SitesBLAST

P07821 Iron(3+)-hydroxamate import ATP-binding protein FhuC; Ferric hydroxamate uptake protein C; Ferrichrome transport ATP-binding protein FhuC; Iron(III)-hydroxamate import ATP-binding protein FhuC; EC 7.2.2.16 from Escherichia coli (strain K12) (see 2 papers)
34% identity, 42% coverage: 7:220/508 of query aligns to 14:228/265 of P07821

query
sites
P07821

F

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Q

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N

I

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S

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A

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N

N

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A

K50 (= K43) mutation to Q: Lack of activity.
D172 (= D165) mutation to E: Lack of activity.
E173 (= E166) mutation to A: Lack of activity.

P75957 Lipoprotein-releasing system ATP-binding protein LolD; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
34% identity, 45% coverage: 4:231/508 of query aligns to 5:233/233 of P75957

query
sites
P75957

F

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E

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G42 (= G37) mutation to D: Loss of lipoprotein release when overexpressed.

1g6hA Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
29% identity, 43% coverage: 3:220/508 of query aligns to 3:230/254 of 1g6hA

query
sites
1g6hA

D

E

F

I

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Y
x
F

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A

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D

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K

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D

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N

G
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G

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G

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T

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N

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A

binding adenosine-5'-diphosphate: F14 (≠ Y14), F17 (≠ V17), N39 (= N39), G40 (= G40), G42 (= G42), K43 (= K43), S44 (= S44), T45 (= T45)

7mdyC Lolcde nucleotide-bound
34% identity, 43% coverage: 4:220/508 of query aligns to 2:222/226 of 7mdyC

query
sites
7mdyC

F

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D

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N

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Q

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H

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N

N

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H

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S

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x
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G
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G

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E

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x
N

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D

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F

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Q

L

L

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D

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G

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H
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H

R

D

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L

D

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E

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L

M

R

R

D

D

G

G

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L

A

T

A

A

binding adp orthovanadate: Y12 (= Y14), G42 (= G40), S43 (≠ A41), G44 (= G42), K45 (= K43), S46 (= S44), T47 (= T45), Q91 (= Q86), H138 (≠ A136), E142 (≠ S140), S144 (= S142), G145 (≠ I143), G146 (= G144), E168 (= E166), N172 (≠ S170), H201 (= H198)
binding magnesium ion: S46 (= S44), Q91 (= Q86)

7arlD Lolcde in complex with lipoprotein and adp (see paper)
34% identity, 43% coverage: 4:220/508 of query aligns to 2:222/222 of 7arlD

query
sites
7arlD

F

L

L

L

E

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F

C

Q

D

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S

C

K

K

G

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Y

Y

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E

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Q

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D

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V

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A

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N

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D

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N

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A

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A

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K

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G

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A

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I

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M

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A

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A

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Q

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V

E

A

I

I

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K

R

A

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T

N

D

N

A

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L

I

V

A

L

L

A

D

D

E

E

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P

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G

S

N

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S

A

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F

F

A

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G

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E

L

L

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N

R

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S

L

N

Q

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G

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A

I

F

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H

H

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D

L

L

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E

L

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A

F

K

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C

S

N

R

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Q

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L

M

R

R

D

D

G

G

R

R

L

L

A

T

A

A

binding adenosine-5'-diphosphate: G42 (= G40), G44 (= G42), K45 (= K43), S46 (= S44)

1g9xB Characterization of the twinning structure of mj1267, an atp-binding cassette of an abc transporter (see paper)
29% identity, 43% coverage: 3:220/508 of query aligns to 3:230/253 of 1g9xB

