SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_019557133.1 NCBI__GCF_000381085.1:WP_019557133.1 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)

P00903 Aminodeoxychorismate synthase component 2; ADC synthase; ADCS; 4-amino-4-deoxychorismate synthase component 2; Aminodeoxychorismate synthase, glutamine amidotransferase component; EC 2.6.1.85 from Escherichia coli (strain K12) (see paper)
60% identity, 99% coverage: 1:192/194 of query aligns to 1:187/187 of P00903

query
sites
P00903

M

M

L

I

L

L

M

L

I

I

D

D

N

N

Y

Y

D

D

S

S

F

F

T

T

Y

W

N

N

I

L

V

Y

Q

Q

Y

Y

F

F

G

C

E

E

L

L

G

G

Q

A

H

D

V

V

E

L

V

V

F

K

R

R

N

N

D

D

Q

A

I

L

T

T

I

L

E

A

G

D

I

I

E

D

A

A

L

L

N

K

P

P

K

Q

Y

K

L

I

V

V

I

I

S

S

P

P

G

G

P

P

C

C

T

T

P

P

A

D

E

E

A

A

G

G

I

I

S

S

V

L

A

D

A

V

I

I

Q

R

Y

H

F

Y

A

A

G

G

K

R

I

L

P

P

I

I

M

L

G

G

V

V

C
|
C

L

L

G

G

H

H

Q

Q

S

A

I

M

G

A

Q

Q

A

A

F

F

G

G

H

K

V

V

I

V

R

R

A

A

K

A

E

K

V

V

M

M

H

H

G

G

K

K

T

T

S

S

P

P

V

I

Y

T

H

H

Q

N

D

G

T

E

G

G

M

V

F

F

A

R

N

G

L

L

P

A

N

N

P

P

V

L

T

T

T

V

T

T

R

R

Y

Y

H

H

S

S

L

L

V

V

I

V

E

E

Q

P

S

D

T

S

L

L

P

P

E

A

C

C

L

F

E

D

I

V

T

T

A

A

W

W

T

S

Q

-

D

-

A

-

N

-

G

-

E

E

L

T

D

R

E

E

I

I

M

M

G

G

V

I

R

R

H

H

K

R

T

Q

L

W

P

D

I

L

E

E

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

S

I

I

L

L

T

S

D

E

Q

Q

G

G

H

H

Q

Q

M

L

L

L

R

A

N

N

F

F

L

L

E

H

Q

R

C79 (= C79) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H173) mutation to Q: Loss of activity.
E170 (= E175) mutation to A: 150-fold decrease in catalytic efficiency.; mutation to D: 4-fold decrease in catalytic efficiency.; mutation E->K,Q: Loss of activity.

Q42565 Anthranilate synthase beta subunit 1, chloroplastic; Anthranilate synthase component 2-1; Anthranilate synthase, glutamine amidotransferase component 2-1; Protein TRYPTOPHAN BIOSYNTHESIS 4; Protein WEAK ETHYLENE INSENSITIVE 7; EC 4.1.3.27 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
49% identity, 98% coverage: 2:191/194 of query aligns to 75:265/276 of Q42565

query
sites
Q42565

L

I

M

V

I

I

D

D

N

N

Y

Y

D

D

S

S

F

F

T

T

Y

Y

N

N

I

L

V

C

Q

Q

Y

Y

F

M

G

G

E

E

L

L

G

G

Q

C

H

H

V

F

E

E

V

V

F

Y

R

R

N

N

D

D

Q

E

I

L

T

T

I

V

E

E

G

E

I

L

E

K

A

K

L

K

N

N

P

P

K

R

Y

G

L

V

V

L

I

I

S

S

P

P

G

G

P

P

C

G

T

T

P

P

A

Q

E

D

A

S

G

G

I

I

S

S

V

L

A

Q

A

T

I

V

Q

L

Y

E

F

L

A

G

G

P

K

L

I

V

P

P

I

L

M

F

G
|
G

V

V

C

C

L

M

G

G

H

L

Q

Q

S

C

I

I

G

G

Q

E

A

A

F

F

G

G

H

K

V

I

I

V

R

R

A

S

K

P

-

F

E

G

V

V

M

M

H

H

G
|
G

K

K

T

S

S

S

P

M

V

V

Y

H

H

Y

Q

D

D

E

T

K

-

G

-

E

G

G

M

L

F

F

A

S

N

G

L

L

P

S

N

N

P

P

V

F

T

I

T

V

T

G

R

R

Y

Y

H

H

S

S

L

L

V

V

I

I

E

E

Q

K

S

D

T

T

L

F

P

P

-

S

E

D

C

E

L

L

E

E

I

V

T

T

A

A

W

W

T

T

Q

E

D

D

A

G

N

-

G

-

E

-

L

-

D

-

E

L

I

V

M

M

G

A

V

A

R

R

H

H

K

R

T

K

L

Y

P

K

-

H

I

I

E

Q

G

G

V

V

Q

Q

F

F

H

H

P

P

E

E

S

S

I

I

L

I

T

T

D

T

Q

E

G

G

H

K

Q

T

M

I

L

V

R

R

N

N

F

F

L

I

E

K

G150 (= G77) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (= G102) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.

