SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012335778.1 NCBI__GCF_000019365.1:WP_012335778.1 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 10 hits to proteins with known functional sites (download)

4xfjB Crystal structure of argininosuccinate synthase from mycobacterium thermoresistibile in complex with amppnp and arginine
29% identity, 82% coverage: 31:373/417 of query aligns to 4:338/397 of 4xfjB

query
sites
4xfjB

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active site: D13 (= D40), R94 (= R119), D123 (≠ S148), S174 (= S197)
binding phosphoaminophosphonic acid-adenylate ester: A7 (≠ M34), Y8 (≠ F35), S9 (= S36), T14 (≠ S41), I34 (≠ V61), G116 (≠ T141), C117 (≠ A142), F127 (≠ L152)
binding arginine: Y86 (= Y111), S90 (= S115), R126 (= R151), A183 (≠ E206), E185 (= E208), E259 (= E294), E269 (= E304), Y271 (≠ R306)

7k5zA Crystal structure of argininosuccinate synthase from legionella pneumophila philadelphia 1 in complex with anppnp and a substrate analogue arginine
28% identity, 84% coverage: 35:384/417 of query aligns to 10:351/390 of 7k5zA

query
sites
7k5zA

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active site: D15 (= D40), R95 (= R119), D124 (≠ S148), S176 (= S197)
binding phosphoaminophosphonic acid-adenylate ester: Y10 (≠ F35), S11 (= S36), C37 (≠ V61), G117 (≠ T141), F128 (≠ L152)
binding arginine: Y88 (= Y111), T92 (≠ S115), D124 (≠ S148), R127 (= R151), S185 (≠ E206), E187 (= E208), E261 (= E294), Y273 (≠ R306)

Sites not aligning to the query:

binding phosphoaminophosphonic acid-adenylate ester: 9

P59846 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see 2 papers)
29% identity, 82% coverage: 31:374/417 of query aligns to 3:334/400 of P59846

query
sites
P59846

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6:14 (vs. 34:42, 67% identical) binding ATP
A33 (≠ V61) binding ATP
G114 (≠ T141) binding ATP

1kh3A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with inhibitor (see paper)
29% identity, 82% coverage: 31:374/417 of query aligns to 3:329/380 of 1kh3A