query
sites
1g9xB

D

E

F

I

L

L

E

R

F

T

Q

E

S

N

I

I

S

V

K

K

G

Y

Y
x
F

P

G

G

E

V
x
F

Q

K

A

A

L

L

S

D

E

G

V

V

S

S

F

I

S

S

V

V

R

C

K

K

G

G

A

D

V

V

H

T

G

L

L

I

M

I

G

G

E

P

N

N

G
|
G

A
x
S

G
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G

K
|
K

S
|
S

T
|
T

L

L

I

I

R

N

V

V

L

I

S

T

G

G

D

F

Q

L

A

K

A

A

D

D

T

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G

G

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V

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Y

I

F

N

E

G

N

E

K

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D

E

A

L

F

Y

N

H

A

Y

G

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I

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I

T

H

F

Q

Q

E

T

L

P

Q

Q

L

P

V

L

P

K

E

E

L

M

T

T

V

V

A

L

E

E

N

N

L

L

W

L

L

I

G

G

R

E

F

I

-

N

P

P

G

G

-

E

-

S

-

P

-

L

-

N

-

S

-

L

-

F

-

Y

K

K

A

K

G

W

V

I

I

P

D

K

R

E

Q

E

L

M

I

V

R

E

V

K

V

A

S

F

D

K

R

I

L

L

A

E

E

F

I

L

G

K

I

L

D

S

V

H

D

L

P

Y

E

D

A

R

K

K

V

A

A

G

S

E

L

L

S

S

I

G

G

G

E

Q

R

M

Q

K

M

L

V

V

E

E

I

I

A

G

K

R

A

A

V

L

M

M

T

T

D

N

A

P

R

K

V

M

I

I

A

V

L

M

D

D

E
|
E

P

P

T

I

S

A

S

G

L

V

S

A

S

P

R

G

E

L

S

A

E

H

I

D

L

I

F

F

A

N

L

H

I

V

D

L

R

E

L

L

R

K

S

A

N

K

G

G

T

I

V

T

I

F

L

L

Y

I

V

I

S

E

H

H

R

R

L

L

D

D

E

I

I

V

F

L

R

N

L

Y

C

I

N

D

S

H

L

L

T

Y

V

V

L

M

R

F

D

N

G

G

R

Q

L

I

A

I

A

A

binding adenosine-5'-diphosphate: F14 (≠ Y14), F17 (≠ V17), G40 (= G40), S41 (≠ A41), G42 (= G42), K43 (= K43), S44 (= S44), T45 (= T45)
binding magnesium ion: S44 (= S44), E176 (= E166)

7v8iD Lolcd(e171q)e with bound amppnp in nanodiscs (see paper)
33% identity, 43% coverage: 4:220/508 of query aligns to 4:224/229 of 7v8iD

query
sites
7v8iD

F

L

L

L

E

Q

F

C

Q

D

S

N

I

L

S

C

K

K

G

R

Y

Y

P

Q

-

E

-

G

G

S

V

V

Q

Q

A

T

-

D

-
x
V

L

L

S

H

E

N

V

V

S

S

F

F

S

S

V

V

R

G

K

E

G

G

A

E

V

M

H

M

G

A

L

I

M

V

G

G

E

S

N
x
S

G
|
G

A

S

G
|
G

K
|
K

S
|
S

T
|
T

L

L

I

L

R

H

V

L

L

L

S

G

G

G

D

L

Q

D

A

T

A

P

D

T

T

S

G

G

E

D

I

V

R

I

I

F

N

N

G

G

E

Q

P

P

Q

M

H

S

Y

K

R

L

S

S

V

S

R

A

-

A

-

K

-

A

D

E

A

L

F

R

N

N

A

Q

G

K

V

L

I

G

V

F

I

I

H

Y

Q
|
Q

E

F

L

H

Q

H

L

L

V

L

P

P

E

D

L

F

T

T

V

A

A

L

E

E

N

N

L

V

W

A

L

M

G

P

R

L

F

L

P

I

G

G

K

K

A

K

-

K

-

P

G

A

V

E

I

I

D

N

R

S

R

R

Q

A

L

L

I

-

R

-

V

-

S

-

D

E

R

M

L

L

A

K

E

A

I

V

G

G

I

L

D

D

V

H

D
x
R

P

A

E

N

A
x
H

K

R

V

P

A

S

S
x
E

L

L

S
|
S

I

G

G
|
G

E
|
E

R

R

Q

Q

M

R

V

V

E

A

I

I

A

A

K

R

A

A

V

L

M

V

T

N

D

N

A

P

R

R

V

L

I

V

A

L

L

A

D

D

E

Q

P

P

T

T

S

G

S

N

L

L

S

D

S

A

R

R

E

N

S

A

E

D

I

S

L

I

F

F

A

Q

L

L

I

L

D

G

R

E

L

L

-

N

R

R

S

L

N

Q

G

G

T

T

V

A

I

F

L

L

Y

V

V

V

S

T

H
|
H

R

D

L

L

D

Q

E

L

I

A

F

K

R

R

L

M

C

S

N

R

S

Q

L

L

T

E

V

-

L

M

R

R

D

D

G

G

R

R

L

L

A

T

A

A

binding phosphoaminophosphonic acid-adenylate ester: V23 (vs. gap), S43 (≠ N39), G44 (= G40), G46 (= G42), K47 (= K43), S48 (= S44), T49 (= T45), Q93 (= Q86), R137 (≠ D133), H140 (≠ A136), E144 (≠ S140), S146 (= S142), G148 (= G144), E149 (= E145), H203 (= H198)
binding magnesium ion: S48 (= S44), Q93 (= Q86)

