SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_009130737.1 NCBI__GCF_000315485.1:WP_009130737.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

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)
39% identity, 57% coverage: 28:216/333 of query aligns to 30:218/265 of P07821

query
sites
P07821

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K50 (= K48) mutation to Q: Lack of activity.
D172 (= D170) mutation to E: Lack of activity.
E173 (= E171) 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)
33% identity, 65% coverage: 1:218/333 of query aligns to 1:218/233 of P75957

query
sites
P75957

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

7z15I E. Coli c-p lyase bound to a phnk/phnl dual abc dimer and adp + pi (see paper)
32% identity, 70% coverage: 3:234/333 of query aligns to 1:232/253 of 7z15I

query
sites
7z15I

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binding adenosine-5'-diphosphate: Y13 (= Y15), K17 (= K19), G18 (≠ Q20), S38 (≠ N44), G39 (= G45), G41 (= G47), K42 (= K48), T43 (≠ S49), T44 (= T50), R136 (≠ K138), T143 (≠ E145), S145 (= S147), M148 (≠ E150)
binding magnesium ion: T43 (≠ S49), Q88 (vs. gap)

7z18I E. Coli c-p lyase bound to a phnk abc dimer and atp (see paper)
32% identity, 70% coverage: 3:234/333 of query aligns to 1:232/250 of 7z18I

query
sites
7z18I

K

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binding adenosine-5'-triphosphate: Y13 (= Y15), S38 (≠ N44), G39 (= G45), S40 (≠ T46), G41 (= G47), K42 (= K48), T43 (≠ S49), T44 (= T50), Q88 (vs. gap), R136 (≠ K138), T143 (≠ E145), S145 (= S147), G147 (= G149), M148 (≠ E150), H202 (= H204)
binding magnesium ion: T43 (≠ S49), Q88 (vs. gap)

7z16I E. Coli c-p lyase bound to phnk/phnl dual abc dimer with amppnp and phnk e171q mutation (see paper)
32% identity, 70% coverage: 3:234/333 of query aligns to 1:232/250 of 7z16I

query
sites
7z16I

K

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binding phosphoaminophosphonic acid-adenylate ester: Y13 (= Y15), K17 (= K19), S38 (≠ N44), G39 (= G45), S40 (≠ T46), G41 (= G47), K42 (= K48), T43 (≠ S49), T44 (= T50), R136 (≠ K138), T143 (≠ E145), S145 (= S147), G147 (= G149), M148 (≠ E150), H202 (= H204)

7v8iD Lolcd(e171q)e with bound amppnp in nanodiscs (see paper)
32% identity, 65% coverage: 2:218/333 of query aligns to 1:217/229 of 7v8iD