P00900 Anthranilate synthase component 2; AS; ASII; Anthranilate synthase, GATase component; Anthranilate synthase, glutamine amidotransferase component; EC 4.1.3.27 from Serratia marcescens (see 3 papers)
43% identity, 97% coverage: 2:190/194 of query aligns to 4:187/193 of P00900

query
sites
P00900

L

I

L

L

M

L

I

L

D

D

N

N

Y

V

D

D

S

S

F

F

T

T

Y

Y

N

N

I

L

V

V

Q

D

Y

Q

F

L

G

R

E

A

L

S

G

G

Q

H

H

Q

V

V

E

V

V

I

F

Y

R

R

N

N

D

Q

-

I

-

G

-

A

Q

E

I

V

T

I

I

I

E

E

G

R

I

L

E

Q

A

H

L

M

N

E

P

Q

K

P

Y

V

L

L

V

M

I

L

S

S

P

P

G

G

P

P

C

G

T

T

P

P

A

S

E

E

A

A

G

G

I

C

S

M

V

P

A

E

A

L

I

L

Q

Q

Y

R

F

L

A

R

G

G

K

Q

I

L

P

P

I

I

M

I

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

S

A

I

I

G

V

Q

E

A

A

F

Y

G

G

H

Q

V

V

I

G

R

Q

A

A

K

G

E

E

V

I

M

L

H

H

G

G

K

K

T

A

S

S

P

A

V

I

Y

A

H

H

Q

D

D

G

T

E

G

G

M

M

F

F

A

A

N

G

L

M

P

A

N

N

P

P

V

L

T

P

T

V

T

A

R

R

Y

Y

H

H

S

S

L

L

V

V

I

-

E

-

Q

G

S

S

T

N

L

I

P

P

E

A

C

D

L

L

E

T

I

V

T

N

A

A

W

R

T

S

Q

-

D

-

A

-

N

-

G

G

E

E

L

M

D

-

E

-

I

V

M

M

G

A

V

V

R

R

H

D

K

D

T

R

L

R

P

R

I

V

E

C

G

G

V

F

Q

Q

F

F

H

H

P

P

E

E

S

S

I

I

L

L

T

T

D

T

Q

H

G

G

H

A

Q

R

M

L

L

L

R

E

N

Q

F

T

L

L

C84 (= C79) active site, Nucleophile; for GATase activity

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
46% identity, 96% coverage: 3:189/194 of query aligns to 7:187/673 of 8hx8A

query
sites
8hx8A

L

L

M

L

I

I

D

D

N

N

Y

Y

D

D

S

S

F

F

T

T

Y

H

N

N

I

L

V

F

Q

Q

Y

Y

F

I

G

G

E

E

-

A

L

T

G

G

Q

Q

H

P

V

P

E

V

V

V

F

V

R

P

N

N

D

D

-

A

-

D

-

W

-

S

Q

R

I

L

T

P

I

V

E

E

G

D

I

F

E

D

A

A

L

I

N

-

P

-

K

-

Y

-

L

-

V

V

I

V

S

S

P

P

G

G

P

P

C

G

T

S

P

P

-

D

-

R

-

E

A

R

E

D

A

F

G

G

I

I

S

S

V

R

A

R

A

A

I

I

Q

T

Y

-

F

-

A

D

G

S

K

G

I

L

P

P

I

V

M

L

G

G

V

V

C

C

L

L

G

G

H

H

Q

Q

S

G

I

I

G

A

Q

Q

A

L

F

F

G

G

H

T

V

V

I

G

R

L

A

A

K

P

E

E

V

P

M

M

H

H

G

G

K

R

T

V

S

S

P

E

V

V

Y

R

H

H

Q

T

D

G

T

E

G

D

M

V

F

F

A

R

N

G

L

L

P

P

N

S

P

P

V

F

T

T

T

A

T

V

R

R

Y

Y

H

H

S

S

L

L

V

A

I

-

E

-

Q

A

S

T

T

D

L

L

P

P

E

D

C

E

L

L

E

E

I

P

T

L

A

A

W

W

T

S

Q

D

D

D

A

G

N

-

G

-

E

-

L

-

D

-

E

V

I

V

M

M

G

G

V

L

R

R

H

H

K

R

T

E

L

K

P

P

I

L

E

W

G

G

V

V

Q

Q

F

F

H

H

P

P

E

E

S

S

I
|
I

L

G

T
x
S

D

D

Q

F

G

G

H

R

Q

E

M

I

L

M

R

A

N

N

F

F

binding magnesium ion: I175 (= I177), S177 (≠ T179)

Sites not aligning to the query:

binding magnesium ion: 521, 655, 658
binding tryptophan: 231, 232, 233, 241, 243, 458, 459, 460, 614

1i7qB Anthranilate synthase from s. Marcescens (see paper)
43% identity, 97% coverage: 2:190/194 of query aligns to 3:186/192 of 1i7qB

