SitesBLAST

R26 (= R13) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
P54 (= P41) 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 (= F74) mutation to L: No effect on phenylalanine transport activity.
F90 (≠ L77) mutation to L: 65% of wild-type phenylalanine transport activity.
Y92 (≠ H79) mutation to L: 41% of wild-type phenylalanine transport activity.
Y94 (= Y81) mutation to L: 69% of wild-type phenylalanine transport activity.
W95 (≠ L82) mutation to L: 10% of wild-type phenylalanine transport activity.
F98 (≠ R85) mutation to L: No effect on phenylalanine transport activity.
F101 (= F88) mutation to L: 38% of wild-type phenylalanine transport activity.
W105 (= W92) mutation to L: 39% of wild-type phenylalanine transport activity.
Y107 (= Y94) mutation to L: No effect on phenylalanine transport activity.
W108 (= W95) mutation to L: 71% of wild-type phenylalanine transport activity.
F111 (≠ W98) 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 (≠ D105) mutation E->G,L,V,N: Loss of activity.
K168 (= K155) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
E226 (= E216) mutation E->A,Q,K,R,W: Loss of activity.
R252 (= R242) mutation R->D,E,F,W,P: Loss of activity.
P341 (= P331) 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 (= P431) 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)
41% identity, 99% coverage: 4:448/448 of query aligns to 9:449/457 of P15993

query
sites
P15993

E

E

K

Q

L

L

E

K

R

R

G

G

L

L

S

K

N

N

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R

H

H

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Q

L

L

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S

A

I

L

G

G

A

A

I

I

G

G

T

T

G

G

L

L

F

F

L

L

A

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S

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A

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R

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G

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Y

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W
x
Y

I

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A

A

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M

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L

L

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T

A

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N

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N

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Y103 (≠ W98) 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%.

Q88CZ8 L-histidine transporter HutT from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
42% identity, 98% coverage: 4:441/448 of query aligns to 5:445/467 of Q88CZ8

query
sites
Q88CZ8

E

Q

K

G

L

L

E

K

R

R

G

G

L

L

S

S

N

A

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R

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T

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A

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x
E

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G

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L

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K

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A

A

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E

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-

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Y

Y

T27 (= T26) mutation T->A,S: Retains 60% of wild-type activity.; mutation to N: Retains 20% of wild-type activity.
E98 (≠ C97) mutation to A: Retains 80% of wild-type activity.
K156 (= K155) mutation K->A,Q: Retains less than 10% of wild-type activity.; mutation to R: Retains 40% of wild-type activity.
F212 (= F210) mutation F->A,Q: Loss of activity.; mutation to Y: No change in activity.
E218 (= E216) mutation E->A,Q: Loss of activity.; mutation to D: Retains 70% of wild-type activity.

P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
37% identity, 100% coverage: 2:448/448 of query aligns to 4:454/469 of P46349

query
sites
P46349

S

S

Q

Q

E

S

K

G

L

L

E

K

R

K

G

E

L

L

S

K

N

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R

R

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M

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M

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A

G

G

A

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A

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F

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A
x
G

S

S

G

G

K

S

S

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I

I

A

H

I

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A

T

G
|
G

P

P

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G

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A

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M

A

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A

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G

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M

R

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M

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G

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A

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N

N

L

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D

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C

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Y

A

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A

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A

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N

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K

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A

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N

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K

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N

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N

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N

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A
x
G

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T

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M

L

L

Y

Y

G

S

L

L

A

A

K

E

D

R

D

N

N

E

A

A

P

P

K

R

T

R

F

F

A

M

K

K

L

L

N

S

K

K

N

K

S

G

T

V

P

P

A

V

M

Q

A

A

L

I

L

V

M

A

S
x
G

S

T

V

F

V
x
F

V

S

G

Y

I

I

T

A

I

V

V

V

L

M

N

N

Y

Y

V

F

M

S

P

P

E

D

G

T

V

V

F

F

S

L

L

F

I

L

S

V

G

N

I

S

S

S

T

G

V

A

C

I

F

A

L

L

F

L

I

V

W

Y

T

L

I

V

I

I

V

A

I

V

C

S

H

Q

M

L

K

K

F

M

L

R

K

K

Q

K

T

L

K

E

D

K

E

T

D

N

R

P

P

E

K

A

F

L

R

K

L

I

K

K

G

M

-

W

-

L

A

F

K

P

V

F

I

L

N

T

I

Y

L

L

S

T

L

I

I

I

F

A

L

I

A

C

L
x
G

I

I

I

L

V

V

I

S

C

M

A

A

V

F

L

I

E

D

S

S

T

M

R

R

I

D

A

E

L

L

F

L

-

L

-

T

-

G

-

V

I

I

T

T

P

G

I

I

W

V

F

L

I

I

A

S

L

Y

L

L

I

V

I

F

Y

R

Q

K

V

R

K

K

F

V

K

S

E

E

Q

K

G33 (≠ A31) mutation to D: Lack of activity.
G42 (= G40) mutation to S: Lack of activity.
G301 (≠ A301) mutation to V: Lack of activity.
G338 (≠ S338) mutation to E: Lack of activity.
F341 (≠ V341) mutation to S: Lack of activity.
G414 (≠ L412) 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)
37% identity, 87% coverage: 6:395/448 of query aligns to 13:413/489 of P25737

query
sites
P25737

L

L

E

R

R

R

G

E

L

L

S

K

N

A

R

R

H

H

V

L

Q

T

L

M

I

I

S

A

I

I

G

G

A

S

I

I

G

G

T

T

G

G

L

L

F

F

L

V

A

A

S

S

G

G

K

A

S

T

I

I

A

S

I

Q

A

A

G

G

P

P

S

G

-

G

V

A

L

L

A

S

Y

Y

M

M

I

L

V

I

G

G

M

L

F

M

V

V

F

Y

F

F

I

L

M

M

R

T

S

S

L

L

G

G

E

E

L

L

L

A

A

Y

N

M

L

P

D

V

C

S

H

G

S

S

F

F

V

A

E

T

L

Y

A

G

H

Q

Q

N

Y

Y

L

V

G

E

R

E

R

G

W

F

A

G

F

F

V

A

T

L

G

G

W

W

T

N

Y
|
Y

W

W

F

Y

C

N

W
|
W

I

A

T

V

V

T

A

I

M

A

S

V

D

D

L

L

T

V

A

A

V

A

G

Q

M

L

Y

V

M

M

R

S

Y

W

W

W

F

F

P

P

H

D

L

T

P

P

Q

G

W

W

I

I

P

W

A

S

L

A

L

L

M

F

L

L

L

G

F

V

L

I

M

F

A

L

L

L

N

N

L

Y

L

I

S

S

V

V

K

R

L

G

F

F

G

G

E

E

I

A

E

E

F

Y

W

W

L

F

A

S

L

L

I

I

K
|
K

I

V

L

T

A

T

I

V

V

I

A

V

L

F

I

I

G

I

V

V

G

G

L

V

Y

L

M

M

I

I

F

I

T

G

H

I

H

F

K

K

L

-

E

-

N

G

G

A

I

Q

V

P

A

A

S

G

F

W

A

S

N

N

L

W

Y

T

Q

I

D

G

G

E

G

A

F

P

F

F

P

A

H

G

G

G

F

F

S

A

G

A

F

M

I

I

L

G

S

V

F

A

Q

M

L

I

A

V

V

G

F
|
F

S

S

F

F

T

Q

G

G

V

T

E
|
E

L

L

V

I

G

G

L

I

T

A

A

A

G

G

E
|
E

T

S

Q

E

D

D

P

P

E

A

K

K

T

N

L

I

P

P

K

R

A

A

I

V

N

R

N

Q

I

V

P

F

V

W

R

R

I

I

L

L

F

F

Y

Y

V

V

G

F

S

A

L

I

A

L

V

I

I

I

M

S

A

L

V

I

Q

I

P

P

W

Y

-

T

-

D

-

P

-

S

-

L

-

R

-

N

N
x
D

I

V

I

K

D
|
D

P

I

T

S

Q

V

S

S

P

P

F

F

V

T

T

L

V

V

F

F

S

Q

S

H

I

A

G

G

I

L

A

L

A

S

A

A

S

A

I

V

I

M

N

N

F

A

V

V

V

I

L

L

S

T

S

A

A

V

A

L

S

S

A

A

C

G

N

N

S

S

A

G

L

M

F

Y

S

A

T

S

S

T

R

R

M

M

L

L

Y

Y

G

T

L

L

A

A

K

C

D

D

D

G

N

K

A

A

P

P

K

R

T

I

F

F

A

A

K

K

L

L

N

S

K

R

N

G

S

G

T

V

P

P

A

R

M

N

A

A

L

L

L

Y

M

A

S

T

V

V

V

I

V

A

G

G

I

L

T

C

I

F

V

L

L

T

N

S

Y

M

V

F

M

G

P

N

E

Q

G

T

V

V

F

Y

S

L

L

W

I

L

S

L

G

N

I

T

S

S

T

G

V

M

C

T

F

G

L

F

F

I

I

A

W

W

T

L

I

G

I

I

V

A

I

I

C

S

H

H

M

Y

K

R

F

F

L

R

K

R

-

G

-

Y

-

V

-

L

Q

Q

T

G

K

H

D

D

E

I

D

N

R

D

P

L

K

P

F

Y

R

R

Y102 (= Y94) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
W106 (= W98) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
K163 (= K155) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
F216 (= F210) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
E222 (= E216) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
E230 (= E224) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
D275 (≠ N261) 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 (= D264) 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)
30% identity, 100% coverage: 1:446/448 of query aligns to 79:549/590 of P04817

