SitesBLAST

F87 (≠ A72) mutation to L: No effect on phenylalanine transport activity.
F90 (≠ Y75) mutation to L: 65% of wild-type phenylalanine transport activity.
Y92 (≠ R77) mutation to L: 41% of wild-type phenylalanine transport activity.
Y94 (≠ A79) mutation to L: 69% of wild-type phenylalanine transport activity.
W95 (≠ I80) mutation to L: 10% of wild-type phenylalanine transport activity.
F98 (≠ K83) mutation to L: No effect on phenylalanine transport activity.
F101 (= F86) mutation to L: 38% of wild-type phenylalanine transport activity.
W105 (= W90) mutation to L: 39% of wild-type phenylalanine transport activity.
Y107 (≠ V92) mutation to L: No effect on phenylalanine transport activity.
W108 (≠ L93) mutation to L: 71% of wild-type phenylalanine transport activity.
F111 (≠ Y96) 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 (≠ I103) mutation E->G,L,V,N: Loss of activity.
K168 (≠ Q153) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
E226 (≠ D207) mutation E->A,Q,K,R,W: Loss of activity.
R252 (≠ I233) mutation R->D,E,F,W,P: Loss of activity.
P341 (= P324) 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.

Sites not aligning to the query:

26 mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
54 P→A: 50% of wild-type phenylalanine transport activity.; P→G: No change in phenylalanine transport activity.; P→L: 26% of wild-type phenylalanine transport activity.
442 P→A: 46% of wild-type phenylalanine transport activity.; P→G: 52% of wild-type phenylalanine transport activity.; P→L: 43% of wild-type phenylalanine transport activity.

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)
27% identity, 83% coverage: 3:366/441 of query aligns to 27:428/629 of P30825

query
sites
P30825

R

R

L

L

Q

S

R

R

T

C

L

L

S

N

L

T

G

F

S

D

V

L

V

V

L

A

F

L

G

G

I

V

A

G

Y

S

M

T

T

L

P

G

I

A

I

G

V

V

L

Y

G

V

T

L

F

A

G

G

I

A

L

V

A

A

Q

R

S

E

T

N

A

A

G

G

M

-

V

-

P

P

A

A

-

I

-

V

-

I

A

S

Y

F

L

L

A

I

A

A

L

A

V

L

A

A

M

S

F

V

F

L

T

A

A

G

M

L

S

C

Y

Y

G

G

R

E

M

F

A

G

S

A

A

R

F

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P

P

V

K

A

T

G

G

S

S

A

A

Y

Y

S

L

Y

Y

V

S

R

Y

K

V

A

T

I

V

S

G

P

E

K

L

L

W

G

A

F

F

I

I

A

T

G

G

W

W

A

N

V

L

L

I

L

L

D

S

Y

Y

L

I

F

I

L

G

P

T

M

S

A

S

I

V

-

A

-

R

-

A

W

W

-

S

-

A

-

T

-

F

-

D

-

E

L

L

I

I

G

G

A

R

-

P

-

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-

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-

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-

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-

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A

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Y

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N

T

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L

A

N

F

A

P

P

A

G

V

V

-

L

-

A

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-

N

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-

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F

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A

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F

I

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L

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L

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G

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K

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A

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N

A

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F

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L

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-

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P

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L

Q

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E

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D

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F

-

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-
x
N

-

T

-

S

-

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-

R

-

L

-

C

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L

N

N

G

N

D

D

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-

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-

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-

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A

A

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L

L

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D

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F

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G

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L

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L

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N

A

L

A

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C

V

V

I

L

N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine

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)
24% identity, 72% coverage: 27:342/441 of query aligns to 35:351/457 of P15993

query
sites
P15993

L

L

G

G

T

S

F

A

G

S

I

V

L

I

A

Q

Q

S

S

A

T

G

A

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A

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A

A

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-

F

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G

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M

A

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P

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V

A

A

G

G

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S

A

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A

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G

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L

Y
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Y

L

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F

L

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A

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M

A

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-

F

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P

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-

G

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A

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A

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F

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D

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F

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A

F

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Q

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L

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P

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K

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A

F

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L

-

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-

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R

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N

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A

A

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L

A

L

L

A

C

L

V

K

L

L

I

D

N

Y103 (= Y96) 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%.

P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
24% identity, 69% coverage: 33:338/441 of query aligns to 43:359/489 of P25737

query
sites
P25737

L

I

A

S

Q

Q

S

A

T

G

A

P

G

G

M

G

V

A

P

L

A

L

A

S

Y

Y

L

M

A

L

A

I

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Y

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N

A

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E

P

E

K

G

L

F

G

G

F

F

I

A

A

L

G

G

W

W

A

N

V
x
Y

L

W

L

Y

D

N

Y
x
W

L

A

F

-

L

V

P

T

M

I

A

A

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D

L

L

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A

A

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F

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A

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F

F

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N

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K

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-

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S
x
D

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V

D

K

S
x
D

-

I

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S

-

V

A

S

A

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D

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A

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G

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A

-

V

F

L

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A

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S

S

A

G

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M

A

Y

S

A

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R

L

M

L

L

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Y

A

T

M

L

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A

R

C

D

D

G

G

V

K

L

A

P

P

K

R

S

I

F

F

F

-

G

-

T

A

L

K

H

L

E

S

R

R

F

G

G

G

T

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P

P

I

R

N

N

S

A

I

L

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L

A

C

T

A

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V

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A

A

L

G

L

L

A

C

Y102 (≠ V92) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
W106 (≠ Y96) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
K163 (≠ Q153) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
F216 (≠ Y201) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
E222 (≠ D207) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
E230 (= E215) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
D275 (≠ S256) 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 (≠ S259) 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.