query
sites
1i7qB

L

I

L

L

M

L

I

L

D

D

N

N

Y

V

D

D

S

S

F

F

T

T

Y

Y

N

N

I

L

V

V

Q

D

Y

Q

F

L

G

R

E

A

L

S

G

G

Q

H

H

Q

V

V

E

V

V

I

F

Y

R

R

N

N

D

Q

-

I

-

G

-

A

Q

E

I

V

T

I

I

I

E

E

G

R

I

L

E

Q

A

H

L

M

N

E

P

Q

K

P

Y

V

L

L

V

M

I

L

S

S

P
|
P

G
|
G

P

P

C
x
G

T

T

P

P

A

S

E

E

A

A

G

G

I

C

S

M

V

P

A

E

A

L

I

L

Q

Q

Y

R

F

L

A

R

G

G

K

Q

I

L

P

P

I

I

M

I

G

G

V

I

C
|
C

L
|
L

G

G

H

H

Q
|
Q

S

A

I

I

G

V

Q

E

A

A

F

Y

G

G

H

Q

V

V

I

G

R

Q

A

A

K

G

E

E

V

I

M

L

H

H

G

G

K

K

T

A

S

S

P

A

V

I

Y

A

H

H

Q

D

D

G

T

E

G

G

M

M

F

F

A

A

N

G

L

M

P

A

N

N

P

P

V

L

T

P

T

V

T

A

R

R

Y

Y

H
|
H

S
|
S

L
|
L

V

V

I

-

E

-

Q

G

S

S

T

N

L

I

P

P

E

A

C

D

L

L

E

T

I

V

T

N

A

A

W

R

T

F

Q

-

D

-

A

-

N

-

G

G

E

E

L

M

D

-

E

-

I

V

M

M

G

A

V

V

R

R

H

D

K

D

T

R

L

R

P

R

I

V

E

C

G

G

V

F

Q

Q

F

F

H
|
H

P

P

E
|
E

S

S

I

I

L

L

T

T

D

T

Q

H

G

G

H

A

Q

R

M

L

L

L

R

E

N

Q

F

T

L

L

active site: G58 (≠ C54), C83 (= C79), L84 (= L80), H169 (= H173), E171 (= E175)
binding glutamic acid: P55 (= P51), G56 (= G52), G58 (≠ C54), C83 (= C79), L84 (= L80), Q87 (= Q83), H132 (= H128), S133 (= S129), L134 (= L130)

8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
35% identity, 96% coverage: 3:189/194 of query aligns to 6:144/632 of 8hx9A

query
sites
8hx9A

L

L

M

L

I

I

D

D

N

N

Y

Y

D

D

S

S

F

F

T

T

Y

H

N

N

I

L

V

F

Q

Q

Y

Y

F

I

G

G

E

E

-

A

L

T

G

G

Q

Q

H

P

V

P

E

V

V

V

F

V

R

P

N

N

D

D

-

A

-

D

-

W

-

S

Q

R

I

L

T

P

I

V

E

E

G

D

I

F

E

D

A

A

L

I

N

-

P

-

K

-

Y

-

L

-

V

V

I

V

S

S

P

P

G

R

P

A

C

I

T

T

P

D

A

S

E

-

A

-

G

-

I

-

S

-

V

-

A

-

I

-

Q

-

Y

-

F

-

A

-

G

-

K

G

I

L

P

P

I

V

M

L

G

G

V

V

C

C

L

L

G

-

H

-

Q

-

S

-

I

-

G

-

Q

-

A

-

F

-

G

-

H

-

V

-

I

-

R

-

A

-

K

-

E

-

V

-

M

M

H

H

G

G

K

R

T

V

S

S

P

E

V

V

Y

R

H

H

Q

T

D

G

T

E

G

D

M

V

F

F

A

R

N

G

L

L

P

P

N

S

P

P

V

F

T

T

T

A

T

V

R

R

Y

Y

H

H

S

-

L

-

V

-

I

-

E

-

Q

-

S

-

T

-

L

-

P

-

E

D

C

E

L

L

E

E

I

P

T

L

A

A

W

W

T

S

Q

D

D

D

A

G

N

-

G

-

E

-

L

-

D

-

E

V

I

V

M

M

G

G

V

L

R

R

H

H

K

R

T

E

L

K

P

P

I

L

E

W

G

G

V

V

Q

Q

F

F

H

H

P

P

E

E

S

S

I

I

L

G

T
x
S

D
|
D

Q

F

G

G

H

R

Q

E

M

I

L

M

R

A

N

N

F

F

binding magnesium ion: S134 (≠ T179), D135 (= D180)

Sites not aligning to the query:

binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: 453, 454, 455, 456, 547, 570, 590, 603, 604, 605, 606, 619, 623
binding tryptophan: 189, 190, 191, 199, 201, 419, 420, 421, 574, 575

7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
31% identity, 98% coverage: 1:191/194 of query aligns to 1:176/183 of 7yc6A

query
sites
7yc6A

M

M

L

I

L

V

M

I

I

L

D

D

N

N

Y

G

D

G

S

Q

F

Y

T

V

Y

H

N

R

I

I

V

H

Q

R

Y

S

F

L

G

K

E

Y

L

I

G

G

Q

V

H

S

V

S

E

K

V

I

F

V

R

P

N

N

D

T

Q

T

I

-

T

P

I

L

E

E

G

E

I

I

E

E

A

S

L

N

N

K

P

E

-

V

K

K

Y

G

L

I

V

I

I

L

S

S

P

G

G

G

P

P

-

D

C

I

T

E

P

K

A

A

E

K

A

N

G

C

I

I

S

D

V

I

A

A

A

-

I

-

Q

-

Y

-

F

L

A

N

G

A

K

K

I

L

P

P

I

I

M

L

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

S

L

I

I

G

A

Q

L

A

A

F

Y

G

G

H

E

V

V

I

G

R

R

A

A

K

-

E

-

V

-

M

-

H

-

G

A

K

L

T

T

S

K

P

V

V

Y

Y

V

H
x
D

Q

K

D

E

T

N

G

P

M

L

F

F

A

K

N

N

L

V

P

P

N

R

P

E

V

F

T

N

T

A

T

W

R

A

Y

S

H

H

S

K

L

-

V

-

I

D

E
|
E

Q

V

S

K

T

K

L

V

P

P

E

E

C

G

L

F

E

E

I

I

T

L

A

A

W

-

T

-

Q

-

D

-

A

-

N
x
H

G

S

E

D

L

I

D
x
C

E

Q

I

V

M

E

G

A

V

M

R

K

H

H

K

K

T

T

L

K

P

P

I

I

E

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E

E

S

V

I

A

L

H

T

T

D

E

Q

Y

G

G

H

N

Q

E

M

I

L

L

R

K

N

N

F

F

L

C

E

K

binding zinc ion: C76 (= C79), D101 (≠ H109), E123 (= E133), E123 (= E133), H136 (≠ N151), C140 (≠ D155), C140 (≠ D155), H158 (= H173)

