SitesBLAST

Y102 (= Y101) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
W106 (= W105) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
K163 (= K162) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
F216 (= F217) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
E222 (= E223) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
E230 (= E231) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
D275 (= D268) 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 (≠ G271) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-275.
E438 (≠ D431) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
D443 (vs. gap) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
D446 (vs. gap) mutation to A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
39% identity, 98% coverage: 8:467/469 of query aligns to 4:458/469 of P46349

query
sites
P46349

S

S

Q

Q

D

S

N

G

F

L

K

K

R

K

T

E

M

L

K

K

V

T

R

R

H

H

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M

V

T

M

M

L

I

S

S

L

I

G

A

G

G

V

V

I

I

G

G

T

A

G

G

L

L

F

F

F

V

N
x
G

T

S

G

G

Y

S

I

V

I

I

S

H

T

S

T

T

G
|
G

A

P

A

-

G

G

T

A

L

V

A

S

Y

Y

L

A

I

L

G

A

A

G

L

L

V

L

V

V

W

I

L

F

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M

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R

C

M

L

L

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G

E

E

L

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A

A

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P

E

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G

A

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F

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Y

Y

A

A

A

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D

Y

A

L

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P

P

A

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A

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A

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L

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Y

Y

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L

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A

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E

L

A

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A

A

A

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G

A

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G

C

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M

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Q

Y

Y

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W

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F

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H

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P

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L

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W

L

L

W

T

C

S

L

L

V

I

F

L

C

T

I

I

A

V

I

L

Y

T

L

L

L

T

N

N

I

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V

Y

S

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T

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R

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F

S

F

F

A

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Y

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K

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-

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A

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N

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L

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C

A

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G
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G

L

L

Y

Y

A

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S

T

G

S

R

R

M

M

L

L

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Y

S

S

L

L

A

A

N

E

E

R

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E

L

A

P

P

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R

C

R

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M

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P

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L

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A

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P

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P

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Y

L

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F

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L

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L

A

C

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L

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L
x
G

A

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L

M

A

A

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N

G33 (≠ N37) mutation to D: Lack of activity.
G42 (= G46) mutation to S: Lack of activity.
G301 (= G308) mutation to V: Lack of activity.
G338 (≠ S345) mutation to E: Lack of activity.
F341 (≠ G348) mutation to S: Lack of activity.
G414 (≠ L423) mutation to R: Lack of activity.

Q88CZ8 L-histidine transporter HutT from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
36% identity, 98% coverage: 10:469/469 of query aligns to 5:460/467 of Q88CZ8

query
sites
Q88CZ8

D

Q

N

G

F

L

K

K

R

R

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S

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A

R

R

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G

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T

G

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N

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A

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G

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Y

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x
E

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M

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I

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A

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D

L

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A

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A

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M

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C

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V

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F

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I

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A

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Y

G

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G

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L

N

N

I

L

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N

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F

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F

A

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E

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M

E

E

F

F

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K

V

V

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A

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A

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M

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L

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A

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-

A

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G

D

T

G

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A

A

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-

G

G

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S

N

N

L

L

-

F

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D

A

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M

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N

G

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G

I

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M

F

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A

A

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N

M

F
|
F

A

A

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G

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I

E
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E

L

I

I

I

G

G

I

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A

T

A

A

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G

E

E

T

A

E

K

Q

D

P

P

Q

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A

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A

A

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T

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Y

I

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A

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D

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A

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G

S

S

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P

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V

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F

F

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K

N

I

L

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G

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S

A

A

D

A

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V

F

L

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N

F

V

V

V

I

V

L

I

T

S

A

A

I

A

L

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S

A

A

A

I

N

N

S

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G

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F

A

G

S

A

G

G

R

R

M

M

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Y

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L

A

A

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Q

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V

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V

A

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M

L

S

Q

R

A

E

G

-

T

Q

L

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Q

A

Q

Q

L

L

A

K

Y

F

R

P

A

V

P

P

L

F

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W

P

P

L

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T

G

P

P

I

A

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G

A

F

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L

A

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C

M

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V

L

F

A

I

C

F

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G

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V

L

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Y

D

F

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S

D

Q

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R

Q

I

A

A

A

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C

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G

G

I

V

P

I

F

W

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V

L

V

F

F

C

L

Y

V

A

A

A

S

Y

Y

H

L

V

L

T

W

H

C

R

K

R

P

N

-

L

-

K

R

A

A

G

G

E

Q

A

G

N

Q

D

P

V

V

A

A

T27 (= T32) mutation T->A,S: Retains 60% of wild-type activity.; mutation to N: Retains 20% of wild-type activity.
E98 (≠ T104) mutation to A: Retains 80% of wild-type activity.
K156 (= K162) mutation K->A,Q: Retains less than 10% of wild-type activity.; mutation to R: Retains 40% of wild-type activity.
F212 (= F217) mutation F->A,Q: Loss of activity.; mutation to Y: No change in activity.
E218 (= E223) mutation E->A,Q: Loss of activity.; mutation to D: Retains 70% of wild-type 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)
34% identity, 99% coverage: 1:466/469 of query aligns to 2:457/457 of P15993

query
sites
P15993

M

M

Q

E

T

G

Q

Q

E

Q

T

H

P

G

S

E

Q

Q

D

-

N

-

F

L

K

K

R

R

T

G

M

L

K

K

V

N

R

R

H

H

L

I

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Q

M

L

L

I

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A

L

L

G

G

V

A

I

I

G

G

T

T

G

G

L

L

F

F

F

L

N

G

T

S

G

A

Y

S

I

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I

I

S

Q

T

S

T

A

G

G

A

P

A

-

G

G

T

I

L

I

L

L

A

G

Y

Y

L

A

I

I

G

A

A

G

L

F

V

I

V

A

W

F

L

L

V

I

M

M

V

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C

Q

L

L

G

G

E

E

L

M

A

V

V

V

A

E

M

E

P

P

E

V

T

A

G

G

A

S

F

F

H

S

V

H

Y

F

A

A

A

Y

R

K

Y

Y

L

W

S

G

P

S

A

F

T

A

G

G

Y

F

T

A

V

S

A

G

W

W

L

N

Y

Y

W

W

L

V

T

L

W
x
Y

T

V

V

L

A

V

L

A

G

M

S

A

S

E

L

L

T

T

A

A

A

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G

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K

C

Y

M

I

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Q

Y

F

W

W

F

Y

P

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T

I

P

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T

W

W

L

V

W

S

C

A

L

A

V

V

F

F

C

F

I

V

A

V

I

I

Y

N

L

A

L

I

N

N

I

L

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S

N

T

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R

K

F

V

F

F

A

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E

G

M

E

E

F

F

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W

F

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A

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K

K

V

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T

A

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A

A

F

M

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I

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F

G

G

A

G

G

W

A

L

M

L

F

F

G

S

F

-

I

-

P

-

M

-

K

G

D

N

G

G

S

G

A

P

A

Q

P

A

G

T

L

V

S

S

N

N

L

L

-

W

T

D

A

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G

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F

L

L

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P

H

H

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M

M

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M

M

M

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A

A

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M

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F

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F

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G

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E

L

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G

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A

A

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A

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A

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D

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P

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K

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A

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A

Y

R

R

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Y

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P

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G

G

I

D

P

T

Y

F

A

V

A

A

D

N

I

A

F

L

N

N

F

I

V

V

I

V

L

L

T

T

A

A

I

A

L

L

S

S

A

V

A

Y

N

N

S

S

G

C

L

V

Y

Y

A

C

S

N

G

S

R

R

M

M

L

L

W

F

S

G

L

L

A

A

N

Q

E

Q

N

G

T

N

L

A

P

P

R

K

C

A

F

L

A

A

R

S

V

V

N

D

H

K

R

R

G

G

V

V

P

P

V

V

L

N

A

T

L

I

T

L

I

V

S

S

M

A

L

L

G

V

G

T

L

A

L

L

A

C

L

V

F

L

S

I

S

N

V

Y

I

L

A

A

P

P

D

E

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S

V

A

F

F

V

G

A

L

L

L

S

M

A

A

I

L

S

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G

V

F

S

A

A

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L

V

V

A

I

V

N

W

W

L

A

S

M

I

I

C

S

A

L

S

A

H

H

Y

M

V

K

F

F

R

R

R

A

H

K

L

Q

Q

E

A

Q

G

G

G

V

T

V

L

T

Q

R

Q

-

L

-

A

-

Y

F

R

P

A

A

P

L

L

L

Y

Y

P

P

L

L

T

G

P

N

I

W

L

I

G

C

F

L

L

L

L

F

C

M

L

A

A

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C

L

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V

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A

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M

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P

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G

Q

M

R

A

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A

S

L

V

W

Y

C

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G

-

I

I

P

P

F

V

V

W

L

L

F

I

C

V

Y

L

A

G

A

I

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G

H

Y

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F

H

K

R

E

R

K

N

T

L

A

K

K

A

A

G

V

E

K

A

A

N

H

Y103 (≠ W105) Key residue for tryptophan transport; mutation to F: Decreases tryptophan transport to less than 50% of wild-type levels and reduces the ability of tryptophan to inhibit phenylalanine transport from 95 to 62%.