7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
23% identity, 82% coverage: 31:392/441 of query aligns to 24:392/455 of 7p9uB

query
sites
7p9uB

G

G

I

V

L

L

A

Q

Q

N

S

T

-

G

T

S

A

V

G

G

M

M

V

S

P

L

A

T

A

I

Y

W

L

T

A

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A

C

L

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V

A

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F

L

F

F

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G

A

A

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S

Y

Y

G

A

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E

M

L

A

G

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A

T

F

I

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K

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K

A

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G

G

S

G

A

H

Y

Y

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Y

Y

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K

E

A

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P

K

L

L

P

G

A

F

F

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A

R

G

V

W

W

A

V

V

E

L

L

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binding glutamic acid: R91 (≠ L99), A94 (= A102), I98 (= I106), Y200 (= Y201), A203 (≠ L204), F206 (≠ D207), Y207 (≠ A208)

7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
23% identity, 82% coverage: 31:392/441 of query aligns to 24:392/453 of 7epzB

query
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7epzB

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binding 2-[(1S)-1-[4-[2-(4-chloranylphenoxy)ethanoyl]piperazin-1-yl]ethyl]-3-(2-ethoxyphenyl)quinazolin-4-one: Q147 (≠ N146), L208 (≠ V209), F210 (≠ T211), F292 (≠ S291)

Sites not aligning to the query:

binding 2-[(1S)-1-[4-[2-(4-chloranylphenoxy)ethanoyl]piperazin-1-yl]ethyl]-3-(2-ethoxyphenyl)quinazolin-4-one: 8

Q9UPY5 Cystine/glutamate transporter; Amino acid transport system xc-; Calcium channel blocker resistance protein CCBR1; Solute carrier family 7 member 11; xCT from Homo sapiens (Human) (see 4 papers)
23% identity, 82% coverage: 31:392/441 of query aligns to 68:436/501 of Q9UPY5

query
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Q9UPY5

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C86 (≠ A48) mutation to S: Does not affect L-cystine transport activity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
R135 (≠ L99) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
C158 (≠ S113) modified: Interchain (with C-210 in SLC3A2); mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
Q191 (≠ N146) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
C197 (≠ V152) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435.
K198 (≠ Q153) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
Y244 (= Y201) binding
F254 (≠ T211) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
C271 (vs. gap) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
C327 (≠ I282) mutation to A: Does not affect L-glutamate transport activity. Does not affect location at cell membrane Does not affect expression level.; mutation to L: Loss of L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Loss of inhibitio nof L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid. Decrease L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to T: Does not affect L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.
F336 (≠ S291) mutation to A: Decreases L-cystine transport activity about 50%. Increases sensitivity to erastin-induced ferroptosis. Significantly decreases the L-cystine transport activity.; mutation to Y: Does not affect L-cystine transport activity.
R396 (≠ A354) mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.; mutation to N: Loss of L-cystine transport activity.
C414 (≠ G372) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
C435 (≠ G391) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.

Q9URZ4 Cationic amino acid transporter 1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
24% identity, 41% coverage: 50:230/441 of query aligns to 127:311/587 of Q9URZ4

query
sites
Q9URZ4

V

I

A

M

M

M

F

F

T

I

A

V

M

Y

S

A

Y

L

G

G

R

E

M

M

A

A

S

V

A

A

F

Y

P

P

V

V

A

A

G

G

S

G

A

F

Y

N

S

T

Y

Y

V

A

R

T

K

R

A

F

I

I

S

D

P

P

K

A

L

W

G

G

F

F

I

A

A

V

G

S

W

W

A

N

V

Y

L

F

L

I

D

N

Y

Y

L

-

F

F

L

V

P

T

M

F

A

P

I

L

W

E

L

L

I

T

G

T

A

C

A

A

Y

I

L

T

N

F

S

R

A

Y

F

W

P

T

A

D

V

I

P

N

Q

S

W

A

V

A

W

W

V

I

L

S

A

I

F

F

I

L

S

V

I

V

T

I

S

I

A

I

I

V

N

N

I

L

V

F

G

G

L

V

K

R

L

A

A

Y

N

G

G

E

I

V

N

E

A

F

L

I

L

L

M

S

L

T

V

V

Q

K

F

V

L

V

V

A

L

T

I

F

A

G

F

F

V

I

A

I

L

L

C

A

V

I

-

I

-

N

-

C

-

G

-

V

-

P

-

T

-

D

H

H

-

R

-

G

Y

Y

V

I

G

G

D

S

A

-

S

-

T

-

P

-

L

I

W

I

S

K

I

H

K

K

P

P

F

F

F

R

N

H

G

G

D

F

M

K

Q

G

M

F

P

C

L

S

I

V

M

F

S

T

G

T

A

A

I

-

A

-

C

-

Y

F

S

S

F

F

L

S

G

G

F

T

D

E

A

V

V

I

S

G

T

L

L

A

T

A

E

A

E

E

T

V

R

D

D

N

P

P

R

Q

R

K

T

A

I

L

P

P

R

H

A

A

I

V

M

K

L

Q

I

V

Sites not aligning to the query:

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

3l1lA Structure of arg-bound escherichia coli adic (see paper)
24% identity, 68% coverage: 36:334/441 of query aligns to 31:316/423 of 3l1lA