Q9LVW7 Carbamoyl phosphate synthase small chain, chloroplastic; Carbamoyl phosphate synthetase glutamine chain; Protein VENOSA 6; EC 6.3.5.5 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
26% identity, 84% coverage: 14:176/194 of query aligns to 254:405/430 of Q9LVW7

query
sites
Q9LVW7

N

N

I

I

V

L

Q

R

Y

R

F

L

G

S

E

S

L

Y

G

G

Q

C

H

Q

V

I

E

T

V

V

F

V

R

P

N

S

D

T

Q

F

I

P

T

A

I

A

E

E

G

A

I

L

E

K

A

-

L

M

N

N

P

P

K

D

Y

G

L

I

V

L

I

F

S

S

P

N

G

G

P

P

C

G

T

D

P

P

A

S

E

A

A

V

G

P

I

Y

S

A

V

V

A

E

A

T

I

V

Q

K

Y

E

F

L

A

L

G

G

K

K

I

V

P

P

I

V

M

Y

G

G

V

I

C

C

L

M

G

G

H

H

Q

Q

S

L

I

L

G

G

Q

Q

A

A

F

L

G

G

H

K

V

T

I

F

R

K

A

M

K

K

E

F

V

G

M

H

H

H

G

G

K

G

T

N

S

H

P

P

V

V

Y

R

H

N

Q

N

D

R

T

T

G

G

M

Q

F

V

A

E

N

-

L

-

P

-

N

-

P

-

V

-

T

I

T

S

T

A

R

Q

Y

N

H

H

S

N

L

Y

V

A

I

V

E

D

Q

P

S

A

T

S

L

L

P

P

E

G

C

G

L

V

E

E

I

V

T

T

A

-

W

-

T

-

Q

-

D

H

A

V

N

N

G

L

E

N

L

D

D

G

E

S

I

C

M

A

G

G

V

L

R

S

H

F

K

P

T

E

L

M

P

N

I

V

E

M

G

S

V

L

Q

Q

F

Y

H

H

P

P

E

E

S

A

Sites not aligning to the query:

410 H→Y: In ven6-1; reticulate leaf phenotype.

2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
28% identity, 98% coverage: 1:191/194 of query aligns to 1:182/475 of 2ywcA

query
sites
2ywcA

M

M

L

V

L

L

M

V

I

L

D

D

N

F

Y

G

D

S

S

Q

F

Y

T

T

Y

R

N

L

I

I

V

A

Q

R

Y

R

F

L

G

R

E

E

L

L

G

R

Q

A

H

F

V

S

E

L

V

I

F

L

R

P

N

G

D

D

Q

A

I

-

T

P

I

L

E

E

G

E

I

V

E

L

A

K

L

H

N

R

P

P

K

Q

Y

A

L

L

V

I

I

L

S

S

P

G

G
|
G

P

P

C
x
R

T

S

P

V

A

F

E

D

A

P

G

D

I

A

S

P

V

R

A

P

A

D

I

P

Q

R

Y

L

F

F

A

S

G

S

K

G

I

L

P

P

I

L

M

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

L

I

L

G

A

Q

Q

A

E

F

L

G

G

H

R

V

V

I

E

R

R

A

A

K

G

E

R

V

A

M

E

H

Y

G

G

K

K

T

A

S

L

P

L

V

T

Y

R

H

H

Q

E

D

G

T

P

G

-

M

L

F

F

A

R

N

G

L

L

P

E

N

G

P

E

V

V

T

Q

T

V

T

W

R

M

Y

S

H

H

S

Q

L

-

V

-

I

-

E

D

Q

A

S

V

T

T

L

A

P

P

E

P

C

-

L

-

E

-

I

-

T

P

A

G

W

W

T

R

Q

V

D

V

A

A

N

E

G

T

E

E

L

E

D

N

E

P

I

V

M

A

G

A

V

I

R

A

H

S

K

P

T

D

L

G

P

R

I

A

E

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

A

L

H

T

T

D

P

Q

K

G

G

H

M

Q

Q

M

I

L

L

R

E

N

N

F

F

L

L

E

E

active site: G51 (= G52), R53 (≠ C54), C78 (= C79), Y79 (≠ L80), H164 (= H173), E166 (= E175)

Sites not aligning to the query:

active site: 221, 343
binding xanthosine-5'-monophosphate: 288, 366, 367, 368, 408, 467, 471, 472, 473