P75831 Macrolide export ATP-binding/permease protein MacB; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
28% identity, 49% coverage: 1:249/508 of query aligns to 1:248/648 of P75831

query
sites
P75831

M

M

Q

T

D

P

F

L

L

L

E

E

F

L

Q

K

S

D

I

I

S

R

K

R

G

S

Y

Y

P

P

G

A

-

G

-

D

-

E

-

Q

V

V

Q

E

A

V

L

L

S

K

E

G

V

I

S

S

F

L

S

D

V

I

R

Y

K

A

G

G

A

E

V

M

H

V

G

A

L

I

M

V

G

G

E

A

N

S

G

G

A

S

G

G

K
|
K

S

S

T

T

L

L

I

M

R

N

V

I

L

L

S

G

G

C

D

L

Q

D

A

K

A

A

D

T

T

S

G

G

E

T

I

Y

R

R

I

V

N

A

G

G

E

Q

P

D

Q

V

H

A

Y

T

R

L

S

D

V

A

-

D

-

A

-

L

-

A

-

Q

-

L

-

R

R

R

D

E

A

H

F

F

N

G

A

-

G

-

V

-

I

-

V

F

I

I

H

F

Q

Q

E

R

L

Y

Q

H

L

L

V

L

P

S

E

H

L

L

T

T

V

A

A

E

E

Q

N

N

L

V

W

-

L

-

G

-

R

E

F

V

P

P

G

A

K

V

A

Y

G

A

V

G

I

L

D

E

R

R

R

K

Q

Q

L

R

I

L

R

L

V

R

V

A

S

Q

D

E

R

L

L

L

A

Q

E

R

I

L

G

G

I

L

D

E

V

D

D

R

P

T

E

E

A

Y

K

Y

V

P

A

A

S

Q

L

L

S

S

I

G

G

G

E

Q

R

Q

Q

Q

M

R

V

V

E

S

I

I

A

A

K

R

A

A

V

L

M

M

T

N

D

G

A

G

R

Q

V

V

I

I

A

L

L

A

D
|
D

E

E

P

P

T

T

S

G

S

A

L

L

S

D

S

S

R

H

E

S

S

G

E

E

I

E

L

V

F

M

A

A

L

I

I

L

D

H

R

Q

L

L

R

R

S

D

N

R

G

G

T

H

V

T

I

V

L

I

Y

I

V

V

S

T

H

H

R

D

L

-

D

P

E

Q

I

V

F

A

R

A

L

Q

C

A

N

E

S

R

L

V

T

I

V

E

L

I

R

R

D

D

G

G

R

E

L

I

A

V

A

R

H

N

H

P

P

P

D

A

I

I

S

E

K

K

V

V

-

N

-

V

-

T

-

G

G

G

R

T

E

E

Q

P

I

V

I

-

A

-

E

-

M

-

V

-

G

-

R

-

E

-

I

V

S

N

N

T

I

V

W

S

G

G

W

W

R

R

K47 (= K43) mutation to L: Lack of activity.
D169 (= D165) mutation to N: Lack of activity.

1ji0A Crystal structure analysis of the abc transporter from thermotoga maritima
28% identity, 42% coverage: 5:218/508 of query aligns to 7:217/240 of 1ji0A

query
sites
1ji0A

L

L

E

E

F

V

Q

Q

S

S

I

L

S

H

K

V

G

Y

Y
|
Y

P

G

G

A

V

I

Q

H

A

A

L

I

S

K

E

G

V

I

S

D

F

L

S

K

V

V

R

P

K

R

G

G

A

Q

V

I

H

V

G

T

L

L

M

I

G

G

E

A

N

N

G
|
G

A

A

G
|
G

K
|
K

S
x
T

T
|
T

L

T

I

L

R

S

V

A

L

I

S

A

G

G

D

L

Q

V

A

R

A

A

D

Q

T

K

G

G

E

K

I

I

R

I

I

F

N

N

G

G

E

Q

P

D

Q

I

H

T

Y

N

R

K

S

P

V

A

R

H

D

V

A

I

F

N

N

R

A

M

G

G

V

I

I

A

V

L

I

V

H

P

Q
x
E

E

G

L

R

Q

R

L

I

V

F

P

P

E

E

L

L

T

T

V

V

A

Y

E

E

N

N

L

L

W

M

L

M

G

G

R

A

F

Y

P

N

G

R

K

K

A

D

G

K

V

E

I

G

D

I

R

K

R

R

Q

D

L

L

I

E

R

W

V

I

V

F

S

S

-

L

-

F

-

P

-

R

-

L

-

K

D

E

R

R

L

L

A

K

E

Q

I

L

G

G

I

-

D

-

V

-

D

-

P

-

E

-

A

-

K

-

V

-

A

G

S

T

L

L

S

S

I

G

G

G

E

E

R

Q

Q

Q

M

M

V

L

E

A

I

I

A

G

K

R

A

A

V

L

M

M

T

S

D

R

A

P

R

K

V

L

I

L

A

M

L

M

D

D

E
|
E

P

P

T

S

S

L

S

G

L

L

S

A

S

P

R

I

E

L

S

V

E

S

I

E

L

V

F

F

A

E

L

V

I

I

D

Q

R

K

L

I

R

N

S

Q

N

E

G

G

T

T

V

T

I

I

L

L

Y

L

V

V

S

E

H

Q

R

N

L

A

D

L

E

G

I

A

F

L

R

K

L

V

C

A

N

H

S

Y

L

G

T

Y

V

V

L

L

R

E

D

T

G

G

R

Q

L

I

binding adenosine-5'-triphosphate: Y16 (= Y14), G42 (= G40), G44 (= G42), K45 (= K43), T46 (≠ S44), T47 (= T45), E88 (≠ Q86), E165 (= E166)