query
sites
3l1lA

S

S

T

T

A

G

G

G

M

I

V

A

P

I

A

Y

A

G

Y

W

L

L

A

V

A

T

L

I

V

I

A

G

M

A

F

L

F

G

T

L

A

S

M

M

S

V

Y

Y

G

A

R

K

M

M

A

S

S

F

A

L

F

D

P

P

V

S

A

P

G

G

S

G

A

S

Y

Y

S

A

Y

Y

V

A

R

R

K

R

A

C

I

F

S

G

P

P

K

F

L

L

G

G

F

Y

I

Q

A

T

G

N

W

V

A

L

V

Y

L

W

L

L

D

A

Y

C

L

W

F

I

L
x
G

P
x
N

M

I

A

A

I

M

W

V

L

V

I

I

G

G

A

V

A

G

Y

Y

L

L

N

S

S

Y

A

F

F

F

P

P

A

I

V

L

P

K

Q

D

W

-

V

P

W

W

V

V

L

L

A

T

F

I

I

T

S

C

I

V

T

V

-

V

-

L

-

W

-

I

-

F

S

V

A

L

I

L

N

N

I

I

V

V

G

G

L

P

K

K

L

M

A

I

N

T

G

R

I

V

N

Q

A

A

L

-

M

-

L

V

V

A

Q

T

F

V

L

L

V

A

L

L

I

I

A

P

F

I

V

V

A

G

L

I

C

A

V

V

H

F

Y

G

V

-

G

-

D

-

A

-

S

-

T

-

P

-

L

-

W

W

S

F

I

-

K

-

P

-

F

W

F

F

N

R

G

G

D

E

M

T

Q

Y

M

M

P

A

L

A

I

I

M

Q

S

S

G

T

A

L

A

N

I

V

A

T

C

L

Y
x
W

S
|
S

F

F

L
x
I

G

G

F

V

D

E

A

S

V

A

S

S

T

V

L

A

T

A

E

G

E

V

T

V

R

K

D

N

P

P

R

K

R

R

T

N

I

V

P

P

R

-

A

-

I

-

M

-

L

-

I

I

T

A

L

T

I

I

G

G

L

V

I

L

F

I

V

A

G

A

V

V

S

C

Y

Y

F

V

V

L

Q

S

I

T

A

T

H

A

-

I

-

M

-

G

-

M

-

I

P

P

S

N

F

A

Q

A

F

L

D

R

S

V

V

S

D

A

S

S

A

P

A

F

Y

G

E

D

I

A

A

A

R

R

N

M

I

A

G

L

G

G

D

D

L

T

F

A

V

G

S

A

I

I

F

V

L

S

I

F

G

C

L

A

I

A

V

A

G

G

Q

C

F

L

A

G

S

S

G

L

L

G

S

G

A
x
W

Q

T

A

L

S

L

G

A

S

G

R

Q

L

T

L

A

Y

K

A

A

M

A

G

A

R

D

D

D

G

G

V

L

L

F

P

P

K

P

S

I

F

F

F

-

G

-

T

A

L

R

H

V

E

N

R

K

F

A

G

G

T

T

P

P

I

V

N

A

S

G

I

L

L

I

C

V

A

G

V

I

V

L

binding arginine: G94 (≠ L99), N95 (≠ P100), W185 (≠ Y201), S186 (= S202), I188 (≠ L204), W276 (≠ A292)

Sites not aligning to the query:

binding arginine: 17, 20, 21

7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
24% identity, 81% coverage: 36:392/441 of query aligns to 27:391/458 of 7cmiB

query
sites
7cmiB

S

E

T

N

A

A

G

G

M

S

V

V

P

G

A

L

A

A

Y

L

L

I

A

V

A

W

L

I

V

V

A

T

M

G

F

F

F

I

T

T

-

V

-

G

A

A

M

L

S

C

Y

Y

G

A

R

E

M

L

A

G

S

V

A

T

F

I

P

P

V

K

A

S

G

G

S

G

A

D

Y

Y

S

S

Y

Y

V

V

R

K

K

D

A

I

I

F

S

G

P

G

K

L

L

A

G

G

F

F

I

L

A

R

G

L

W

W

-

I

A

A

V

V

L

L

L

V

D

I

Y

Y

L

P

F

T

L
x
N

P

Q

M

A

A

V

I

I

W

A

L

L

I

T

G

F

A

S

A

N

Y

Y

-

V

L

L

N

Q

S

P

A

L

F

F

P

P

A

T

V

C

-

F

-

P

P

P

Q

E

-

S

-

G

-

L

W

R

V

L

W

L

V

A

L

A

A

I

F

C

I

L

S

L

I

L

T

L

S

T

A

W

I

V

N

N

I

C

V

S

G

S

L

V

K

R

L

W

A

A

N

T

G

R

I

V

N

Q

A

D

L

I

-

F

-

T

-

A

-

G

-

K

L

L

M

L

L

A

V

L

Q

A

F

L

L

I

V

I

L

I

I

M

A

G

F

I

V

V

A

Q

L

I

C

C

V

K

-

G

H

E

Y

Y

V

F

G

W

G

L

D

E

A

P

S

K

T

N

P

A

L

F

W

E

S

N

I

F

K

Q

P

E

F

P

F

D

N

I

G

G

D

L

M

V

Q

A

M

L

P

A

L

F

I

L

M

Q

S

G

G

S

A
x
F

A

A

I

Y

A
x
G

C

G

Y

W

S

N

F

F

L

L

G

N

F

Y

D

-

A

-

V

-

S

-

T

-

L

V

T

T

E

E

T

L

R

V

D

D

P

P

R

Y

R

K

T

N

I

L

P

P

R

R

A

A

I

I

M

F

L

I

I

S

T

I

L

P

I

L

G

V

G

T

L

F

I

V

F

Y

V

V

G

-

V

-

S

-

Y

-

F

F

V

A

Q

N

I

V

A

A

H

Y

P

V

S

T

F

A

Q

M

F

S

D

P

S

Q

V

E

D

L

S

L

A

A

A

S

Y

N

E

A

I

V

A

A

R

V

N

T

I

F

G

G

G

E

D

K

L

L

F

L

-

G

-

V

-

M

V

A

S

W

I

I

F

M

L

P

I

I

G

S

L

V

I

A

V

L

G

S

Q

T

F

F

A

G

S

G

G

V

L

N

S

G

A

S

Q

L

A

F

S

T

G

S

S

S

R

R

L

L

L

F

Y

F

A

A

M

G

G

A

R

R

D

E

G

G

V

H

L

L

P

P

K

-

S

S

F

V

F

L

G

A

T

M

L

I

H

H

E

V

R

K

F

R

G

C

T

T

P

P

I

I

N

P

S

A

I

L

L

L

L

F

C

T

A

C

V

I

V

S

A

T

L

L

A

M

L

L

-

V

K

T

L

S

D

D

V

M

T

Y

T

T

S

L

T

I

S

N

F

Y

I

V

N

G

F

F

G

I

A

N

F

Y

L

L

A

F

F

Y

S

G

L

V

V

T

N

V

L

A

S

G

V

Q

I

I

F

V

H

L

Y

R

W

W

I

-

G

-

G

K

E

K

K

P

K

D

G

I

P

P

R

R

E

P

F

I

V

K

L

I

F

N

L

L

F

F

P

P

F

I

I

I

G

Y

L

L

binding leucine: N94 (≠ L99), F203 (≠ A196), G206 (≠ A199)