query
sites
P04817

M

V

S

Q

Q

N

E

A

K

E

L

V

E

K

R

R

G

E

L

L

S

K

N

Q

R

R

H

H

V

I

Q

G

L

M

I

I

S

A

I

L

G

G

A

T

I

I

G

G

T

T

G

G

L

L

F

F

L

I

A

G

S

L

G

S

K

T

S
x
P

I

L

A

T

I

N

A

A

G

G

P

P

-

V

S

G

V

A

L

L

L

I

A

S

Y

Y

M

L

I

F

V

M

G

G

M

S

F

L

V

A

F

Y

F

S

I

V

M

T

R

Q

S

S

L

L

G

G

E

E

L

M

L

A

L

T

A

F

N

I

L
x
P

D
x
V

C

T

H

S

S
|
S

F

F

V

T

E

V

L

F

A

S

H

Q

Q

R

Y

F

L

L

G

S

R

P

R

A

W

F

A

G

F

A

V

A

T

N

G

G

W

Y

T

M

Y
|
Y

W

W

F

F

C

S

W

W

I

A

T

I

V

T

A

F

M

A

S

L

D

E

L

L

T

S

A

V

V

V

G

G

M

Q

Y

V

M

I

R

Q

Y

F

W

W

F

T

P

Y

H

K

L

V

P

P

-

L

-

A

Q

A

W

W

I

I

P

S

A

I

L

F

L

W

M

V

L

I

F

T

L

I

M

M

A

-

L

-

N

N

L

L

L

F

S

P

V

V

K

K

L

Y

F

Y

G

G

E

E

I

F

E

E

F

F

W

W

L

V

A

A

L

S

I

I

K

K

I

V

L

L

A

A

I

I

V

I

A

G

L

F

I

L

-

I

-

Y

-

C

-

F

-

C

-

M

-

V

-

C

G

G

V

A

G

G

L

V

Y

T

M

G

I

P

F

V

T

G

H

F

H

R

K

Y

L

W

E

R

N

N

-

P

-

G

-

A

-

W

-

G

-

P

G

G

I

I

V

I

A

S

S

K

F

D

A

K

N

N

L

-

Y

-

Q

-

D

E

G

G

G

R

F

F

F

L

P

-

H

-

G

-

F

-

S

-

G

G

F

W

I

V

L

S

S

S

F

L

Q

I

L

N

A

A

V

A

F

F

S

T

F

F

T

Q

G

G

V

T

E

E

L

L

V

V

G

G

L

I

T

T

A

A

G
|
G

E

E

T

A

Q

A

D

N

P
|
P

E

R

K

K

T

S

L

V

P

P

K

R

A

A

I

I

N

K

I

V

P

V

V

F

R

R

I

I

L

L

L

T

F

F

Y

Y

V

I

G

G

S

S

L

L

A

L

V

F

I

I

M

G

A

L

V

L

Q

V

P

P

W

Y

N

N

I

D

I

P

D

K

P

L

T

T

Q

Q

S

S

-
x
T

-
x
S

-
x
Y

-

V

-

S

-

T

-

S

P

P

F

F

V

I

T

I

V

A

F

I

S

E

S

N

I

S

G

G

I

T

A

K

A

V

A

L

A

P

S

H

I

I

I

F

N

N

F

A

V

V

V

I

L

L

S

T

A

I

S

S

A

A

C

A

N

N

S

S

A

N

L

I

F

Y

S

V

T

G

S

S

R

R

M

I

L

L

Y

F

G

G

L

L

A

S

K

K

D

N

D

K

N

L

A

A

P

P

K

K

T

F

F

L

A

S

K

R

L

T

N

T

K

K

N

G

S

G

T

V

P

P

A

Y

M

I

A

A

L

V

L

F

M

V

S

T

S

A

V

A

V

F

V

G

G

A

I

L

T

A

I

Y

V

M

L

E

N

T

Y

S

V

T

M

G

P

G

E

D

G

K

V

V

F

F

S

E

L
x
W

I

L

S

L

G

N

I

I

S

T

T

G

V

V

C

A

F

G

L
x
F

F

F

I

A

W

W

T

L

I

F

I

I

V

S

I

I

C

S

H

H

M

I

K

R

F

F

L

M

K

Q

Q

A

T

L

K

K

-

Y

-

R

-

G

-

I

D

S

E

R

D

D

R

E

P

L

K

P

F

F

R

K

L

A

K

K

G

L

A

M

K

P

V

G

I

L

N

A

I

Y

L

Y

S

A

L

A

I

T

F

F

L

M

A

T

L

I

I

I

V

I

I

I

C

Q

A

G

V

F

L

T

E

A

-

F

-

A

-

P

-

K

-

F

-

N

-

G

S

V

T

S

R

F

I

A

A

A

L

A

F

Y

I

I

T

S

P

I

I

F

W

L

F

F

I

L

A

A

L

V

L

W

I

I

I

L

Y

F

Q

Q

V

C

K

I

F

F

K

R

P113 (≠ S35) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
P148 (≠ L69) 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 (≠ D70) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
S152 (= S73) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
Y173 (= Y94) 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 (= G223) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
P313 (= P228) 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 (≠ L359) 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 (≠ L369) 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)
32% identity, 84% coverage: 6:382/448 of query aligns to 80:465/587 of Q9URZ4

query
sites
Q9URZ4

L

L

E

K

R

R

G

S

L

L

S

K

N

S

R

R

H

H

V

M

Q

Q

L

M

I

I

S

S

I

I

G

G

A

A

I

I

G

G

T

T

G

G

L

L

F

Y

L

V

A

G

S

S

G

G

K

S

S

S

I

L

A

A

I

D

A

G

G

G

P

P

-

A

S

S

V

V

L

I

A

N

Y

Y

M

S

I

L

V

I

G

G

M

I

F

M

V

M

F

F

I

I

M

V

R

Y

S

A

L

L

G

G

E

E

L

M

L

A

L

V

A

A

N

Y

L

P

D

V

C

A

H

G

S

G

F

F

V

N

E

T

L

Y

A

A

H

T

Q

R

Y

F

L

I

G

D

R

P

R

A

W

W

A

G

F

F

V

A

T

V

G

S

W

W

T

N

Y

Y

W

F

F

I

C

N

W

Y

I

F

T

V

V

T

A

F

M

P

S

L

D

E

L

L

T

T

A

T

V

C

G

A

M

I

Y

T

M

F

R

R

Y

Y

W

W

F

T

P

D

-

I

H

N

L

S

P

A

Q

A

W

W

I

I

P

S

A

I

L

F

L

L

M

V

L

V

L

I

F

I

L

I

M

-

A

-

L

V

N

N

L

L

L

F

S

G

V

V

K

R

L

A

F

Y

G

G

E

E

I

V

E

E

F

F

W

I

L

L

A

S

L

T

I

V

K

K

I

V

L

V

A

A

I

T

V

F

A

G

L

F

I

I

G

I

V

L

G

A

L

I

Y

I

M

I

-

N

-

C

-

G

I

V

F

P

T

T

H

D

H

H

K

R

L

-

E

-

N

-

G

G

I

Y

V

I

A

G

S

G

F

S

A

I

N

I

L

K

Y

H

Q

K

D

P

G

-

F

-

F

F

P

R

H

H

G

G

F

F

S

K

G

G

F

F

I

C

L

S

S

V

F

F

Q

T

L

T

A

A

V

A

F

F

S

S

F

F

T

S

G

G

V

T

E

E

L

V

V

I

G

G

L

L

T

A

A

A

G

A

E

E

T

V

Q

D

D

N

P

P

E

Q

K

K

T

A

L

L

P

P

K

H

A

A

I

V

N

K

N

Q

I

V

P

F

V

W

R

R

I

I

L

A

L

I

F

F

Y

Y

V

V

G

V

S

S

L

L

A

I

V

L

I

I

-

G

M

L

A

L

V

I

Q

S

P

P

W

-

N

-

I

-

I

D

D

D

P

P

-

N

-

L

-

M

-

G

-

N

-

G

-

S

-

T

T

S

Q

V

S

S

P

P

F

F

V

V

T

L

V

A

F

I

S

K

S

E

I

A

G

N

I

I

A

K

A

G

A

L

A

P

S

S

I

V

I

F

N

N

F

A

V

V

V

I

L

I

S

I

S

S

A

V

S

S

A

V

C

T

N

N

S

S

A

S

L

T

F

Y

S

T

T

A

S

G

R

R

M

T

L

L

Y

H

G

G

L

M

A

A

K

N

D

L

D

K

N

Q

A

A

P

P

K

S

T

F

F

F

A

K

K

Y

L

T

N

D

K

R

N

L

S

G

T

R

P

P

A

L

M

L

A

A

L

M

L

I

M

V

S

-

S

V

V

L

V

F

G

G

I

F

T

F

I

A

V

Y

L

I

N

N

Y

E

V

A

M

D

P

K

E

N

G

G

-

N

-

D

-

V

-

S

-

D

-

T

V

V

F

F

S

N

L

W

I

L

S

L

G

A

I

L

S

S

T

G

V

L

C

S

F

N

L

F

F

F

I

T

W

W

T

G

I

S

I

I

V

C

I

L

C

C

H

H

M

I

K

I

F

F

Sites not aligning to the query:

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

P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
30% identity, 87% coverage: 2:391/448 of query aligns to 82:483/602 of P19145

query
sites
P19145

S

A

Q

Q

E

T

K

P

L

L

E

K

R

H

G

H

L

L

S

K

N

N

R

R

H

H

V

L

Q

Q

L

M

I

I

S

A

I

I

G

G

A

A

I

I

G

G

T

T

G

G

L

L

F

L

L

V

A

G

S

S

G

G

K

T

S

A

I

L

A

R

I

T

A

G

G

G

P

P

-

A

S

S

V

L

L

L

L

I

A

G

Y

W

M

G

I

S

V

T

G

G

M

T

F

M

V

I

F

Y

F

A

I

M

M

V

R

M

S

A

L

L

G

G

E

E

L

L

L

A

L

V

A

I

N

F

L

P

D

I

C

S

H

G

S

G

F

F

V

T

E

T

L

Y

A

A

H

T

Q

R

Y

F

L

I

G

D

R

E

R

S

W

F

A

G

F

Y

V

A

T

N

G

N

W

F

T

N

Y

Y

W

M

F

L

C

Q

W

W

I

L

T

V

V

V

A

L

M

P

S

L

D

E

L

I

T

V

A

S

V

A

G

S

M

I

Y

T

M

V

R

N

Y

F

W

W

F

G

P

T

H

D

L

-

P

P

Q

K

W

Y

I

R

P

D

A

G

L

F

L

V

M

A

L

L

L

F

F

W

L

L

-

A

-

I

M

V

A

I

L

I

N

N

L

M

L

F

S

G

V

V

K

K

L

G

F

Y

G

G

E

E

I

A

E

E

F

F

W

V

L

F

A

S

L

F

I

I

K

K

I

V

L

I

A

T

I

V

V

V

A

G

L

F

I

I

G

I

V

L

G

G

L

I

Y

I

M

L

I

-

F

-

T

-

H

N

H

C

K

G

L

G

E

G

N

P

G

T

I

G

V

G

A

Y

S

I

F

G

A

G

N

K

L

Y

Y

W

Q

H

D

D

G

P

G

G

F

A

F

F

P

A

H

G

G

D

-

T

-

P

-

G

-

A

-

K

F

F

S

K

G

G

F

V

I

C

L

S

S

V

F

F

Q

V

L

T

A

A

V

A

F

F

S

S

F

F

T
x
A

G

G

V

S

E

E

L

L

V

V

G

G

L

L

T

A

A

A

G

S

E

E

T

S

Q

V

D

E

P

P

E

R

K

K

T

S

L

V

P

P

K

K

A

A

I

A

N

K

N

Q

I

V

P

F

V

W

R

R

I

I

L

T

L

L

F

F

Y

Y

V

I

G

L

S

S

L

L

A

L

V

M

I

I

M

G

A

L

V

L

Q

V

P

P

W

Y

N

N

I

D

-

K

-

S

-

L

-

I

-

G

-

A

-

S

I

V

D

D

P

A

T

A

Q

A

S

S

P

P

F

F

V

V

T

I

V

A

F

I

S

K

S

T

I

H

G

G

I

I

A

K

A

G

A

L

A

P

S

S

I

V

N

N

F

V

V

V

V

I

L

L

S

I

S

A

A

V

A

L

S

S

A

V

C

G

N

N

S

S

A

A

L

I

F

Y

S

A

T

C

S

S

R

R

M

T

L

M

Y

V

G

A

L

L

A

A

K

E

D

Q

D

R

N

F

A

L

P

P

K

E

T

I

F

F

A

S

K

Y

L

V

N

D

K

R

N

K

S

G

T

R

P

P

A

L

M

V

A

G

L

I

L

A

M

V

S

T

S

S

V

A

V

F

V

G

G

L

I

I

T

A

I

F

V

V

L

A

N

A

Y

S

V

K

M

K

P

E

E

G

G

E

V

V

F

F

S

N

L

W

I

L

S

L

G

A

I

L

S

S

T

G

V

L

C

S

F

S

L

L

F

F

I

T

W

W

T

G

I

G

I

I

V

C

I

I

C

C

H

H

M

I

K

R

F

F

L

R

K

K

Q

A

T

L

K

A

D

A

E

Q

D

G

R

R

A297 (≠ T213) 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)
28% identity, 87% coverage: 1:391/448 of query aligns to 140:542/663 of P48813

query
sites
P48813

M

Q

S

K

Q

Q

E

E

K

N

L

L

E

K

R

K

G

S

L

I

S

K

N

P

R

R

H

H

V

T

Q

V

L

M

I

M

S

S

I

L

G

G

G

T

A

G

I

I

G

G

T

T

G

G

L

L

F

L

L

V

A

G

S

N

G

S

K

K

S

V

I

L

A

N

I

N

A

A

G

G

P

P

S

G

-

G

V

L

L

I

A

G

Y

Y

M

A

I

I

V

M

G

G

M

S

F

C

V

V

F

Y

F

C

I

I

M

I

R

Q

S

A

L

C

G

G

E

E

L

L

-

A

-

V

-

I

-

Y

-

S

-

D

L

L

L

I

A

G

N

G

L

F

D

N

C

T

H

Y

S

P

F

L

V

F

E

-

L

L

A

V

H

D

Q

P

Y

A

L

L

G

G

R

-

W

-

A

-

F

F

V

S

T

V

G

A

W

W

T

L

Y

F

W

C

F

L

C

Q

W

W

I

L

T

C

V

V

A

C

M

P

S

L

D

E

L

L

T

V

A

T

V

A

G

S

M

M

Y

T

M

I

R

K

Y

Y

W

W

F

T

P

T

H

S

L

V

P

N

Q

P

W

D

I

V

P

F

A

V

L

V

L

I

M

F

L

Y

L

V

F

L

L

I

M

V

A

V

L

I

N

N

L

V

L

F

S

G

V

A

K

K

L

G

F

Y

G

A

E

E

I

A

E

D

F

F

W

F

L

F

A

N

L

C

I

C

K

K

I

I

L

L

A

M

I

I

V

V

A

G

L

F

I

F

G

I

V

L

G

A

L

I

Y

-

M

I

I

I

F

D

T

C

H

G

K

A

L

G

E

T

N

D

G

G

I

Y

V

I

A

G

S

S

F

-

A

-

N

K

L

Y

Y

W

Q

R

D

D

G

P

G

G

F

A

F

F

P

R

-

G

-

D

-

T

-

P

-

I

H

Q

G

R

F

F

S

K

G

G

F

V

I

V

L

A

S

T

F

F

Q

V

L

T

A

A

V

A

F

F

S

A

F

F

T

G

G

M

V

S

E

E

L

Q

V

L

G

A

L

M

T

T

A

A

G

S

E

E

T

Q

Q

S

D

N

P

P

E

R

K

K

T

A

L

I

P

P

K

S

A

A

I

A

N

K

I

M

P

I

V

Y

R

R

I

I

L

L

L

F

F

V

Y

F

V

L

G

A

S

S

L

L

A

T

V

L

I

V

M

G

A

F

V

L

Q

V

P

P

W

Y

N

T

I

S

I

D

D

Q

-

L

-

G

-

A

-

G

-

S

-

A

P

T

T

K

Q

A

S

S

P

P

F

Y

V

V

T

I

V

A

F

V

S

S

I

H

G

G

I

V

A

R

A

V

A

P

S

H

I

F

I

I

N

N

F

A

V

V

V

I

L

L

S

L

S

S

A

V

A

L

S

S

A

V

C

A

N

N

S

G

A

A

L

F

F

Y

S

T

T

S

S

S

R

R

M

I

L

L

Y

M

G

S

L

L

A

A

K

K

D

Q

D

G

N

N

A

A

P

P

K

K

T

C

F

F

A

D

K

Y

L

I

N

D

K

R

N

E

S

G

T

R

P

P

A

A

M

A

A

A

L

M

L

L

M

V

S

S

S

A

V

L

V

F

V

G

G

V

I

I

T

A

I

F

V

C

L

A

N

S

Y

S

V

K

M

K

P

E

E

E

G

D

V

V

F

F

S

T

L

W

I

L

S

L

G

A

I

I

S

S

T

G

V

L

C

S

F

Q

L

L

F

F

I

T

W

W

T

I

I

T

I

I

V

C

I

L

C

S

H

H

M

I

K

R

F

F

L

R

K

R

Q

A

T

M

K

K

D

V

E

Q

D

G

R

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)
26% identity, 85% coverage: 6:388/448 of query aligns to 277:736/852 of Q03770