query
sites
1kh3A

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I

E

A

L

Y

A

A

E

E

A

A

G

-

L

-

G

H

A

G

M

I

A

P

E

V

R

P

A

P

L

Y

S
|
S

G
x
M

D
|
D

E

A

N

N

L

L

W

L

C

H

R

I

E
x
S

F

Y

E
|
E

S

G

G

G

P

V

L

L

D

E

D

D

P

P

E

W

D

A

F

-

R

E

I

P

P

P

E

K

E

G

A

M

F

F

H

R

W

M

T

T

R

Q

G

D

R

-

P

-

A

-

P

P

G

E

E

E

G

A

A

P

A

D

S

-

G

-

A

-

G

-

P

-

V

-

A

-

L

-

A

A

P

P

E

E

E

Y

I

V

A

E

L

V

T

E

F

F

E

F

R

E

G

G

D

D

L

P

V

V

A

A

L

V

D

N

G

G

R

E

P

R

I

L

A

S

L

P

I

A

D

A

A

L

I

L

A

Q

E

R

L

L

N

N

Q

E

R

I

V

G

G

G

R

R

F

H

G

G

H

V

G

G

R

R

Y

V

V

D

G

I

L

V

E
|
E

H

N

L

R

S

F

G

V

G

G

E

M

K

K

V

S

L

R

E

G

V

V

R
x
Y

E

E

A

T

P

P

A

G

A

T

I

I

L

L

M

Y

D

H

A

A

L

R

R

R

H

A

L

V

E

E

T

S

A

L

C

T

V

L

E

D

T

R

R

E

A

V

I

L

V

H

V

Q

K

R

Q

D

R

M

L

L

E

S

Q

P

D

K

W

Y

V

A

Q

E

E

L

A

V

V

Y

S

Y

G

G

R

F

W

W

G

-

S

-

T

-

L

-

H

Y

A

A

M

P

C

E

G

R

E

E

A

A

I

L

R

Q

Q

A

A

Y

L

F

A

D

C

H

V

V

S

A

G

R

T

S

V

V

T

T

active site: D12 (= D40), R92 (= R119), D121 (≠ S148), S168 (= S197)
binding phosphoaminophosphonic acid-adenylate ester: A6 (≠ M34), T13 (≠ S41), T32 (≠ A60), A33 (≠ V61), H113 (= H140), G114 (≠ T141), F125 (≠ L152), S168 (= S197), M169 (≠ G198)
binding arginine: Y84 (= Y111), T88 (≠ S115), R124 (= R151), S168 (= S197), M169 (≠ G198), D170 (= D199), S177 (≠ E206), E179 (= E208), E253 (= E294), Y265 (≠ R306)
binding aspartic acid: A115 (= A142), T116 (≠ N143), G119 (≠ Q146), N120 (= N147), D121 (≠ S148)

1j20A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with product (see paper)
29% identity, 82% coverage: 31:374/417 of query aligns to 3:329/386 of 1j20A