Sites not aligning to the query:

binding leucine: 13, 15, 17

7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
24% identity, 81% coverage: 36:392/441 of query aligns to 27:391/458 of 7cmhB

query
sites
7cmhB

S

E

T

N

A

A

G

G

M

S

V

V

P

G

A

L

A

A

Y

L

L

I

A

V

A

W

L

I

V

V

A

T

M

G

F

F

F

I

T

T

-

V

-

G

A

A

M

L

S

C

Y

Y

G

A

R

E

M

L

A

G

S

V

A

T

F

I

P

P

V

K

A

S

G

G

S

G

A

D

Y

Y

S

S

Y

Y

V

V

R

K

K

D

A

I

I

F

S

G

P

G

K

L

L

A

G

G

F

F

I

L

A

R

G

L

W

W

-

I

A

A

V

V

L

L

L

V

D

I

Y

Y

L

P

F

T

L
x
N

P

Q

M

A

A

V

I

I

W

A

L

L

I

T

G

F

A

S

A

N

Y

Y

-

V

L

L

N

Q

S

P

A

L

F

F

P

P

A

T

V

C

-

F

-

P

P

P

Q

E

-

S

-

G

-

L

W

R

V

L

W

L

V

A

L

A

A

I

F

C

I

L

S

L

I

L

T

L

S

T

A

W

I

V

N

N

I

C

V

S

G

S

L

V

K

R

L

W

A

A

N

T

G

R

I

V

N

Q

A

D

L

I

-

F

-

T

-

A

-

G

-

K

L

L

M

L

L

A

V

L

Q

A

F

L

L

I

V

I

L

I

I

M

A

G

F

I

V

V

A

Q

L

I

C

C

V

K

-

G

H

E

Y

Y

V

F

G

W

G

L

D

E

A

P

S

K

T

N

P

A

L

F

W

E

S

N

I

F

K

Q

P

E

F

P

F

D

N

I

G

G

D

L

M

V

Q

A

M

L

P

A

L

F

I

L

M

Q

S

G

G

S

A
x
F

A
|
A

I

Y

A
x
G

C

G

Y

W

S

N

F

F

L

L

G

N

F

Y

D

-

A

-

V

-

S

-

T

-

L

V

T

T

E

E

T

L

R

V

D

D

P

P

R

Y

R

K

T

N

I

L

P

P

R

R

A

A

I

I

M

F

L

I

I

S

T

I

L

P

I

L

G

V

G

T

L

F

I

V

F

Y

V

V

G

-

V

-

S

-

Y

-

F

F

V

A

Q

N

I

V

A

A

H

Y

P

V

S

T

F

A

Q

M

F

S

D

P

S

Q

V

E

D

L

S

L

A

A

A

S

Y

N

E

A

I

V

A

A

R

V

N

T

I

F

G

G

G

E

D

K

L

L

F

L

-

G

-

V

-

M

V

A

S

W

I

I

F

M

L

P

I

I

G

S

L

V

I

A

V

L

G

S

Q

T

F

F

A

G

S

G

G

V

L

N

S

G

A

S

Q

L

A

F

S

T

G

S

S

S

R

R

L

L

L

F

Y

F

A

A

M

G

G

A

R

R

D

E

G

G

V

H

L

L

P

P

K

-

S

S

F

V

F

L

G

A

T

M

L

I

H

H

E

V

R

K

F

R

G

C

T

T

P

P

I

I

N

P

S

A

I

L

L

L

L

F

C

T

A

C

V

I

V

S

A

T

L

L

A

M

L

L

-

V

K

T

L

S

D

D

V

M

T

Y

T

T

S

L

T

I

S

N

F

Y

I

V

N

G

F

F

G

I

A
x
N

F

Y

L

L

A

F

F

Y

S

G

L

V

V

T

N

V

L

A

S

G

V

Q

I

I

F

V

H

L

Y

R

W

W

I

-

G

-

G

K

E

K

K

P

K

D

G

I

P

P

R

R

E

P

F

I

V

K

L

I

F

N

L

L

F

F

P

P

F

I

I

I

G

Y

L

L

binding tryptophan: N94 (≠ L99), F203 (≠ A196), A204 (= A197), G206 (≠ A199), N355 (≠ A354)

Sites not aligning to the query:

binding tryptophan: 15, 17

5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
21% identity, 68% coverage: 36:334/441 of query aligns to 33:329/437 of 5j4nA

