

F

L

E
|
E

M
x
Y

V

G

I

V

V
x
A

A

S

I

S

A

A

D

V

V

A

T

V

A

G

F

W

-

S

G

G

I

Y

Y

F

M

Q

G

G

F

L

-

L

-

S

-

G

-

E

-

L

-

P

-

K

-

A

-

L

-

T

-

S

-

A

W

Y

F

D

P

P

E

A

V

K

A

G

R

T

W

F

I

I

W

D

V

L

L

P

G

A

I

I

V

I

F

I

L

V

I

L

G

F

G

I

L

T

N

F

L

L

C

L

N

N

V

L

K

G

V

A

F

K

G

K

E

S

M
x
A

E
x
R

F

F

W

N

L

A

S

V

L

I

L

V

K
x
A

V
x
I

G

K

A

V

I
x
A

V

V

A

V

M

L

I
x
L

L

F

A

L

G

A

L

V

G

G

I

V

-
x
W

-
x
Y

-

V

-

K

-

P

-

E

-

N

-

W

-

T

-

P

-

F

M

M

A

P

F

Y

G

G

F

F

S

S

Q

G

V

V

G

A

T

T

G

G

H

A

A

-

V

-

G

-

M

-

S

-

N

-

L

-

F

-

D

-

H

-

G

-

F

-

M

-

P

-

N

-

G

-

V

-

G

-

L

-

I

-

A

-

S

-

F

-

A

A

V

T

V

V

M

F

F
|
F

A
|
A

F

Y

G
x
I

G

G

I

F

E

D

I

A

I

V

G

S

V

T

T

A

A

A

G

E

E

E

A

V

K

R

D

N

P

P

Q

Q

R

R

V

D

I

M

P

P

K

I

A

G

I

I

N

I

A

V

V

S

P

L

L

L

R

V

I

C

L

T

L

L

F

L

Y

Y

V

I

L

A

T

V

L

S

F

L

V

V

L

L

M

T

C

G

L

I

Y

V

P

P

W

Y

P

E

Q

Q

I

L

G

N

S

V

Q

K

G

-

S

N

P

P

F

V

V

A

Q

F

I

A

F

L

S

N

N

Y

L

I

G

H

I
x
Q

G

D

S

W

A
x
V

A

A

A

G

V

F

L

I

N

S

V

L

V

G

V

A

I

I

S

A

A

G

A

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

L

I

A

S

Q

R

Q

D

G

G

H

L

A

L

P

P

R

K

G

V

F

F

S

A

K

R

L

I

S

S

-

P

K

T

H

R

G

Q

V

V

P

P

W

Y

M

V

T

N

V

T

V

W

V

L

M

T

G

G

A

A

L

V

L

A

I

V

G

-

V

-

L

-

L

F

N

A

Y

G

L

I

I

I

P

P

E

L

N

N

V

K

F

L

L

A

L

E

I

L

A

T

S

N

I

I

A

G

T

T

-

L

-

F

-

A

F

F

A

I

T

T

V

V

W

S

V

I

W

G

L

V

M

L

I

V

L

L

L

R

-

K

T

T

Q

Q

V

P

A

D

M

L

R

K

R

R

S

A

M

-

S

-

R

-

E

-

Q

-

V

-

A

-

Q

-

L

-

K

-

F

F

P

R

V

V

P

P

F

F

W

V

P

P

Y

V

G

V

P

P

A

I

M

L

A

A

I

V

A

L

F

F

binding arginine: E115 (= E98), Y116 (≠ M99), A119 (≠ V102), F228 (= F212), A229 (= A213), I231 (≠ G215), V314 (≠ A299)
binding cholesterol: W201 (vs. gap), Y202 (vs. gap)
binding : A178 (≠ M148), R179 (≠ E149), A186 (≠ K156), I187 (≠ V157), A190 (≠ I160), L194 (≠ I164), Q296 (≠ I281), V299 (≠ A284)

Sites not aligning to the query:

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

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, 68% coverage: 2:318/467 of query aligns to 23:369/629 of P30825

query
sites
P30825

Q

R

Q

E

A

E

Q

T

G

R

L

L

K

S

R

R

G

C

L

L

S

N

A

T

R

F

H

D

I

L

R

V

F

A

M

L

A

G

L

V

G

G

S

S

A

T

I

L

G

G

T

A

G

G

L

V

F

Y

-

V

Y

L

G

A

S

G

A

A

S

V

A

A

I

R

Q

E

M

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

V

S

F

V

M

L

V

A

M

G

R

L

A

C

L

Y

G

G

E

E

M

F

A

G

V

A

H

R

N

V

P

P

V

K

A

T

G

G

S

S

F

A

G

Y

H

L

Y

Y

A

S

T

Y

T

V

Y

T

L

V

G

G

P

E

M

L

A

W

G

A

F

F

I

I

L

T

G

G

W

W

T

N

Y

L

A

I

F

L

E

S

M

Y

V

I

I

I

-

G

-

T

-

S

V

V

A

A

I

R

A

A

D

W

V

S

T

A

A

T

F

F

G

D

I

E

Y

L

M

I

G

G

F

R

W

P

F

I

P

G

E

E

V

F

A

S

R

R

W

T

I

H

W

M

V

T

L

L

G

N

I

A

V

P

F

G

L

V

I

L

G

A

G

E

L

-

N

-

L

-

C

-

N

N

V

P

K

D

V

I

F

F

G

A

-

V

-

I

-

L

-

I

E

L

M

T

E

G

F

L

W

L

L

T

S

L

L

G

L

V

K

K

V

E

G

S

A

A

I

M

V

V

A

N

M

K

I

I

L

F

A

T

G

C

L

I

G

N

I

V

M

L

A

V

F

L

G

G

F

F

-

I

-

M

-

V

-

S

-

G

-

F

-

V

-

K

-

G

-

S

-

V

-

K

-

N

-

W

-

Q

-

L

S

T

Q

E

V

E

G

D

T

F

G

G

H
x
N

A

T

V

S

G

G

M

R

S

L

N

C

L

L

F

N

D

N

H

D

-

T

-

K

-

E

-

G

-

K

-

P

-

G

-

V

G

G

F

F

M

M

P

P

N

F

G

G

V

F

G

S

G

G

L

V

I

L

A

S

S

G

F

A

A

A

V

T

V

C

M

F

F

Y

A

A

F

F

G

V

G

G

I

F

E

D

I

C

I

I

G

A

V

T

T

T

A

G

G

E

E

E

A

V

K

K

D

N

P

P

Q

Q

R

K

V

A

I

I

P

P

K

V

A

G

I

I

N

V

A

A

V

S

P

L

L

L

R

I

I

C

L

F

L

I

F

A

Y

Y

V

F

L

G

T

V

L

S

F

A

V

A

L

L

M

T

C

L

L

M

Y

M

P

P

W

Y

P

F

Q

C

I

L

G

-

S

D

Q

N

G

N

S

S

P

P

F

L

V

P

Q

D

I

A

F

F

S

K

N

H

L

V

G

G

I

W

G

E

S

G

A

A

A

K

A

Y

V

A

L

V

N

A

V

V

V

G

V

S

I

L

S

C

A

A

A

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

L

M

A

A

Q

E

Q

D

G

G

N226 (≠ H182) modified: carbohydrate, N-linked (GlcNAc...) asparagine

5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
23% identity, 81% coverage: 35:413/467 of query aligns to 50:418/456 of 5oqtA