query
sites
Q03770

L

I

E

Q

R

R

G

K

L

L

S

K

N

V

R

R

H

H

V

I

Q

Q

L

M

I

L

S

S

I

I

G

G

G

A

A

C

I

F

G

S

T

V

G

G

L

L

F

F

L

L

A

T

S

S

G

G

K

K

S

A

I

F

A

S

I

I

A

A

G

G

P

P

-

F

S

G

V

T

L

L

A

G

Y

F

M

G

I

L

V

T

G

G

M

S

F

I

V

I

F

L

F

A

I

T

M

M

R

L

S

S

L

F

G

T

E

E

L

L

L

S

L

T

A

L

N

I

L

P

D

V

C

S

H

S

S

G

F

F

V

S

E

G

L

L

A

A

H

S

Q

R

Y

F

L

V

G

E

R

D

R

A

W

F

A

G

F

F

V

A

T

L

G

G

W

W

T

T

Y

Y

W

W

F

I

C

S

W

C

I

M

T

L

V

A

A

L

M

P

S

A

D

Q

L

V

T

S

A

S

V

S

G
x
T

M

F

Y

Y

M

L

R

S

Y

Y

W

Y

F

N

P

N

-

V

H

N

L

I

P

S

Q

K

W

G

I

V

P

T

A

A

L

G

L

F

M

I

L

T

L

L

-

F

-

S

-

A

F

F

L

S

M

I

A

V

L

V

N

N

L

L

S

D

V

V

K

S

L

I

F

M

G

G

E

E

I

I

E

V

F

Y

W

V

L

A

A

G

L

I

I

S

K

K

I

V

L

I

A

I

I

A

V

I

A

L

L

M

I

V

-

F

-

T

-

M

-

I

-

L

-

N

-

A

-

G

-

H

-

G

-

N

-

D

-

I

-

H

-

E

G

G

V

V

G

G

L

F

Y

R

M

Y

I

W

F

D

T

S

H

S

H

K

K

S

L

V

E

R

N

N

-

L

-

T

-

Y

G

G

I

L

V

Y

A

R

S

P

F

T

A

F

N

D

L

L

Y

A

Q

D

D

A

G

G

G

E

F

G

F

S

P

K

H

K

G

G

F

I

S

S

G

G

-

P

-

K

-

G

-

R

F

F

I

L

L

A

S

T

F

A

Q

S

-

V

-

M

-

L

L

I

A

S

V

T

F

F

S

A

F

F

T

S

G

G

V

V

E

E

L

M

V

T

G

F

L

L

T

A

A

S

G

G

E

E

T

A

Q

I

D

N

P

P

E

R

K

K

T

T

L

I

P

P

K

S

A

A

I

T

N

K

N

R

-

T

-

F

-

S

-

I

-

V

-

L

I

I

P

S

V

Y

R

V

I

F

L

L

L

I

F

F

Y

S

V

V

G

G

-

I

-

N

-

I

-

Y

-

S

-

G

-

D

-

P

-

R

-

L

-

S

-

Y

-

F

-

P

-

G

-

I

-

S

-

E

-

K

-

R

S

Y

L

E

A

A

V

I

I

I

M

K

A

G

V

T

-

G

Q

M

P

D

W

W

N

R

I

L

-

R

-

T

-

N

-

C

-

R

-

G

I

I

D

D

P

Y

T

R

Q

Q

-

I

-

S

-

V

-

G

-

T

-

G

-

Y

-

S

S

S

P

P

F

W

V

V

T

V

V

A

F

L

S

Q

S

N

I

F

G

G

I

L

A

C

A

T

A

F

A

A

S

S

I

A

I

F

N

N

F

A

V

I

V

L

L

I

S

F

A

T

A

A

S

T

A

A

C

G

N

I

S

S

A

S

L

L

F

F

S

S

T

C

S

S

R

R

M

T

L

L

Y

Y

G

A

L

M

A

S

K

V

D

Q

D

R

N

K

A

A

P

P

K

P

T

V

F

F

A

E

K

I

L

C

N

S

K

K

N

R

S

G

T

V

P

P

A

Y

M

V

A

S

L

V

L

I

M

F

S

S

V

L

V

F

V

S

G

V

I

I

T

A

-

Y

I

I

V

A

L

V

N

D

Y

Q

V

T

M

A

P

I

E

E

G

N

V

-

F

F

S

D

L

V

I

L

S

A

G

N

I

V

S

S

T

S

V

A

C

S

F

T

L

S

F

I

I

I

W

W

T

M

I

G

I

L

V

N

I

L

C

S

H

F

M

L

K

R

F

F

-

Y

-

A

L

L

K

K

Q

Q

T

R

K

K

D

D

T382 (≠ G110) 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.

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)
22% identity, 77% coverage: 2:344/448 of query aligns to 24:398/629 of P30825

query
sites
P30825

S

E

Q

E

E

T

K

R

L

L

E

S

R

R

G

C

L

L

S

N

N

T

R

F

H

D

V

L

Q

V

L

A

I

L

S

G

I

V

G

G

G

S

A

T

I

L

G

G

T

A

G

G

L

V

F

Y

-

V

L

L

A

A

S

G

G

A

K

V

S

A

I

R

A

E

I

N

A

A

G

G

P

P

S

A

V

I

L

V

L

I

A

S

Y

F

M

L

I

I

V

A

G

A

M

L

F

A

V

S

F

V

F

L

I

A

M

G

R

L

S

C

L

Y

G

G

E

E

L

F

L

G

L

A

A

R

N

V

L

P

D

K

C

T

H

G

S

S

F

A

V

Y

E

L

L

Y

A

S

H

Y

Q

V

Y

T

L

V

G

G

R

E

R

L

W

W

A

A

F

F

V

I

T

T

G

G

W

W

T

N

Y

L

W

I

F

L

C

S

W

Y

I

I

T

I

V

G

A

T

M

S

S

S

D

V

L

A

T

R

A

A

-

W

-

S

-

A

-

T

-

F

-

D

-

E

-

L

-

I

-

G

-

R

-

P

V

I

G

G

M

E

Y

F

M

S

R

R

Y

T

W

-

F

-

P

-

H

H

L

M

P

T

Q

L

W

N

I

A

P

P

A

G

L

V

L

L

M

A

-

E

-

N

-

P

-

D

L

I

L

F

F

A

L

V

M

I

A

I

L

I

N

L

L

I

L

L

S

T

V

G

K

L

L

L

F

T

G

L

E

G

I

V

E

K

F

E

W

S

L

A

A

M

L

V

I

N

K

K

I

I

L

F

A

T

I

C

V

I

A

N

L

V

I

L

G

V

V

L

G

G

L

F

Y

I

M

M

I

V

-

S

-

G

F

F

T

V

H

K

H

G

K

S

L

V

E

K

N

N

-

W

-

Q

-

L

-

T

-

E

-

D

-

F

G

G

I
x
N

V

T

A

S

S

G

F

R

A

L

N

C

L

L

Y

N

Q

N

D

D

-

T

-

K

-

E

-

G

-

K

-

P

-

G

-

V

G

G

F

F

F

M

P

P

H

F

G

G

F

F

S

S

G

G

F

V

I

L

L

S

S

G

F

A

Q

A

L

T

A

C

V

F

F

Y

S

A

F

F

T

V

G

G

V

F

E

D

L

C

V

I

G

A

L

T

T

T

A

G

G

E

E

E

T

V

Q

K

D

N

P

P

E

Q

K

K

T

A

L

I

P

P

K

V

A

G

I

I

N

V

N

A

I

S

P

L

V

L

R

I

I

C

L

F

L

I

F

A

Y

Y

V

F

G

G

S

V

L

S

A

A

V

A

I

L

M

T

A

L

V

M

Q

M

P

P

W

Y

N

F

I

C

I

L

D

D

P

-

T

N

Q

N

S

S

P

P

F

L

V

P

T

D

V

A

F

F

S

K

S

H

I

V

G

G

I

W

A

E

A

G

A

A

A

K

S

Y

I

A

I

V

N

A

F

V

V

G

V

S

L

L

S

C

S

A

A

L

A

S

S

A

A

S

C

L

N

L

S

G

A

S

L

M

F

F

S

P

T

M

S

P

R

R

M

V

L

I

Y

Y

G

A

L

M

A

A

K

E

D

D

D

G

N

L

A

L

P

F

K

K

T

F

F

L

A

A

K

N

L

V

N

N

-

D

K

R

N

T

S

K

T

T

P

P

A

I

M

I

A

A

L

T

L

L

M

A

S

S

S

G

V

A

V

V

V

A

G

A

I

V

N226 (≠ I180) modified: carbohydrate, N-linked (GlcNAc...) asparagine

6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
21% identity, 50% coverage: 193:415/448 of query aligns to 211:426/458 of 6f34A