query
sites
5j4nA

S

S

T

T

A

G

G

G

M

I

V

A

P

I

A

Y

A

G

Y

W

L

L

A

V

A

T

L

I

V

I

A

G

M

A

F

L

F

G

T

L

A

S

M

M

S

V

Y

Y

G

A

R

K

M

M

A

S

S

F

A

L

F

D

P

P

V

S

A

P

G

G

S

G

A

S

Y

Y

S

A

Y

Y

V

A

R

R

K

R

A

C

I

F

S

G

P

P

K

F

L

L

G

G

F

Y

I

Q

A

T

G

N

W

V

A

L

V

Y

L

W

L

L

D
x
A

Y
x
C

L

W

F

I

L
x
G

P
x
N

M

I

A

A

I
x
M

W

V

L

V

I

I

G

G

A

V

A

G

Y

Y

L

L

N

S

S

Y

A

F

F

F

P

P

A

I

V

L

P

K

Q

D

-

P

-

L

-

V

-

L

-

T

-

I

-

T

-

C

-

V

-

L

W

W

V

I

W

F

V

V

L

L

A

-

F

-

I

-

S

-

I

-

T

-

S

-

A

-

I

L

N

N

I

I

V

V

G

G

L

P

K

K

L

M

A

I

N

T

G

R

I

V

N

Q

A

A

L

V

L

A

M

T

L

V

V

L

Q

A

F

L

L

I

V

P

L

I

I

V

A

G

F

I

V

A

A

V

L

F

C

G

V

W

H

F

Y

W

V

F

G

R

G

G

D

E

A

T

S

Y

T

M

P

A

L

A

W

W

S

N

I

V

K

-

P

-

F

-

N

S

G

G

D

L

M

G

Q

T

M

F

P

G

L

A

I

I

M

Q

S

S

G

T

A

L

A

N

I

V

A

T

C

L

Y

W

S

S

F

F

L

I

G

G

F

V

D

E

A

S

V

A

S

S

T

V

L

A

T

A

E

G

E

V

T

V

R

K

D

N

P

P

R

K

R

R

T

N

I

V

P

P

R

-

A

-

I

-

M

-

L

-

I

I

T

A

L

T

I

I

G

G

L

V

I

L

F

I

V

A

G

A

V

V

S

C

Y

Y

F

V

V

L

Q

S

I

T

A

T

H

A

-

I

-

M

-

G

-

M

-

I

P

P

S

N

F

A

Q

A

F

L

D

R

S

V

V

S

D

A

S

S

A

P

A

F

Y

G

E

D

I

A

A

A

R

R

N

M

I

A

G

L

G

G

D

D

L

T

F

A

V

G

S

A

I

I

F

V

L

S

I

F

G

C

L

A

I

A

V

A

G

G

Q

C

F

L

A

G

S

S

G

L

L

G

S

G

A
x
W

Q

T

A

L

S

L

G

A

S

G

R

Q

L

T

L

A

Y

K

A

A

M

A

G

A

R

D

D

D

G

G

V

L

L

F

P

P

K

P

S

I

F

F

F

-

G

-

T

A

L

R

H

V

E

N

R

K

F

A

G

G

T

T

P

P

I

V

N

A

S

G

I

L

L

I

C

V

A

G

V

I

V

L

binding agmatine: A92 (≠ D95), C93 (≠ Y96), G96 (≠ L99), N97 (≠ P100), M100 (≠ I103), W289 (≠ A292)

Sites not aligning to the query:

binding agmatine: 19

P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
23% identity, 47% coverage: 36:243/441 of query aligns to 37:239/445 of P60061

query
sites
P60061

S

S

T

T

A

G

G

G

M

I

V

A

P

I

A

Y

A

G

Y

W

L

L

A

V

A

T

L

I

V

I

A

G

M

A

F

L

F

G

T

L

A

S

M

M

S

V

Y

Y

G

A

R

K

M

M

A

S

S

F

A

L

F

D

P

P

V

S

A

P

G

G

S

G

A

S

Y

Y

S

A

Y

Y

V

A

R

R

K

R

A

C

I

F

S

G

P

P

K

F

L

L

G

G

F

Y

I

Q

A

T

G

N

W

V

A

L

V
x
Y

L

W

L

L

D
x
A

Y
x
C

L

W

F

I

L

G

P
x
N

M

I

A

A

I
x
M

W

V

L

V

I

I

G

G

A

V

A

G

Y

Y

L

L

N

S

S

Y

A

F

F

F

P

P

A

I

V

L

P

K

Q

D

-

P

-

L

-

V

-

L

-

T

-

I

-

T

-

C

-

V

-

L

W

W

V

I

W

F

V

V

L

L

A

-

F

-

I

-

S

-

I

-

T

-

S

-

A

-

I

L

N

N

I

I

V

V

G

G

L

P

K

K

L

M

A

I

N

T

G

R

I

V

N

Q

A

A

L

V

L

A

M

T

L

V

V

L

Q

A

F

L

L

I

V

P

L

I

I

V

A

G

F

I

V

A

A

V

L

F

C

G

V

W

H

F

Y

W

V

F

G

R

G

G

D

E

A

T

S

Y

T

M

P

A

L

A

W

W

S

N

I

V

K

-

P

-

F

-

N

S

G

G

D

L

M

G

Q

T

M

F

P

G

L

A

I

I

M

Q

S

S

G

T

A

L

A

N

I

V

A

T

C

L

Y
x
W

S
|
S

F

F

L
x
I

G

G

F

V

D

E

A

S

V

A

S

S

T

V

L

A

T

A

E

G

E

V

T

V

R

K

D

N

P

P

R

K

R

R

T

N

I

V

P

P

R

-

A

-

I

-

M

-

L

-

I

I

T

A

L

T

I

I

G

G

L

V

I

L

F

I

V

A

G

A

V

V

S

C

Y

Y

Y93 (≠ V92) mutation to L: Greatly decreased Arg uptake into liposomes.
A96 (≠ D95) binding ; binding
C97 (≠ Y96) binding
N101 (≠ P100) binding ; mutation to A: Vmax for Arg-Agm exchange 1% of wild-type, KM increases 3-fold.; mutation to D: Nearly wild-type Arg-Agm exchange.
M104 (≠ I103) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
W202 (≠ Y201) binding ; mutation to L: Halves Arg uptake into liposomes.
S203 (= S202) binding
I205 (≠ L204) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.

Sites not aligning to the query:

23 binding ; binding
26 binding
293 binding ; mutation W->C,H,L: Loss of Arg-Agm exchange.; mutation W->F,Y: Less than 20% Arg-Agm exchange activity. Vmax 15% of wild-type rate.
357 binding ; S→A: 20% decreased affinity for Arg, 40% decrease affinity for Agm.