query
sites
7v8iD

E

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A

S

N
x
S

G
|
G

T

S

G
|
G

K
|
K

S
|
S

T
|
T

L

L

R

H

T

L

L

L

A

G

S

L

Q

D

P

T

A

P

L

T

S

S

G

G

E

D

L

V

L

I

V

F

E

N

D

G

K

Q

P

P

L

M

S

S

A

K

Y

L

S

S

E

S

K

A

E

A

-

K

-

A

-

E

-

L

R

R

S

N

R

Q

T

K

I

L

G

G

V

F

V

I

L

Y

T
x
Q

D

F

K

H

T

H

Q

L

A

L

G

P

G

D

L

F

T

T

V

A

Y

L

E

E

L

N

V

V

A

A

L

M

G

P

R

L

Q

-

P

-

H

-

T

-

G

-

F

L

F

I

G

G

R

K

L

K

N

K

K

P

A

A

D

E

-

I

H

N

A

S

I

R

I

A

E

L

E

E

A

M

L

L

E

K

A

A

V

V

S

G

I

L

S

D

H

H

K
x
R

A

A

Q

N

S
x
H

Y

R

T

P

A

S

E
|
E

L

L

S
|
S

D

G

G
|
G

E
|
E

R

R

Q

Q

K

R

V

V

M

A

I

I

A

A

K

R

A

A

L

L

V

V

Q

N

E

N

C

P

P

R

L

L

I

V

L

L

L

A

D

D

E

Q

P

P

T

T

A

G

F

N

L

L

D

D

V

A

V

R

S

N

R

A

I

D

E

S

I

I

M

F

T

Q

L

L

H

G

R

E

L

L

A

N

V

R

E

L

Q

Q

S

G

K

T

A

A

I

F

L

L

L

V

S

V

T

T

H
|
H

D

D

I

L

E

Q

Q

L

A

A

L

K

V

R

L

M

A

S

D

R

K

Q

L

L

W

E

L

M

binding phosphoaminophosphonic acid-adenylate ester: V23 (= V24), S43 (≠ N44), G44 (= G45), G46 (= G47), K47 (= K48), S48 (= S49), T49 (= T50), Q93 (≠ T90), R137 (≠ K138), H140 (≠ S141), E144 (= E145), S146 (= S147), G148 (= G149), E149 (= E150), H203 (= H204)
binding magnesium ion: S48 (= S49), Q93 (≠ T90)

7arlD Lolcde in complex with lipoprotein and adp (see paper)
32% identity, 64% coverage: 5:218/333 of query aligns to 2:215/222 of 7arlD

query
sites
7arlD

V

L

I

L

T

Q

A

C

N

D

N

N

L

L

C

C

I

K

G

R

Y

Y

R

Q

Q

E

G

G

K

S

Q

V

E

Q

K

T

R

D

V

V

H

L

E

H

H

N

L

V

S

S

F

F

Q

S

L

V

Y

G

P

E

G

G

E

E

L

M

T

M

C

A

L

I

L

V

G

G

A

S

N

S

G
|
G

T

S

G
|
G

K
|
K

S
|
S

T

T

L

L

R

H

T

L

L

L

A

G

S

L

Q

D

P

T

A

P

L

T

S

S

G

G

E

D

L

V

L

I

V

F

E

N

D

G

K

Q

P

P

L

M

S

S

A

K

Y

L

S

S

E

S

K

A

E

A

-

K

-

A

-

E

-

L

R

R

S

N

R

Q

T

K

I

L

G

G

V

F

V

I

L

Y

T

Q

D

F

K

H

T

H

Q

L

A

L

G

P

G

D

L

F

T

T

V

A

Y

L

E

E

L

N

V

V

A

A

L

M

G

P

R

L

Q

-

P

-

H

-

T

-

G

-

F

L

F

I

G

G

R

K

L

K

N

K

K

P

A

A

D

E

-

I

H

N

A

S

I

R

I

A

E

L

E

E

A

M

L

L

E

K

A

A

V

V

S

G

I

L

S

D

H

H

K

R

A

A

Q

N

S

H

Y

R

T

P

A

S

E

E

L

L

S

S

D

G

G

G

E

E

R

R

Q

Q

K

R

V

V

M

A

I

I

A

A

K

R

A

A

L

L

V

V

Q

N

E

N

C

P

P

R

L

L

I

V

L

L

L

A

D

D

E

E

P

P

T

T

A

G

F

N

L

L

D

D

V

A

V

R

S

N

R

A

I

D

E

S

I

I

M

F

T

Q

L

L

H

G

R

E

L

L

A

N

V

R

E

L

Q

Q

S

G

K

T

A

A

I

F

L

L

L

V

S

V

T

T

H

H

D

D

I

L

E

Q

Q

L

A

A

L

K

V

R

L

M

A

S

D

R

K

Q

L

L

W

E

L

M

binding adenosine-5'-diphosphate: G42 (= G45), G44 (= G47), K45 (= K48), S46 (= S49)