query
sites
1j20A

V

I

V

V

T

L

M
x
A

F

Y

S

S

G

G

L

L

D
|
D

S
x
T

S

S

Y

I

L

I

L

L

H

K

R

W

L

L

R

K

G

E

L

T

G

Y

F

R

A

A

H

E

V

V

H

I

A

A

V

F

A

T

V
x
A

D

D

V

I

G

G

A

Q

P

G

L

E

D

E

-

V

-

E

-

A

-

R

E

E

P

K

A

A

L

L

R

R

R

T

A

G

A

A

S

S

L

-

F

-

G

-

A

-

E

K

F

A

V

I

R

A

L

L

D

D

G

L

R

K

G

E

H

E

F

F

V

V

E

R

G

D

H

F

V

V

R

F

P

P

A

M

I

M

R

R

A

A

H

G

A

A

K

V

Y

Y

L

E

G

G

I

Y

Y
|
Y

P

L

L

L

S

G

S
x
T

S

S

L

I

S

A

R
|
R

P

P

A

L

I

I

A

A

E

K

L

H

V

L

A

V

R

R

Y

I

A

A

R

E

V

E

G

G

A

A

D

E

L

A

I

I

L

A

H
|
H

T
x
G

A
|
A

N
x
T

L

G

S

K

Q
x
G

N
|
N

S
x
D

L

Q

P

V

R
|
R

L
x
F

N

E

N

L

S

T

L

A

A

Y

R

A

L

L

G

K

F

P

P

D

G

I

Q

K

Y

V

G

I

S

A

P

P

Y

W

E

R

Q

E

S

W

A

S

I

F

S

Q

R

G

Q

R

Q

K

K

E

A

M

A

I

E

A

L

Y

A

A

E

E

A

A

G

-

L

-

G

H

A

G

M

I

A

P

E

V

R

P

A

P

L

Y

S
|
S

G

M

D

D

E

A

N

N

L

L

W

L

C

H

R

I

E
x
S

F

Y

E
|
E

S

G

G

G

P

V

L

L

D

E

D

D

P

P

E

W

D

A

F

-

R

E

I

P

P

P

E

K

E

G

A

M

F

F

H

R

W

M

T

T

R

Q

G

D

R

-

P

-

A

-

P

P

G

E

E

E

G

A

A

P

A

D

S

-

G

-

A

-

G

-

P

-

V

-

A

-

L

-

A

A

P

P

E

E

E

Y

I

V

A

E

L

V

T

E

F

F

E

F

R

E

G

G

D

D

L

P

V

V

A

A

L

V

D

N

G

G

R

E

P

R

I

L

A

S

L

P

I

A

D

A

A

L

I

L

A

Q

E

R

L

L

N

N

Q

E

R

I

V

G

G

G

R

R

F

H

G

G

H

V

G

G

R

R

Y

V

V

D

G

I

L

V

E
|
E

H

N

L

R

S

F

G

V

G

G

E

M

K

K

V

S

L

R

E

G

V

V

R
x
Y

E

E

A

T

P

P

A

G

A

T

I

I

L

L

M

Y

D

H

A

A

L

R

R

R

H

A

L

V

E

E

T

S

A

L

C

T

V

L

E

D

T

R

R

E

A

V

I

L

V

H

V

Q

K

R

Q

D

R

M

L

L

E

S

Q

P

D

K

W

Y

V

A

Q

E

E

L

A

V

V

Y

S

Y

G

G

R

F

W

W

G

-

S

-

T

-

L

-

H

Y

A

A

M

P

C

E

G

R

E

E

A

A

I

L

R

Q

Q

A

A

Y

L

F

A

D

C

H

V

V

S

A

G

R

T

S

V

V

T

T

active site: D12 (= D40), R92 (= R119), D121 (≠ S148), S168 (= S197)
binding adenosine monophosphate: A6 (≠ M34), T13 (≠ S41), A33 (≠ V61), R92 (= R119), H113 (= H140), G114 (≠ T141), F125 (≠ L152)
binding argininosuccinate: Y84 (= Y111), T88 (≠ S115), A115 (= A142), T116 (≠ N143), G119 (≠ Q146), N120 (= N147), D121 (≠ S148), R124 (= R151), S177 (≠ E206), E179 (= E208), E253 (= E294), Y265 (≠ R306)

1j1zA Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with substrate (see paper)
29% identity, 82% coverage: 31:374/417 of query aligns to 3:329/386 of 1j1zA