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
30% identity, 74% coverage: 33:176/194 of query aligns to 221:355/379 of 1ce8B

query
sites
1ce8B

Q

Q

I

T

T

S

I

A

E

E

G

D

I

V

E

L

A

K

L

M

N

N

P

P

K

D

Y

G

L

I

V

F

I

L

S

S

P

N

G

G

P

P

C

G

T

D

P

P

A

A

E

P

A

C

G

D

I

Y

S

A

V

I

A

T

A

A

I

I

Q

Q

Y

K

F

F

-

L

A

E

G

T

K

D

I

I

P

P

I

V

M

F

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

S

L

I

L

G

A

Q

L

A

A

F

S

G

G

G

A

H

K

V

T

I

V

R

K

A

M

K

K

E

F

V

G

M

H

H

H

G

G

K

G

T

N

S

H

P

P

V

V

Y

K

H

D

Q

V

D

E

T

K

G

N

M

V

F

V

A

-

N

-

L

-

P

-

N

-

P

-

V

M

T

I

T

T

T

A

R

Q

Y

N

H

H

S

G

L

F

V

A

I

V

E

D

Q

E

S

A

T

T

L

L

P

P

E

A

C

N

L

L

E

R

I

V

T

T

A

H

W

K

T

S

Q

L

D

-

A

F

N

D

G

G

E

T

L

L

D

-

E

-

I

-

M

Q

G

G

V

I

R

H

H

R

K

T

T

D

L

K

P

P

I

A

E

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

active site: C268 (= C79), H352 (= H173), E354 (= E175)

Sites not aligning to the query:

binding L-ornithine: 119, 122

P0A6F1 Carbamoyl phosphate synthase small chain; Carbamoyl phosphate synthetase glutamine chain; EC 6.3.5.5 from Escherichia coli (strain K12) (see paper)
30% identity, 74% coverage: 33:176/194 of query aligns to 222:356/382 of P0A6F1

query
sites
P0A6F1

Q

Q

I

T

T

S

I

A

E

E

G

D

I

V

E

L

A

K

L

M

N

N

P

P

K

D

Y

G

L

I

V

F

I

L

S

S

P

N

G
|
G

P

P

C
x
G

T

D

P

P

A

A

E

P

A

C

G

D

I

Y

S

A

V

I

A

T

A

A

I

I

Q

Q

Y

K

F

F

-

L

A

E

G

T

K

D

I

I

P

P

I

V

M

F

G

G

V

I

C

C

L
|
L

G

G

H

H

Q
|
Q

S

L

I

L

G

A

Q

L

A

A

F

S

G

G

G

A

H

K

V

T

I

V

R

K

A

M

K

K

E

F

V

G

M

H

H

H

G

G

K

G

T

N

S

H

P

P

V

V

Y

K

H

D

Q

V

D

E

T

K

G

N

M

V

F

V

A

-

N

-

L

-

P

-

N

-

P

-

V

M

T

I

T

T

T

A

R

Q

Y
x
N

H

H

S
x
G

L
x
F

V

A

I

V

E

D

Q

E

S

A

T

T

L

L

P

P

E

A

C

N

L

L

E

R

I

V

T

T

A

H

W

K

T

S

Q

L

D

-

A

F

N

D

G

G

E

T

L

L

D

-

E

-

I

-

M

Q

G

G

V

I

R

H

H

R

K

T

T

D

L

K

P

P

I

A

E

F

G

S

V

F

Q

Q

F

G

H

H

P

P

E

E

S

A

G241 (= G52) binding L-glutamine
G243 (≠ C54) binding L-glutamine
L270 (= L80) binding L-glutamine
Q273 (= Q83) binding L-glutamine
N311 (≠ Y127) binding L-glutamine
G313 (≠ S129) binding L-glutamine
F314 (≠ L130) binding L-glutamine

Sites not aligning to the query:

47 binding L-glutamine

1gpmA Escherichia coli gmp synthetase complexed with amp and pyrophosphate (see paper)
27% identity, 98% coverage: 2:192/194 of query aligns to 8:198/501 of 1gpmA

query
sites
1gpmA

L

I

L

L

M

I

I

L

D

D

N

F

Y

G

D

S

S

Q

F

Y

T

T

Y

Q

N

L

I

V

V

A

Q

R

Y

R

F

V

G

R

E

E

L

L

G

G

Q

V

H

Y

V

C

E

E

V

L

F

W

R

A

N

W

D

D

Q

-

I

V

T

T

I

E

E

A

G

Q

I

I

E

R

A

D

L

F

N

N

P

P

K

S

Y

G

L

I

V

I

I

L

S

S

P

G

G
|
G

P

P

C

E

T

S

P

T

A

T

E

E

A

E

G

N

I

S

S

P

V

R

A

A

A

P

I

Q

Q

Y

Y

V

F

F

A

E

G

A

K

G

I

V

P

P

I

V

M

F

G

G

V

V

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

T

I

M

G

A

Q

M

A

Q

F

L

G

G

H

H

V

V

I

E

R

A

A

S

K

N

E

E

V

R

M

E

H

F

G

G

K

Y

T

A

S

Q

P

V

V

E

Y

V

H

V

Q

N

D

D

T

S

G

A

M

L

F

V

A

R

N

G

L

I

P

E

N

D

P

A

V

L

T

T

T

A

T

D

R

G

Y

K

H

P

S

L

L

L

V

D

I

V

E

W

Q

M

S

S

-

H

-

G

-

D

-

K

-

V

-

T

T

A

L

I

P

P

E

S

C

D

L

F

E

I

I

T

T

V

A

A

W

S

T

T

Q

E

D

S

A

C

N

P

G

F

E

-

L

-

D

-

E

A

I

I

M

M

G

A

V

N

R

E

H

E

K

K

T

R

L

F

P

-

I

-

E

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

T

L

H

T

T

D

R

Q

Q

G

G

H

M

Q

R

M

M

L

L

R

E

N

R

F

F

L

V

E

R

Q

D

active site: G57 (= G52), C84 (= C79), Y85 (≠ L80), H179 (= H173), E181 (= E175)