query
sites
6f34A

F

F

F

M

P

P

H

Y

G

G

F

F

S

S

G

G

F

V

I

A

L

T

S

G

F

A

Q

A

L

T

A

V

V

F

F
|
F

S
x
A

F

Y

T
x
I

G

G

V

F

E

D

L

A

V

V

G

S

L

T

T

A

A

A

G

E

E

E

T

V

Q

R

D

N

P

P

E

Q

K

R

T

D

L

M

P

P

K

I

A

G

I

I

N

I

N

V

I

S

P

L

V

L

R

V

I

C

L

T

L

L

F

L

Y

Y

V

I

G

A

S

V

L

S

A

L

V

V

I

L

M

T

A

G

V

I

Q

V

P

P

W

Y

N

E

I

Q

I

L

D

N

P

-

T

V

Q

K

S

N

P

P

F

V

V

A

T

F

V

A

F

L

S

N

S

Y

I

I

G

H

I
x
Q

A

D

A

W

A
x
V

A

A

S

G

I

F

I

I

N

S

F

L

V

G

V

A

L

I

S

A

S

G

A

I

A

T

S

T

A
x
V

C

L

N

L

S

V

A

S

L

M

F

Y

S

G

T

Q

S

T

R

R

M

L

L

F

Y

Y

G

A

L

I

A

S

K

R

D

D

D

G

N

L

A

L

P

P

K

K

T

V

F

F

A

A

K

R

L

I

N

S

K

P

-

T

N

R

S

Q

T

V

P

P

A

Y

M

V

A

N

L

T

L

W

M

L

S

T

S

G

V

A

V

V

G

A

I

-

T

-

I

-

V

V

L

F

N

A

Y

G

V

I

M

I

P

P

E

L

G

N

V

K

F

L

S

A

L

E

I

L

S

T

G

N

I

I

S

G

T

T

V

L

C

-

F

F

L

A

F

F

I

-

W

-

T

-

I

I

I

T

V

V

I

S

C

I

H

G

M

V

K

L

F

V

L

L

K

R

Q

K

T

T

K

Q

D

P

E

D

D

L

R

K

P

R

K

A

F

F

R

R

L

V

K

P

G

F

A

V

K

P

V

V

I

V

N

P

I

I

L

L

S

A

L

V

I

L

F

F

L

C

A

G

L

Y

I

L

I

V

V

L

binding arginine: F228 (= F210), A229 (≠ S211), I231 (≠ T213), V314 (≠ A297)
binding : Q296 (≠ I279), V299 (≠ A282)

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

P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
24% identity, 71% coverage: 78:394/448 of query aligns to 77:387/445 of P60061

query
sites
P60061

A

A

H

R

Q

R

Y

C

L

F

G

G

R

P

R

F

W

L

A

G

F

Y

V

Q

T

T

G

N

W

V

T

L

Y
|
Y

W

W

F

L

-
x
A

C
|
C

W

W

I

I

T

G

V
x
N

A

I

M

A

S
x
M

D

V

L

V

T

I

A

G

V

V

G

G

M

-

Y

Y

M

L

R

S

Y

Y

W

F

F

F

P

P

H

I

L

L

P

K

Q

D

-

P

-

L

-

V

-

L

W

T

I

I

P

T

A

C

L

V

M

V

L

L

L

W

F

I

L

F

M

V

A

L

L

L

N

N

L

I

L

V

S

G

V

P

K

K

L

M

F

I

G

T

E

R

I

V

E

Q

F

-

W

-

L

-

A

A

L

V

I

A

K

T

I

V

L

L

A

A

I

L

V

I

A

P

L

I

I

V

G

G

V

I

G

A

L

V

Y

F

M

G

I

W

F

F

T

W

H

F

H

R

K

G

L

-

E

-

N

-

G

-

I

-

V

-

A

E

S

T

F

Y

A

M

N

A

L

A

Y

W

Q

N

D

V

G

S

G

G

F

L

F

-

P

-

H

G

G

T

F

F

S

G

G

A

F

I

I

Q

L

S

S

T

F

L

Q

N

L

V

A

T

V

L

F
x
W

S
|
S

F

F

T
x
I

G

G

V

V

E

E

L

S

V

A

G

S

L

V

T

A

A

A

G

G

E

V

T

V

Q

K

D

N

P

P

E

K

K

R

T

N

L

V

P

P

K

I

A

A

I

T

N

I

N

G

I

G

P

V

V

L

R

I

I

A

L

A

L

V

F

C

Y

Y

V

V

G

L

S

S

L

T

A

T

V

A

I

I

M

M

A

G

V

M

Q

I

P

P

W

N

N

A

I

A

I

L

D

R

P

V

T

S

Q

A

S

S

P

P

F

F

V

G

T

D

V

A

F

A

S

R

S

M

I

A

G

L

I

G

A

D

A

T

A

A

A

G

S

A

I

I

I

V

N

S

F

F

V

-

L

-

S

-

S

C

A

A

S

A

A

G

C

C

N

L

S

G

A

S

L

L

F

G

S

G

T
x
W

S

T

R

L

M

L

L

A

Y

G

G

Q

L

T

A

A

K

K

-

A

D

D

N

G

A

L

-

F

P

P

K

P

T

I

F

F

A

A

K

R

L

V

N

N

K

K

N

A

S

G

T

T

P

P

A

V

M

A

A

G

L

L

L

I

M

I

S

V

S

G

V

I

V

L

V

M

G

T

I

I

T

-

I

F

V

Q

L

L

N

S

Y

S

V

I

M

S

P

P

E

N

G

A

V

T

-

K

-

E

F

F

S

G

L

L

I

V

S

S

G

S

I

V

S
|
S

T

V

V

I

C

F

F

T

L

L

-

V

-

P

F

Y

I

L

W

Y

T

T

-

C

-

A

I

L

V

L

I

L

C

G

H

H

M

G

K

H

F

F

L

G

K

K

Q

A

T

-

K

-

D

-

E

-

D

-

R

R

P

P

K

A

F

Y

Y93 (= Y94) mutation to L: Greatly decreased Arg uptake into liposomes.
A96 (vs. gap) binding agmatine; binding L-arginine
C97 (= C97) binding agmatine
N101 (≠ V101) 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 (≠ S104) binding agmatine; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
W202 (≠ F210) binding L-arginine; mutation to L: Halves Arg uptake into liposomes.
S203 (= S211) binding agmatine
I205 (≠ T213) binding agmatine; binding L-arginine; mutation to A: About wild-type affinity for Arg and Agm.
W293 (≠ T305) 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 (= S364) binding L-arginine; mutation to A: 20% decreased affinity for Arg, 40% decrease affinity for Agm.

Sites not aligning to the query:

23 binding agmatine; binding L-arginine
26 binding L-arginine

P60063 Arginine/agmatine antiporter from Escherichia coli O157:H7 (see 3 papers)
24% identity, 71% coverage: 78:394/448 of query aligns to 77:387/445 of P60063