P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
30% identity, 41% coverage: 12:218/508 of query aligns to 13:219/343 of P30750

query
sites
P30750

K

Q

G

G

Y

T

P

R

G

T

V

I

Q

Q

A

A

L

L

S

N

E

N

V

V

S

S

F

L

S

H

V

V

R

P

K

A

G

G

A

Q

V

I

H

Y

G

G

L

V

M

I

G

G

E

A

N
x
S

G
|
G

A
|
A

G
|
G

K
|
K

S
|
S

T
|
T

L

L

I

I

R

R

V

C

L

V

S

N

G

L

D

L

Q

E

A

R

A

P

D

T

T

E

G

G

E

S

I

V

R

L

I

V

N

D

G

G

E

Q

P

E

Q

L

H

T

Y

T

R

L

S

S

V

E

R

S

D

E

A

L

F

T

N

K

A

A

-

R

G

Q

V

I

I

G

V

M

I

I

H

F

Q

Q

E

H

L

F

Q

N

L

L

V

L

P

S

E

S

L

R

T

T

V

V

A

F

E

G

N

N

L

V

W

A

L

L

G

-

R

-

F

-

P

P

G

L

K

E

A

L

G

D

V

N

I

T

D

P

R

K

R

D

Q

E

L

V

I

K

R

R

V

R

V

V

S

T

D

E

R

L

L

L

A

S

E

L

I

V

G

G

I

L

D

G

V

D

D

K

P

H

E

D

A

S

K

Y

V

P

A

S

S

N

L

L

S

S

I

G

G

G

E

Q

R

K

Q

Q

M

R

V

V

E

A

I

I

A

A

K

R

A

A

V

L

M

A

T

S

D

N

A

P

R

K

V

V

I

L

A

L

L

C

D

D

E
|
E

P

A

T

T

S

S

S

A

L

L

S

D

S

P

R

A

E

T

S

T

-

R

E

S

I

I

L

L

F

E

A

L

L

L

I

K

D

D

R

I

L

N

R

R

S

R

N

L

G

G

T

L

V

T

I

I

L

L

Y

L

V

I

S

T

H

H

R

E

L

M

D

D

E

V

I

V

F

K

R

R

L

I

C

C

N

D

S

C

L

V

T

A

V

V

L

I

R

S

D

N

G

G

R

E

L

L

40:46 (vs. 39:45, 86% identical) binding
E166 (= E166) mutation to Q: Exhibits little ATPase activity.

Sites not aligning to the query:

278:283 binding
295 N→A: Reduces the binding of L-methionine to undetectable levels.
295:296 binding

7nezA Structure of topotecan-bound abcg2 (see paper)
30% identity, 43% coverage: 5:223/508 of query aligns to 3:221/563 of 7nezA

query
sites
7nezA

L

L

E

S

F

F

Q

H

S

N

I

I

S

C

K

-

G

-

Y

Y

P

R

G

V

V

K

Q

E

A

I

L

L

S

S

E

N

V

I

S

N

F

-

S

G

V

I

R

M

K

K

G

P

A

G

V

L

H

N

G

A

L

I

M

L

G

G

E

P

N

T

G

G

A

G

G

G

K

K

S

S

T

S

L

L

I

L

R

D

V

V

L

L

S

A

G

A

-

R

-

K

D

D

Q

P

A

S

A

G

D

L

T

S

G

G

E

D

I

V

R

L

I

I

N

N

G

G

E

A

P

P

Q

-

H

-

Y

-

R

R

S

P

V

A

R

N

D

F

A

K

F

C

N

N

A

S

G

G

V

Y

I

V

V

V

I

-

H

-

Q

Q

E

D

L

D

Q

V

L

V

V

M

P

G

E

T

L

L

T

T

V

V

A

R

E

E

N

N

L

L

W

Q

L

F

G

S

R

A

F

A

P

L

G

R

K

L

A

A

G

T

V

T

I

M

D

T

R

N

R

H

Q

E

L

K

I

N

R

E

V

R

V

I

S

N

D

R

R

V

L

I

A

Q

E

E

I

L

G

G

I

L

D

D

V

K

D

V

P

A

E

D

A

S

K

K

V

V

A

G

S

T

-

Q

-

F

-

I

-

R

-

G

L

V

S

S

I

G

G

G

E

E

R

R

Q

K

M

R

V

T

E

S

I

I

A

G

K

M

A

E

V

L

M

I

T

T

D

D

A

P

R

S

V

I

I

L

A

F

L

L

D

D

E

E

P

P

T

T

S

T

S

G

L

L

S

D

S

S

R

S

E

T

S

A

E

N

I

A

L

V

F

L

A

L

L

L

I

L

D

K

R

R

L

M

R

S

S

K

N

Q

G

G

T

R

V

T

I

I

L

I

Y

F

V

S

S

I

H

H

R

Q

L

P

-

R

D

Y

E

S

I

I

F

F

R

K

L

L

C

F

N

D

S

S

L

L

T

T

V

L

L

L

R

A

D

S

G

G

R

R

L

L

A

M

A

F

H

H

H

G

P

P

Sites not aligning to the query:

binding (s)-10-[(dimethylamino)methyl]-4-ethyl-4,9-dihydroxy-1h-pyrano[3',4':6,7]inolizino[1,2-b]-quinoline-3,14(4h,12h)-dione: 345, 348, 458