query
sites
5oqtA

S

A

A

A

I

A

Q

E

M

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

M

F

V

A

M

A

R

L

A

C

L

Y

G

A

E

E

M

F

A

A

V

S

H

T

N

V

P

P

V

V

A

S

G

G

S

S

F

A

G

Y

H

T

Y

Y

A

S

T

Y

T

A

Y

T

L

F

G

G

P

E

M

L

A

I

G

A

F

W

I

I

L

L

G

G

W

W

T

D

Y

L

A

I

F

L

E

E

M

Y

V

G

I

V

V

A

A

S

I

S

A

A

D

V

V

A

T

V

A

G

F

W

-

S

G

G

I

Y

Y

F

M

Q

G

G

F

L

-

L

-

S

-

G

-

E

-

L

-

P

-

K

-

A

-

L

-

T

-

S

-

A

W

Y

F

D

P

P

E

A

V

K

A

G

R

T

W

F

I

I

W

D

V

L

L

P

G

A

I

I

V

I

F

I

L

V

I

L

G

F

G

I

L

T

N

F

L

L

C

L

N

N

V

L

K

G

V

A

F

K

G

K

E

S

M
x
A

E
x
R

F

F

W

N

L

A

S

V

L

I

L

V

K
x
A

V

I

G

K

A

V

I
x
A

V

V

A

V

M

L

I
x
L

L

F

A

L

G

A

L

V

G

G

I

V

-

W

-

Y

-

V

-

K

-

P

-

E

-

N

-

W

-

T

-

P

-

F

M

M

A

P

F

Y

G

G

F

F

S

S

Q

G

V

V

G

A

T

T

G

G

H

A

A

-

V

-

G

-

M

-

S

-

N

-

L

-

F

-

D

-

H

-

G

-

F

-

M

-

P

-

N

-

G

-

V

-

G

-

L

-

I

-

A

-

S

-

F

-

A

A

V

T

V

V

M

F

F
|
F

A
|
A

F

Y

G
x
I

G

G

I

F

E

D

I

A

I

V

G

S

V

T

T

A

A

A

G

E

E

E

A

V

K

R

D

N

P

P

Q

Q

R

R

V

D

I

M

P

P

K

I

A

G

I

I

N

I

A

V

V

S

P

L

L

L

R

V

I

C

L

T

L

L

F

L

Y

Y

V

I

L

A

T

V

L

S

F

L

V

V

L

L

M

T

C

G

L

I

Y

V

P

P

W

Y

P

E

Q

Q

I

L

G

N

S

V

Q

K

G

-

S

N

P

P

F

V

V

A

Q

F

I

A

F

L

S

N

N

Y

L

I

G

H

I
x
Q

G

D

S

W

A
x
V

A

A

A

G

V

F

L

I

N

S

V

L

V

G

V

A

I

I

S

A

A

G

A

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

L

I

A

S

Q

R

Q

D

G

G

H

L

A

L

P

P

R

K

G

V

F

F

S

A

K

R

L

I

S

S

-

P

K

T

H

R

G

Q

V

V

P

P

W

Y

M

V

T

N

V

T

V

W

V

L

M

T

G

G

A

A

L

V

L

A

I

V

G

-

V

-

L

-

L

F

N

A

Y

G

L

I

I

I

P

P

E

L

N

N

V

K

F

L

L

A

L

E

I

L

A

T

S

N

I

I

A

G

T

T

-

L

-

F

-

A

F

F

A

I

T

T

V

V

W

S

V

I

W

G

L

V

M

L

I

V

L

L

L

R

-

K

T

T

Q

Q

V

P

A

D

M

L

R

K

R

R

S

A

M

-

S

-

R

-

E

-

Q

-

V

-

A

-

Q

-

L

-

K

-

F

F

P

R

V

V

P

P

F

F

W

V

P

P

Y

V

G

V

P

P

A

I

M

L

A

A

I

V

A

L

F

F

binding alanine: F226 (= F212), A227 (= A213), I229 (≠ G215)
binding : A176 (≠ M148), R177 (≠ E149), A184 (≠ K156), A188 (≠ I160), L192 (≠ I164), 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)
27% identity, 41% coverage: 47:238/467 of query aligns to 58:242/461 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