P60063 Arginine/agmatine antiporter from Escherichia coli O157:H7 (see 3 papers)
23% identity, 47% coverage: 36:243/441 of query aligns to 37:239/445 of P60063

query
sites
P60063

S

S

T

T

A

G

G

G

M

I

V

A

P

I

A

Y

A

G

Y

W

L

L

A

V

A

T

L

I

V

I

A

G

M

A

F

L

F

G

T

L

A

S

M

M

S

V

Y

Y

G

A

R

K

M

M

A

S

S

F

A

L

F

D

P

P

V

S

A

P

G

G

S

G

A

S

Y
|
Y

S

A

Y

Y

V

A

R

R

K

R

A

C

I

F

S

G

P

P

K

F

L

L

G

G

F
x
Y

I

Q

A

T

G

N

W

V

A

L

V
x
Y

L

W

L

L

D
x
A

Y
x
C

L

W

F

I

L

G

P
x
N

M

I

A

A

I

M

W

V

L

V

I

I

G

G

A

V

A

G

Y

Y

L

L

N

S

S

Y

A

F

F

F

P

P

A

I

V

L

P

K

Q

D

-

P

-

L

-

V

-

L

-

T

-

I

-

T

-

C

-

V

-

L

W

W

V

I

W

F

V

V

L

L

A

-

F

-

I

-

S

-

I

-

T

-

S

-

A

-

I

L

N

N

I

I

V

V

G

G

L

P

K

K

L

M

A

I

N

T

G

R

I

V

N

Q

A

A

L

V

L

A

M

T

L

V

V

L

Q

A

F

L

L

I

V

P

L

I

I

V

A

G

F

I

V

A

A

V

L

F

C

G

V

W

H

F

Y

W

V

F

G

R

G

G

D

E

A

T

S

Y

T

M

P

A

L

A

W

W

S

N

I

V

K

-

P

-

F

-

N

S

G

G

D

L

M

G

Q

T

M

F

P

G

L

A

I

I

M

Q

S

S

G

T

A

L

A

N

I

V

A

T

C

L

Y
x
W

S

S

F

F

L
x
I

G
|
G

F
x
V

D
x
E

A
x
S

V
x
A

S

S

T

V

L

A

T

A

E

G

E

V

T

V

R

K

D

N

P

P

R

K

R

R

T

N

I

V

P

P

R

-

A

-

I

-

M

-

L

-

I

I

T

A

L

T

I

I

G

G

L

V

I

L

F

I

V

A

G

A

V

V

S

C

Y

Y

Y74 (= Y73) 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 (≠ F86) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
Y93 (≠ V92) 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 (≠ D95) binding
C97 (≠ Y96) binding
N101 (≠ P100) binding
W202 (≠ Y201) Periplasmic (proximal) gate; binding
I205 (≠ L204) binding
GVESA 206:210 (≠ GFDAV 205:209) Helix-breaking GVESA motif TM6
E208 (≠ D207) mutation E->A,D: 5-10% Agm antiport.

Sites not aligning to the query:

22 N→A: No change in antiport activity, 6-fold higher affinity for Arg.
23 binding
25:27 Helix-breaking GSG motif TM1
26 binding ; S→K: 5% Agm antiport.
27 binding
293 binding
337 F→A: Severely decreased antiport.
357 binding
365 Y→A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.

6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
22% identity, 89% coverage: 7:399/441 of query aligns to 11:399/433 of 6f2wA