P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
33% identity, 98% coverage: 1:458/469 of query aligns to 1:458/458 of P24207

query
sites
P24207

M

M

Q

K

T

N

Q

A

E

S

T

T

P

V

S

S

Q

E

D

D

N

T

-

A

-

S

-

N

-

Q

-

E

-

P

-

T

F

L

K

H

R

R

T

G

M

L

K

H

V

N

R
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R

H

H

L

I

V

Q

M

L

L

I

S

A

L

L

G

G

V

A

I

I

G

G

T

T

G

G

L

L

F

F

F

L

N

G

T

I

G

G

Y

P

I

A

I

I

S

Q

T

M

T

A

G

G

A
x
P

A

A

G

-

T

V

L

L

A

G

Y

Y

L

G

I

V

G

A

A

G

L

I

V

I

V

A

W

F

L

L

V

I

M

M

V

R

C

Q

L

L

G

G

E

E

L

M

A

V

V

V

A

E

M

E

P

P

E

V

T

S

G

G

A

S

F
|
F

H

A

V

H

Y
x
F

A

A

A
x
Y

R

K

Y
|
Y

L
x
W

S

G

P

P

A
x
F

T

A

G

G

Y
x
F

T

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V

S

A

G

W
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W

L

N

Y
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Y

W
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W

L

V

T

M

W
x
F

T

V

V

L

A

V

L

G

G

M

S

A

S
x
E

L

L

T

T

A

A

G

G

F

I

C

Y

M

M

Q

Q

Y

Y

W

W

F

F

P

P

T

D

T

V

P

P

V

T

W

W

L

I

W

W

C

A

L

A

V

A

F

F

C

F

I

I

A

I

I

I

Y

N

L

A

L

V

N

N

I

L

V

V

S

N

T

V

R

R

F

L

F

Y

A

G

E

E

G

T

E

E

F

F

W

W

F

F

S

A

I

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K
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K

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V

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F

M

I

I

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F

G

G

A

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G

W

A

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M

L

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F

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F

-

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M

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K

G

D

H

G

G

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G

A

E

A

K

P

A

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D

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N

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L

-

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R

A

Y

S

G

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F

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A

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P

G

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M

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A

A

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V

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M

F

F

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F

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E
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E

L

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G

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R

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N

F

F

V

V

I

I

L

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T

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A

A

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S

A

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A

Y

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N

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S

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G

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Y

A

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S

N

G

S

R

R

M

M

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G

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N

G

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N

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R

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V

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R

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P

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I

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M

I

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S

M

G

L

A

G

I

G

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A

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L

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F

L

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S

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Y

I

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P

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K

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A

F

F

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G

A

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M

A

A

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G

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F

A

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A

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N

W

W

L

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M

I

I

C

C

A

L

S

A

H

H

Y

L

V

R

F

F

R

R

R

A

H

M

L

R

Q

R

A

Q

G

G

G

-

T

-

L

-

Q

R

Q

E

L

T

A

Q

Y

F

R

K

A

A

P

L

L

L

Y

Y

P

P

L

F

-

G

-

N

-

Y

-

L

-

C

T

I

P

A

I

F

L

L

G

G

F

M

L

I

L

L

C

L

L

L

L

M

A

C

C

T

V

M

G

D

L

D

A

M

F

R

D

L

P

S

S

A

Q

I

R

L

I

L

A
x
P

L

V

W

W

C

-

G

-

I

-

P

-

F

-

V

I

L

V

F

F

C

L

Y

F

A

M

A

A

Y

F

H

K

V

T

T

L

H

R

R

R

R

K

R26 (= R19) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
P54 (≠ A47) 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 (= F81) mutation to L: No effect on phenylalanine transport activity.
F90 (≠ Y84) mutation to L: 65% of wild-type phenylalanine transport activity.
Y92 (≠ A86) mutation to L: 41% of wild-type phenylalanine transport activity.
Y94 (= Y88) mutation to L: 69% of wild-type phenylalanine transport activity.
W95 (≠ L89) mutation to L: 10% of wild-type phenylalanine transport activity.
F98 (≠ A92) mutation to L: No effect on phenylalanine transport activity.
F101 (≠ Y95) mutation to L: 38% of wild-type phenylalanine transport activity.
W105 (= W99) mutation to L: 39% of wild-type phenylalanine transport activity.
Y107 (= Y101) mutation to L: No effect on phenylalanine transport activity.
W108 (= W102) mutation to L: 71% of wild-type phenylalanine transport activity.
F111 (≠ W105) 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 (≠ S112) mutation E->G,L,V,N: Loss of activity.
K168 (= K162) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
E226 (= E223) mutation E->A,Q,K,R,W: Loss of activity.
R252 (= R249) mutation R->D,E,F,W,P: Loss of activity.
P341 (= P338) 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 (≠ A437) 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.

P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
33% identity, 85% coverage: 13:411/469 of query aligns to 85:496/590 of P04817

query
sites
P04817

K

K

R

R

T

E

M

L

K

K

V

Q

R

R

H

H

L

I

V

G

M

M

L

I

S

A

L

L

G

G

V

T

I

I

G

G

T

T

G

G

L

L

F

F

F

I

N

G

T

L

G

S

Y

T

I
x
P

I

L

S

T

T

N

T

A

G

G

A

P

A

V

G

G

T

A

L

L

L

I

A

S

Y

Y

L

L

I

F

G

M

A

G

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L

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Y

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L

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G

E

E

L

M

A

A

V

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A

F

M

I

P
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P

E
x
V

T

T

G

S

A
x
S

F

F

H

T

V

V

Y

F

A

S

A

Q

R

R

Y

F

L

L

S

S

P

P

A

A

T

F

G

G

Y

A

T

A

V

N

A

G

W

Y

L

M

Y
|
Y

W

W

L

F

T

S

W

W

T

A

V

I

A

T

L

F

G

A

S

L

S

E

L

L

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A

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G

G

F

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C

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M

I

Q

Q

Y

F

W

W

F

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Y

T

K

T

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W

A

L

A

W

W

C

I

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S

V

I

F

F

C

W

I

V

A

I

I

I

Y

T

L

I

L

M

N

N

I

L

V

F

S

P

T

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R

K

F

Y

A

G

E

E

G

F

E

E

F

F

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W

F

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A

I

S

I

I

K

K

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V

V

L

T

A

I

I

A

G

F

F

I

L

I

I

L

Y

-

C

-

F

-

C

-

M

-

V

-

C

G

G

A

A

G

G

A

V

M

T

-

G

-

P

F

V

G

G

F

F

I

R

P

Y

M

W

K

R

D

N

-

P

G

G

S

A

A

W

A

G

P

P

G

G

L

I

S

I

N

S

L

K

T

D

A

K

S

N

-

E

-

G

-

R

-

F

-

L

G

G

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W

L

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H

-

G

-

T

-

L

-

P

-

I

-

L

-

M

-

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M

L

V

I

A

N

V

A

N

A

F

F

A

T

F

F

S

Q

G

G

T

T

E

E

L

L

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G

G

I

I

A

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A

A

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G

E

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T

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P

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K

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D

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D

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G

K

I

L

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K

Q

-

S

-
x
T

-
x
S

-
x
Y

-

V

-

S

-

T

S

S

P

P

F

F

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F

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N

F

A

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V

I

I

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L

T

T

A

T

I

I

L

I

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S

A

A

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N

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S

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Y

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M

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S

I

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A

G

P

G

D

D

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K

V

V

F

F

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A
x
W

L

L

S

L

A

N

I

I

S

T

G

G

F

V

A

A

V

G

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x
F

A

F

V

A

W

W

L

L

S

F

I

I

C

S

A

I

S

S

H

H

Y

I

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R

F

F

R

M

R

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R

A

H

L

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K

Q

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A

R

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G

G

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T

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L

L

Y

M

P

P

P113 (≠ I41) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
P148 (= P76) 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 (≠ E77) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
S152 (≠ A80) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
Y173 (= Y101) 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 (= G230) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
P313 (= P235) 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 (≠ A366) 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 (≠ V376) 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)
30% identity, 97% coverage: 13:468/469 of query aligns to 81:554/587 of Q9URZ4