M

F

V

T

M

A

R

I

A

S

L

Y

G

G

E

K

M

L

A

V

V

R

H

Q

N

F

P

P

V

E

A

A

G

G

S

S

F

A

G

Y

H

T

Y

Y

A

A

T

Q

T

K

Y

S

L

I

G

N

P

P

M

H

A

V

G

G

F

F

I

M

L

V

G

G

W

W

T

S

Y

S

A

L

F

L

E

D

M
x
Y

V

L

I

F

V

L

A

P

I

M

A

I

D

N

V

V

T

L

A

L

F

A

G

K

I

I

Y

Y

M

L

G

S

F

A

W

L

F

F

P

P

E

E

V

V

A

P

R

P

W

W

I

V

W

W

V

V

L

V

G

T

I

F

V

V

F

A

L

I

I

L

G

T

G

A

L

A

N

N

L

L

C

K

N

S

V

V

K

N

V

L

F

V

G

A

E

N

M

F

E

N

F

T

W

L

L

F

S

V

L

L

L

V

K

Q

V

I

G

S

A

I

I

M

V

V

A

V

M

F

I

I

L

F

A

L

G

V

L

V

G

Q

I

G

M

L

A

H

F

K

G

G

F

-

S

E

Q

G

V

V

G

G

T

T

G

V

H

W

A

S

V

L

G

-

M

Q

S

P

N

F

L

I

F

S

D

E

H

N

G

A

G

H

F

L

M

I

P

P

N

-

G

-

V

-

G

-

L

I

I

I

A

T

S

G

F

A

A

T

V

I

V

V

M

C

F

F

A

S

F

F

G

L

G

G

I

F

E

D

I

A

I

V

G

T

V

T

T

L

A

S

G

E

E

E

A

T

K

P

D

D

P

A

Q

A

R

R

V

V

I

I

P

P

K

K

A

A

I

I

Y110 (≠ M99) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.

6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
24% identity, 94% coverage: 19:455/467 of query aligns to 12:433/433 of 6f2wA