query
sites
P60063

A

A

H

R

Q

R

Y

C

L

F

G

G

R

P

R

F

W

L

A

G

F
x
Y

V

Q

T

T

G

N

W

V

T

L

Y
|
Y

W

W

F

L

-
x
A

C
|
C

W

W

I

I

T

G

V
x
N

A

I

M

A

S

M

D

V

L

V

T

I

A

G

V

V

G

G

M

-

Y

Y

M

L

R

S

Y

Y

W

F

F

F

P

P

H

I

L

L

P

K

Q

D

-

P

-

L

-

V

-

L

W

T

I

I

P

T

A

C

L

V

M

V

L

L

L

W

F

I

L

F

M

V

A

L

L

L

N

N

L

I

L

V

S

G

V

P

K

K

L

M

F

I

G

T

E

R

I

V

E

Q

F

-

W

-

L

-

A

A

L

V

I

A

K

T

I

V

L

L

A

A

I

L

V

I

A

P

L

I

I

V

G

G

V

I

G

A

L

V

Y

F

M

G

I

W

F

F

T

W

H

F

H

R

K

G

L

-

E

-

N

-

G

-

I

-

V

-

A

E

S

T

F

Y

A

M

N

A

L

A

Y

W

Q

N

D

V

G

S

G

G

F

L

F

-

P

-

H

G

G

T

F

F

S

G

G

A

F

I

I

Q

L

S

S

T

F

L

Q

N

L

V

A

T

V

L

F
x
W

S

S

F

F

T
x
I

G
|
G

V
|
V

E
|
E

L
x
S

V
x
A

G

S

L

V

T

A

A

A

G

G

E

V

T

V

Q

K

D

N

P

P

E

K

K

R

T

N

L

V

P

P

K

I

A

A

I

T

N

I

N

G

I

G

P

V

V

L

R

I

I

A

L

A

L

V

F

C

Y

Y

V

V

G

L

S

S

L

T

A

T

V

A

I

I

M

M

A

G

V

M

Q

I

P

P

W

N

N

A

I

A

I

L

D

R

P

V

T

S

Q

A

S

S

P

P

F

F

V

G

T

D

V

A

F

A

S

R

S

M

I

A

G

L

I

G

A

D

A

T

A

A

A

G

S

A

I

I

I

V

N

S

F

F

V

-

L

-

S

-

S

C

A

A

S

A

A

G

C

C

N

L

S

G

A

S

L

L

F

G

S

G

T
x
W

S

T

R

L

M

L

L

A

Y

G

G

Q

L

T

A

A

K

K

-

A

D

D

N

G

A

L

-

F

P

P

K

P

T

I

F

F

A

A

K

R

L

V

N

N

K

K

N

A

S

G

T

T

P

P

A

V

M

A

A

G

L

L

L

I

M

I

S

V

S

G

V

I

V

L

V

M

G

T

I

I

T

-

I
x
F

V

Q

L

L

N

S

Y

S

V

I

M

S

P

P

E

N

G

A

V

T

-

K

-

E

F

F

S

G

L

L

I

V

S

S

G

S

I

V

S
|
S

T

V

V

I

C

F

F

T

L

L

-

V

-

P

F
x
Y

I

L

W

Y

T

T

-

C

-

A

I

L

V

L

I

L

C

G

H

H

M

G

K

H

F

F

L

G

K

K

Q

A

T

-

K

-

D

-

E

-

D

-

R

R

P

P

K

A

F

Y

Y87 (≠ F88) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
Y93 (= Y94) 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 (vs. gap) binding L-arginine
C97 (= C97) binding L-arginine
N101 (≠ V101) binding L-arginine
W202 (≠ F210) Periplasmic (proximal) gate; binding L-arginine
I205 (≠ T213) binding L-arginine
GVESA 206:210 (≠ GVELV 214:218) Helix-breaking GVESA motif TM6
E208 (= E216) mutation E->A,D: 5-10% Agm antiport.
W293 (≠ T305) binding L-arginine
F337 (≠ I346) mutation to A: Severely decreased antiport.
S357 (= S364) binding L-arginine
Y365 (≠ F370) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.

Sites not aligning to the query:

22 N→A: No change in antiport activity, 6-fold higher affinity for Arg.
23 binding L-arginine
25:27 Helix-breaking GSG motif TM1
26 binding L-arginine; S→K: 5% Agm antiport.
27 binding L-arginine
74 Y→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.; Y→F: Approximately wild-type antiport.

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: 78:394/448 of query aligns to 73:383/437 of 5j4nA

query
sites
5j4nA

A

A

H

R

Q

R

Y

C

L

F

G

G

R

P

R

F

W

L

A

G

F

Y

V

Q

T

T

G

N

W

V

T

L

Y

Y

W

W

F

L

-
x
A

C
|
C

W

W

I

I

T
x
G

V
x
N

A

I

M

A

S
x
M

D

V

L

V

T

I

A

G

V

V

G

G

M

-

Y

Y

M

L

R

S

Y

Y

W

F

F

F

P

P

H

I

L

L

P

K

Q

D

-

P

-

L

-

V

-

L

W

T

I

I

P

T

A

C

L

V

M

V

L

L

L

W

F

I

L

F

M

V

A

L

L

L

N

N

L

I

L

V

S

G

V

P

K

K

L

M

F

I

G

T

E

R

I

V

E

Q

F

-

W

-

L

-

A

A

L

V

I

A

K

T

I

V

L

L

A

A

I

L

V

I

A

P

L

I

I

V

G

G

V

I

G

A

L

V

Y

F

M

G

I

W

F

F

T

W

H

F

H

R

K

G

L

-

E

-

N

-

G

-

I

-

V

-

A

E

S

T

F

Y

A

M

N

A

L

A

Y

W

Q

N

D

V

G

S

G

G

F

L

F

-

P

-

H

G

G

T

F

F

S

G

G

A

F

I

I

Q

L

S

S

T

F

L

Q

N

L

V

A

T

V

L

F

W

S

S

F

F

T

I

G

G

V

V

E

E

L

S

V

A

G

S

L

V

T

A

A

A

G

G

E

V

T

V

Q

K

D

N

P

P

E

K

K

R

T

N

L

V

P

P

K

I

A

A

I

T

N

I

N

G

I

G

P

V

V

L

R

I

I

A

L

A

L

V

F

C

Y

Y

V

V

G

L

S

S

L

T

A

T

V

A

I

I

M

M

A

G

V

M

Q

I

P

P

W

N

N

A

I

A

I

L

D

R

P

V

T

S

Q

A

S

S

P

P

F

F

V

G

T

D

V

A

F

A

S

R

S

M

I

A

G

L

I

G

A

D

A

T

A

A

A

G

S

A

I

I

I

V

N

S

F

F

V

-

L

-

S

-

S

C

A

A

S

A

A

G

C

C

N

L

S

G

A

S

L

L

F

G

S

G

T
x
W

S

T

R

L

M

L

L

A

Y

G

G

Q

L

T

A

A

K

K

-

A

D

D

N

G

A

L

-

F

P

P

K

P

T

I

F

F

A

A

K

R

L

V

N

N

K

K

N

A

S

G

T

T

P

P

A

V

M

A

A

G

L

L

L

I

M

I

S

V

S

G

V

I

V

L

V

M

G

T

I

I

T

-

I

F

V

Q

L

L

N

S

Y

S

V

I

M

S

P

P

E

N

G

A

V

T

-

K

-

E

F

F

S

G

L

L

I

V

S

S

G

S

I

V

S

S

T

V

V

I

C

F

F

T

L

L

-

V

-

P

F

Y

I

L

W

Y

T

T

-

C

-

A

I

L

V

L

I

L

C

G

H

H

M

G

K

H

F

F

L

G

K

K

Q

A

T

-

K

-

D

-

E

-

D

-

R

R

P

P

K

A

F

Y

binding agmatine: A92 (vs. gap), C93 (= C97), G96 (≠ T100), N97 (≠ V101), M100 (≠ S104), W289 (≠ T305)

Sites not aligning to the query:

binding agmatine: 19

5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
21% identity, 50% coverage: 193:415/448 of query aligns to 209:424/456 of 5oqtA

query
sites
5oqtA

F

F

F

M

P

P

H

Y

G

G

F

F

S

S

G

G

F

V

I

A

L

T

S

G

F

A

Q

A

L

T

A

V

V

F

F
|
F

S
x
A

F

Y

T
x
I

G

G

V

F

E

D

L

A

V

V

G

S

L

T

T

A

A

A

G

E

E

E

T

V

Q

R

D

N

P

P

E

Q

K

R

T

D

L

M

P

P

K

I

A

G

I

I

N

I

N

V

I

S

P

L

V

L

R

V

I

C

L

T

L

L

F

L

Y

Y

V

I

G

A

S

V

L

S

A

L

V

V

I

L

M

T

A

G

V

I

Q

V

P

P

W

Y

N

E

I

Q

I

L

D

N

P

-

T

V

Q

K

S

N

P

P

F

V

V

A

T

F

V

A

F

L

S

N

S

Y

I

I

G

H

I
x
Q

A

D

A

W

A
x
V

A

A

S

G

I

F

I

I

N

S

F

L

V

G

V

A

L

I

S

A

S

G

A

I

A

T

S

T

A

V

C

L

N

L

S

V

A

M

L

M

F

Y

S

G

T

Q

S

T

R

R

M

L

L

F

Y

Y

G

A

L

I

A

S

K

R

D

D

D

G

N

L

A

L

P

P

K

K

T

V

F

F

A

A

K

R

L

I

N

S

K

P

-

T

N

R

S

Q

T

V

P

P

A

Y

M

V

A

N

L

T

L

W

M

L

S

T

S

G

V

A

V

V

G

A

I

-

T

-

I

-

V

V

L

F

N

A

Y

G

V

I

M

I

P

P

E

L

G

N

V

K

F

L

S

A

L

E

I

L

S

T

G

N

I

I

S

G

T

T

V

L

C

-

F

F

L

A

F

F

I

-

W

-

T

-

I

I

I

T

V

V

I

S

C

I

H

G

M

V

K

L

F

V

L

L

K

R

Q

K

T

T

K

Q

D

P

E

D

D

L

R

K

P

R

K

A

F

F

R

R

L

V

K

P

G

F

A

V

K

P

V

V

I

V

N

P

I

I

L

L

S

A

L

V

I

L

F

F

L

C

A

G

L

Y

I

L

I

V

V

L

binding alanine: F226 (= F210), A227 (≠ S211), I229 (≠ T213)
binding : Q294 (≠ I279), V297 (≠ A282)

Sites not aligning to the query:

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

3l1lA Structure of arg-bound escherichia coli adic (see paper)
24% identity, 65% coverage: 78:366/448 of query aligns to 71:342/423 of 3l1lA

query
sites
3l1lA

A

A

H

R

Q

R

Y

C

L

F

G

G

R

P

R

F

W

L

A

G

F

Y

V

Q

T

T

G

N

W

V

T

L

Y

Y

W

W

F

L

-

A

C

C

W

W

I

I

T
x
G

V
x
N

A

I

M

A

S

M

D

V

L

V

T

I

A

G

V

V

G

G

M

-

Y

Y

M

L

R

S

Y

Y

W

F

F

F

P

P

H

I

L

L

P

K

Q

D

-

P

W

W

-

V

-

L

-

T

I

I

P

T

A

C

L

V

M

V

L

L

L

W

F

I

L

F

M

V

A

L

L

L

N

N

L

I

L

V

S

G

V

P

K

K

L

M

F

I

G

T

E

R

I

V

E

Q

F

-

W

-

L

-

A

A

L

V

I

A

K

T

I

V

L

L

A

A

I

L

V

I

A

P

L

I

I

V

G

G

V

I

G

A

L

V

Y

F

M

G

I

W

F

F

T

W

H

F

H

R

K

G

L

-

E

-

N

-

G

-

I

-

V

-

A

E

S

T

F

Y

A

M

N

A

L

A

Y

I

Q

Q

D

S

G

-

F

-

P

-

H

-

G

-

F

-

S

-

G

-

F

-

I

-

L

-

S

T

F

L

Q

N

L

V

A

T

V

L

F
x
W

S
|
S

F

F

T
x
I

G

G

V

V

E

E

L

S

V

A

G

S

L

V

T

A

A

A

G

G

E

V

T

V

Q

K

D

N

P

P

E

K

K

R

T

N

L

V

P

P

K

I

A

A

I

T

N

I

N

G

I

G

P

V

V

L

R

I

I

A

L

A

L

V

F

C

Y

Y

V

V

G

L

S

S

L

T

A

T

V

A

I

I

M

M

A

G

V

M

Q

I

P

P

W

N

N

A

I

A

I

L

D

R

P

V

T

S

Q

A

S

S

P

P

F

F

V

G

T

D

V

A

F

A

S

R

S

M

I

A

G

L

I

G

A

D

A

T

A

A

A

G

S

A

I

I

I

V

N

S

F

F

V

-

L

-

S

-

S

C

A

A

S

A

A

G

C

C

N

L

S

G

A

S

L

L

F

G

S

G

T
x
W

S

T

R

L

M

L

L

A

Y

G

G

Q

L

T

A

A

K

K

-

A

D

D

N

G

A

L

-

F

P

P

K

P

T

I

F

F

A

A

K

R

L

V

N

N

K

K

N

A

S

G

T

T

P

P

A

V

M

A

A

G

L

L

L

I

M

I

S

V

S

G

V

I

V

L

V

M

G

T

I

I

T

-

I

F

V

Q

L

L

N

S

Y

S

V

I

M

S

P

P

E

N

G

A

V

T

-

K

-

E

F

F

S

G

L

L

I

V

S

S

G

S

I

V

S

S

T

V

V

I

binding arginine: G94 (≠ T100), N95 (≠ V101), W185 (≠ F210), S186 (= S211), I188 (≠ T213), W276 (≠ T305)

Sites not aligning to the query:

binding arginine: 17, 20, 21

8xxiA Structure of y+lat1 bound with leu
21% identity, 88% coverage: 2:393/448 of query aligns to 1:384/465 of 8xxiA

query
sites
8xxiA

S

E

Q

Q

E

V

K

K

L

L

E

K

R

K

G

E

L

I

S

S

N

L

R

L

H

N

V

G

Q

V

L

C

I

L

S

I

I

V

G

G

G
x
N

A
x
M

I
|
I

G
|
G

T
x
S

G
|
G

L

I

F

F

L

V

A

-

S

S

G

P

K

K

S

G

I

V

A

L

I

I

A

Y

G

S

P

A

S

S

V

F

-

G

-

L

-

S

L

L

L

V

A

I

Y

W

M

A

I

V

V

G

G

G

M

L

F

F

V

S

F

V

F

F

I

G

M

A

R

L

S

C

L

Y

G

A

E

E

L

L

L

G

L

T

A

T

N

I

L

K

D

K

C

S

H

G

S

A

F

S

V

Y

E

A

L

Y

A

I

H

L

Q

E

Y

A

L

F

G

G

R

G

R

F

W

L

A

A

F

F

V

I

T

R

G

L

W

W

T

T

Y

S

W

L

F

L

-

I

-

E

-

P

-

T

-

S

-

Q

C

A

W

I

I

I

T

A

V

I

A

T

M

F

S

A

D

N

L

Y

T

M

A

V

V

Q

G

P

M

L

Y

F

M

P

R

S

Y

C

W

F

F

A

P

P

H

Y

L

A

P

A

Q

S

W

R

I

L

P

L

A

A

L

A

M

C

L

I

L

C

F

L

L

L

M

T

A

F

L

I

N

N

L

C

L

A

S

Y

V

V

K

K

L

W

F

G

G

T

E

L

I

V

E

Q

F

D

W

I

L

F

A

T

L

Y

I

A

K

K

I

V

L

L

A

A

I

L

V

I

A

A

L

V

I

I

G

V

V

A

G

G

L

I

Y

V

M

-

I

-

F

-

T

-

H

-

K

R

L

L

E

G

N

Q

G

G

I

A

V

S

A

T

S

H

F

F

A

E

N

N

L

S

Y

F

Q

E

D

G

G

S

F

F

F

-

P

-

H

-

G

A

F

V

S

G

G

D

F

I

I

A

L

L

S

A

F

L

Q

Y

L

S

A

A

V

L

F

F

S
|
S

F

Y

T
x
S

G
|
G

V

W

E

D

L

T

V

L

G

N

L

Y

T

V

A

T

G

E

E

E

T

I

Q

K

D

N

P

P

E

E

K

R

T

N

L

L

P

P

K

L

A

S

I

I

N

G

-

I

N

S

I

M

P

P

V

I

R

V

I

T

L

I

F

Y

Y

I

V

L

G

T

S

N

L

V

A

A

V

Y

I

Y

M

T

A

V

V

L

Q

D

P

M

W

R

N

D

I

I

I

L

D

-

P

A

T

S

Q

D

S

A

P

V

F

A

V

V

T

T

V

F

F

A

S

D

S

Q

I

I

G

-

I

-

A

-

A

F

S

G

I

I

I

F

N

N

F

W

V

I

L

P

S

L

S

S

A

V

A

A

S

L

A

S

C

C

-

F

-

G

-

L

N

N

S

A

A

S

L

I

F

V

S

A

T

A

S

S

R

R

M

L

L

F

Y

F

G

V

L

G

A

S

K

R

D

E

D

G

N

H

A

L

P

P

K

D

T

A

F

I

A

C

K

M

L

I

N

H

-

V

K

E

N

R

S

F

T

T

P

P

A

V

M

P

A

S

L

L

M

F

S

N

S

G

V

I

V

-

G

-

I

-

T

-

I

M

V

A

L

L

N

I

Y

Y

V

L

M

C

P

V

E

E

G

D

V

I

F

F

S

Q

L

L

I

I

S

N

G

Y

I

Y

S

S

T

F

V

S

C

Y

F

W

L

F

F

F

I

V

W

G

T

L

I

S

I

I

V

V

I

-

C

-

H

-

M

G

K

Q

F

L

L

Y

K

L

Q

R

T

W

K

K

D

E

E

P

D

D

R

R

P

P

K

R

binding leucine: N21 (≠ G22), M22 (≠ A23), I23 (= I24), G24 (= G25), S25 (≠ T26), G26 (= G27), S210 (= S211), S212 (≠ T213), G213 (= G214)

8xyjA Structure of y+lat1 bound with lys
21% identity, 88% coverage: 2:393/448 of query aligns to 1:384/459 of 8xyjA