query
sites
1j1zA

V

I

V

V

T

L

M
x
A

F

Y

S

S

G

G

L

L

D
|
D

S
x
T

S

S

Y

I

L

I

L

L

H

K

R

W

L

L

R

K

G

E

L

T

G

Y

F

R

A

A

H

E

V

V

H

I

A

A

V

F

A

T

V
x
A

D

D

V

I

G

G

A

Q

P

G

L

E

D

E

-

V

-

E

-

A

-

R

E

E

P

K

A

A

L

L

R

R

R

T

A

G

A

A

S

S

L

-

F

-

G

-

A

-

E

K

F

A

V

I

R

A

L

L

D

D

G

L

R

K

G

E

H

E

F

F

V

V

E

R

G

D

H

F

V

V

R

F

P

P

A

M

I

M

R

R

A

A

H

G

A

A

K

V

Y

Y

L

E

G

G

I

Y

Y
|
Y

P

L

L

L

S

G

S
x
T

S

S

L

I

S

A

R
|
R

P

P

A

L

I
|
I

A

A

E

K

L

H

V

L

A

V

R

R

Y

I

A

A

R

E

V

E

G

G

A

A

D

E

L

A

I

I

L

A

H
|
H

T
x
G

A
|
A

N
x
T

L

G

S

K

Q
x
G

N
|
N

S
x
D

L

Q

P

V

R
|
R

L
x
F

N

E

N

L

S

T

L

A

A

Y

R

A

L

L

G

K

F

P

P

D

G

I

Q

K

Y

V

G

I

S

A

P

P

Y

W

E

R

Q

E

S

W

A

S

I

F

S

Q

R

G

Q

R

Q

K

K

E

A

M

A

I

E

A

L

Y

A

A

E

E

A

A

G

-

L

-

G

H

A

G

M

I

A

P

E

V

R

P

A

P

L

Y

S
|
S

G
x
M

D

D

E

A

N

N

L

L

W

L

C

H

R

I

E
x
S

F

Y

E
|
E

S

G

G

G

P

V

L

L

D

E

D

D

P

P

E

W

D

A

F

-

R

E

I

P

P

P

E

K

E

G

A

M

F

F

H

R

W

M

T

T

R

Q

G

D

R

-

P

-

A

-

P

P

G

E

E

E

G

A

A

P

A

D

S

-

G

-

A

-

G

-

P

-

V

-

A

-

L

-

A

A

P

P

E

E

E

Y

I

V

A

E

L

V

T

E

F

F

E

F

R

E

G

G

D

D

L

P

V

V

A

A

L

V

D

N

G

G

R

E

P

R

I

L

A

S

L

P

I

A

D

A

A

L

I

L

A

Q

E

R

L

L

N

N

Q

E

R

I

V

G

G

G

R

R

F

H

G

G

H

V

G

G

R

R

Y

V

V

D

G

I

L

V

E
|
E

H

N

L

R

S

F

G

V

G

G

E

M

K

K

V

S

L

R

E

G

V

V

R
x
Y

E

E

A

T

P

P

A

G

A

T

I

I

L

L

M

Y

D

H

A

A

L

R

R

R

H

A

L

V

E

E

T

S

A

L

C

T

V

L

E

D

T

R

R

E

A

V

I

L

V

H

V

Q

K

R

Q

D

R

M

L

L

E

S

Q

P

D

K

W

Y

V

A

Q

E

E

L

A

V

V

Y

S

Y

G

G

R

F

W

W

G

-

S

-

T

-

L

-

H

Y

A

A

M

P

C

E

G

R

E

E

A

A

I

L

R

Q

Q

A

A

Y

L

F

A

D

C

H

V

V

S

A

G

R

T

S

V

V

T

T

active site: D12 (= D40), R92 (= R119), D121 (≠ S148), S168 (= S197)
binding aspartic acid: A115 (= A142), T116 (≠ N143), G119 (≠ Q146), N120 (= N147), D121 (≠ S148)
binding adenosine-5'-triphosphate: A6 (≠ M34), T13 (≠ S41), A33 (≠ V61), R92 (= R119), I95 (= I122), H113 (= H140), G114 (≠ T141), F125 (≠ L152)
binding citrulline: Y84 (= Y111), T88 (≠ S115), R124 (= R151), S168 (= S197), M169 (≠ G198), S177 (≠ E206), E179 (= E208), E253 (= E294), Y265 (≠ R306)

2nz2A Crystal structure of human argininosuccinate synthase in complex with aspartate and citrulline (see paper)
27% identity, 83% coverage: 31:377/417 of query aligns to 4:349/402 of 2nz2A