6vxhA Structure of abcg2 bound to imatinib (see paper)
30% identity, 43% coverage: 5:223/508 of query aligns to 3:221/565 of 6vxhA

query
sites
6vxhA

L

L

E

S

F

F

Q

H

S

N

I

I

S

C

K

-

G

-

Y

Y

P

R

G

V

V

K

Q

E

A

I

L

L

S

S

E

N

V

I

S

N

F

-

S

G

V

I

R

M

K

K

G

P

A

G

V

L

H

N

G

A

L

I

M

L

G

G

E

P

N

T

G

G

A

G

G

G

K

K

S

S

T

S

L

L

I

L

R

D

V

V

L

L

S

A

G

A

-

R

-

K

D

D

Q

P

A

S

A

G

D

L

T

S

G

G

E

D

I

V

R

L

I

I

N

N

G

G

E

A

P

P

Q

-

H

-

Y

-

R

R

S

P

V

A

R

N

D

F

A

K

F

C

N

N

A

S

G

G

V

Y

I

V

V

V

I

-

H

-

Q

Q

E

D

L

D

Q

V

L

V

V

M

P

G

E

T

L

L

T

T

V

V

A

R

E

E

N

N

L

L

W

Q

L

F

G

S

R

A

F

A

P

L

G

R

K

L

A

A

G

T

V

T

I

M

D

T

R

N

R

H

Q

E

L

K

I

N

R

E

V

R

V

I

S

N

D

R

R

V

L

I

A

Q

E

E

I

L

G

G

I

L

D

D

V

K

D

V

P

A

E

D

A

S

K

K

V

V

A

G

S

T

-

Q

-

F

-

I

-

R

-

G

L

V

S

S

I

G

G

G

E

E

R

R

Q

K

M

R

V

T

E

S

I

I

A

G

K

M

A

E

V

L

M

I

T

T

D

D

A

P

R

S

V

I

I

L

A

F

L

L

D

D

E

E

P

P

T

T

S

T

S

G

L

L

S

D

S

S

R

S

E

T

S

A

E

N

I

A

L

V

F

L

A

L

L

L

I

L

D

K

R

R

L

M

R

S

S

K

N

Q

G

G

T

R

V

T

I

I

L

I

Y

F

V

S

S

I

H

H

R

Q

L

P

-

R

D

Y

E

S

I

I

F

F

R

K

L

L

C

F

N

D

S

S

L

L

T

T

V

L

L

L

R

A

D

S

G

G

R

R

L

L

A

M

A

F

H

H

H

G

P

P

Sites not aligning to the query:

Q9UNQ0 Broad substrate specificity ATP-binding cassette transporter ABCG2; ATP-binding cassette sub-family G member 2; Breast cancer resistance protein; CDw338; Mitoxantrone resistance-associated protein; Placenta-specific ATP-binding cassette transporter; Urate exporter; CD338 antigen; EC 7.6.2.2 from Homo sapiens (Human) (see 20 papers)
31% identity, 39% coverage: 27:223/508 of query aligns to 70:269/655 of Q9UNQ0