query
sites
6f2wA

M

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

Q

G

M

A

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

M

A

V

G

M

G

R

L

A

T

L

V

G

A

E

E

M

I

A

G

V

T

H

I

N

Y

P

P

V

Q

A

T

G

G

S

G

F

M

G

M

H

I

Y

Y

A

L

T

E

T

K

Y

V

L

Y

G

G

P

R

M

W

A

L

G

G

F

F

I

L

L

V

G

G

W

W

T

A

Y

-

A

-

F

-

E

Q

M

M

V

V

I

I

V

Y

A

Y

I

P

A

A

D

N

V

I

T

A

A

A

F

L

G

A

I

I

Y

I

M

F

G

A

F

T

W

Q

F

F

P

V

E

N

V

L

A

F

R

A

W

L

-

S

-

D

-

S

-

T

-

I

-

V

-

P

I

T

W

A

V

I

L

L

G

T

I

S

V

I

F

F

L

L

I

M

G

G

G

-

L

V

N

N

L

F

C

L

N

G

V

T

K

K

V

Y

F

S

G

G

E

W

M

I

E

Q

F

T

W

L

L

A

S

T

L

I

L

L

K

K

V

L

G

I

A

P

I

L

V

V

A

V

M

I

I

I

L

V

A

A

G

G

L

L

-

L

-

Y

-

P

-

G

G

G

I

V

M

I

A

R

F

L

G

V

F

P

S

F

Q

S

V

V

G

E

T

T

G

-

H

H

A

P

V

V

G

-

M

-

S

-

N

-

L

L

F

T

D

S

H

F

G

G

G

S

F

-

M

-

P

-

N

-

G

-

V

-

G

-

G

A

L

L

I

I

A

A

S

T

F

-

A

-

V

-

M

L

F
|
F

A
|
A

F

Y

G
x
D

G

G

I

W

E

I

I

N

I

V

G

G

V

T

T

L

A

A

G

G

E

E

A

M

K

K

D

N

P

P

Q

G

R

K

V

M

I

L

P

P

K

K

A

V

I

I

N

I

A

G

V

G

P

L

L

S

R

I

I

V

L

M

L

A

F

V

Y

Y

V

L

L

L

T

T

L

N

F

I

V

A

L

Y

M

L

C

F

L

V

Y

L

P

D

W

S

P

S

Q

Q

I

L

G

A

S

G

Q

T

G

D

S

T

P

P

F

A

V

A

Q

L

I

V

F

A

S

S

N

H

L

L

G

F

I

E

G

G

S

I

A

G

A

S

A

K

V

L

L

V

N

T

V

I

V

G

V

I

I

L

S

I

A

S

A

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

L

L

A

A

Q

T

Q

Q

G

K

H

M

A

L

P

P

R

-

G

-

F

F

S

S

K

D

L

W

S

F

K

A

H

R

G

I

V

N

P

P

W

K

M

T

T

N

V

L

V

P

V

I

M

N

G

G

A

G

A

L

L

V

L

M

I

L

G

G

V

I

L

A

L

I

N

-

Y

V

L

M

I

I

P

L

E

T

N

G

V

Q

F

F

L

N

L

Q

I

L

A

T

S

D

I

L

A

I

T

V

F

F

A

V

T

-

V

-

W

-

V

I

W

W

L

F

M

F

I

I

L

T

L

L

T

T

Q

F

V

I

A

A

M

V

R

I

S

L

M

R

S

K

R

T

E

Q

Q

P

V

D

A

I

Q

E

L

R

K

P

F

Y

P

R

V

V

P

P

F

F

W

Y

P

P

Y

V

G

I

P

P

A

L

M

I

A

A

-

I

I

I

A

G

F

G

M

L

V

Y

F

I

I

I

F

F

G

N

V

T

L

L

G

I

Y

V

F

Q

P

P

D

K

T

N

Q

A

A

-

L

-

I

F

V

I

G

G

V

I

I

L

W

L

V

T

V

L

F

I

L

G

V

I

A

P

S

I

Y

Y

L

-

L

F

W

Y

C

C

K

K

P

K

R

K

A

Y

G

G

Q

S

binding alpha-aminoisobutyric acid: V17 (≠ A24), G19 (= G26), A20 (≠ T27), G21 (= G28), F199 (= F212), A200 (= A213), D202 (≠ G215)

9h76A Bacterial lat transporter basc in complex with l-ala and nb53 (see paper)
24% identity, 93% coverage: 19:454/467 of query aligns to 10:430/430 of 9h76A