7mdyC Lolcde nucleotide-bound
32% identity, 64% coverage: 5:218/333 of query aligns to 2:215/226 of 7mdyC

query
sites
7mdyC

V

L

I

L

T

Q

A

C

N

D

N

N

L

L

C

C

I

K

G

R

Y
|
Y

R

Q

Q

E

G

G

K

S

Q

V

E

Q

K

T

R

D

V

V

H

L

E

H

H

N

L

V

S

S

F

F

Q

S

L

V

Y

G

P

E

G

G

E

E

L

M

T

M

C

A

L

I

L

V

G

G

A

S

N

S

G
|
G

T
x
S

G
|
G

K
|
K

S
|
S

T
|
T

L

L

R

H

T

L

L

L

A

G

S

L

Q

D

P

T

A

P

L

T

S

S

G

G

E

D

L

V

L

I

V

F

E

N

D

G

K

Q

P

P

L

M

S

S

A

K

Y

L

S

S

E

S

K

A

E

A

-

K

-

A

-

E

-

L

R

R

S

N

R

Q

T

K

I

L

G

G

V

F

V

I

L

Y

T
x
Q

D

F

K

H

T

H

Q

L

A

L

G

P

G

D

L

F

T

T

V

A

Y

L

E

E

L

N

V

V

A

A

L

M

G

P

R

L

Q

-

P

-

H

-

T

-

G

-

F

L

F

I

G

G

R

K

L

K

N

K

K

P

A

A

D

E

-

I

H

N

A

S

I

R

I

A

E

L

E

E

A

M

L

L

E

K

A

A

V

V

S

G

I

L

S

D

H

H

K

R

A

A

Q

N

S
x
H

Y

R

T

P

A

S

E
|
E

L

L

S
|
S

D
x
G

G
|
G

E

E

R

R

Q

Q

K

R

V

V

M

A

I

I

A

A

K

R

A

A

L

L

V

V

Q

N

E

N

C

P

P

R

L

L

I

V

L

L

L

A

D

D

E
|
E

P

P

T

T

A

G

F
x
N

L

L

D

D

V

A

V

R

S

N

R

A

I

D

E

S

I

I

M

F

T

Q

L

L

H

G

R

E

L

L

A

N

V

R

E

L

Q

Q

S

G

K

T

A

A

I

F

L

L

L

V

S

V

T

T

H
|
H

D

D

I

L

E

Q

Q

L

A

A

L

K

V

R

L

M

A

S

D

R

K

Q

L

L

W

E

L

M

binding adp orthovanadate: Y12 (= Y15), G42 (= G45), S43 (≠ T46), G44 (= G47), K45 (= K48), S46 (= S49), T47 (= T50), Q91 (≠ T90), H138 (≠ S141), E142 (= E145), S144 (= S147), G145 (≠ D148), G146 (= G149), E168 (= E171), N172 (≠ F175), H201 (= H204)
binding magnesium ion: S46 (= S49), Q91 (≠ T90)

5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
33% identity, 62% coverage: 3:209/333 of query aligns to 1:206/226 of 5xu1B