query
sites
2nz2A

V

V

T

L

M

A

F

Y

S

S

G

G

L

L

D
|
D

S

T

S

S

Y

C

L

I

L

L

H

V

R

W

L

L

R

K

G

E

L

Q

G

G

F

Y

A

-

H

D

V

V

H

I

A

A

V

Y

A

L

V

A

D

N

V

I

G

G

A

Q

P

K

L

E

D

D

E

F

P

E

A

E

L

A

R

R

R

K

A

K

A

A

S

L

L

K

F

L

G

G

A

A

E

K

F

K

V

V

R

F

L

I

-

E

D

D

G

V

R

S

G

R

H

E

F

F

V

V

E

E

G

E

H

F

V

I

R

W

P

P

A

A

I

I

R

Q

A

S

H

S

A

A

K

L

Y

Y

L

E

G

D

I

R

Y
|
Y

P

L

L

L

S

G

S
x
T

S

S

L

L

S

A

R
|
R

P

P

A

C

I

I

A

A

E

R

L

K

V

Q

A

V

R

E

Y

I

A

A

R

Q

R

R

V

E

G

G

A

A

D

K

L

Y

I

V

L

S

H

H

T

G

A
|
A

N
x
T

L

G

S

K

Q
x
G

N
|
N

S
x
D

L

Q

P

V

R
|
R

L

F

N

E

N

L

S

S

L

C

A

Y

R

S

L

L

G

A

F

P

P

Q

G

I

Q

K

Y

V

G

I

S

A

P

P

Y

W

E

R

Q

M

S

P

A

E

I

F

S

Y

R

N

Q

R

Q

F

K

K

A

R

A

N

E

D

L

L

A

M

E

E

A

Y

G

A

-

K

-

Q

-

H

-

G

-

I

-

P

L

I

G

P

A

V

M

T

A

P

E

K

R

N

A

P

L

W

S
|
S

G

M

D
|
D

E

E

N

N

L

L

W

M

C

H

R

I

E
x
S

F

Y

E
|
E

S

A

G

G

P

I

L

L

D

E

D

N

P

P

E

K

D

N

F

Q

R

A

I

P

P

P

E

-

A

G

F

L

H

Y

W

T

T

K

R

T

G

Q

R

D

P

P

A

A

P

K

G

A

E

P

G

N

A

-

S

-

G

-

A

-

G

-

P

-

V

-

A

-

L

-

A

T

P

P

E

D

E

I

I

L

A

E

L

I

T

E

F

F

E

K

R

K

G

G

D

V

L

P

V

V

A

K

L

V

-

T

-

N

-

V

-

K

D

D

G

G

R

T

P

T

I

H

A

Q

L

T

-

S

I

L

D

E

A

L

I

F

A

M

E

Y

L

L

N

N

Q

E

R

V

V

A

G

G

R

K

F

H

G

G

H

V

G

G

R

R

Y

I

V

D

G

I

L

V

E
|
E

H

N

L

R

S

F

G

I

G

G

E

M

K

K

V

S

L

R

E

G

V

I

R
x
Y

E

E

A

T

P

P

A

A

A

G

A

T

I

I

L

L

M

Y

D

H

A

A

L

H

R

L

H

D

L

I

E

E

T

A

A

F

C

T

V

M

E

D

T

R

R

E

A

V

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active site: D13 (= D40), R92 (= R119), D121 (≠ S148), S176 (= S197)
binding aspartic acid: A115 (= A142), T116 (≠ N143), G119 (≠ Q146), N120 (= N147), D121 (≠ S148)
binding citrulline: Y84 (= Y111), T88 (≠ S115), N120 (= N147), R124 (= R151), D178 (= D199), S185 (≠ E206), E187 (= E208), E266 (= E294), Y278 (≠ R306)

P00966 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Homo sapiens (Human) (see 16 papers)
27% identity, 83% coverage: 31:377/417 of query aligns to 7:353/412 of P00966

query
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P00966

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V64 (≠ G88) to I: in CTLN1; uncertain significance; dbSNP:rs556297791
Y87 (= Y111) binding L-citrulline
T91 (≠ S115) to P: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs769018733
S92 (= S116) binding L-citrulline
R95 (= R119) to S: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity
P96 (= P120) to H: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; to L: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; loss of argininosuccinate synthase activity; to S: in CTLN1; no effect on thermal stability; decreased argininosuccinate synthase activity
G117 (≠ T141) to S: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770944877
A118 (= A142) to T: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs775305020
T119 (≠ N143) binding L-aspartate; to I: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity
N123 (= N147) binding L-aspartate; binding L-citrulline
D124 (≠ S148) binding L-aspartate; to N: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs936192871
R127 (= R151) binding L-citrulline; to L: increased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs201623252; to Q: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs201623252; to W: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs771794639
R157 (vs. gap) to C: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770585183; to H: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908637
K165 (vs. gap) modified: N6-acetyllysine; by CLOCK; mutation K->Q,R: Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-176 or R-176.
K176 (≠ E193) modified: N6-acetyllysine; by CLOCK; mutation K->Q,R: Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-165 or R-165.
W179 (≠ L196) to R: in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908646
S180 (= S197) binding L-citrulline; to I: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs121908638; to N: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908638
S189 (≠ E206) binding L-citrulline
E191 (= E208) to Q: in CTLN1; loss of argininosuccinate synthase activity
A192 (≠ S209) to V: in CTLN1; decreased protein abundance
V263 (≠ H287) to M: in CTLN1; mild clinical course; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs192838388
R265 (= R289) to C: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs148918985
E270 (= E294) binding L-citrulline; to Q: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs775163147
R272 (≠ L296) to C: in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs762387914; to H: in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs768215008; to L: in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs768215008
G280 (≠ E304) to R: in CTLN1; loss of argininosuccinate synthase activity
Y282 (≠ R306) binding L-citrulline
T284 (≠ A308) to I: in CTLN1; mild clinical course; dbSNP:rs886039853
M302 (≠ V326) to V: in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity
R304 (≠ T328) to W: in CTLN1; decreased protein abundance; dbSNP:rs121908642
G324 (= G348) to S: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908639
G347 (= G371) to R: in CTLN1; severe clinical course