Sites not aligning to the query:

active site: 237, 357
binding adenosine monophosphate: 231, 232, 233, 258, 313
binding pyrophosphate 2-: 233, 235, 236, 237, 238, 357

1c3oB Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
29% identity, 74% coverage: 33:176/194 of query aligns to 221:355/379 of 1c3oB

query
sites
1c3oB

Q

Q

I

T

T

S

I

A

E

E

G

D

I

V

E

L

A

K

L

M

N

N

P

P

K

D

Y

G

L

I

V

F

I

L

S

S

P
x
N

G
|
G

P

P

C
x
G

T

D

P

P

A

A

E

P

A

C

G

D

I

Y

S

A

V

I

A

T

A

A

I

I

Q

Q

Y

K

F

F

-

L

A

E

G

T

K

D

I

I

P

P

I

V

M

F

G

G

V

I

C
x
S

L
|
L

G

G

H

H

Q

Q

S

L

I

L

G

A

Q

L

A

A

F

S

G

G

G

A

H

K

V

T

I

V

R

K

A

M

K

K

E

F

V

G

M

H

H

H

G

G

K

G

T

N

S

H

P

P

V

V

Y

K

H

D

Q

V

D

E

T

K

G

N

M

V

F

V

A

-

N

-

L

-

P

-

N

-

P

-

V

M

T

I

T

T

T

A

R

Q

Y
x
N

H
|
H

S
x
G

L
x
F

V

A

I

V

E

D

Q

E

S

A

T

T

L

L

P

P

E

A

C

N

L

L

E

R

I

V

T

T

A

H

W

K

T

S

Q

L

D

-

A

F

N

D

G

G

E

T

L

L

D

-

E

-

I

-

M

Q

G

G

V

I

R

H

H

R

K

T

T

D

L

K

P

P

I

A

E

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

active site: S268 (≠ C79), H352 (= H173), E354 (= E175)
binding glutamine: N239 (≠ P51), G240 (= G52), G242 (≠ C54), S268 (≠ C79), L269 (= L80), N310 (≠ Y127), H311 (= H128), G312 (≠ S129), F313 (≠ L130)

Sites not aligning to the query:

active site: 201
binding glutamine: 46

P05990 Multifunctional protein r; Protein rudimentary; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Drosophila melanogaster (Fruit fly) (see 2 papers)
29% identity, 66% coverage: 47:175/194 of query aligns to 235:355/2224 of P05990

query
sites
P05990

L

L

V

F

I

L

S

S

P

N

G

G

P

P

C

G

T

N

P

P

A

E

E

S

A

C

G

D

I

Q

S

I

V

V

A

Q

I

V

Q

R

Y

K

F

V

-

I

-

E

A

E

G

G

K

Q

I

K

P

P

I

V

M

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

L

I

L

G

A

Q

K

A

A

F

I

G

G

G

C

H

S

V

T

I

Y

R

K

A

M

K

K

E

Y

V

G

M

N

H

R

G

G

K

H

T

N

S

L

P

P

V

C

Y

L

H

H

Q

R

D

A

T

T

G

G

M

R

F

C

A

-

N

-

L

-

P

-

N

-

P

-

V

L

T

M

T

T

T

S

R

Q

Y

N

H

H

S

G

L

Y

V

A

I

V

E

D

Q

L

S

E

T

Q

L

L

P

P

E

D

C

-

L

-

E

-

I

-

T

-

A

G

W

W

T

S

Q

E

-

L

-

F

-

V

D

N

A

A

N

N

G

D

E

G

L

T

D

N

E

E

I

-

M

-

G

G

V

I

R

V

H

H

K

A

T

S

L

K

P

P

I

Y

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

Sites not aligning to the query:

1167 E→K: Severely diminishes UTP inhibition of CPSase; in Su(b).
1883 modified: Phosphoserine
1885 modified: Phosphoserine
1892 modified: Phosphoserine
1894 modified: Phosphoserine

3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
25% identity, 80% coverage: 34:189/194 of query aligns to 35:214/517 of 3uowA