query
sites
5xu1B

K

K

A

Q

V

L

I

I

T

S

A

L

N

K

N

N

L

I

C

F

I

R

G

S

Y

Y

R

R

Q

N

G

G

K

D

Q

Q

E

E

K

L

R

Q

V

V

H

L

E

K

H

N

L

I

S

N

F

L

Q

E

L

V

Y

N

P

E

G

G

E

E

L

F

T

V

C

A

L

I

L

M

G

G

A

P

N

S

G

G

T

S

G
|
G

K
|
K

S
|
S

T

T

L

L

L

M

R

N

T

T

L

I

A

G

A

M

S

L

Q

D

P

T

A

P

L

T

S

S

G

G

E

E

L

Y

V

L

E

E

D

G

K

Q

P

E

L

V

S

A

A

G

Y

L

S

G

E

E

K

K

E

Q

-

L

-

A

-

K

-

V

R

R

S

N

R

Q

T

Q

I

I

G

G

V

F

V

V

L

F

T

Q

D

Q

K

F

T

F

Q

L

A

L

G

S

G

K

L

L

T

N

V

A

Y

L

E

Q

L

N

V

V

A

E

L

L

G

-

R

-

Q

-

P

P

H

L

T

I

G

-

F

Y

F

A

G

G

R

V

L

S

N

S

K

S

A

K

D

R

H

R

A

K

I

L

I

A

E

E

A

Y

L

L

E

D

A

K

V

V

S

E

I

L

S

T

H

E

K

R

A

S

Q

H

S

H

Y

L

T

P

A

S

E

E

L

L

S

S

D

G

G

G

E

Q

R

K

Q

Q

K

R

V

V

M

A

I

I

A

A

K

R

A

A

L

L

V

V

Q

N

E

N

C

P

P

S

L

I

I

I

L

L

L

A

D

D

E

E

P

P

T

T

A

G

F

A

L

L

D

D

V

T

V

K

S

T

R

G

I

N

E

Q

I

I

M

M

T

Q

L

L

H

V

R

D

L

L

A

N

V

K

E

E

Q

-

S

G

K

K

A

T

I

I

L

I

L

M

S

V

T

T

H

H

D

E

I

P

E

E

Q

I

A

A

binding magnesium ion: G45 (= G47), K46 (= K48), S47 (= S49)

6z67B Ftse structure of streptococcus pneumoniae in complex with amppnp at 2.4 a resolution (see paper)
34% identity, 53% coverage: 28:205/333 of query aligns to 23:198/229 of 6z67B

query
sites
6z67B

L

V

S

S

F

V

Q

S

L

V

Y

Q

P

P

G

G

E

E

L

F

T

A

C

Y

L

I

L

V

G

G

A

P

N
x
S

G
|
G

T

A

G
|
G

K
|
K

S
|
S

T
|
T

L

F

L

I

R

R

T

S

L

L

A

Y

A

R

S

E

Q

V

P

K

A

I

L

D

S

K

G

G

E

S

L

L

L

S

V

V

E

A

D

G

K

F

P

N

L

L

S

V

A

K

Y

I

S

K

E

K

K

K

E

D

R

V

S

P

-

L

-

R

R

R

T

S

I

V

G

G

V

V

L

F

T

Q

D

D

K

Y

T

K

Q

L

A

L

G

P

G

K

L

K

T

T

V

V

Y

Y

E

E

L

N

V

I

A

A

L

Y

G

A

R

M

Q

E

P

-

H

-

T

-

G

-

F

V

F

I

G

G

R

E

L

N

N

R

K

R

A

N

D

I

H

K

A

R

I

R

I

V

E

M

E

E

A

V

L

L

E

D

A

L

V

V

S

G

I

L

S

K

H

H

K

K

A

V

Q

R

S

S

Y

F

T

P

A

N

E

E

L

L

S

S

D

G

G

G

E

E

R

Q

Q

Q

K

R

V

I

M

A

I

I

A

A

K

R

A

A

L

I

V

V

Q

N

E

N

C

P

P

K

L

V

I

L

L

I

L

A

D

D

E

E

P

P

T

T

A

G

F

N

L

L

D

D

V

P

V

D

S

N

R

S

I

W

E

E

I

I

M

M

T

N

L

L

H

E

R

R

L

I

A

N

V

L

E

-

Q

Q

S

G

K

T

A

T

I

I

L

L

L

M

S

A

T

T

H

H

D

N

binding phosphoaminophosphonic acid-adenylate ester: S39 (≠ N44), G40 (= G45), G42 (= G47), K43 (= K48), S44 (= S49), T45 (= T50)

Sites not aligning to the query:

binding phosphoaminophosphonic acid-adenylate ester: 13, 16, 19

6z4wA Ftse structure from streptococcus pneumoniae in complex with adp (space group p 1) (see paper)
34% identity, 53% coverage: 28:205/333 of query aligns to 23:198/230 of 6z4wA