query
sites
8xyjA

S

E

Q

Q

E

V

K

K

L

L

E

K

R

K

G

E

L

I

S

S

N

L

R

L

H

N

V

G

Q

V

L

C

I

L

S

I

I

V

G

G

G
x
N

A
x
M

I

I

G
|
G

T

S

G

G

L

I

F

F

L

V

A

-

S

S

G

P

K

K

S

G

I

V

A

L

I

I

A

Y

G

S

P

A

S

S

V

F

-

G

-

L

-

S

L

L

L

V

A

I

Y

W

M

A

I

V

V

G

G

G

M

L

F

F

V

S

F

V

F

F

I

G

M

A

R

L

S

C

L

Y

G

A

E

E

L

L

L

G

L

T

A

T

N

I

L

K

D

K

C

S

H

G

S

A

F

S

V

Y

E

A

L

Y

A

I

H

L

Q

E

Y

A

L

F

G

G

R

G

R

F

W

L

A

A

F

F

V

I

T

R

G

L

W

W

T

T

Y

S

W

L

F

L

-

I

-

E

-

P

-

T

-

S

-

Q

C

A

W

I

I

I

T

A

V

I

A

T

M

F

S

A

D

N

L

Y

T

M

A

V

V

Q

G

P

M

L

Y

F

M

P

R

S

Y

C

W

F

F

A

P

P

H

Y

L

A

P

A

Q

S

W

R

I

L

P

L

A

A

L

A

M

C

L

I

L

C

F

L

L

L

M

T

A

F

L

I

N

N

L

C

L

A

S

Y

V

V

K

K

L

W

F

G

G

T

E

L

I

V

E

Q

F

D

W

I

L

F

A

T

L

Y

I

A

K

K

I

V

L

L

A

A

I

L

V

I

A

A

L

V

I

I

G

V

V

A

G

G

L

I

Y

V

M

-

I

-

F

-

T

-

H

-

K

R

L

L

E

G

N

Q

G

G

I

A

V

S

A

T

S

H

F

F

A

E

N

N

L

S

Y

F

Q

E

D

G

G

S

F

F

F

-

P

-

H

-

G

A

F

V

S

G

G

D

F

I

I

A

L

L

S

A

F

L

Q

Y

L

S

A

A

V

L

F

F

S

S

F

Y

T
x
S

G
|
G

V

W

E

D

L

T

V

L

G

N

L

Y

T

V

A

T

G

E

E

E

T

I

Q

K

D

N

P

P

E

E

K

R

T

N

L

L

P

P

K

L

A

S

I

I

N

G

-

I

N

S

I

M

P

P

V

I

R

V

I

T

L

I

F

Y

Y

I

V

L

G

T

S

N

L

V

A

A

V

Y

I

Y

M

T

A

V

V

L

Q

D

P

M

W

R

N

D

I

I

I

L

D

-

P

A

T

S

Q

D

S

A

P

V

F

A

V

V

T

T

V

F

F

A

S

D

S

Q

I

I

G

-

I

-

A

-

A

F

S

G

I

I

I

F

N

N

F

W

V

I

L

P

S

L

S

S

A

V

A

A

S

L

A

S

C

C

-

F

-

G

-

L

N

N

S

A

A

S

L

I

F

V

S

A

T

A

S

S

R

R

M

L

L

F

Y

F

G

V

L

G

A

S

K

R

D

E

D

G

N

H

A

L

P

P

K

D

T

A

F

I

A

C

K

M

L

I

N

H

-

V

K

E

N

R

S

F

T

T

P

P

A

V

M

P

A

S

L

L

M

F

S

N

S

G

V

I

V

-

G

-

I

-

T

-

I

M

V

A

L

L

N

I

Y

Y

V

L

M

C

P

V

E

E

G

D

V

I

F

F

S

Q

L

L

I

I

S

N

G

Y

I

Y

S

S

T

F

V

S

C

Y

F

W

L

F

F

F

I

V

W

G

T

L

I

S

I

I

V

V

I

-

C

-

H

-

M

G

K

Q

F

L

L

Y

K

L

Q

R

T

W

K

K

D

E

E

P

D

D

R

R

P

P

K

R

binding lysine: N21 (≠ G22), M22 (≠ A23), G24 (= G25), S212 (≠ T213), G213 (= G214)

P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
22% identity, 81% coverage: 87:448/448 of query aligns to 82:430/444 of P0AAE8

query
sites
P0AAE8

A

G

F

F

V

Q

T

T

G

G

W

V

T

L

Y
|
Y

W
x
Y

F

H

C

A

-

N

W

W

I

I

T

G

V

N

A

L

M

A

S

I

D

G

L

I

T

T

A

A

V

V

G

S

M

-

Y
|
Y

M

L

R

S

Y

T

W

F

F

F

P

P

H

V

L

L

P

N

Q

D

W

P

I

V

P

P

A

A

L

G

L

I

M

A

L
x
C

L

I

F

A

L

I

M

V

A

W

L

V

N

F

L

T

L

F

S

V

V

N

K

M

L

L

F

G

G

G

E

T

I

-

E

-

F

-

W

W

L

V

A

S

L

R

I

L

K

T

I

T

L

I

A

G

I

L

V

V

-

L

A

V

L

L

I

I

G

P

V

V

G

V

L

M

Y

T

M

A

I

I

F

V

T

G

H

W

H

H

K

W

L

F

E

D

N

A

G

A

I

T

V
x
Y

A

A

S

A

F

N

A

W

N

N

L

T

Y

A

Q

D

-

T

D
|
D

G

G

G

-

F

-

P

-

H

-

G

-

F

-

S

H

G

A

F

I

I

I

L

K

S

S

F

I

Q

L

L

L

A
x
C

V

L

F

W

S

A

F

F

T

V

G

G

V

V

E
|
E

L

S

V

A

G

A

L

V

T

S

A

T

G

G

E

M

T

V

Q

K

D

N

P

P

E

K

K

R

T

T

L

V

P

P

K

L

A

A

I

T

N

M

N

L

I

G

P

T

V

G

R

L

I

A

L

G

L

I

F

V

Y
|
Y

V

I

G

A

S

A

L

T

A

Q

V

V

I

L

M

S

A

G

V

M

Q
x
Y

P

P

W

S

N

S

I

V

I

M

D

A

P

A

T

S

Q

G

S

A

P

P

F

F

V

A

T

I

V

S

F

A

S

S

S

T

I

I

G

L

I

G

A

N

A

W

A

A

S

P

I

L

I

V

N

S

F

A

V

F

V

T

L

A

S

F

S

A

A
x
C

A

L

S

T

A

S

C

L

N

G

S

S

A

W

L

M

F

M

S

L

T

V

S

G

R

Q

M

A

L

G

Y

V

G
x
R

L

A

A

A

K

N

D
|
D

D

G

N

N

A

F

P

P

K

K

T

V

F
x
Y

A

G

K

E

L

V

N

D

K

S

N

N

S

G

T

I

P

P

A

K

M

K

A

G

L

L

M

L

S

A

V

V

V

K

V

M

G

T

I

A

T

L

I

M

V

I

L

L

N

I

Y

T

V

L

M

M

-

N

-

S

-

A

-

G

-

K

P

A

E

S

G

D

V

L

F

F

S

G

L

E

I

L

S

T

G

G

I

I

S

A

T

-

V

-

C

-

F

-

L

-

F

-

I

-

W

-

T

-

I

-

I

V

V

L

I

L

C

T

H

M

M

L

K

P

F
x
Y

L

F

K
x
Y

Q

S

T
x
C

K

V

D

D

E

-

D

-

R

-

P

-

K

L

F

I

R

R

L

F

K
x
E

G

G

A

V

K

N

V

I

I

R

N

N

I

F

L

V

S

S

L

L

I

I

F
x
C

L

S

A

V

L

L

I

G

I
x
C

V

V

I

F

C
|
C

-

F

-

I

A

A

V

L

L

M

E

G

S

A

T

S

R

S

I

F

A
x
E

L

L

F

A

I

G

T

T

P

F

I

I

W

V

F

S

I

L

A

I

L

I

L

L

I

M

I

F

Y
|
Y

Q

A

V

R

K

K

F

M

K

H

E

E

Q

R

Y89 (= Y94) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 10-fold increase in Km for cadaverine for cadaverine uptake and 5-fold increase in Km for cadaverine for cadaverine excretion.
Y90 (≠ W95) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
Y107 (= Y112) mutation to L: Strong decrease in cadaverine uptake.
C125 (≠ L130) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
Y174 (≠ V181) mutation to L: Moderate decrease in cadaverine uptake.
D185 (= D190) mutation to N: Moderate decrease in cadaverine uptake.
C196 (≠ A208) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
E204 (= E216) mutation to Q: Strong decrease in both cadaverine excretion and cadaverine uptake. 22-fold increase in Km for cadaverine for cadaverine uptake and 6-fold increase in Km for cadaverine for cadaverine excretion.
Y235 (= Y247) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 23-fold increase in Km for cadaverine for cadaverine uptake and 7-fold increase in Km for cadaverine for cadaverine excretion.
Y246 (≠ Q258) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
C282 (≠ A294) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
R299 (≠ G311) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
D303 (= D315) mutation to N: Strong decrease in both cadaverine excretion and cadaverine uptake. 24-fold increase in Km for cadaverine for cadaverine uptake and 9-fold increase in Km for cadaverine for cadaverine excretion.
Y310 (≠ F322) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
Y366 (≠ F382) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
Y368 (≠ K384) mutation to L: Strong decrease in cadaverine uptake.
C370 (≠ T386) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
E377 (≠ K397) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
C389 (≠ F409) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
C394 (≠ I414) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
C397 (= C417) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
E408 (≠ A426) mutation to Q: Moderate decrease in cadaverine uptake.
Y423 (= Y441) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.

Sites not aligning to the query:

12 C→S: Does not affect cadaverine excretion and cadaverine uptake.
41 W→L: Moderate decrease in cadaverine uptake.
43 W→L: Strong decrease in cadaverine uptake.
55 Y→L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
57 Y→L: Strong decrease in cadaverine uptake.
73 Y→L: Strong decrease in both cadaverine excretion and cadaverine uptake. 9-fold increase in Km for cadaverine for cadaverine uptake and 10-fold increase in Km for cadaverine for cadaverine excretion.
76 E→Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.

Query Sequence

>WP_009490181.1 NCBI__GCF_000313915.1:WP_009490181.1
MSQEKLERGLSNRHVQLISIGGAIGTGLFLASGKSIAIAGPSVLLAYMIVGMFVFFIMRS
LGELLLANLDCHSFVELAHQYLGRRWAFVTGWTYWFCWITVAMSDLTAVGMYMRYWFPHL
PQWIPALLMLLFLMALNLLSVKLFGEIEFWLALIKILAIVALIGVGLYMIFTHHKLENGI
VASFANLYQDGGFFPHGFSGFILSFQLAVFSFTGVELVGLTAGETQDPEKTLPKAINNIP
VRILLFYVGSLAVIMAVQPWNIIDPTQSPFVTVFSSIGIAAAASIINFVVLSSAASACNS
ALFSTSRMLYGLAKDDNAPKTFAKLNKNSTPAMALLMSSVVVGITIVLNYVMPEGVFSLI
SGISTVCFLFIWTIIVICHMKFLKQTKDEDRPKFRLKGAKVINILSLIFLALIIVICAVL
ESTRIALFITPIWFIALLIIYQVKFKEQ

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