query
sites
9h76A

M

V

A

V

L

V

G

G

S

T

A

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

Q

G

M

A

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

M

A

V

G

M

G

R

L

A

T

L

V

G

A

E

E

M

I

A

G

V

T

H

I

N

Y

P

P

V

Q

A

T

G

G

S

G

F

M

G

M

H

I

Y

Y

A

L

T

E

T

K

Y

V

L

Y

G

G

P

R

M

W

A

L

G

G

F

F

I

L

L

V

G

G

W

W

T

A

Y

-

A

-

F

-

E

Q

M

M

V

V

I

I

V

Y

A

Y

I

P

A

A

D

N

V

I

T

A

A

A

F

L

G

A

I

I

Y

I

M

F

G

A

F

T

W

Q

F

F

P

V

E

N

V

L

A

F

R

A

W

L

-

S

-

D

-

S

-

T

-

I

-

V

-

P

I

T

W

A

V

I

L

L

G

T

I

S

V

I

F

F

L

L

I

M

G

G

G

-

L

V

N

N

L

F

C

L

N

G

V

T

K

K

V

Y

F

S

G

G

E

W

M

I

E

Q

F

T

W

L

L

A

S

T

L

I

L

L

K

K

V

L

G

I

A

P

I

L

V

V

A

V

M

I

I

I

L

V

A

A

G

G

L

L

-

L

-

Y

-

P

-

G

G

G

I

V

M

I

A

R

F

L

G

V

F

P

S

F

Q

S

V

V

G

E

T

T

G

-

H

H

A

P

V

V

G

-

M

-

S

-

N

-

L

L

F

T

D

S

H

F

G

G

G

S

F

-

M

-

P

-

N

-

G

-

V

-

G

-

G

A

L

L

I

I

A

A

S

T

F

-

A

-

V

-

M

L

F

F

A

A

F

Y

G
x
D

G

G

I

W

E

I

I

N

I

V

G

G

V

T

T

L

A

A

G

G

E

E

A

M

K

K

D

N

P

P

Q

G

R

K

V

M

I

L

P

P

K

K

A

V

I

I

N

I

A

G

V

G

P

L

L

S

R

I

I

V

L

M

L

A

F

V

Y

Y

V

L

L

L

T

T

L

N

F

I

V

A

L

Y

M

L

C

F

L

V

Y

L

P

D

W

S

P

S

Q

Q

I

L

G

A

S

G

Q

T

G

D

S

T

P

P

F

A

V

A

Q

L

I

V

F

A

S

S

N

H

L

L

G

F

I

E

G

G

S

I

A

G

A

S

A

K

V

L

L

V

N

T

V

I

V

G

V

I

I

L

S

I

A

S

A

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

L

L

A

A

Q

T

Q

Q

G

K

H

M

A

L

P

P

R

-

G

-

F

F

S

S

K

D

L

W

S

F

K

A

H

R

G

I

V

N

P

P

W

K

M

T

T

N

V

L

V

P

V

I

M

N

G

G

A

G

A

L

L

V

L

M

I

L

G

G

V

I

L

A

L

I

N

-

Y

V

L

M

I

I

P

L

E

T

N

G

V

Q

F

F

L

N

L

Q

I

L

A

T

S

D

I

L

A

I

T

V

F

F

A

V

T

-

V

-

W

-

V

I

W

W

L

F

M

F

I

I

L

T

L

L

T

T

Q

F

V

I

A

A

M

V

R

I

S

L

M

R

S

K

R

T

E

Q

Q

P

V

D

A

I

Q

E

L

R

K

P

F

Y

P

R

V

V

P

P

F

F

W

Y

P

P

Y

V

G

I

P

P

A

L

M

I

A

A

-

I

I

I

A

G

F

G

M

L

V

Y

F

I

I

I

F

F

G

N

V

T

L

L

G

I

Y

V

F

Q

P

P

D

K

T

N

Q

A

A

-

L

-

I

F

V

I

G

G

V

I

I

L

W

L

V

T

V

L

F

I

L

G

V

I

A

P

S

I

Y

Y

L

-

L

F

W

Y

C

C

K

K

P

K

R

K

A

Y

G

G

binding alanine: G17 (= G26), A18 (≠ T27), G19 (= G28), D200 (≠ G215)

Q7YQK4 Large neutral amino acids transporter small subunit 1; 4F2 light chain; 4F2 LC; 4F2LC; L-type amino acid transporter 1; LAT1; Solute carrier family 7 member 5 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
23% identity, 54% coverage: 174:424/467 of query aligns to 211:469/503 of Q7YQK4