query
sites
6f2wA

T

T

L

V

S

V

L

V

G

G

S

T

V
|
V

V

I

L
x
G

F
x
A

G
|
G

I

I

A

-

Y

F

M

F

T

K

P

P

I

T

I

A

V

V

L

Y

G

G

T

-

F

-

G

-

I

-

L

-

A

A

Q

A

S

G

T

A

A

P

G

G

M

L

V

G

P

L

A

L

A

A

Y

W

L

F

A

V

A

A

L

G

V

I

A

I

M

T

F

I

F

A

T

G

A

G

M

L

S

T

Y

V

G

A

R

E

M

I

A

G

S

T

A

I

F

Y

P

P

V

Q

A

T

G

G

S

G

A

M

Y

M

S

I

Y

Y

V

L

R

E

K

K

A

V

I

Y

S

G

P

R

K

W

L

L

G

G

F

F

I

L

A

V

G

G

W

W

A

A

V

Q

L

M

L

V

D

I

Y

Y

L

Y

F

P

L

A

P

N

M

I

A

A

I

A

W

L

L

A

I

I

-

I

-

F

G

A

A

T

A

Q

Y

F

L

V

N

N

-

L

-

F

-

A

-

L

S

S

A

D

F

S

P

T

A

I

V

V

P

P

Q

T

W

A

V

I

W

L

V

T

L

S

A

I

F

F

I

L

S

-

I

-

T

-

S

M

A

G

I

V

N

N

I

F

V

L

G

G

L

T

K

K

L

Y

A

S

N

G

G

W

I

I

N

Q

A

T

L

L

L

A

M

T

L

I

V

L

Q

K

F

L

L

I

V

P

L

L

I

V

A

V

F

I

V

I

A

V

L

A

C

G

V

L

H

L

Y

Y

V

P

G

G

D

G

A

-

S

-

T

-

P

-

L

V

W

I

S

R

I

L

K

V

P

P

F

F

F

-

N

-

G

S

D

V

M

E

Q

T

M

H

P

P

L

V

I

L

M

T

S

S

-

F

G

G

A

S

A

A

I

L

-

I

-

A

A

T

C

L

Y
x
F

S
x
A

F

Y

L
x
D

G

G

F

W

D

I

A

N

V

V

S

G

T

T

L

L

T

A

E

G

E

E

T

M

R

K

D

N

P

P

R

G

R

K

T

M

I

L

P

P

R

K

A

V

I

I

M

-

L

-

I

-

T

-

L

-

I

I

G

G

L

L

-

S

I

I

F

V

V

M

G

A

V

V

S

Y

Y

L

F

L

V

T

Q

N

I

I

A

A

H

Y

-

L

-

F

-

V

-

L

P

D

S

S

F

S

Q

Q

F

L

D

A

S

G

V

T

D

D

S

T

A

P

A

A

Y

A

E

L

I

V

A

A

R

S

N

H

I

L

G

F

G

E

D

G

L

I

F

G

V

S

S

K

I

L

F

V

L

T

I

I

G

G

L

I

I

L

V

I

G

S

Q

V

F

F

A

G

S

G

G

I

L

N

S

G

A

Y

Q

I

A

I

S

S

G

G

S

L

R

R

L

V

L

P

Y

Y

A

A

M

L

G

A

R

T

D

Q

G

K

V

M

L

L

P

P

K

F

S

S

-

D

F

W

F

F

G

A

T

R

L

I

H

N

E

P

R

K

F

T

G

N

T

L

P

P

I

I

N

N

-

G

S

G

I

L

L

V

L

M

C

L

A

G

V

I

V

A

A

I

L

V

L

M

A

I

L

L

K

T

L

G

D

Q

V

F

T

N

T

Q

S

L

T

T

S

D

F

L

I

I

N

V

F

F

G

V

A

I

F

W

L

F

A

F

F

I

S

T

L

L

V

T

N

F

L

I

S

A

V

V

I

I

F

I

H

L

Y

R

W

K

I

T

G

Q

G

P

E

D

K

I

K

E

G

R

P

P

R

Y

E

R

F

V

V

P

L

F

F

Y

L

P

L

V

F

I

P

P

F

L

I

I

G

A

L

I

S

I

A

G

D

G

L

L

W

Y

L

I

M

I

binding alpha-aminoisobutyric acid: V17 (= V13), G19 (≠ L15), A20 (≠ F16), G21 (= G17), F199 (≠ Y201), A200 (≠ S202), D202 (≠ L204)

P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
21% identity, 92% coverage: 27:431/441 of query aligns to 32:449/469 of P46349

query
sites
P46349

L

V

G
|
G

T

S

F

G

G

S

I

V

L

I

A

H

Q

S

S

T

T
x
G

A

P

G

G

M

A

V

V

P

V

A

S

A

Y

Y

A

L

L

A

A

A

G

L

L

V

L

A

V

M

I

F

F

F

I

T

M

A

R

M

M

S

-

Y

L

G

G

R

E

M

M

A

S

S

A

A

V

F

N

P

P

V

T

A

S

G

G

S

S

A

F

Y

S

S

Q

Y

Y

V

A

R

H

K

D

A

A

I

I

S

G

P

P

K

W

L

A

G

G

F

F

I

T

A

I

G

G

W

W

A

L

V

Y

L

W

L

F

D

F

Y

W

L

V

F

I

L

V

P

I

M

A

A

I

I

E

W

A

L

I

I

A

G

G

A

A

A

G

Y

I

L

I

N

Q

S

Y

A

W

F

F

P

H

A

D

V

I

P

P

Q

L

W

W

V

L

W

T

V

S

L

L

A

I

F

L

I

T

S

I

I

V

T

L

S

T

A

L

I

T

N

N

I

V

V

Y

G

S

L

V

K

K

L

S

A

F

N

G

G

E

I

F

N

E

A

Y

L

W

L

F

M

S

L

L

V

I

Q

K

F

V

L

V

V

T

L

I

I

I

A

A

F

F

V

L

A

I

L

V

C

G

V

F

H

A

Y

F

V

I

G

F

G

G

D

F

A

A

-

P

-

G

S

S

T

E

P

P

-

V

-

G

-

F

-

S

-

N

L

L

W

T

S

G

I

K

K

G

P

G

F

F

N

P

G

E

D

G

M

I

Q

S

M

S

P

V

L

L

I

L

M

-

S

-

G

G

A

I

A

V

I

V

A

V

C

I

Y

F

S

S

F

F

L

M

G

G

F

T

D

E

A

I

V

V

S

A

T

I

L

A

T

A

E

G

E

E

T

T

R

S

D

N

P

P

R

I

R

E

T

S

I

V

P

T

R

K

A

A

I

T

M

R

L

S

I

V

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V

L

W

I

R

G

I

L

V

I

F

F

Y

V

V

G

G

V

S

S

I

Y

A

F

I

V

V

Q

V

I

A

A

L

H

L

P

P

S

W

F

N

Q

S

F

A

D

N

S

I

V

L

D

E

S

S

A

P

A

F

Y

V

E

A

I

V

A

L

R

E

N

H

I

I

G

G

G

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D

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L

A

F

A

V

A

S

Q

I

I

F

M

L

N

I

F

G

I

L

V

I

L

V

T

G

A

Q

V

F

L

A

S

S

C

G

L

L

N

S

S

A
x
G

Q

L

A

Y

S

T

G

T

S

S

R

R

L

M

L

L

Y

Y

A

S

M

L

G

A

R

E

D

R

G

N

V

E

L

A

P

P

K

R

S

R

F

F

F

M

G

K

T

L

L

-

H

-

E

S

R

K

F

K

G

G

T

V

P

P

I

V

N

Q

S

A

I

I

L

V

L

A

C
x
G

A

T

V

F

V
x
F

A

S

L

Y

L

I

A

A

L

V

K

V

L

M

D

N

-

Y

-

F

-

S

-

P

-

D

-

T

-

V

-

F

-

L

-

F

V

L

T

V

T

N

S

S

T

S

S

G

F

A

I

I

N

A

F

L

G

L

A

V

F

Y

L

L

A

V

F

I

S

A

L

V

V

S

N

Q

L

L

S

K

V

M

I

R

F

K

H

K

Y

L

W

-

I

-

G

-

E

E

K

K

K

T

G

N

P

P

R

E

E

A

F

L

V

K

L

I

F

K

L

M

-

W

L

L

F

F

P

P

F

F

-

L

-

T

-

Y

-

L

-

T

-

I

I

I

G

A

L

I

S

C

A
x
G

D

I

L

L

W

V

L

S

M

M

V

A

S

F

L

I

D

D

H

S

L

M

A

R

V

D

Y

E

L

L

G

L

L

L

S

T

W

G

L

V

A

I

I

T

G

G

V

I

V

V

Y

L

L

I

A

S

V

Y

L

L

T

V

G

-

F

F

R

R

R

K

Q

R

G33 (= G28) mutation to D: Lack of activity.
G42 (≠ T37) mutation to S: Lack of activity.
G301 (≠ A292) mutation to V: Lack of activity.
G338 (≠ C331) mutation to E: Lack of activity.
F341 (≠ V334) mutation to S: Lack of activity.
G414 (≠ A394) mutation to R: Lack of activity.