query
sites
6z4wA

L

V

S

S

F

V

Q

S

L

V

Y

Q

P

P

G

G

E

E

L

F

T

A

C

Y

L

I

L

V

G

G

A

P

N

S

G
|
G

T

A

G
|
G

K
|
K

S
|
S

T
|
T

L

F

L

I

R

R

T

S

L

L

A

Y

A

R

S

E

Q

V

P

K

A

I

L

D

S

K

G

G

E

S

L

L

L

S

V

V

E

A

D

G

K

F

P

N

L

L

S

V

A

K

Y

I

S

K

E

K

K

K

E

D

R

V

S

P

-

L

-

R

R

R

T

S

I

V

G

G

V

V

L

F

T

Q

D

D

K

Y

T

K

Q

L

A

L

G

P

G

K

L

K

T

T

V

V

Y

Y

E

E

L

N

V

I

A

A

L

Y

G

A

R

M

Q

E

P

-

H

-

T

-

G

-

F

V

F

I

G

G

R

E

L

N

N

R

K

R

A

N

D

I

H

K

A

R

I

R

I

V

E

M

E

E

A

V

L

L

E

D

A

L

V

V

S

G

I

L

S

K

H

H

K

K

A

V

Q

R

S

S

Y

F

T

P

A

N

E

E

L

L

S

S

D

G

G

G

E

E

R

Q

Q

Q

K

R

V

I

M

A

I

I

A

A

K

R

A

A

L

I

V

V

Q

N

E

N

C

P

P

K

L

V

I

L

L

I

L

A

D

D

E

E

P

P

T

T

A

G

F

N

L

L

D

D

V

P

V

D

S

N

R

S

I

W

E

E

I

I

M

M

T

N

L

L

H

E

R

R

L

I

A

N

V

L

E

-

Q

Q

S

G

K

T

A

T

I

I

L

L

L

M

S

A

T

T

H

H

D

N

binding adenosine-5'-diphosphate: G40 (= G45), G42 (= G47), K43 (= K48), S44 (= S49), T45 (= T50)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 13, 17, 19

A0A0H2ZM82 Cell division ATP-binding protein FtsE from Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) (see paper)
34% identity, 53% coverage: 28:205/333 of query aligns to 23:198/230 of A0A0H2ZM82

query
sites
A0A0H2ZM82

L

V

S

S

F

V

Q

S

L

V

Y

Q

P

P

G

G

E

E

L

F

T

A

C

Y

L

I

L

V

G

G

A

P

N

S

G

G

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A

G

G

K
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K

S

S

T

T

L

F

L

I

R

R

T

S

L

L

A

Y

A

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A

I

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D

S

K

G

G

E

S

L

L

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V

E

A

D

G

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N

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K

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D

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K

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A

L

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G

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K

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Y

Y

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V

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A

L

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A

R

M

Q

E

P

-

H

-

T

-

G

-

F

V

F

I

G

G

R

E

L

N

N

R

K

R

A

N

D

I

H

K

A

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I

R

I

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M

E

E

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A

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A

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C

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I

L

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D
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D

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E

P

P

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N

L

L

D

D

V

P

V

D

S

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I

W

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M

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-

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N

K43 (= K48) mutation to A: Growth cessation and formation of spherical cells with aberrant division planes.
D164 (= D170) mutation to A: Growth cessation and formation of spherical cells with aberrant division planes.
E165 (= E171) mutation to A: Growth cessation and formation of spherical cells with aberrant division planes.

8wm7D Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
30% identity, 63% coverage: 24:233/333 of query aligns to 23:225/257 of 8wm7D

query
sites
8wm7D

V
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V

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D

H

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G

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C

L

L

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I

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H

N
x
S

G
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G

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x
C

G
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G

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K

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S

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T

L

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A

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A

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D

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K

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P

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A

-

Y

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-

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M

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M

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-

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-

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G

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V

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V

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A

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F

F

F

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G

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P

N

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K

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A

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A

A

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I

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R

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E

A

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A

A

M

V

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I

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V

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binding adenosine-5'-diphosphate: V23 (= V24), S43 (≠ N44), G44 (= G45), C45 (≠ T46), G46 (= G47), K47 (= K48), S48 (= S49), T49 (= T50)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 14, 21

O95477 Phospholipid-transporting ATPase ABCA1; ATP-binding cassette sub-family A member 1; ATP-binding cassette transporter 1; ABC-1; ATP-binding cassette 1; Cholesterol efflux regulatory protein; EC 7.6.2.1 from Homo sapiens (Human) (see 35 papers)
31% identity, 71% coverage: 3:239/333 of query aligns to 896:1122/2261 of O95477

query
sites
O95477

K

K

A

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A

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x
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N