query
sites
Q9URZ4

K

K

R

R

T

S

M

L

K

K

V

S

R

R

H

H

L

M

V

Q

M

M

L

I

S

S

L

I

G

G

V

A

I

I

G

G

T

T

G

G

L

L

F

Y

F

V

N

G

T

S

G

G

Y

S

I

S

I

L

S

A

T

D

T

G

G

G

A

P

A

A

G

S

T

V

L

I

A

N

Y

Y

L

S

I

L

G

I

A

G

L

I

V

M

W

F

L

F

V

I

M

V

V

Y

C

A

L

L

G

G

E

E

L

M

A

A

V

V

A

A

M

Y

P

P

E

V

T

A

G

G

A

G

F

F

H

N

V

T

Y

Y

A

A

A

T

R

R

Y

F

L

I

S

D

P

P

A

A

T

W

G

G

Y

F

T

A

V

V

A

S

W

W

L

N

Y

Y

W

F

L

I

T

N

W

Y

T

F

V

V

A

T

L

F

G

P

S

L

S

E

L

L

T

T

A

T

A

C

G

A

F

I

C

T

M

F

Q

R

Y

Y

W

W

F

T

P

D

T

I

T

N

P

S

V

A

W

-

L

A

W

W

C

I

L

S

V

I

F

F

C

L

I

V

A

V

I

I

Y

I

L

I

L

V

N

N

I

L

V

F

S

G

T

V

R

R

F

A

F

Y

A

G

E

E

G

V

E

E

F

F

W

I

F

L

S

S

I

T

I

V

K

K

V

V

T

A

I

T

I

F

A

G

F

F

I

I

L

L

G

A

A

I

G

I

A

I

M

N

F

C

G

G

F

G

I

V

P

P

M

T

K

D

D

H

G

R

S

G

A

Y

A

I

P

G

G

G

L

-

S

-

N

S

L

I

T

I

A

K

S

H

G

K

W

P

L

F

P

R

H

H

G

G

T

F

L

K

P

G

I

F

L

C

M

S

T

V

M

F

V

T

A

T

V

A

N

A

F

F

A

S

F

F

S

S

G

G

T

T

E

E

L

V

I

I

G

G

I

L

A

A

G

A

E

E

T

V

E

D

Q

N

P

P

Q

Q

K

K

A

A

L

L

P

P

L

H

A

A

I

V

R

K

T

Q

T

V

V

F

A

W

R

R

L

I

I

A

I

I

F

F

F

Y

I

V

G

V

T

S

V

L

F

I

V

L

L

I

A

G

A

L

L

L

I

I

P

S

M

P

D

D

Q

D

A

P

G

N

I

L

V

M

K

G

-

N

-

G

-

S

-

T

-

S

-

V

S

S

P

P

F

F

V

V

L

L

V

A

F

I

E

K

K

E

I

A

G

N

I

I

P

K

Y

G

A

L

A

P

D

S

I

V

F

F

N

N

F

A

V

V

I

I

L

I

T

I

A

S

I

V

L

V

S

S

A

V

A

T

N

N

S

S

G

S

L

T

Y

Y

A

T

S

A

G

G

R

R

M

T

L

L

W

H

S

G

L

M

A

A

N

N

E

L

N

K

T

Q

L

A

P

P

R

S

C

F

F

F

A

K

R

Y

V

T

N

D

H

R

R

L

G

G

V

R

P

P

V

L

L

L

A

A

L

M

T

I

I

V

S

V

M

L

L

L

G

F

G

G

L

F

A

A

L

Y

F

I

S

N

S

E

V

A

I

D

A

K

-

N

-

G

-

N

-

D

-

V

P

S

D

D

T

T

V

V

F

F

V

N

A

W

L

L

S

L

A

A

I

L

S

S

G

G

F

L

A

S

V

N

V

F

A

F

V

T

W

W

L

G

S

S

I

I

C

C

A

L

S

C

H

H

Y

I

V

I

F

F

R

R

R

L

R

A

H

F

L

K

Q

K

A

Q

G

G

G

H

T

S

L

L

Q

K

Q

E

L

L

A

G

Y

F

R

V

A

S

P

P

L

M

Y

G

P

I

L

W

T

G

P

S

I

C

L

I

G

G

F

L

-

F

-

N

L

I

L

L

C

C

L

L

L

M

A

A

C

Q

-

F

-

Y

-

V

-

S

-

L

-

F

-

P

V

I

G

G

L

G

A

K

F

P

D

N

P

A

S

N

Q

D

R

F

I

F

A

Q

L

G

W

Y

C

L

G

A

I

A

P

P

F

V

V

T

L

L

F

A

C

F

Y

F

A

I

A

G

Y

Y

H

K

V

I

T

Y

H

D

R

R

R

S

N

H

L

I

K

P

A

S

G

L

E

D

A

K

N

L

D

D

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)
31% identity, 87% coverage: 2:409/469 of query aligns to 136:553/663 of P48813

query
sites
P48813

Q

Q

T

E

Q

Q

E

E

T

Q

P

-

S

K

Q

Q

D

E

N

N

F

L

K

K

R

K

T

S

M

I

K

K

V

P

R

R

H

H

L

T

V

V

M

M

L

M

S

S

L

L

G

G

G

T

V

G

I

I

G

G

T

T

G

G

L

L

F

L

F

V

N

G

T

N

G

S

Y

K

I

V

I

L

S

N

T

N

T

A

G

G

A

P

A

G

G

G

T

L

L

I

A

G

Y

Y

L

A

I

I

G

M

A

G

L

S

V

C

V

V

W

Y

L

C

V

I

M

I

V

Q

C

A

L

C

G

G

E

E

L

L

A

A

V

V

A

I

M

Y

P

S

E

D

-

L

T

I

G

G

A

G

F

F

H

N

V

T

Y

Y

A

P

A

L

R

F

Y

L

L

V

S

D

P

P

A

A

T

L

G

G

Y

F

T

S

V

V

A

A

W

W

L

L

Y

F

W

C

L

L

T

Q

W

W

T

L

V

C

A

V

L

C

G

P

S

L

S

E

L

L

T

V

A

T

A

A

G

S

F

M

C

T

M

I

Q

K

Y

Y

W

W

F

T

P

T

T

S

T

V

P

N

V

P

W

D

L

V

W

F

C

V

L

V

V

I

F

F

C

Y

I

V

A

L

I

I

Y

V

L

V

L

I

N

N

I

V

V

F

S

G

T

A

R

K

F

G

F

Y

A

A

E

E

G

A

E

D

F

F

W

F

F

F

S

N

I

C

K

K

V

I

V

L

T

M

I

I

I

V

A

G

F

F

I

F

I

I

L

L

-

A

-

I

-

D

-

C

G

G

A

G

G

A

A

G

M

T

F

D

G

G

F

Y

I

I

P

G

M

S

K

K

-

Y

-

W

-

R

D

D

G

P

S

G

A

A

A

F

P

R

G

G

L

D

S

T

N

P

L

I

T

-

A

-

S

-

G

-

W

-

L

-

P

-

H

Q

G

R

T

F

L

K

P

G

I

V

L

V

M

A

T

T

M

F

V

V

A

T

V

A

N

A

F

F

A

A

F

F

S

G

G

M

T

S

E

E

L

Q

I

L

G

A

I

M

A

T

A

A

G

S

E

E

T

Q

E

S

Q

N

P

P

Q

R

K

K

A

A

L

I

P

P

L

S

A

A

I

A

R

K

T

K

T

M

V

I

A

Y

R

R

L

I

I

L

I

F

F

V

F

F

I

L

G

A

T

S

V

L

F

T

V

L

L

V

A

G

A

F

L

L

I

V

P

P

M

Y

-

T

-

S

D

D

Q

Q

-

L

-

G

-

A

-

G

A

S

G

A

I

T

V

K

K

A

S

S

P

P

F

Y

V

V

L

I

V

A

F

V

E

S

K

S

I

H

G

G

I

V

P

R

Y

V

A

V

A

P

D

H

I

F

F

I

N

N

F

A

V

V

I

I

L

L

T

L

A

S

I

V

L

L

S

S

A

V

A

A

N

N

S

G

G

A

L

F

Y

Y

A

T

S

S

G

S

R

R

M

I

L

L

W

M

S

S

L

L

A

A

N

K

E

Q

N

G

T

N

L

A

P

P

R

K

C

C

F

F

A

D

R

Y

V

I

N

D

H

R

R

E

G

G

V

R

P

P

V

A

L

A

A

A

L

M

T

L

I

V

S

S

M

A

L

L

G

F

G

G

L

V

L

I

A

A

L

F

F

C

S

A

S

S

V

S

I

K

A

K

P

E

D

E

T

D

V

V

F

F

V

T

A

W

L

L

S

L

A

A

I

I

S

S

G

G

F

L

A

S

V

Q

V

L

A

F

V

T

W

W

L

I

S

T

I

I

C

C

A

L

S

S

H

H

Y

I

V

R

F

F

R

R

R

A

H

M

L

K

Q

V

A

Q

G

G

G

R

T

S

L

L

Q

G

Q

E

L

V

A

G

Y

Y

R

K

A

S

P

Q

L

V

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, 97% coverage: 8:461/469 of query aligns to 82:555/602 of P19145

query
sites
P19145

S

A

Q

Q

D

T

N

P

F

L

K

K

R

H

T

H

M

L

K

K

V

N

R

R

H

H

L

L

V

Q

M

M

L

I

S

A

L

I

G

G

V

A

I

I

G

G

T

T

G

G

L

L

F

L

F

V

N

G

T

S

G

G

Y

T

I

A

I

L

S

R

T

T

T

G

G

G

A

P

A

A

G

S

T

L

L

L

L

I

A

G

Y

W

L

G

I

S

G

T

A

G

L

T

V

M

V

I

W

Y

L

A

V

M

M

V

V

M

C

A

L

L

G

G

E

E

L

L

A

A

V

V

A

I

M

F

P

P

E

I

T

S

G

G

A

G

F

F

H

T

V

T

Y

Y

A

A

A

T

R

R

Y

F

L

I

S

D

P

E

A

S

T

F

G

G

Y

Y

T

A

V

N

A

N

W

F

L

N

Y

Y

W

M

L

L

T

Q

W

W

T

L

V

V

A

V

L

L

G

P

S

L

S

E

L

I

T

V

A

S

A

A

G

S

F

I

C

T

M

V

Q

N

Y

F

W

W

F

-

P

G

T

T

T

D

P

P

V

K

W

Y

L

R

W

D

C

G

L

F

V

V

-

A

-

L

F

F

C

W

I

L

A

A

I

I

Y

V

L

I

N

N

I

M

V

F

S

G

T

V

R

K

F

G

F

Y

A

G

E

E

G

A

E

E

F

F

W

V

F

F

S

S

I

F

I

I

K

K

V

V

V

I

T

T

I

V

A

G

F

F

I

I

L

L

G

G

-

I

-

L

-

N

-

C

A

G

G

G

A

G

M

P

F

T

G

G

F

G

I

Y

P

I

M

G

K

G

D

K

G

Y

S

W

A

H

A

D

P

P

G

G

L

A

S

F

N

A

L

G

T

D

A

T

S

P

G

G

W

A

L

K

P

F

H

K

G

G

T

V

L

C

P

S

I

V

L

F

M

V

T

T

M

A

V

A

A

-

V

-

N

-

F

F

A

S

F

F

S
x
A

G

G

T

S

E

E

L

L

I

V

G

G

I

L

A

A

G

S

E

E

T

S

E

V

Q

E

P

P

Q

R

K

K

A

S

L

V

P

P

L

K

A

A

I

A

R

K

T

Q

T

V

V

F

A

W

R

R

L

I

I

T

I

L

F

F

F

Y

I

I

G

L

T

S

V

L

F

L

V

M

L

I

A

G

A

L

L

L

I

V

P

P

M

Y

D

N

Q

D

A

K

G

S

I

L

V

I

-

G

-

A

-

S

-

V

-

D

-

A

K

A

S

S

P

P

F

F

V

V

L

I

V

A

F

I

E

K

K

T

I

H

G

G

I

I

P

K

Y

G

A

L

A

P

D

S

I

V

F

V

N

N

F

V

V

V

I

I

L

L

T

I

A

A

I

V

L

L

S

S

A

V

A

G

N

N

S

S

G

A

L

I

Y

Y

A

A

S

C

G

S

R

R

M

T

L

M

W

V

S

A

L

L

A

A

N

E

E

Q

N

R

T

F

L

L

P

P

R

E

C

I

F

F

A

S

R

Y

V

V

N

D

H

R

R

K

G

G

V

R

P

P

V

L

L

V

A

G

L

I

T

A

I

V

S

T

M

S

L

A

G

F

G

G

L

L

L

I

A

A

L

F

F

V

S

A

V

S

I

K

A

K

P

E

D

G

T

E

V

V

F

F

V

N

A

W

L

L

S

L

A

A

I

L

S

S

G

G

F

L

A

S

V

S

V

L

A

F

V

T

W

W

L

G

S

G

I

I

C

C

A

I

S

C

H

H

Y

I

V

R

F

F

R

R

R

K

R

A

H

L

L

A

Q

A

A

Q

G

G

G

R

T

G

L

L

Q

D

Q

E

L

L

A

S

Y

F

R

K

A

S

P

P

L

T

Y

G

P

V

L

W

T

G

P

S

I

Y

L

W

G

G

F

L

L

F

L

M

C

V

L

I

-

M

-

F

-

I

-

A

-

Q

-

F

-

Y

-

V

A

A

C

V

V

F

G

P

L

V

A

G

F

D

D

S

P

P

S

S

Q

A

R

E

-

G

-

F

I

F

A

E

L

A

W

Y

C

L

G

S

I

F

P

P

F

L

V

V

L

M

F

V

C

M

Y

Y

A

I

A

G

Y

-

H

H

V

K

T

I

H

Y

R

K

R

R

N

N

L

W

K

K

A297 (≠ S220) 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, 94% coverage: 13:454/469 of query aligns to 278:804/852 of Q03770