query
sites
Q9UNQ0

V

I

R
x
M

K

K

G

P

A

G

V

L

H

N

G

A

L

I

M

L

G
|
G

E
x
P

N
x
T

G
|
G

A
x
G

G
|
G

K
|
K

S
|
S

T

S

L

L

I

L

R

D

V

V

L

L

S

A

G

A

-

R

-

K

D

D

Q

P

A

S

A

G

D

L

T

S

G

G

E

D

I

V

R

L

I

I

N

N

G

G

E

A

P

P

Q

-

H

-

Y

-

R

R

S

P

V

A

R

N

D

F

A

K

F

C

N

N

A

S

G

G

V

Y

I

V

V

V

I

-

H

-

Q

Q

E

D

L

D

Q

V

L

V

V

M

P

G

E

T

L

L

T

T

V

V

A

R

E

E

N

N

L

L

W
x
Q

L

F

G

S

R

A

F

A

P

L

G
x
R

K

L

A

A

G

T

V

T

I

M

D
x
T

R

N

R

H

Q

E

L

K

I

N

R

E

V
x
R

V

I

S

N

D

R

R

V

L

I

A
x
Q

E

E

I

L

G

G

I

L

D

D

V

K

D

V

P

A

E

D

A

S

K

K

V

V

A

G

S

T

-

Q

-

F

-

I

-
x
R

-
x
G

L
x
V

S
|
S

I
x
G

G
|
G

E
|
E

R

R

Q

K

M

R

V

T

E

S

I

I

A

G

K

M

A

E

V

L

M

I

T

T

D

D

A

P

R

S

V
x
I

I

L

A
x
F

L

L

D

D

E
|
E

P

P

T

T

S

T

S

G

L

L

S

D

S

S

R

S

E

T

S

A

E

N

I

A

L

V

F

L

A

L

L

L

I

L

D

K

R

R

L

M

R

S

S

K

N

Q

G

G

T

R

V

T

I

I

L

I

Y

F

V

S

S

I

H
|
H

R

Q

L

P

-

R

D

Y

E

S

I

I

F

F

R

K

L

L

C

F

N

D

S

S

L

L

T

T

V

L

L

L

R

A

D

S

G

G

R

R

L

L

A

M

A

F

H

H

H

G

P

P

M71 (≠ R28) mutation to V: Decreased protein abundance. No effect on substrate transmembrane transport.
80:87 (vs. 37:44, 63% identical) binding
K86 (= K43) mutation to M: Decreased protein abundance. Decreased localization to the plasma membrane and retained intracellularly. Loss of ATPase-coupled transmembrane transporter activity.
Q141 (≠ W101) to K: associated with high serum levels of uric acid and increased risk of gout; results in lower urate transport rates compared to wild-type; decreased protein abundance; dbSNP:rs2231142
R147 (≠ G107) to W: loss of protein expression; loss of localization to the plasma membrane; dbSNP:rs372192400
T153 (≠ D113) to M: decreased protein abundance; no effect on localization to the plasma membrane; no effect on substrate transmembrane transport; decreased ATPase activity; no effect on ATPase-coupled transmembrane transporter activity; dbSNP:rs753759474
R160 (≠ V120) to Q: in dbSNP:rs528655917
Q166 (≠ A126) to E: in dbSNP:rs1061017
184:190 (vs. 141:145, 43% identical) binding
I206 (≠ V161) to L: in dbSNP:rs12721643
F208 (≠ A163) to S: in dbSNP:rs1061018
E211 (= E166) binding ; mutation to Q: Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport.
H243 (= H198) binding

Sites not aligning to the query:

12 V → M: found in Jr(a-) blood group phenotype; dbSNP:rs2231137
13 S → L: in dbSNP:rs1319203095
296 D → H: in dbSNP:rs41282401
316 natural variant: T -> P
354 G → R: in dbSNP:rs138606116
360 natural variant: Missing (no effect on protein abundance; no effect on localization to the plasma membrane; no effect on ATPase activity; no effect on substrate transmembrane transport)
362 modified: Phosphothreonine; by PIM1; T→A: Loss of phosphorylation by PIM1. Decreased localization to the plasma membrane. Decreased homooligomerization. Loss of function in resistance to drug treatment.; T→D: Loss of phosphorylation by PIM1. Constitutive drug resistance independent of PIM1.
373 F → C: decreased protein abundance; decreased localization to the plasma membrane; no effect on ATPase-coupled transmembrane transporter activity; dbSNP:rs752626614
383 R→C: Loss of protein expression.
418 Not glycosylated; N→Q: No effect.
421 T → A: no effect on protein abundance; no effect on substrate transmembrane transport; dbSNP:rs199854112
431 natural variant: F -> L
434 T → M: no effect on protein abundance; no effect on localization to the plasma membrane; increased ATPase activity; decreased ATPase-coupled transmembrane transporter activity; dbSNP:rs769734146
435 T→A: No effect on stability. Increased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Increased substrate-induced ATP hydrolysis. Increased substrate transport.; T→F: No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport.
436 N→A: No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport.
439 F→A: No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport.
441 S → N: in dbSNP:rs1354553769
476 S → P: no effect on protein abundance; no effect on localization to the plasma membrane; no effect on ATPase activity; decreased ATPase-coupled transmembrane transporter activity; dbSNP:rs1274428653
482 R→D: Decreases ATPase activity.; mutation R->G,N,S,T: Increases ATPase activity.; mutation R->K,I,M,Y: No change in ATPase activity.; mutation R->T,Y: Decreases transport activity.
489 F → L: in dbSNP:rs192169063
528 A → T: in dbSNP:rs45605536
546 V→A: No effect on stability. No effect on estrone-3 sulfate ATPase-coupled transmembrane transporter activity. No effect on substrate-induced ATP hydrolysis. No effect on substrate transport.; V→F: No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Increased basal and substrate-induced ATP hydrolysis. Decreased substrate transport.
549 M→A: No effect on stability. No effect on estrone-3 sulfate ATPase-coupled transmembrane transporter activity. No effect on substrate-induced ATP hydrolysis. No effect on substrate transport.
554 L→A: No effect on stability. Increased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Increased basal and substrate-induced ATP hydrolysis. Increased substrate transport.
555 L→A: Loss of protein expression.
557 Not glycosylated; N→Q: No effect.
572 S → R: decreased protein abundance; loss of localization to the plasma membrane; dbSNP:rs200894058
583 H→A: Strongly reduced binding to hemin but not to PPIX.
590 N → Y: in dbSNP:rs34264773
592 modified: Disulfide link with 608
596 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Loss of glycosylation.
603 modified: Interchain; C→A: Strongly reduced binding to hemin but not to PPIX.
605 Y→A: No effect on hemin binding.
608 modified: Disulfide link with 592
620 D → N: no effect on protein abundance; no effect on substrate transmembrane transport; dbSNP:rs34783571