query
sites
3uowA

I

V

T

E

I

L

E

K

G

D

I

I

E

K

A

D

L

M

N

N

P

I

K

K

Y

G

L

V

V

I

I

L

S

S

P

G

G
|
G

P

P

C

Y

T

S

P

V

A

T

E

E

A

A

G

G

-

S

-

P

-

H

I

L

S

K

V

K

A

E

A

V

I

F

Q

E

Y

Y

F

F

-

L

A

E

G

K

K

K

I

I

P

P

I

I

M

F

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

E

I

I

G

A

Q

V

A

Q

F

M

G

N

G

G

H

E

V

V

I

K

R

K

A

S

K

K

E

T

V

S

M

E

H

Y

G

G

K

C

T

T

-

D

-

V

-

N

-

I

-

L

-

R

-

N

-

D

-

N

-

I

-

N

-

I

-

T

-

Y

-

C

-

R

-

N

-

F

-

S

-

A

-

M

-

D

-

L

-

Y

S

S

P

N

V

Y

Y

K

H

L

Q

M

D

N

T

C

G

C

M

L

F

F

A

E

N

N

L

I

P

K

N

S

P

D

V

I

T

T

T

V

R

-

Y

W

H

M

S

N

L

H

V

N

I

D

E

E

Q

V

S

T

T

K

L

I

P

P

E

E

C

N

L

F

E

Y

I

L

T

V

A

S

W

S

T

S

Q

E

D

N

A

C

N

-

G

-

E

-

L

-

D

-

E

L

I

I

M

C

G

S

V

I

R

Y

H

N

K

K

T

E

L

Y

P

N

I

I

E

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

S

V

I

Y

L

E

T

S

D

L

Q

D

G

G

H

E

Q

L

M

M

L

F

R

Y

N

N

F

F

active site: G53 (= G52), C84 (= C79), Y85 (≠ L80), H198 (= H173), E200 (= E175)

Sites not aligning to the query:

active site: 255, 381
binding xanthosine-5'-monophosphate: 325, 404, 405, 406, 446, 509, 513, 514, 515

Q8IJR9 GMP synthase [glutamine-hydrolyzing]; PfGMPS; Glutamine amidotransferase; Guanosine monophosphate synthetase; EC 6.3.5.2 from Plasmodium falciparum (isolate 3D7) (see 3 papers)
24% identity, 80% coverage: 34:189/194 of query aligns to 40:224/555 of Q8IJR9

query
sites
Q8IJR9

I

V

T

E

I

L

E

K

G

D

I

I

E

K

A

D

L

M

N

N

P

I

K

K

Y

G

L

V

V

I

I

L

S

S

P

G

G

G

P

P

C

Y

T

S

P

V

A

T

E

E

A

A

G

G

-

S

-

P

-

H

I

L

S

K

V

K

A

E

A

V

I

F

Q

E

Y

Y

F

F

-

L

A

E

G

K

K

K

I

I

P

P

I

I

M

F

G

G

V

I

C
|
C

L

Y

G

G

H

M

Q
|
Q

S

E

I

I

G

A

Q

V

A

Q

F

M

G

N

G

G

H

E

V

V

I

K

R

K

A

S

K

K

E

T

V

S

M

E

H

Y

G

G

K
x
C

T

T

S

D

-

V

-

N

-

I

-

L

-

R

-

N

-

D

-

N

-

I

-

N

-

I

-

T

-

Y

-

C

-

R

-

N

-

F

-

G

-

D

-

S

-

A

-

M

-

D

-

L

-

Y

-

S

-

N

-

Y

P

K

V

L

Y

M

H

N

Q

E

D

T

T

C

G

C

M

L

F

F

A

E

N

N

L

I

P
x
K

N

S

P

D

V

I

T

T

T

V

R

-

Y
x
W

H

M

S
x
N

L

H

V

N

I
x
D

E

E

Q

V

S

T

T

K

L

I

P

P

E

E

C

N

L

F

E

Y

I

L

T

V

A

S

W

S

T

S

Q

E

D

N

A

C

N

-

G

-

E

-

L

-

D

-

E

L

I

I

M

C

G

S

V

I

R

Y

H

N

K

K

T

E

L

Y

P

N

I

I

E

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

E

E

S

V

I
x
Y

L
x
E

T

S

D

L

Q

D

G

G

H

E

Q

L

M

M

L

F

R

Y

N

N

F

F

C89 (= C79) mutation to A: Loss of glutaminase activity, however, glutamine binding is not affected. In presence of exogenous ammonia, the amination of XMP to produce GMP is normal. 2.3-fold decrease in affinity for ATP and 1.8-fold decrease in affinity for XMP. 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-113.
Q93 (= Q83) binding L-glutamine
C113 (≠ K103) mutation to A: 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-89.
K160 (≠ P119) mutation to L: No effect on glutaminase activity. 1.2-fold decrease in affinity for ATP. 1.8-fold decrease in affinity for XMP.
W167 (≠ Y127) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
N169 (≠ S129) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
D172 (≠ I132) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
H208 (= H173) binding L-glutamine
Y212 (≠ I177) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
E213 (≠ L178) mutation to A: 40 percent decrease in glutaminase activity. 1.4-fold decrease in affinity for glutamine. 1.3-fold decrease in affinity for ATP. 1.8-fold decrease in affinity for XMP.

Sites not aligning to the query:

18 Y→F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
20 H→A: Slight decrease in affinity for glutamine. 1.8-fold increase in affinity for ATP. Slight increase in affinity for XMP. Moderate reduction in glutaminase activity.
24 K→L: 50 percent decrease in glutaminase activity. 5.3-fold decrease in affinity for glutamine. 1.7-fold increase in affinity for ATP. 2.8-fold decrease in affinity for XMP.
25 R→L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
336 binding XMP
371 Important for ATPPase activity; D→A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
374 E→L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
376 K→L: 20 percent decrease in glutaminase activity. 4.4-fold decrease in affinity for glutamine. 1.8-fold decrease in affinity for XMP.
386 K→L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
387 T→A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
388 Important for ATPPase activity; H→A: Moderate decrease in ATP pyrophosphatase (ATPPase) activity. Reduces 49 percent decrease in glutaminase activity. Impaired GMP formation.
389 Important for ATPPase activity; H→A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
390 N→A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
411 K→L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
412 D→A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
413 D→A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
415 K→L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
476 binding XMP
539 R→L: 85 percent decrease in glutaminase activity.
547 binding XMP; K→L: 85 percent decrease in glutaminase activity.
552 binding XMP
553 binding XMP; E→L: 85 percent decrease in glutaminase activity.
555 E→L: 20 percent decrease in glutaminase activity. No effect on GMP formation.