query
sites
Q03770

K

Q

R

R

T

K

M

L

K

K

V

V

R

R

H

H

L

I

V

Q

M

M

L

L

S

S

L

I

G

G

G

A

V

C

I

F

G

S

T

V

G

G

L

L

F

F

F

L

N

T

T

S

G

G

Y

K

I

A

I

F

S

S

T

I

T

A

G

G

A

P

A

F

G

G

T

T

L

L

A

G

Y

F

L

G

I

L

G

T

A

G

L

S

V

I

W

L

L

A

V

T

M

M

V

L

C

S

L

F

G

T

E

E

L

L

A

S

V

T

A

L

M

I

P

P

E

V

T

S

G

S

A

G

F

F

H

S

V

G

Y

L

A

A

A

S

R

R

Y

F

L

V

S

E

P

D

A

A

T

F

G

G

Y

F

T

A

V

L

A

G

W

W

L

T

Y

Y

W

W

L

I

T

S

W

C

T

M

V

L

A

A

L

L

G

P

S

A

S

Q

L

V

T

S

A

S

G
x
T

F

F

C

Y

M

L

Q

S

Y

Y

W

Y

F

N

P

N

-

V

-

N

-

I

-

S

-

K

-

G

-

V

T

T

T

A

P

G

V

F

W

I

L

T

W

L

C

F

L

S

V

A

F

F

C

S

I

I

A

V

I

V

Y

N

L

L

N

D

I

V

V

S

S

-

T

-

R

-

F

-

A

I

E

M

G

G

E

E

F

I

W

V

F

Y

-

V

-

A

-

G

-

I

-

S

-

K

S

V

I

I

K

A

V

I

V

L

T

M

I

V

I

F

A

T

F

M

I

I

L

L

G

N

A

A

G

G

-

H

-

G

-

N

A

D

M

I

F

H

G

E

F

G

I

V

P

G

M

F

K

R

D

Y

G

W

S

D

A

S

P

K

G

S

L

V

S

R

N

N

L

L

T

T

A

Y

S

G

G

L

W

Y

L

R

P

P

-

T

-

F

-

D

-

L

-

A

-

D

-

A

-

G

H

E

G

G

T

S

-

K

-

G

-

I

-

S

-

G

-

P

-

K

-

G

-

R

-

F

L

L

P

A

I

T

L

A

M

S

T

V

M

M

V

L

A

I

V

S

N

T

F

F

A

A

F

F

S

S

G

G

T

V

E

E

L

M

I

T

G

F

I

L

A

A

A

S

G

G

E

E

T

A

E

I

Q

N

P

P

Q

R

K

K

A

T

L

I

P

P

L

S

A

A

I

T

R

K

T

R

T

T

V

F

A

S

R

I

L

V

I

L

I

I

F

S

F

Y

I

V

G

F

T

L

V

I

F

F

V

S

L

V

-

G

-

I

-

N

-

I

-

Y

-

S

-

G

-

D

-

P

-

R

-

L

-

S

-

Y

-

F

-

P

-

G

-

I

-

S

-

E

-

K

-

R

-

Y

A

E

A

A

L

I

I

I

P

K

-

G

-

T

-

G

M

M

D

D

-

W

-

R

-

L

-

R

-

T

-

N

-

C

Q

R

A

G

G

G

I

I

-

D

-

Y

-

R

-

Q

-

I

-

S

-

V

-

G

-

T

-

G

V

Y

K

S

S

S

P

P

F

W

V

V

L

V

V

A

F

L

E

Q

K

N

I

F

G

G

I

L

P

C

Y

T

A

F

A

A

D

S

I

A

F

F

N

N

F

A

V

I

I

L

L

I

T

F

A

F

I

T

L

A

S

T

A

A

A

G

N

I

S

S

G

S

L

L

Y

F

A

S

S

C

G

S

R

R

M

T

L

L

W

Y

S

A

L

M

A

S

N

V

E

Q

N

R

T

K

L

A

P

P

R

P

C

V

F

F

A

E

R

I

V

C

N

S

H

K

R

R

G

G

V

V

P

P

V

Y

L

V

A

S

L

V

T

I

I

F

S

S

M

S

L

L

G

F

G

S

L

V

L

I

A

A

L

Y

F

I

S

A

S

V

V

D

I

Q

A

T

P

A

D

I

T

E

V

N

F

F

V

D

A

V

L

L

S

A

A

N

I

V

S

S

G

S

F

A

A

S

V

T

V

S

A

I

V

I

W

W

L

M

S

G

I

L

C

N

A

L

S

S

-

F

-

L

-

R

-

F

H

Y

Y

Y

V

A

F

L

R

K

R

Q

R

R

H

K

L

D

Q

I

A

I

G

S

G

R

T

N

L

D

Q

S

L

Y

A

P

Y

Y

R

K

A

S

P

P

L

F

Y

Q

P

P

L

Y

T

L

P

A

I

I

L

Y

G

G

F

L

L

V

L

G

C

C

L

S

L

L

A

F

C

V

V

I

G

F

L

M

A

G

F

Y

D

-

P

P

S

N

Q

F

R

I

I

H

A

H

L

F

W

W

C

S

-

T

-

K

-

A

-

F

-

S

-

A

-

Y

-

G

G

G

I

L

P

M

F

F

V

F

L

F

F

I

C

S

Y

Y

A

T

A

A

Y

Y

H

K

V

V

T382 (≠ G117) mutation T->H,L: Constitutively active, up-regulates amino acid permease transcription in response to subthreshold concentrations of amino acids.; mutation to K: In SSY1-102; constitutively active, up-regulates amino acid permease transcription in the absence of amino-acids.; mutation to R: Constitutively active, up-regulates amino acid permease transcription in the absence of amino acids.

P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
25% identity, 90% coverage: 8:427/469 of query aligns to 2:404/445 of P60061

query
sites
P60061

S

S

Q

S

D

D

N

A

F

D

K

A

R

H

T

K

M

V

K

G

V

L

R

I

H

P

L

V

V

T

M

L

L

M

S

V

L

S

G

G

G

N

V
x
I

I

M

G

G

T
x
S

G

G

L

V

F

F

F

L

N

L

T

P

G

A

Y

N

I

L

I

A

S

S

T

T

T

G

G

G

A

I

A

A

-

I

G

Y

T

G

L

W

L

L

A

V

Y

T

L

I

I

I

G

G

A

A

L

L

V

G

V

L

W

S

L

M

V

V

M

Y

V

-

C

-

L

-

G

A

E

K

L

M

A

S

V

F

A

L

M

D

P

P

E

S

T

P

G

G

A

G

F

S

H

Y

V

A

Y

Y

A

A

A

R

R

R

Y

C

L

F

S

G

P

P

A

F

T

L

G

G

Y

Y

T

Q

V

T

A

N

W

V

L

L

Y
|
Y

W

W

L

L

T
x
A

-
x
C

W

W

T

I

V

G

A
x
N

L

I

G

A

S
x
M

S

V

L

V

T

I

A

G

A

V

G

G

F

Y

C

-

M

L

Q

S

Y

Y

W

F

F

F

P

P

T

I

T

L

P

K

V

D

W

P

L

L

W

V

C

L

L

T

V

I

F

T

C

C

I

V

A

V

I

V

Y

L

-

W

-

I

-

F

-

V

L

L

N

N

I

I

V

V

S

G

T

P

R

K

F

M

F

I

A

T

E

R

G

-

E

-

F

-

W

-

F

-

S

-

I

V

I

Q

K

A

V

V

V

A

T

T

I

V

I

L

A

A

F

L

I

I

I

P

L

I

G

V

A

G

G

I

A

A

M

V

F

F

G

G

F

W

I

F

P

W

M

F

K

R

D

G

G

E

S

T

-

Y

-

M

A

A

P

W

G

N

L

V

S

S

N

G

L

L

T

G

A

T

S

F

G

G

W

-

L

-

P

-

H

-

G

-

T

-

L

-

P

A

I

I

L

Q

M

S

T

T

M

L

V

N

A

V

V

T

N

L

F
x
W

A
x
S

F

F

S
x
I

G

G

T

V

E

E

L

S

I

A

G

S

I

V

A

A

G

G

E

V

T

V

E

K

Q

N

P

P

Q

K

K

R

A

N

L

V

P

P

L

I

A

A

I

T

R

I

T

G

V

V

A

L

R

I

L

A

I

A

I

V

F

C

F

Y

I

V

G

L

T

S

V

T

F

T

V

A

L

I

A

M

A

G

L

M

I

I

P

P

M

N

D

A

Q

A

A

L

G

R

I

V

V

S

K

A

S

S

P

P

F

F

V

G

L

D

V

A

F

A

E

R

K

M

I

A

G

L

I

G

P

D

Y

T

A

A

A

G

D

A

I

I

F

V

N

S

F

F

V

C

I

A

L

A

T

A

A

G

I

C

L

L

S

G

A

S

A

L

N

G

S

G

G
x
W

L

T

Y

L

A

L

S

A

G

G

R

Q

M

T

L

A

W

K

S

A

L

A

A

A

N

D

E

D

N

G

T

L

L

F

P

P

R

P

C

I

F

F

A

A

R

R

V

V

N

N

H

K

R

A

G

G

V

T

P

P

V

V

L

A

A

G

L

L

T

I

I

I

S

-

M

-

L

V

G

G

G

I

L

L

L

M

A

T

L

I

F

F

S

Q

-

L

S

S

V

S

I

I

A

S

P

P

D

N

T

A

V

T

-

K

-

E

F

F

V

G

A

L

L

V

S

S

A

S

I

V

S
|
S

G

V

F

I

A

F

V

T

V

L

A

V

V

P

W

Y

L

L

S

Y

I

T

C

C

A

A

S

A

H

L

Y

L

V

L

F

L

R

G

R

H

R

G

H

H

L

F

Q

G

A

K

G

A

G

-

T

-

L

-

Q

-

L

-

A

-

Y

-

R

-

A

R

P

P

L

A

Y

Y

P

L

L

A

T

V

P

T

I

T

L

I

G

A

F

F

L

L

L

Y

C

C

L

I

L

W

A

A

C

V

V

V

G

G

I23 (≠ V29) binding agmatine; binding L-arginine
S26 (≠ T32) binding L-arginine
Y93 (= Y101) mutation to L: Greatly decreased Arg uptake into liposomes.
A96 (≠ T104) binding agmatine; binding L-arginine
C97 (vs. gap) binding agmatine
N101 (≠ A108) 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 (≠ S111) binding agmatine; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
W202 (≠ F217) binding L-arginine; mutation to L: Halves Arg uptake into liposomes.
S203 (≠ A218) binding agmatine
I205 (≠ S220) binding agmatine; binding L-arginine; mutation to A: About wild-type affinity for Arg and Agm.
W293 (≠ G308) 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 (= S371) binding L-arginine; mutation to A: 20% decreased affinity for Arg, 40% decrease affinity for Agm.