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M

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D917 (≠ E26) to Y: in a colorectal cancer sample; somatic mutation
T929 (= T38) to I: in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; loss protein subcellular localization to the plasma membrane
N935 (= N44) to S: in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; dbSNP:rs28937313
K939 (= K48) mutation to M: Inhibits ATPase activity; when associated with M-1952. Decreases translocase activity; when associated with M-1952. Does not affect protein subcellular localization in plasma membrane and endosome; when associated with M-1952.
S1042 (≠ M155) modified: Phosphoserine; by PKA
P1065 (≠ V178) natural variant: P -> S
M1091 (≠ I206) to T: in FHA1; loss of localization to plasma membrane; decreased cholesterol efflux; decreased phospholipid efflux
C1110 (= C227) modified: S-palmitoyl cysteine; mutation to S: Decreased palmitoylation; when associated with S-3, S-23 and S-1111.
C1111 (≠ G228) modified: S-palmitoyl cysteine; mutation to S: Decreased palmitoylation; when associated with S-3, S-23 and S-1110.

Sites not aligning to the query:

3 modified: S-palmitoyl cysteine; C→S: Mild decrease of palmitoylation. Loss of localization to plasma membrane. Decreased cholesterol efflux. Decreased phospholipid efflux. Decreased palmitoylation; when associated with S-23, S-1110 and S-1111.
23 modified: S-palmitoyl cysteine; C→S: Mild decrease of palmitoylation. Loss of localization to plasma membrane. Decreased palmitoylation; when associated with S-3, S-1110 and S-1111.
74 I→C: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with C-371.; I→K: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with E-371.
75 modified: Disulfide link with 309
85 P → L: in FHA1; Alabama; dbSNP:rs145183203
98 modified: carbohydrate, N-linked (GlcNAc...) asparagine
100 S→C: Highly decreased protein abundance. Highly decreased ATPase activity. Highly decreased phospholipid translocase activity.
210 E → D: in a colorectal cancer sample; somatic mutation
219 R → K: in dbSNP:rs2230806
230 R → C: in dbSNP:rs9282541
244 modified: carbohydrate, N-linked (GlcNAc...) asparagine
248 P → A: in dbSNP:rs142625938
255 A → T: in TGD; deficient cellular cholesterol efflux; dbSNP:rs758100110
304 V→C: No effect on phospholipid and cholesterol efflux or localization to cell membrane; when associated with C-308.
308 V→C: No effect on phospholipid and cholesterol efflux or localization to cell membrane; when associated with C-304.
309 modified: Disulfide link with 75
364 S → C: in dbSNP:rs775035559
371 I→C: No effect on phospholipid and cholesterol efflux or localization to cell membrane. 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with C-74 or C-375.; I→E: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-74.
375 L→C: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with C-371.
399 V → A: in dbSNP:rs9282543
401 K → Q: in dbSNP:rs138487227
496 R → W: in dbSNP:rs147675550
568 K→A: 60-65% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane.
573 Y→F: No effect on phospholipid and cholesterol efflux and on localization to cell membrane.
581 D→K: 80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-584 and K-585.
583 F→K: 90-95% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with E-590.
584 E→K: 80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-581 and K-585.
585 D→K: 80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-581 and K-584.
590 W → S: in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; dbSNP:rs137854496; W→E: 90-95% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-583.
593 F→L: Moderately decreased protein abundance. Highly decreased ATPase activity. Highly decreased phospholipid translocase activity.
638 R → Q: in dbSNP:rs374190304
771 V → M: in dbSNP:rs2066718
774 T → P: in dbSNP:rs35819696; natural variant: T -> S
776 K → N: in dbSNP:rs138880920
815 E → G: in dbSNP:rs145582736
825 V → I: in dbSNP:rs2066715
883 I → M: in dbSNP:rs2066714
1172 E → D: in dbSNP:rs33918808
1181 S → F: in dbSNP:rs76881554
1216 G → V: in dbSNP:rs562403512
1341 R → T: in dbSNP:rs147743782
1376 S → G: in dbSNP:rs145689805
1379 L → F: in TGD; the mutant protein is retained in the endoplasmic reticulum while the wild-type protein is located at the plasma membrane
1407 A → T: in a colorectal cancer sample; somatic mutation; dbSNP:rs189206655
1463 modified: Disulfide link with 1477
1477 modified: Disulfide link with 1463; C → R: in TGD; loss of interaction with APOE; unable to generate APOE-containing high density lipoproteins; moderately decreased protein abundance; moderately decreased ATPase activity; moderately decreased phospholipid translocase activity; dbSNP:rs137854494
1512 T→M: Moderately decreased protein abundance. Does not affect ATPase activity. Moderately decreased phospholipid translocase activity.
1555 I → T: in dbSNP:rs1997618
1587 K → R: in dbSNP:rs2230808
1611 N → D: in FHA1; deficient cellular cholesterol efflux
1615 R → Q: in dbSNP:rs1251839800
1648 L → P: in dbSNP:rs1883024
1670 A → T: in dbSNP:rs1203589782
1680 R → Q: in dbSNP:rs150125857
1704 V → D: in TGD; the mutant protein is retained in the endoplasmic reticulum while the wild-type protein is located at the plasma membrane
1731 S → C: in dbSNP:rs760507032
1897 R → W: in FHA1; uncertain significance; dbSNP:rs760768125
1925 R → Q: in Scott syndrome; shows impaired trafficking of the mutant protein to the plasma membrane; dbSNP:rs142688906
1952 K→M: Inhibits ATPase activity; when associated with M-939. Decreases translocase activity; when associated with M-939. Does not affect protein subcellular localization in plasma membrane and endosome; when associated with M-939.
2054 modified: Phosphoserine; by PKA
2081 R → W: in TGD; highly decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; loss protein subcellular localization to the plasma membrane; dbSNP:rs137854501
2109 A → T: in a colorectal cancer sample; somatic mutation
2150 P → L: in FHA1; moderately decreased protein abundance; does not affect ATPase activity; moderately decreased phospholipid translocase activity; dbSNP:rs369098049
2163 natural variant: F -> S
2168 L → P: in dbSNP:rs2853577
2243 D → E: in dbSNP:rs34879708
2244 V → I: in dbSNP:rs144588452