query
sites
Q7YQK4

G

G

F

F

S

V

Q

Q

V

I

G

G

T

K

G

G

H

-

A

-

V

-

G
|
G

M

V

S

S

N

N

L

L

F

D

D

P

H

K

G

F

G

S

F

F

M

E

P

G

N

T

G

N

-
x
W

-

D

V

V

G

G

G

N

L

I

I

V

A

L

S

A

F

L

A

Y

V

S

V

G

M

L

F

F

A

A

F

Y

G

G

I

W

E

N

I

Y

I

L

G

N

V

F

T

V

A

T

G

E

E

E

A

M

K

I

D

N

P

P

Q

Y

R

R

V

N

I

L

P

P

K

L

A

A

-

I

I

I

N

I

A

S

V

L

P

P

L

I

R

C

I

T

L

L

L

V

F

Y

Y

V

V

L

L

T

T

N

L

L

F

A

V

Y

L

F

M

T

C

T

L

L

Y

S

P

P

W

E

P

Q

Q

M

I

L

G

A

S

S

Q

E

G

A

S

-

P

-

F

V

V

A

Q

V

I

D

F

F

S

G

N

N

L

H

G

H

I

L

G

G

S

V

A

M

A

S

A

W

V

V

L

I

N

P

V

V

V

F

V

V

I

G

S

L

A

S

A
x
C

I

F

S

G

A

S

I

V

N

N

S

G

D

S

I

L

F

F

G

T

A

S

G

S

R

R

M

L

M

F

Y

F

G

V

L

G

A

S

Q

R

Q

E

G

G

H

H

A

L

P

P

R

S

G

V

F

L

S

S

K

M

L

I

S

H

K

-

H

-

G

-

V

-

P

P

W

Q

M

L

T

L

V

T

V

P

V

V

M

P

G

S

A

L

A

V

L

F

L

T

I
x
C

G

A

V

M

L

T

L

L

N

L

Y

Y

L

A

I

F

P

S

E

R

N

D

V

I

F

F

L

-

I

-

A

-

S

S

I

V

A

I

T

N

F

F

A

F

T

S

V

F

W

F

V

N

W

W

L

L

M
x
C

I

V

L

A

L

L

T

A

Q

I

V

I

A

G

M

M

-

M

-

W

-

L

-

R

-

Y

-

K

R

K

R

P

S

E

M

L

S

E

R

R

E

P

Q

I

V

K

A

V

Q

N

L

L

K

A

F

L

P

P

-

V

-

F

-

I

-

L

-

A

-
x
C

-

L

-

F

-

L

-

I

-

A

V

V

P

S

F

F

W

W

P

K

Y

T

G

P

P

V

A

E

M
x
C

A

G

I

I

A

G

F

F

M

T

V

I

F

I

I

L

F

S

G

G

V

L

L

P

G

V

Y

Y

F

F

G219 (= G185) mutation to D: Decreased KM and Vmax for Trp. Increased KM and Vmax for Phe; when associated with L-234.
W234 (vs. gap) mutation to L: Decreased KM and Vmax for Trp. Increased KM but decreased Vmax for Phe. Increased KM and Vmax for Phe; when associated with D-219.
C331 (≠ A296) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
C377 (≠ I346) mutation to S: No significant effect on inhibition by HgCl(2).
C403 (≠ M376) mutation to S: No significant effect on inhibition by HgCl(2).
C439 (vs. gap) mutation to S: Prevents insertion into the plasma membrane and possibly protein folding.
C454 (≠ M409) mutation to S: No significant effect on inhibition by HgCl(2). Slightly increased KM but slightly decreased Vmax for Phe.

Sites not aligning to the query:

88 C→S: No significant effect on inhibition by HgCl(2). Decreased KM and Vmax for Phe. Similar affect on KM and Vmax for Phe; when associated with S-183.
98 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe. Slightly less decreased KM and Vmax for Phe; when associated with S-183.
160 C→S: No change to KM or Vmax for Phe.
172 C→S: No change to KM or Vmax for Phe.
174 C→S: No change to KM or Vmax for Phe.
183 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe. Similar affect on KM and Vmax for Phe; when associated with S-88. Slightly less decreased KM and Vmax for Phe; when associated with S-98.
492 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe.

5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
24% identity, 71% coverage: 16:346/467 of query aligns to 11:332/437 of 5j4nA