P60063 Arginine/agmatine antiporter from Escherichia coli O157:H7 (see 3 papers)
25% identity, 90% coverage: 8:427/469 of query aligns to 2:404/445 of P60063

query
sites
P60063

S

S

Q

S

D

D

N

A

F

D

K

A

R

H

T

K

M

V

K

G

V

L

R

I

H

P

L

V

V

T

M

L

L

M

S

V

L

S

G

G

G
x
N

V
x
I

I

M

G
|
G

T
x
S

G
|
G

L

V

F

F

F

L

N

L

T

P

G

A

Y

N

I

L

I

A

S

S

T

T

T

G

G

G

A

I

A

A

-

I

G

Y

T

G

L

W

L

L

A

V

Y

T

L

I

I

I

G

G

A

A

L

L

V

G

V

L

W

S

L

M

V

V

M

Y

V

-

C

-

L

-

G

A

E

K

L

M

A

S

V

F

A

L

M

D

P

P

E

S

T

P

G

G

A

G

F

S

H
x
Y

V

A

Y

Y

A

A

A

R

R

R

Y

C

L

F

S

G

P

P

A

F

T

L

G

G

Y
|
Y

T

Q

V

T

A

N

W

V

L

L

Y
|
Y

W

W

L

L

T
x
A

-
x
C

W

W

T

I

V

G

A
x
N

L

I

G

A

S

M

S

V

L

V

T

I

A

G

A

V

G

G

F

Y

C

-

M

L

Q

S

Y

Y

W

F

F

F

P

P

T

I

T

L

P

K

V

D

W

P

L

L

W

V

C

L

L

T

V

I

F

T

C

C

I

V

A

V

I

V

Y

L

-

W

-

I

-

F

-

V

L

L

N

N

I

I

V

V

S

G

T

P

R

K

F

M

F

I

A

T

E

R

G

-

E

-

F

-

W

-

F

-

S

-

I

V

I

Q

K

A

V

V

V

A

T

T

I

V

I

L

A

A

F

L

I

I

I

P

L

I

G

V

A

G

G

I

A

A

M

V

F

F

G

G

F

W

I

F

P

W

M

F

K

R

D

G

G

E

S

T

-

Y

-

M

A

A

P

W

G

N

L

V

S

S

N

G

L

L

T

G

A

T

S

F

G

G

W

-

L

-

P

-

H

-

G

-

T

-

L

-

P

A

I

I

L

Q

M

S

T

T

M

L

V

N

A

V

V

T

N

L

F
x
W

A

S

F

F

S
x
I

G
|
G

T
x
V

E
|
E

L
x
S

I
x
A

G

S

I

V

A

A

G

G

E

V

T

V

E

K

Q

N

P

P

Q

K

K

R

A

N

L

V

P

P

L

I

A

A

I

T

R

I

T

G

V

V

A

L

R

I

L

A

I

A

I

V

F

C

F

Y

I

V

G

L

T

S

V

T

F

T

V

A

L

I

A

M

A

G

L

M

I

I

P

P

M

N

D

A

Q

A

A

L

G

R

I

V

V

S

K

A

S

S

P

P

F

F

V

G

L

D

V

A

F

A

E

R

K

M

I

A

G

L

I

G

P

D

Y

T

A

A

A

G

D

A

I

I

F

V

N

S

F

F

V

C

I

A

L

A

T

A

A

G

I

C

L

L

S

G

A

S

A

L

N

G

S

G

G
x
W

L

T

Y

L

A

L

S

A

G

G

R

Q

M

T

L

A

W

K

S

A

L

A

A

A

N

D

E

D

N

G

T

L

L

F

P

P

R

P

C

I

F

F

A

A

R

R

V

V

N

N

H

K

R

A

G

G

V

T

P

P

V

V

L

A

A

G

L

L

T

I

I

I

S

-

M

-

L

V

G

G

G

I

L

L

L

M

A

T

L

I

F
|
F

S

Q

-

L

S

S

V

S

I

I

A

S

P

P

D

N

T

A

V

T

-

K

-

E

F

F

V

G

A

L

L

V

S

S

A

S

I

V

S
|
S

G

V

F

I

A

F

V

T

V

L

A

V

V

P

W
x
Y

L

L

S

Y

I

T

C

C

A

A

S

A

H

L

Y

L

V

L

F

L

R

G

R

H

R

G

H

H

L

F

Q

G

A

K

G

A

G

-

T

-

L

-

Q

-

L

-

A

-

Y

-

R

-

A

R

P

P

L

A

Y

Y

P

L

L

A

T

V

P

T

I

T

L

I

G

A

F

F

L

L

L

Y

C

C

L

I

L

W

A

A

C

V

V

V

G

G

N22 (≠ G28) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
I23 (≠ V29) binding L-arginine
GSG 25:27 (≠ GTG 31:33) Helix-breaking GSG motif TM1
S26 (≠ T32) binding L-arginine; mutation to K: 5% Agm antiport.
G27 (= G33) binding L-arginine
Y74 (≠ H82) mutation to A: 50% antiport activity at pH 6.0, 10-fold higher than wild-type antiport activity at pH 7.5, i.e. loss of pH-dependence of substrate transport. No change in binding of Arg or Agm.; mutation Y->C,H,L,M,Q,S: Loss of pH-dependence of substrate transport.; mutation to F: Approximately wild-type antiport.
Y87 (= Y95) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
Y93 (= Y101) 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 (≠ T104) binding L-arginine
C97 (vs. gap) binding L-arginine
N101 (≠ A108) binding L-arginine
W202 (≠ F217) Periplasmic (proximal) gate; binding L-arginine
I205 (≠ S220) binding L-arginine
GVESA 206:210 (≠ GTELI 221:225) Helix-breaking GVESA motif TM6
E208 (= E223) mutation E->A,D: 5-10% Agm antiport.
W293 (≠ G308) binding L-arginine
F337 (= F354) mutation to A: Severely decreased antiport.
S357 (= S371) binding L-arginine
Y365 (≠ W379) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.

5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
25% identity, 86% coverage: 27:427/469 of query aligns to 17:400/437 of 5j4nA

query
sites
5j4nA

G

G

G

N

V
x
I

I

M

G

G

T

S

G

G

L

V

F

F

F

L

N

L

T

P

G

A

Y

N

I

L

I

A

S

S

T

T

T

G

G

G

A

I

A

A

-

I

G

Y

T

G

L

W

L

L

A

V

Y

T

L

I

I

I

G

G

A

A

L

L

V

G

V

L

W

S

L

M

V

V

M

Y

V

-

C

-

L

-

G

A

E

K

L

M

A

S

V

F

A

L

M

D

P

P

E

S

T

P

G

G

A

G

F

S

H

Y

V

A

Y

Y

A

A

A

R

R

R

Y

C

L

F

S

G

P

P

A

F

T

L

G

G

Y

Y

T

Q

V

T

A

N

W

V

L

L

Y

Y

W

W

L

L

T
x
A

-
x
C

W

W

T

I

V
x
G

A
x
N

L

I

G

A

S
x
M

S

V

L

V

T

I

A

G

A

V

G

G

F

Y

C

-

M

L

Q

S

Y

Y

W

F

F

F

P

P

T

I

T

L

P

K

V

D

W

P

L

L

W

V

C

L

L

T

V

I

F

T

C

C

I

V

A

V

I

V

Y

L

-

W

-

I

-

F

-

V

L

L

N

N

I

I

V

V

S

G

T

P

R

K

F

M

F

I

A

T

E

R

G

-

E

-

F

-

W

-

F

-

S

-

I

V

I

Q

K

A

V

V

V

A

T

T

I

V

I

L

A

A

F

L

I

I

I

P

L

I

G

V

A

G

G

I

A

A

M

V

F

F

G

G

F

W

I

F

P

W

M

F

K

R

D

G

G

E

S

T

-

Y

-

M

A

A

P

W

G

N

L

V

S

S

N

G

L

L

T

G

A

T

S

F

G

G

W

-

L

-

P

-

H

-

G

-

T

-

L

-

P

A

I

I

L

Q

M

S

T

T

M

L

V

N

A

V

V

T

N

L

F

W

A

S

F

F

S

I

G

G

T

V

E

E

L

S

I

A

G

S

I

V

A

A

G

G

E

V

T

V

E

K

Q

N

P

P

Q

K

K

R

A

N

L

V

P

P

L

I

A

A

I

T

R

I

T

G

V

V

A

L

R

I

L

A

I

A

I

V

F

C

F

Y

I

V

G

L

T

S

V

T

F

T

V

A

L

I

A

M

A

G

L

M

I

I

P

P

M

N

D

A

Q

A

A

L

G

R

I

V

V

S

K

A

S

S

P

P

F

F

V

G

L

D

V

A

F

A

E

R

K

M

I

A

G

L

I

G

P

D

Y

T

A

A

A

G

D

A

I

I

F

V

N

S

F

F

V

C

I

A

L

A

T

A

A

G

I

C

L

L

S

G

A

S

A

L

N

G

S

G

G
x
W

L

T

Y

L

A

L

S

A

G

G

R

Q

M

T

L

A

W

K

S

A

L

A

A

A

N

D

E

D

N

G

T

L

L

F

P

P

R

P

C

I

F

F

A

A

R

R

V

V

N

N

H

K

R

A

G

G

V

T

P

P

V

V

L

A

A

G

L

L

T

I

I

I

S

-

M

-

L

V

G

G

G

I

L

L

L

M

A

T

L

I

F

F

S

Q

-

L

S

S

V

S

I

I

A

S

P

P

D

N

T

A

V

T

-

K

-

E

F

F

V

G

A

L

L

V

S

S

A

S

I

V

S

S

G

V

F

I

A

F

V

T

V

L

A

V

V

P

W

Y

L

L

S

Y

I

T

C

C

A

A

S

A

H

L

Y

L

V

L

F

L

R

G

R

H

R

G

H

H

L

F

Q

G

A

K

G

A

G

-

T

-

L

-

Q

-

L

-

A

-

Y

-

R

-

A

R

P

P

L

A

Y

Y

P

L

L

A

T

V

P

T

I

T

L

I

G

A

F

F

L

L

L

Y

C

C

L

I

L

W

A

A

C

V

V

V

G

G

binding agmatine: I19 (≠ V29), A92 (≠ T104), C93 (vs. gap), G96 (≠ V107), N97 (≠ A108), M100 (≠ S111), W289 (≠ G308)