7neqA Structure of tariquidar-bound abcg2 (see paper)
30% identity, 43% coverage: 5:223/508 of query aligns to 3:221/566 of 7neqA

query
sites
7neqA

L

L

E

S

F

F

Q

H

S

N

I

I

S

C

K

-

G

-

Y

Y

P

R

G

V

V

K

Q

E

A

I

L

L

S

S

E

N

V

I

S

N

F

-

S

G

V

I

R

M

K

K

G

P

A

G

V

L

H

N

G

A

L

I

M

L

G

G

E

P

N

T

G

G

A

G

G

G

K

K

S

S

T

S

L

L

I

L

R

D

V

V

L

L

S

A

G

A

-

R

-

K

D

D

Q

P

A

S

A

G

D

L

T

S

G

G

E

D

I

V

R

L

I

I

N

N

G

G

E

A

P

P

Q

-

H

-

Y

-

R

R

S

P

V

A

R

N

D

F

A

K

F

C

N

N

A

S

G

G

V

Y

I

V

V

V

I

-

H

-

Q

Q

E

D

L

D

Q

V

L

V

V

M

P

G

E

T

L

L

T

T

V

V

A

R

E

E

N

N

L

L

W

Q

L

F

G

S

R

A

F

A

P

L

G

R

K

L

A

A

G

T

V

T

I

M

D

T

R

N

R

H

Q

E

L

K

I

N

R

E

V

R

V

I

S

N

D

R

R

V

L

I

A

Q

E

E

I

L

G

G

I

L

D

D

V

K

D

V

P

A

E

D

A

S

K

K

V

V

A

G

S

T

-

Q

-

F

-

I

-

R

-

G

L

V

S

S

I

G

G

G

E

E

R

R

Q

K

M

R

V

T

E

S

I

I

A

G

K

M

A

E

V

L

M

I

T

T

D

D

A

P

R

S

V

I

I

L

A

F

L

L

D

D

E

E

P

P

T

T

S

T

S

G

L

L

S

D

S

S

R

S

E

T

S

A

E

N

I

A

L

V

F

L

A

L

L

L

I

L

D

K

R

R

L

M

R

S

S

K

N

Q

G

G

T

R

V

T

I

I

L

I

Y

F

V

S

S

I

H

H

R

Q

L

P

-

R

D

Y

E

S

I

I

F

F

R

K

L

L

C

F

N

D

S

S

L

L

T

T

V

L

L

L

R

A

D

S

G

G

R

R

L

L

A

M

A

F

H

H

H

G

P

P

Sites not aligning to the query:

6vxjA Structure of abcg2 bound to sn38 (see paper)
30% identity, 43% coverage: 5:223/508 of query aligns to 3:221/566 of 6vxjA