7dsqB Overall structure of the lat1-4f2hc bound with 3,5-diiodo-l-tyrosine (see paper)
25% identity, 84% coverage: 4:375/441 of query aligns to 3:379/464 of 7dsqB

query
sites
7dsqB

L

L

Q

Q

R

R

T

N

L

I

S

T

L

L

-

L

-

N

G

G

S

V

V

A

V

I

L

I

F

V

G

G

I
x
T

A
x
I

Y

I

M
x
G

T

S

P

G

I

I

I

F

V

V

L

T

G

P

T

T

F

-

G

G

I

V

L

L

A

K

Q

E

S

A

-

G

T

S

A

P

G

G

M

L

V

A

P

L

A

V

Y

W

L

A

A

A

A

C

L

G

V

V

A

F

M

S

F

I

F

V

T

G

A

A

M

L

S

C

Y

Y

G

A

R

E

M

L

A

G

S

T

A

T

F

I

P

S

V

K

A

S

G

G

S

G

A

D

Y

Y

S

A

Y

Y

V

M

R

L

K

E

A

V

I

Y

S

G

P

S

K

L

L

P

G

A

F

F

I

L

A

K

G

L

W

W

A

I

V

E

L

L

D

-

Y

-

L

I

F

I

L

R

P

P

M

S

A

S

I

Q

W

Y

L

I

I

V

G

A

A

L

A

V

Y

F

-

A

-

T

-

Y

-

L

L

L

N

K

S

P

A

L

F

F

P

P

A

T

V

C

P

P

-

V

-

P

-

E

-

A

Q

A

W

K

V

L

W

V

V

A

L

C

A

L

F

C

I

V

S

L

I

L

T

L

S

T

A

A

I

V

N

N

I

C

V

Y

G

S

L

V

K
|
K

L

A

A

A

N

T

G

R

I
x
V

N

Q

A

D

L

A

L

F

M

A

L

A

V

A

Q

K

F

L

L

L

V

A

L

L

I

A

A

L

F

I

V

I

A

L

L

L

C

G

V

F

H

V

Y

Q

V

I

G

G

-

K

G

G

D

D

A

V

S

S

T

-

P

-

L

-

W

-

S

N

I

L

K

D

P

P

F

N

F

F

N

S

G

F

D

E

M

-

Q

G

M

T

P

K

L

L

I

D

M

V

S

G

G

N

A

I

A

V

I

L

A

A

C

L

Y

Y

S

S

F

G

L

L

-

F

-

A

-

Y

-
x
G

G
|
G

F

W

D

N

A
x
Y

V

L

S

N

T

F

L

V

T

T

E

E

T

M

R

I

D

N

P

P

R

Y

R

R

T

N

I

L

P

P

R

L

A

A

I

I

M

I

L

I

I

S

T

L

L

P

I

I

G

V

G

T

L

L

I

V

F

Y

V

V

-

L

-

T

G

N

V

L

S

A

Y

Y

F

F

V

T

Q

T

I

L

A

S

H

-

P

-

S

T

F

E

Q

Q

F

M

D

L

S

S

V

S

D

E

S

A

A

V

A

A

Y

V

E

D

I

F

A

G

R

N

N

Y

I

-

G

-

D

H

L

L

F

G

V

V

S

M

I

S

F

W

L

I

I

I

G

P

L

V

I

F

V

V

G

G

-

L

-

S

Q

C

F

F

A

G

S

S

G

V

L

N

S

G

A

S

Q

L

A

F

S

T

G

S

S

S

R

R

L

L

L

F

Y

F

A

V

M

G

G

S

R

R

D

E

G

G

V

H

L

L

P

P

K

-

S

S

F

I

F

L

G

S

T

M

L

I

H

H

E

P

R

Q

F

L

G

L

T

T

P

P

I

V

N

P

S

S

I

L

L

V

L

F

C

T

A

C

V

V

V

M

A

T

L

L

-

Y

A

A

L

F

K

S

L

K

D

D

V

I

T

F

T

-

S

-

T

-

S

S

F

V

I

I

N

N

F

F

G
x
F

A

S

F

F

L

F

A
x
N

F

W

S

L

L

C

V

V

N

A

L

L

S

A

V

I

I

I

F

G

H

M

Y

I

W

W

I

L

G

R

G

H

E

R

K

K

binding 3,5-diiodotyrosine: T19 (≠ I18), I20 (≠ A19), G22 (≠ M21), G212 (vs. gap), G213 (= G205), Y216 (≠ A208), F357 (≠ G353), N361 (≠ A357)
binding cholesterol hemisuccinate: K148 (= K140), V153 (≠ I145)

Query Sequence

>PfGW456L13_4782 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_4782
MARLQRTLSLGSVVLFGIAYMTPIIVLGTFGILAQSTAGMVPAAYLAALVAMFFTAMSYG
RMASAFPVAGSAYSYVRKAISPKLGFIAGWAVLLDYLFLPMAIWLIGAAYLNSAFPAVPQ
WVWVLAFISITSAINIVGLKLANGINALLMLVQFLVLIAFVALCVHYVGGDASTPLWSIK
PFFNGDMQMPLIMSGAAIACYSFLGFDAVSTLTEETRDPRRTIPRAIMLITLIGGLIFVG
VSYFVQIAHPSFQFDSVDSAAYEIARNIGGDLFVSIFLIGLIVGQFASGLSAQASGSRLL
YAMGRDGVLPKSFFGTLHERFGTPINSILLCAVVALLALKLDVTTSTSFINFGAFLAFSL
VNLSVIFHYWIGGEKKGPREFVLFLLFPFIGLSADLWLMVSLDHLAVYLGLSWLAIGVVY
LAVLTGGFRRQPPEMDFQEAA

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