P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
23% identity, 83% coverage: 7:395/469 of query aligns to 13:392/461 of P76037

query
sites
P76037

P

P

S

G

Q

K

D

T

N

R

F

L

K

R

R

K

T

S

M

L

K

K

V

L

R

W

H

Q

L

V

V

V

M

M

L

M

S

G

L

L

G

A

G

Y

V

L

I

T

G

P

T

M

G

T

L

V

F

F

F

-

N

D

T

T

G

F

Y

G

I

I

I

V

S

S

T

G

T

I

G

S

A

D

A

G

G

H

T

V

L

P

L

A

A

S

Y

Y

L

L

I

L

G

A

A

L

L

A

V

G

V

V

W

L

L

F

V

T

M

A

V

I

C

S

L

Y

G

G

E

K

L

L

A

V

V

R

A

Q

M

F

P

P

E

E

T

A

G

G

A

S

F

A

H

Y

V

T

Y

Y

A

A

A

Q

R

K

Y

S

L

I

S

N

P

P

A

H

T

V

G

G

Y

F

T

M

V

V

A

G

W

W

L

S

Y

S

W

L

L

L

T

D

W
x
Y

T

L

V

F

A

L

L

P

G

M

S

I

S

N

L

V

T

L

A

L

A

A

G

K

F

I

C

Y

M

L

Q

S

Y

A

W

L

F

F

P

P

T

E

T

V

P

P

V

P

W

W

L

V

W

W

C

V

L

V

V

T

F

F

C

V

I

A

A

I

I

L

Y

T

L

A

N

N

I

L

V

K

S

S

T

V

R

N

F

L

F

V

A

A

E

N

G

F

E

N

F

T

W

L

F

F

S

V

I

L

I

V

K

Q

V

I

V

S

T

I

I

M

I

V

A

V

F

F

I

I

I

F

L

L

-

V

-

Q

-

G

-

L

-

H

-

K

-

G

-

E

G

G

A

V

G

G

A

T

M

V

F

W

G

S

F

L

I

Q

P

P

M

F

K

I

D

S

G

E

S

N

A

A

A

H

P

-

G

-

L

-

S

-

N

-

L

-

T

-

A

-

S

-

G

-

W

-

L

-

P

-

H

-

G

-

T

L

L

I

P

P

I

I

L

I

M

T

T

G

M

A

V

T

A

I

V

V

N

C

F

F

A

S

F

F

S

L

G

G

T

F

E

D

L

A

I

V

G

T

I

T

A

L

A

S

G

E

E

E

T

T

E

P

Q

D

P

A

Q

A

K

R

A

V

L

I

P

P

L

K

A

A

I

I

R

F

T

L

T

T

V

A

A

V

R

Y

L

G

I

G

I

V

F

I

F

F

I

I

G

A

T

A

V

S

F

F

V

F

L

M

A

Q

A

L

L

F

I

F

P

P

M

-

D

-

Q

D

A

I

G

S

I

R

V

F

K

K

S

D

P

P

F

D

V

A

L

A

V

L

F

P

E

E

K

-

I

I

G

A

I

L

P

Y

Y

V

A

G

D

K

I

L

F

F

N

Q

F

S

V

I

I

F

L

L

-

C

T

T

A

T

I

F

L

V

S

N

A

T

A

L

N

A

S

S

G

G

L

L

-

A

-

S

Y

H

A

A

S

S

-

V

G

S

R

R

M

L

L

L

W

Y

S

V

L

M

A

G

N

R

E

D

N

N

T

V

L

F

P

P

-

E

R

R

C

V

F

F

A

G

R

Y

V

V

N

-

H

H

R

P

G

K

V

W

P

R

V

T

L

P

A

A

L

L

T

N

I

V

S

I

M

M

L

V

G

G

-

I

-

V

G

A

L

L

L

S

A

A

L

L

F

F

S

F

S

D

V

L

I

V

A

T

P

A

D

-

T

T

V

A

F

L

V

I

A

N

L

F

S

G

A

A

I

L

S

V

G

A

F

F

A

T

V

F

V

V

A

-

V

-

W

-

L

-

S

N

I

L

C

S

A

V

S

F

H

N

Y

H

V

F

F

W

R

R

R

K

H

G

L

M

Q

N

Y110 (≠ W105) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.

3l1lA Structure of arg-bound escherichia coli adic (see paper)
25% identity, 86% coverage: 27:427/469 of query aligns to 15:387/423 of 3l1lA

query
sites
3l1lA

G

G

G

A

V
x
I

I

M

G

G

T
x
S

G
|
G

L

V

F

F

F

L

N

L

T

P

G

A

Y

N

I

L

I

A

S

S

T

T

T

G

G

G

A

I

A

A

-

I

G

Y

T

G

L

W

L

L

A

V

Y

T

L

I

I

I

G

G

A

A

L

L

V

G

V

L

W

S

L

M

V

V

M

Y

V

-

C

-

L

-

G

A

E

K

L

M

A

S

V

F

A

L

M

D

P

P

E

S

T

P

G

G

A

G

F

S

H

Y

V

A

Y

Y

A

A

A

R

R

R

Y

C

L

F

S

G

P

P

A

F

T

L

G

G

Y

Y

T

Q

V

T

A

N

W

V

L

L

Y

Y

W

W

L

L

T

A

-

C

W

W

T

I

V
x
G

A
x
N

L

I

G

A

S

M

S

V

L

V

T

I

A

G

A

V

G

G

F

Y

C

-

M

L

Q

S

Y

Y

W

F

F

F

P

P

T

I

-

L

T

K

P

D

V

P

W

W

-

V

-

L

-

T

L

I

W

T

C

C

L

V

V

V

F

V

C

L

I

W

A

I

I

F

Y

V

L

L

N

N

I

I

V

V

S

G

T

P

R

K

F

M

F

I

A

T

E

R

G

V

E

Q

F

-

W

-

F

-

S

-

I

-

K

A

V

V

V

A

T

T

I

V

I

L

A

A

F

L

I

I

I

P

L

I

G

V

A

G

G

I

A

A

M

V

F

F

G

G

F

W

I

F

P

W

M

F

K

R

D

G

G

E

S

T

A

Y

A

M

P

A

G

A

L

I

-

Q

S

S

N

T

L

L

T

N

A

V

S

T

G

L

W
|
W

L

-

P

-

H

-

G

-

T

-

L

-

P

-

I

-

L

-

M

-

T

-

M

-

V

-

A

-

V

-

N

-

F

-

A
x
S

F

F

S
x
I

G

G

T

V

E

E

L

S

I

A

G

S

I

V

A

A

G

G

E

V

T

V

E

K

Q

N

P

P

Q

K

K

R

A

N

L

V

P

P

L

I

A

A

I

T

R

I

T

G

V

V

A

L

R

I

L

A

I

A

I

V

F

C

F

Y

I

V

G

L

T

S

V

T

F

T

V

A

L

I

A

M

A

G

L

M

I

I

P

P

M

N

D

A

Q

A

A

L

G

R

I

V

V

S

K

A

S

S

P

P

F

F

V

G

L

D

V

A

F

A

E

R

K

M

I

A

G

L

I

G

P

D

Y

T

A

A

A

G

D

A

I

I

F

V

N

S

F

F

V

C

I

A

L

A

T

A

A

G

I

C

L

L

S

G

A

S

A

L

N

G

S

G

G
x
W

L

T

Y

L

A

L

S

A

G

G

R

Q

M

T

L

A

W

K

S

A

L

A

A

A

N

D

E

D

N

G

T

L

L

F

P

P

R

P

C

I

F

F

A

A

R

R

V

V

N

N

H

K

R

A

G

G

V

T

P

P

V

V

L

A

A

G

L

L

T

I

I

I

S

-

M

-

L

V

G

G

G

I

L

L

L

M

A

T

L

I

F

F

S

Q

-

L

S

S

V

S

I

I

A

S

P

P

D

N

T

A

V

T

-

K

-

E

F

F

V

G

A

L

L

V

S

S

A

S

I

V

S

S

G

V

F

I

A

F

V

T

V

L

A

V

V

P

W

Y

L

L

S

Y

I

T

C

C

A

A

S

A

H

L

Y

L

V

L

F

L

R

G

R

H

R

G

H

H

L

F

Q

G

A

K

G

A

G

-

T

-

L

-

Q

-

L

-

A

-

Y

-

R

-

A

R

P

P

L

A

Y

Y

P

L

L

A

T

V

P

T

I

T

L

I

G

A

F

F

L

L

L

Y

C

C

L

I

L

W

A

A

C

V

V

V

G

G

binding arginine: I17 (≠ V29), S20 (≠ T32), G21 (= G33), G94 (≠ V107), N95 (≠ A108), W185 (= W200), S186 (≠ A218), I188 (≠ S220), W276 (≠ G308)