8w9mD Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
29% identity, 63% coverage: 24:233/333 of query aligns to 21:223/256 of 8w9mD

query
sites
8w9mD

V

V

H

L

E

D

H

G

L

I

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F

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V

Y

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P

E

G

G

E

E

L

F

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V

C

C

L

L

L

I

G

G

A
x
H

N
x
S

G
|
G

T

C

G
|
G

K
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K

S
|
S

T
|
T

L

L

R

N

T

M

L

I

A

S

A

G

S

F

Q

N

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T

A

P

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G

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V

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V

L

L

V

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D

D

K

K

P

P

L

I

S

T

A

-

Y

-

S

-

E

E

K

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G

R

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D

R

R

T

M

I

M

G

-

V

-

V

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x
Q

D

N

K

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T

C

Q

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A

L

G

P

G

W

L

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N

V

V

Y

F

E

E

L

N

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Y

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T

A

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V

F

F

F

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G

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K

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K

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A

A

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I

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R

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E

A

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A

A

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V

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K

A

A

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K

Y

K

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P

A

S

E
x
Q

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S
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S

D

G

G
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G

E
x
M

R

K

Q

Q

K

R

V

V

M

A

I

I

A

A

K

R

A

A

L

L

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Q

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C

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P

Q

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I

L

L

I

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D

D

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Q

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F

A

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A

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A

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K

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T

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H
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H

D

D

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I

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D

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E

A

A

L

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V

F

L

L

A

A

D

D

K

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V

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K

N

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N

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I

binding adenosine-5'-triphosphate: H40 (≠ A43), S41 (≠ N44), G42 (= G45), G44 (= G47), K45 (= K48), S46 (= S49), T47 (= T50), Q82 (≠ T90), Q135 (≠ E145), S137 (= S147), G139 (= G149), M140 (≠ E150), H194 (= H204)
binding magnesium ion: S46 (= S49), Q82 (≠ T90)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 12