Sites not aligning to the query:

359 Y → D: in CTLN1; mild clinical course
362 G → V: in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908647
390 G → R: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908641

5us8A 2.15 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis
26% identity, 82% coverage: 35:374/417 of query aligns to 21:364/445 of 5us8A

query
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active site: D26 (= D40), R110 (= R119), D139 (≠ S148), S195 (= S197)
binding adenosine: E321 (≠ V332), R324 (≠ Q335), E325 (≠ R336), R328 (≠ Q339), K329 (≠ D340)

6e5yA 1.50 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis in complex with amp.
26% identity, 82% coverage: 35:374/417 of query aligns to 17:360/438 of 6e5yA

query
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I

V

D

E

A

L

I

L

A

L

E

E

L

A

N

N

Q

R

R

I

V

G

G

G

R

R

F

H

G

G

H

L

G

G

R

M

Y

S

V

D

G

Q

L

I

E

E

H

N

L

R

S

I

G

I

G

E

E

A

K

K

V

S

L

R

E

G

V

I

R

Y

E

E

A

A

P

P

A

G

A

L

A

A

I

L

L

L

M

F

D

I

A

A

L

Y

R

E

H

R

L

L

E

V

T

T

A

G

C

I

V

H

E

N

T

E

R

D

A

T

I

I

V

E

V

Q

K

Y

Q

R

R

E

L

N

E

G

Q

R

D

K

W

L

V

G

Q

R

E

L

A

L

V

Y

S

Q

G

G

R

R

W

W

G

F

S

D

T

P

L

Q

H

A

A

I

M

M

C

L

G

R

E

E

A

T

I

A

R

Q

Q

R

A

W

L

V

A

A

-

R

C

A

V

I

S

T

G

G

T

E

V

V

T

T

active site: D22 (= D40), R106 (= R119), D135 (≠ S148), S191 (= S197)
binding adenosine monophosphate: T41 (≠ A60), A42 (≠ V61), D193 (= D199)

Sites not aligning to the query:

binding adenosine monophosphate: 16

Query Sequence

>WP_012335778.1 NCBI__GCF_000019365.1:WP_012335778.1
MNFISPLARSSVRVIRSFDHLTGGPTRTAPVVTMFSGGLDSSYLLHRLRGLGFAHVHAVA
VDVGAPLDEPALRRAASLFGAEFVRLDGRGHFVEGHVRPAIRAHAKYLGIYPLSSSLSRP
AIAELVARYARRVGADLILHTANLSQNSLPRLNNSLARLGFPGQYGSPYEQSAISRQQKA
AELAEAGLGAMAERALSGDENLWCREFESGPLDDPEDFRIPEEAFHWTRGRPAPGEGAAS
GAGPVALAPEEIALTFERGDLVALDGRPIALIDAIAELNQRVGRFGHGRYVGLEHLSGGE
KVLEVREAPAAAILMDALRHLETACVETRAIVVKQRLEQDWVQEAVSGRWGSTLHAMCGE
AIRQALACVSGTVTYRVDAERFLPRAIVADAPLYIRDRDLWESREAGRACLGIPRAA

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