6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
22% identity, 47% coverage: 200:421/469 of query aligns to 211:421/458 of 6f34A

query
sites
6f34A

W

F

L

M

P

P

H

Y

G

G

T

F

L

S

P

G

I

V

L

A

M

T

T

G

M

A

V

A

A

T

V

V

N

F

F
|
F

A
|
A

F

Y

S
x
I

G

G

T

F

E

D

L

A

I

V

G

S

I

T

A

A

G

E

E

E

T

V

E

R

Q

N

P

P

Q

Q

K

R

A

D

L

M

P

P

L

I

A

G

I

I

R

I

T

V

T

S

V

L

A

L

R

V

L

C

I

T

I

L

F

L

F

Y

I

I

G

A

T

V

V

S

F

L

V

V

L

L

A

T

A

G

L

I

I

V

P

P

M

Y

D

E

Q

Q

A

L

G

N

I

-

V

V

K

K

S

N

P

P

F

V

V

A

L

F

V

A

F

L

E

N

K

Y

I

I

G

H

I
x
Q

P

D

Y

W

A
x
V

A

A

D

G

I

F

F

I

N

S

F

L

V

G

I

A

L

I

T

A

A

G

I

I

L

T

S

T

A
x
V

A

L

N

L

S

V

G

S

L

M

Y

Y

A

G

S

Q

G

T

R

R

M

L

L

F

W

Y

S

A

L

I

A

S

N

R

E

D

N

G

T

L

L

L

P

P

R

K

C

V

F

F

A

A

R

R

V

I

N

S

-

P

H

T

R

R

G

Q

V

V

P

P

V

Y

L

V

A

N

L

T

T

W

I

L

S

T

M

-

L

-

G

G

G

A

L

A

L

V

A

A

L

V

F

F

S

A

S

G

V

I

I

I

A

P

P

L

D

N

T

K

V

-

F

-

V

-

A

-

L

L

S

A

A

E

I

L

S

T

G

N

F

I

A

G

V

T

V

L

A

F

V

A

W

F

L

I

S

T

I

V

C

S

A

I

S

G

H

V

Y

L

V

V

F

L

R

R

R

K

R

T

H

Q

L

P

Q

D

A

L

G

-

T

-

L

-

Q

-

Q

K

L

R

A

A

Y

F

R

R

A

V

P

P

L

F

Y

V

P

P

L

V

T

V

P

P

I

I

L

L

G

A

F

V

L

L

L

F

C

C

binding arginine: F228 (= F217), A229 (= A218), I231 (≠ S220), V314 (≠ A304)
binding : Q296 (≠ I286), V299 (≠ A289)

Sites not aligning to the query:

binding arginine: 40, 42, 43, 44, 115, 116, 119
binding cholesterol: 201, 202
binding : 28, 30, 31, 34, 178, 179, 186, 187, 190, 194

5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
22% identity, 47% coverage: 200:421/469 of query aligns to 209:419/456 of 5oqtA

query
sites
5oqtA

W

F

L

M

P

P

H

Y

G

G

T

F

L

S

P

G

I

V

L

A

M

T

T

G

M

A

V

A

A

T

V

V

N

F

F
|
F

A
|
A

F

Y

S
x
I

G

G

T

F

E

D

L

A

I

V

G

S

I

T

A

A

G

E

E

E

T

V

E

R

Q

N

P

P

Q

Q

K

R

A

D

L

M

P

P

L

I

A

G

I

I

R

I

T

V

T

S

V

L

A

L

R

V

L

C

I

T

I

L

F

L

F

Y

I

I

G

A

T

V

V

S

F

L

V

V

L

L

A

T

A

G

L

I

I

V

P

P

M

Y

D

E

Q

Q

A

L

G

N

I

-

V

V

K

K

S

N

P

P

F

V

V

A

L

F

V

A

F

L

E

N

K

Y

I

I

G

H

I
x
Q

P

D

Y

W

A
x
V

A

A

D

G

I

F

F

I

N

S

F

L

V

G

I

A

L

I

T

A

A

G

I

I

L

T

S

T

A

V

A

L

N

L

S

V

G

M

L

M

Y

Y

A

G

S

Q

G

T

R

R

M

L

L

F

W

Y

S

A

L

I

A

S

N

R

E

D

N

G

T

L

L

L

P

P

R

K

C

V

F

F

A

A

R

R

V

I

N

S

-

P

H

T

R

R

G

Q

V

V

P

P

V

Y

L

V

A

N

L

T

T

W

I

L

S

T

M

-

L

-

G

G

G

A

L

A

L

V

A

A

L

V

F

F

S

A

S

G

V

I

I

I

A

P

P

L

D

N

T

K

V

-

F

-

V

-

A

-

L

L

S

A

A

E

I

L

S

T

G

N

F

I

A

G

V

T

V

L

A

F

V

A

W

F

L

I

S

T

I

V

C

S

A

I

S

G

H

V

Y

L

V

V

F

L

R

R

R

K

R

T

H

Q

L

P

Q

D

A

L

G

-

T

-

L

-

Q

-

Q

K

L

R

A

A

Y

F

R

R

A

V

P

P

L

F

Y

V

P

P

L

V

T

V

P

P

I

I

L

L

G

A

F

V

L

L

L

F

C

C

binding alanine: F226 (= F217), A227 (= A218), I229 (≠ S220)
binding : Q294 (≠ I286), V297 (≠ A289)

Sites not aligning to the query:

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

9h76A Bacterial lat transporter basc in complex with l-ala and nb53 (see paper)
21% identity, 91% coverage: 26:452/469 of query aligns to 12:429/430 of 9h76A

query
sites
9h76A

L

V

G

G

G

T

V

V

I

I

G
|
G

T
x
A

G
|
G

L

I

F

F

N

K

T

P

G

T

Y

A

I

V

I

Y

S

G

T

A

G

G

A

A

A

P

G

G

T

L

-

G

L

L

A

A

Y

W

L

F

I

V

G

A

A

G

L

I

V

I

V

T

W

I

L

A

V

G

M

G

V

L

C

T

L

V

G

A

E

E

L

I

A

G

V

T

A

I

M

Y

P

P

E

Q

T

T

G

G

A

G

F

M

H

M

V

I

Y

Y

A

L

A

E

R

K

Y

V

L

Y

S

G

P

R

A

W

T

L

G

G

Y

F

T

L

V

V

A

G

W

W

L

A

Y

Q

W

M

L

V

T

I

W

Y

-

Y

-

P

-

A

T

N

V

I

A

A

L

A

G

L

S

A

S

I

L

I

T

F

A

A

A

T

G

Q

F

F

C

V

M

N

Q

L

Y

F

W

A

F

L

P

S

T

D

T

S

P

T

V

I

W

V

L

P

W

T

C

A

L

I

V

L

F

T

C

S

I

I

A

F

I

L

Y

M

L

G

L

V

N

N

I

F

V

L

S

G

T

T

R

K

F

Y

F

S

A

G

E

W

G

I

E

Q

F

T

W

L

F

A

S

T

I

I

I

L

K

K

V

L

V

I

T

P

I

L

I

V

A

V

F

I

I

I

I

V

L

A

G

G

-

L

-

Y

-

P

A

G

G

G

A

G

M

V

F

I

G

R

F

L

I

V

P

P

M

F

K

S

D

V

G

-

S

E

A

T

A

H

P

P

G

V

L

L

S

T

N

S

L

F

T

G

A

S

S

A

G

-

W

-

L

-

P

-

H

-

G

-

T

-

L

-

P

-

I

-

L

-

M

-

T

-

M

L

V

I

A

A

V

T

N

L

F

F

A

A

F

Y

S
x
D

G

G

T

W

E

I

L

N

I

V

G

G

I

T

A

L

A

A

G

G

E

E

T

M

E

K

Q

N

P

P

Q

G

K

K

A

M

L

L

P

P

L

K

A

V

I

I

R

I

T

G

V

L

A

S

R

I

L

V

I

M

I

A

F

V

F

Y

I

L

G

L

T

T

V

N

F

I

V

A

L

Y

A

L

A

F

L

V

I

L

P

D

M

S

D

S

Q

Q

A

L

G

A

I

G

V

T

K

D

S

T

P

P

F

A

V

A

L

L

V

V

-

A

-

S

-

H

-

L

F

F

E

E

K

G

I

I

G

G

I

-

P

-

Y

-

A

-

A

S

D

K

I

L

F

V

N

T

F

I

V

G

I

I

L

L

T

I

A

S

I

V

L

F

S

G

A

G

A

I

N

N

S

G

G

Y

L

I

Y

I

A

S

S

G

G

L

R

R

M

V

L

P

W

Y

S

A

L

L

A

A

N

T

E

Q

N

K

T

M

L

L

P

P

R

F

C

S

-

D

-

W

F

F

A

A

R

R

V

I

N

N

H

P

R

K

G

-

V

-

P

-

V

-

L

-

A

-

L

T

T

N

I

L

S

P

M

I

L

N

G

G

L

L

L

V

A

M

L

L

F

G

S

I

S

A

V

I

I

V

A

M

P

I

D

L

T

T

V

-

F

-

V

G

A

Q

L

F

S

N

A

Q

I

L

S

T

G

D

F

L

A

I

V

V

V

F

A

V

V

I

W

W

L

F

S

F

I

I

C

T

A

L

S

T

H

F

Y

I

-

A

V

V

F

I

R

I

R

L

R

R

H

K

L

T

Q

Q

A

P

G

D

G

-

T

-

L

-

Q

I

Q

E

L

R

A

P

Y

Y

R

R

A

V

P

P

L

F

Y

Y

P

P

L

V

T

I

P

P

I

L

L

I

G

A

F

I

L

I

L

G

C

G

L

L

L

Y

A

I

C

I

V

F

G

N

-

T

L

L

A

I

F

V

D

Q

P

P

S

K

Q

N

R

A

-

F

-

I

-

G

-

I

I

L

A

L

L

T

W

L

C

I

G

G

I

I

P

P

F

I

V

Y

L

F

F

Y

C

C

Y

K

A

K

Y

Y

binding alanine: G17 (= G31), A18 (≠ T32), G19 (= G33), D200 (≠ S220)