7tbwA The structure of atp-bound abca1 (see paper)
30% identity, 70% coverage: 6:239/333 of query aligns to 754:977/1928 of 7tbwA

query
sites
7tbwA

I

V

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S

A

I

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Q

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Y

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D

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K

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N

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G

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K

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x
T

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binding adenosine-5'-triphosphate: Y763 (= Y15), D765 (≠ Q17), K768 (= K22), N790 (= N44), G791 (= G45), G793 (= G47), K794 (= K48), T795 (≠ S49), Q835 (≠ T90), Q887 (≠ E145), S889 (= S147), H944 (= H204)
binding magnesium ion: Q835 (≠ T90), D912 (= D170), Q913 (≠ E171)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 1630, 1633, 1657, 1658, 1660, 1661, 1662, 1663, 1702, 1753, 1755, 1756, 1757, 1779, 1783, 1811
binding cholesterol: 218, 219, 360, 367
binding magnesium ion: 1662, 1702

P41233 Phospholipid-transporting ATPase ABCA1; ATP-binding cassette sub-family A member 1; ATP-binding cassette transporter 1; ABC-1; ATP-binding cassette 1; EC 7.6.2.1 from Mus musculus (Mouse) (see paper)
30% identity, 70% coverage: 6:239/333 of query aligns to 899:1122/2261 of P41233

query
sites
P41233

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Sites not aligning to the query:

489 modified: carbohydrate, N-linked (GlcNAc...) asparagine

8iddA Cryo-em structure of mycobacterium tuberculosis atp bound ftsex/ripc complex in peptidisc (see paper)
34% identity, 54% coverage: 26:205/333 of query aligns to 21:198/225 of 8iddA

query
sites
8iddA

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binding adenosine-5'-triphosphate: S39 (≠ N44), G42 (= G47), K43 (= K48), S44 (= S49)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 12

8igqA Cryo-em structure of mycobacterium tuberculosis adp bound ftsex/ripc complex in peptidisc (see paper)
34% identity, 54% coverage: 26:205/333 of query aligns to 21:198/227 of 8igqA

query
sites
8igqA

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binding adenosine-5'-diphosphate: G40 (= G45), S41 (≠ T46), K43 (= K48), S44 (= S49)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 12

P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
29% identity, 62% coverage: 24:228/333 of query aligns to 18:216/371 of P68187

query
sites
P68187

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A85 (≠ T93) mutation to M: Suppressor of EAA loop mutations in MalFG.
K106 (≠ L118) mutation to C: Suppressor of EAA loop mutations in MalFG.
V114 (≠ I126) mutation to C: Suppressor of EAA loop mutations in MalFG.
V117 (≠ A129) mutation to M: Suppressor of EAA loop mutations in MalFG.
E119 (= E131) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
A124 (≠ S136) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
G137 (= G149) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
D158 (= D170) mutation to N: Loss of maltose transport but retains ability to repress mal genes.

Sites not aligning to the query:

228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
267 W→G: Normal maltose transport but constitutive mal gene expression.
278 G→P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
282 S→L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
284 G→S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
302 G→D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
308 E→Q: Maltose transport is affected but retains ability to interact with MalT.
322 S→F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
340 G→A: Maltose transport is affected but retains ability to interact with MalT.
346 G→S: Normal maltose transport but constitutive mal gene expression.
355 F→Y: Maltose transport is affected but retains ability to interact with MalT.

Query Sequence

>WP_009130737.1 NCBI__GCF_000315485.1:WP_009130737.1
MEKAVITANNLCIGYRQGKQEKRVHEHLSFQLYPGELTCLLGANGTGKSTLLRTLAASQP
ALSGELLVEDKPLSAYSEKERSRTIGVVLTDKTQAGGLTVYELVALGRQPHTGFFGRLNK
ADHAIIEEALEAVSISHKAQSYTAELSDGERQKVMIAKALVQECPLILLDEPTAFLDVVS
RIEIMTLLHRLAVEQSKAILLSTHDIEQALVLADKLWLLSKENGLQCGVTEDMILSHRMD
GLFSRNDIRFDYAHGVYYPKVDSHRNIIVEASDEVLLHWTTNALNRHGYACCSDSVAETS
SLPRLQVLSAEDFRLHKEKEYKFHSFEQLLANV

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