query
sites
6vxjA

L

L

E

S

F

F

Q

H

S

N

I

I

S

C

K

-

G

-

Y

Y

P

R

G

V

V

K

Q

E

A

I

L

L

S

S

E

N

V

I

S

N

F

-

S

G

V

I

R

M

K

K

G

P

A

G

V

L

H

N

G

A

L

I

M

L

G

G

E

P

N

T

G

G

A

G

G

G

K

K

S

S

T

S

L

L

I

L

R

D

V

V

L

L

S

A

G

A

-

R

-

K

D

D

Q

P

A

S

A

G

D

L

T

S

G

G

E

D

I

V

R

L

I

I

N

N

G

G

E

A

P

P

Q

-

H

-

Y

-

R

R

S

P

V

A

R

N

D

F

A

K

F

C

N

N

A

S

G

G

V

Y

I

V

V

V

I

-

H

-

Q

Q

E

D

L

D

Q

V

L

V

V

M

P

G

E

T

L

L

T

T

V

V

A

R

E

E

N

N

L

L

W

Q

L

F

G

S

R

A

F

A

P

L

G

R

K

L

A

A

G

T

V

T

I

M

D

T

R

N

R

H

Q

E

L

K

I

N

R

E

V

R

V

I

S

N

D

R

R

V

L

I

A

Q

E

E

I

L

G

G

I

L

D

D

V

K

D

V

P

A

E

D

A

S

K

K

V

V

A

G

S

T

-

Q

-

F

-

I

-

R

-

G

L

V

S

S

I

G

G

G

E

E

R

R

Q

K

M

R

V

T

E

S

I

I

A

G

K

M

A

E

V

L

M

I

T

T

D

D

A

P

R

S

V

I

I

L

A

F

L

L

D

D

E

E

P

P

T

T

S

T

S

G

L

L

S

D

S

S

R

S

E

T

S

A

E

N

I

A

L

V

F

L

A

L

L

L

I

L

D

K

R

R

L

M

R

S

S

K

N

Q

G

G

T

R

V

T

I

I

L

I

Y

F

V

S

S

I

H

H

R

Q

L

P

-

R

D

Y

E

S

I

I

F

F

R

K

L

L

C

F

N

D

S

S

L

L

T

T

V

L

L

L

R

A

D

S

G

G

R

R

L

L

A

M

A

F

H

H

H

G

P

P

Sites not aligning to the query:

6vxiA Structure of abcg2 bound to mitoxantrone (see paper)
30% identity, 43% coverage: 5:223/508 of query aligns to 3:221/566 of 6vxiA

query
sites
6vxiA

L

L

E

S

F

F

Q

H

S

N

I

I

S

C

K

-

G

-

Y

Y

P

R

G

V

V

K

Q

E

A

I

L

L

S

S

E

N

V

I

S

N

F

-

S

G

V

I

R

M

K

K

G

P

A

G

V

L

H

N

G

A

L

I

M

L

G

G

E

P

N

T

G

G

A

G

G

G

K

K

S

S

T

S

L

L

I

L

R

D

V

V

L

L

S

A

G

A

-

R

-

K

D

D

Q

P

A

S

A

G

D

L

T

S

G

G

E

D

I

V

R

L

I

I

N

N

G

G

E

A

P

P

Q

-

H

-

Y

-

R

R

S

P

V

A

R

N

D

F

A

K

F

C

N

N

A

S

G

G

V

Y

I

V

V

V

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N

N

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Sites not aligning to the query:

6feqA Structure of inhibitor-bound abcg2 (see paper)
30% identity, 43% coverage: 5:223/508 of query aligns to 3:221/566 of 6feqA

query
sites
6feqA

L

L

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Sites not aligning to the query:

binding ~{N}-[5-[1-[4-[2-[6-methoxy-7-[2-[2-(2-methoxyethoxy)ethoxy]ethoxy]-3,4-dihydro-1~{H}-isoquinolin-2-yl]ethyl]phenyl]-1,2,3-triazol-4-yl]-2-propanoyl-phenyl]quinoline-2-carboxamide: 348, 351, 455, 458, 461

6etiA Structure of inhibitor-bound abcg2 (see paper)
30% identity, 43% coverage: 5:223/508 of query aligns to 3:221/566 of 6etiA

query
sites
6etiA

L

L

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L

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G

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Sites not aligning to the query:

binding ~{tert}-butyl 3-[(2~{S},5~{S},8~{S})-14-cyclopentyloxy-2-(2-methylpropyl)-4,7-bis(oxidanylidene)-3,6,17-triazatetracyclo[8.7.0.0^{3,8}.0^{11,16}]heptadeca-1(10),11,13,15-tetraen-5-yl]propanoate: 309, 313, 351, 455, 458, 461

6hijA Cryo-em structure of the human abcg2-mz29-fab complex with cholesterol and pe lipids docked (see paper)
31% identity, 39% coverage: 27:223/508 of query aligns to 28:227/572 of 6hijA

query
sites
6hijA

V

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K

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N

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T

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E

N

N

L

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A

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Sites not aligning to the query:

Query Sequence

>SM_b20507 FitnessBrowser__Smeli:SM_b20507
MQDFLEFQSISKGYPGVQALSEVSFSVRKGAVHGLMGENGAGKSTLIRVLSGDQAADTGE
IRINGEPQHYRSVRDAFNAGVIVIHQELQLVPELTVAENLWLGRFPGKAGVIDRRQLIRV
VSDRLAEIGIDVDPEAKVASLSIGERQMVEIAKAVMTDARVIALDEPTSSLSSRESEILF
ALIDRLRSNGTVILYVSHRLDEIFRLCNSLTVLRDGRLAAHHPDISKVGREQIIAEMVGR
EISNIWGWRARTLGAARLTVERVSGANLPQPISFTVRAGEILGFFGLIGAGRSEMARLVY
GADRRRQGKVLVDGLAVPADSPRLSIRAGVVLCPEDRKFDGIVQGRSIEENMAISSRRHF
SPFGVVDKGKEAELAERFIAKLRVRTPSRHQDIVNLSGGNQQKVILGRWLSEEGVKVLLI
DEPTRGIDVGAKSEIYEILYELAAQGMAIVVISSELPEVMGIADRILVMCEGRIAAEIDR
SDFDEHRILAAALPDASATTATLPEQVS

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