6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
21% identity, 91% coverage: 26:452/469 of query aligns to 14:431/433 of 6f2wA

query
sites
6f2wA

L

V

G

G

G

T

V
|
V

I

I

G
|
G

T
x
A

G
|
G

L

I

F

F

N

K

T

P

G

T

Y

A

I

V

I

Y

S

G

T

A

G

G

A

A

A

P

G

G

T

L

-

G

L

L

A

A

Y

W

L

F

I

V

G

A

A

G

L

I

V

I

V

T

W

I

L

A

V

G

M

G

V

L

C

T

L

V

G

A

E

E

L

I

A

G

V

T

A

I

M

Y

P

P

E

Q

T

T

G

G

A

G

F

M

H

M

V

I

Y

Y

A

L

A

E

R

K

Y

V

L

Y

S

G

P

R

A

W

T

L

G

G

Y

F

T

L

V

V

A

G

W

W

L

A

Y

Q

W

M

L

V

T

I

W

Y

-

Y

-

P

-

A

T

N

V

I

A

A

L

A

G

L

S

A

S

I

L

I

T

F

A

A

A

T

G

Q

F

F

C

V

M

N

Q

L

Y

F

W

A

F

L

P

S

T

D

T

S

P

T

V

I

W

V

L

P

W

T

C

A

L

I

V

L

F

T

C

S

I

I

A

F

I

L

Y

M

L

G

L

V

N

N

I

F

V

L

S

G

T

T

R

K

F

Y

F

S

A

G

E

W

G

I

E

Q

F

T

W

L

F

A

S

T

I

I

I

L

K

K

V

L

V

I

T

P

I

L

I

V

A

V

F

I

I

I

I

V

L

A

G

G

-

L

-

Y

-

P

A

G

G

G

A

G

M

V

F

I

G

R

F

L

I

V

P

P

M

F

K

S

D

V

G

-

S

E

A

T

A

H

P

P

G

V

L

L

S

T

N

S

L

F

T

G

A

S

S

A

G

-

W

-

L

-

P

-

H

-

G

-

T

-

L

-

P

-

I

-

L

-

M

-

T

-

M

L

V

I

A

A

V

T

N

L

F
|
F

A
|
A

F

Y

S
x
D

G

G

T

W

E

I

L

N

I

V

G

G

I

T

A

L

A

A

G

G

E

E

T

M

E

K

Q

N

P

P

Q

G

K

K

A

M

L

L

P

P

L

K

A

V

I

I

R

I

T

G

V

L

A

S

R

I

L

V

I

M

I

A

F

V

F

Y

I

L

G

L

T

T

V

N

F

I

V

A

L

Y

A

L

A

F

L

V

I

L

P

D

M

S

D

S

Q

Q

A

L

G

A

I

G

V

T

K

D

S

T

P

P

F

A

V

A

L

L

V

V

-

A

-

S

-

H

-

L

F

F

E

E

K

G

I

I

G

G

I

-

P

-

Y

-

A

-

A

S

D

K

I

L

F

V

N

T

F

I

V

G

I

I

L

L

T

I

A

S

I

V

L

F

S

G

A

G

A

I

N

N

S

G

G

Y

L

I

Y

I

A

S

S

G

G

L

R

R

M

V

L

P

W

Y

S

A

L

L

A

A

N

T

E

Q

N

K

T

M

L

L

P

P

R

F

C

S

-

D

-

W

F

F

A

A

R

R

V

I

N

N

H

P

R

K

G

-

V

-

P

-

V

-

L

-

A

-

L

T

T

N

I

L

S

P

M

I

L

N

G

G

L

L

L

V

A

M

L

L

F

G

S

I

S

A

V

I

I

V

A

M

P

I

D

L

T

T

V

-

F

-

V

G

A

Q

L

F

S

N

A

Q

I

L

S

T

G

D

F

L

A

I

V

V

V

F

A

V

V

I

W

W

L

F

S

F

I

I

C

T

A

L

S

T

H

F

Y

I

-

A

V

V

F

I

R

I

R

L

R

R

H

K

L

T

Q

Q

A

P

G

D

G

-

T

-

L

-

Q

I

Q

E

L

R

A

P

Y

Y

R

R

A

V

P

P

L

F

Y

Y

P

P

L

V

T

I

P

P

I

L

L

I

G

A

F

I

L

I

L

G

C

G

L

L

L

Y

A

I

C

I

V

F

G

N

-

T

L

L

A

I

F

V

D

Q

P

P

S

K

Q

N

R

A

-

F

-

I

-

G

-

I

I

L

A

L

L

T

W

L

C

I

G

G

I

I

P

P

F

I

V

Y

L

F

F

Y

C

C

Y

K

A

K

Y

Y

binding alpha-aminoisobutyric acid: V17 (= V29), G19 (= G31), A20 (≠ T32), G21 (= G33), F199 (= F217), A200 (= A218), D202 (≠ S220)

O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
21% identity, 87% coverage: 8:416/469 of query aligns to 3:395/438 of O34739

query
sites
O34739

S

T

Q

E

D

D

N

N

-

G

F

L

K

K

R

K

T

E

M

I

K

G

V

L

R

L

H

F

L

A

V

L

M

T

L

L

S

V

L

I

G

G

G

T

V

I

I

I

G

G

T

S

G

G

L

V

F

F

F

M

N

K

T

P

G

G

Y

A

I

V

I

L

S

A

T

Y

T

S

G

G

A

D

A

S

G

K

-

M

T

A

L

L

L

F

A

A

Y

W

L

L

I

L

G

G

A

G

L

I

V

L

V

T

W

L

L

A

V

G

M

G

V

L

C

T

L

I

G

A

E

E

L

I

A

G

V

T

A

Q

M

I

P

P

E

K

T

T

G

G

A

G

F

L

H

Y

V

T

Y

Y

A

L

A

E

R

E

Y

V

L

Y

S

G

P

E

A

F

T

W

G

G

Y

F

T

L

V
x
C

A

G

W

W

L

V

Y

Q

W

I

L

I

T

I

W

Y

-

G

-

P

-

A

-

I

T

I

V

G

A

A

L

L

G

G

-

L

-

Y

-

F

S

G

S

S

L

L

T

M

A

A

A

N

G

L

F

F

C

G

M

W

Q

G

Y

S

W

G

F

L

P

S

T

K

T

V

P

I

V

G

W

I

L

I

W

A

C

V

L

L

V

F

F

L

C
|
C

I

V

A

-

I

-

Y

-

L

-

L

I

N

N

I

I

V

I

S

G

T

T

R

K

F

Y

F

G

A

G

E

F

G

V

E

Q

F

T

W

L

F

T

S

T

I

I

I

G

K

K

V

L

V

I

T

P

I

I

I

A

A
x
C

F

I

I

I

I

V

L

F

G

G

-

L

-

W

A

K

G

G

A

D

M

Q

F

H

G

I

F

F

I

T

P

A

M

V

K

N

D

E

G

-

S

-

A

-

P

-

G

S

L

I

S

S

N

D

L

M

T

N

A

F

S

G

G

A

W

-

L

-

P

-

H

-

G

-

T

-

L

-

P

-

I

-

L

-

M

-

T

A

M

I

V

L

A

A

V

T

N

L

F

F

A

A

F

Y

S

D

G

G

T

W

E

I

L

L

I

L

G

A

I

A

A

L

A

G

G

G

E

E

T

M

E

K

Q

N

P

P

Q

E

K

K

A

L

L

L

P

P

L

R

A

A

I

M

R

T

T

G

V

L

A

L

R

I

L

V

I

T

I

A

F

I

F

Y

I

I

G

F

T

I

V

N

F

F

V

A

L

L

A

L

A

H

L

I

I

L

P

S

M

A

D

N

Q

E

-

I

-

V

-

T

-

L

-

G

A

E

G

N

I

A

V

T

K

S

S

T

P

A

F

A

V

T

L

M

V

L

F

F

E

G

K

S

I

I

G

G

I

-

P

-

Y

-

A

-

A

G

D

K

I

L

F

I

N

S

F

V

V

G

I

I

L

I

T

V

A

S

I

I

L

F

S

G

A
x
C

A

L

N

N

S

G

G

K

L

V

Y

L

A

S

S

F

G

P

R

R

M

V

L

S

W

F

S

A

L

M

A

A

N

E

E

R

N

K

T

Q

L

L

P

P

R

F

C

A

F

-

A

E

R

K

V

L

N

S

H

H

R

V

G

H

-

P

-

S

-

F

-

R

V

T

P

P

V

W

L

I

A

A

L

I

T

S

I

F

S

Q

M

I

L

A

G

L

G

A

L

L

L

I

A

M

L

M

F

L

S

I

S

S

V

-

I

-

A

N

P

P

D

D

T

K

V

-

F

-

V

-

A

-

L

L

S

S

A

E

I

I

S

S

G

I

F

F

A

M

V

I

V

Y

A

I

V

F

W

Y

L

V

S

M

I

A

C

F

A

F

S

A

H

V

Y

F

V

I

F

L

R

R

R

K

R

R

H

-

L

-

Q

-

A

A

G

K

G

G

T

-

L

-

Q

E

Q

K

L

R

A

A

Y

Y

R

S

A

V

P

P

L

L

Y

Y

P

P

L

F

T

M

P

P

I

I

L

L

C94 (≠ V97) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
C141 (= C137) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
C168 (≠ A168) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
C291 (≠ A304) 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.

Query Sequence

>WP_084936496.1 NCBI__GCF_002095475.1:WP_084936496.1
MQTQETPSQDNFKRTMKVRHLVMLSLGGVIGTGLFFNTGYIISTTGAAGTLLAYLIGALV
VWLVMVCLGELAVAMPETGAFHVYAARYLSPATGYTVAWLYWLTWTVALGSSLTAAGFCM
QYWFPTTPVWLWCLVFCIAIYLLNIVSTRFFAEGEFWFSIIKVVTIIAFIILGAGAMFGF
IPMKDGSAAPGLSNLTASGWLPHGTLPILMTMVAVNFAFSGTELIGIAAGETEQPQKALP
LAIRTTVARLIIFFIGTVFVLAALIPMDQAGIVKSPFVLVFEKIGIPYAADIFNFVILTA
ILSAANSGLYASGRMLWSLANENTLPRCFARVNHRGVPVLALTISMLGGLLALFSSVIAP
DTVFVALSAISGFAVVAVWLSICASHYVFRRRHLQAGGTLQQLAYRAPLYPLTPILGFLL
CLLACVGLAFDPSQRIALWCGIPFVLFCYAAYHVTHRRNLKAGEANDVA

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