query
sites
5j4nA

I

V

R

T

F

L

M

M

A

V

L

S

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

Q

S

M

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

M

M

V

V

M

Y

R

-

A

-

L

-

G

A

E

K

M

M

A

S

V

F

H

L

N

D

P

P

V

S

A

P

G

G

S

G

F

S

G

Y

H

A

Y

Y

A

A

T

R

Y

C

L

F

G

G

P

P

M

F

A

L

G

G

F

Y

I

Q

L

T

G

N

W

V

T

L

Y

Y

A

W

F

L

E
x
A

M
x
C

V

W

I

I

V
x
G

A
x
N

I

I

A

A

D
x
M

V

V

T

V

A

I

F

G

G

V

I

G

Y

Y

M

L

G

S

F

Y

W

F

F

F

P

P

-

I

-

L

-

K

-

D

-

P

-

L

-

V

-

L

-

T

-

I

-

T

-

C

E

V

V

V

A

V

R

L

W

W

I

I

W

F

V

V

L

L

G

-

I

-

V

-

F

-

L

-

I

-

G

-

L

L

N

N

L

I

C

V

N

G

V

P

K

K

V

M

F

I

G

T

E

R

M

V

E

Q

F

A

W

V

L

A

S

T

L

V

L

L

K

A

V

L

G

I

A

P

I

I

V

V

A

-

M

-

I

-

L

-

A

-

G

-

L

-

G

G

I

I

M

A

A

V

F

F

G

G

F

W

S

F

Q

W

V

F

G

R

T

G

G

E

H

T

A

Y

V

M

G

A

M

A

S

W

N

N

L

V

F

S

D

G

H

L

G

G

G

T

F

F

M

-

P

-

N

-

G

-

V

-

G

G

G

A

L

I

I

Q

A

S

S

T

F

L

A

N

V

V

V

T

M

L

F

W

A

S

F

F

G

I

G

G

I

V

E

E

I

S

I

A

G

S

V

V

T

A

A

A

G

G

E

V

A

V

K

K

D

N

P

P

Q

K

R

R

V

N

I

V

P

P

K

I

A

A

I

T

N

I

A

G

V

G

P

V

L

L

R

I

I

A

L

A

L

V

F

C

Y

Y

V

V

L

L

T

S

L

T

F

T

V

A

L

I

M

M

C

G

L

M

Y

I

P

P

W

N

P

A

Q

A

I

L

G

R

S

V

Q

S

G

A

S

S

P

P

F

F

V

G

Q

D

I

A

F

-

S

A

N

R

L

M

G

A

I

L

G

G

-

D

S

T

A

A

A

G

A

A

V

I

L

V

N

S

V

F

V

C

V

A

I

A

S

A

A

G

A

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

L

A

A

A

Q

D

G

G

H

L

A

F

P

P

R

P

G

I

F

F

S

A

K

R

L

V

S

N

K

K

H

A

G

G

V

T

P

P

W

V

M

A

T

G

V

L

V

I

M

V

G

G

A

I

A

L

L

M

L

T

I

I

binding agmatine: I19 (≠ A24), A92 (≠ E98), C93 (≠ M99), G96 (≠ V102), N97 (≠ A103), M100 (≠ D106), W289 (≠ D303)

P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
24% identity, 74% coverage: 2:346/467 of query aligns to 3:336/445 of P60061

query
sites
P60061

Q

S

Q

D

A

A

Q

D

G

A

L

H

K

K

R

V

G

G

L

L

S

-

A

-

R

I

H

P

I

V

R

T

F

L

M

M

A

V

L

S

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

Q

S

M

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

M

M

V

V

M

Y

R

-

A

-

L

-

G

A

E

K

M

M

A

S

V

F

H

L

N

D

P

P

V

S

A

P

G

G

S

G

F

S

G

Y

H

A

Y

Y

A

A

T

R

Y

C

L

F

G

G

P

P

M

F

A

L

G

G

F

Y

I

Q

L

T

G

N

W

V

T

L

Y
|
Y

A

W

F

L

E
x
A

M
x
C

V

W

I

I

V

G

A
x
N

I

I

A

A

D
x
M

V

V

T

V

A

I

F

G

G

V

I

G

Y

Y

M

L

G

S

F

Y

W

F

F

F

P

P

-

I

-

L

-

K

-

D

-

P

-

L

-

V

-

L

-

T

-

I

-

T

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C

E

V

V

V

A

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R

L

W

W

I

I

W

F

V

V

L

L

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L

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K

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I23 (≠ A24) binding agmatine; binding L-arginine
S26 (≠ T27) binding L-arginine
Y93 (= Y95) mutation to L: Greatly decreased Arg uptake into liposomes.
A96 (≠ E98) binding agmatine; binding L-arginine
C97 (≠ M99) binding agmatine
N101 (≠ A103) 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 (≠ D106) binding agmatine; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
W202 (≠ F212) binding L-arginine; mutation to L: Halves Arg uptake into liposomes.
S203 (≠ A213) binding agmatine
I205 (≠ G215) binding agmatine; binding L-arginine; mutation to A: About wild-type affinity for Arg and Agm.
W293 (≠ D303) 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.

Sites not aligning to the query:

357 binding L-arginine; S→A: 20% decreased affinity for Arg, 40% decrease affinity for Agm.

Query Sequence

>PP_5031 FitnessBrowser__Putida:PP_5031
MQQAQGLKRGLSARHIRFMALGSAIGTGLFYGSASAIQMAGPAVLLAYLIGGAAVFMVMR
ALGEMAVHNPVAGSFGHYATTYLGPMAGFILGWTYAFEMVIVAIADVTAFGIYMGFWFPE
VARWIWVLGIVFLIGGLNLCNVKVFGEMEFWLSLLKVGAIVAMILAGLGIMAFGFSQVGT
GHAVGMSNLFDHGGFMPNGVGGLIASFAVVMFAFGGIEIIGVTAGEAKDPQRVIPKAINA
VPLRILLFYVLTLFVLMCLYPWPQIGSQGSPFVQIFSNLGIGSAAAVLNVVVISAAISAI
NSDIFGAGRMMYGLAQQGHAPRGFSKLSKHGVPWMTVVVMGAALLIGVLLNYLIPENVFL
LIASIATFATVWVWLMILLTQVAMRRSMSREQVAQLKFPVPFWPYGPAMAIAFMVFIFGV
LGYFPDTQAALIVGVIWVVFLVASYLLWCKPRAGQGQPVAEPAELHR

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