Q18990 Multifunctional protein pyr-1; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Caenorhabditis elegans (see 3 papers)
30% identity, 66% coverage: 47:175/194 of query aligns to 221:341/2198 of Q18990

query
sites
Q18990

L

L

V

F

I

L

S

S

P

N

G

G

P

P

C

G

T

D

P

P

A

E

E

I

A

C

G

A

-

P

-

L

I

V

S

D

V

R

A

L

A

A

I

K

Q

V

Y

I

F

A

A

R

G

G

K

D

I

K

P

P

I

I

M

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

I

I

L

G

S

Q

R

A

A

F

I

G

G

G

A

H

K

V

T

I

Y

R

K

A

L

K

K

E

Y

V

G

M

N

H

R

G

G

K

H

T

N

S

Q

P

P

V

C

Y

T

H

H

Q

Y

D

A

T

T

G

G

M

-

F

-

A

-

N

-

L

-

P

-

N

R

P

C

V

Y

T

I

T

T

T

S

R

Q

Y

N

H

H

S

G

L

Y

V

A

I

V

E

D

Q

P

S

D

T

S

L

L

P

P

E

A

C

-

L

-

E

D

I

W

T

K

A

A

W

L

T

F

Q

T

D

N

A

E

N

N

G

D

E

K

L

T

D

N

E

E

I

-

M

-

G

G

V

I

R

V

H

H

K

S

T

S

L

K

P

P

I

F

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

Sites not aligning to the query:

1602 H→Q: In cu8; probable loss of dihydroorotase activity. Severe late stage embryonic lethality in 50% of animals. The few surviving mutants have a shorter and thicker pharyngeal isthmus, an abnormal knobbed tail, mild egg-laying defects, moderate fluid accumulation in the coelom and a slower growth. Actin and intermediate filaments are disorganized in the pharynx. Moderate reduction in heparan sulfate levels and increased levels of chondroitin sulfate. In an umps-1 zu456 mutant background, prevents the formation of abnormally enlarged gut granules in embryos. Complete embryonic lethality in a rnst-2 qx245 mutant background.

P08955 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Mesocricetus auratus (Golden hamster) (see paper)
28% identity, 85% coverage: 11:175/194 of query aligns to 185:338/2225 of P08955

query
sites
P08955

F

L

T

K

Y

Y

N

N

I

Q

V

I

Q

R

Y

C

F

L

G

C

E

Q

L

L

G

G

Q

A

H

E

V

V

E

T

V

V

F

V

R

P

N

W

D

N

Q

H

I

-

T

-

I

-

E

-

G

-

I

-

E

E

A

L

L

D

N

S

P

Q

K

K

Y

Y

-

D

-

G

L

L

V

F

I

L

S

S

P

N

G

G

P

P

C

G

T

D

P

P

A

A

E

S

A

Y

G

P

I

G

S

V

V

V

A

A

A

T

I

L

Q

N

Y

R

F

V

A

L

G

S

K

E

-

P

-

N

-

P

I

R

P

P

I

V

M

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

L

I

L

G

A

Q

L

A

A

F

I

G

G

G

A

H

K

V

T

I

Y

R

K

A

M

K

R

E

Y

V

G

M

N

H

R

G

G

K

H

T

N

S

Q

P

P

V

C

Y

L

H

L

Q

V

D

G

T

T

G

G

M

R

F

C

A

-

N

-

L

-

P

-

N

-

P

-

V

F

T

L

T

T

T

S

R

Q

Y

N

H

H

S

G

L

F

V

A

I

V

E

D

Q

A

S

D

T

S

L

L

P

P

E

-

C

-

L

-

E

-

I

-

T

A

A

G

W

W

T

T

-

P

-

L

-

F

Q

T

D

N

A

A

N

N

G

D

E

C

L

S

D

N

E

E

I

-

M

-

G

G

V

I

R

V

H

H

K

D

T

S

L

L

P

P

I

F

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

Sites not aligning to the query:

1406 modified: Phosphoserine; by PKA; S→A: No effect on enzyme kinetics.; S→D: Increases CPSase activity and reduces sensitivity to feedback inhibition by UTP.

4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
27% identity, 80% coverage: 34:189/194 of query aligns to 34:213/525 of 4wioA

query
sites
4wioA

I

V

T

E

I

L

E

K

G

D

I

I

E

K

A

D

L

M

N

N

P

I

K

K

Y

G

L

V

V

I

I

L

S

S

P

G

G
|
G

P

P

C

Y

T

S

P

V

A

T

E

E

A

A

G

G

-

S

-

P

-

H

I

L

S

K

V

K

A

E

A

V

I

F

Q

E

Y

Y

F

F

-

L

A

E

G

K

K

K

I

I

P

P

I

I

M

F

G

G

V

I

C
x
A

L
x
Y

G

G

H

M

Q
|
Q

S

E

I

I

G

A

Q

V

A

Q

F

M

G

N

G

G

H

E

V

V

I

K

R

K

A

S

K

K

E

T

V

S

M

E

H

Y

G

G

K

C

T

T

S

-

P

-

V

-

Y

-

H

-

Q

-

D

D

T

V

G

N

M

I

F

L

A

R

N

N

L

D

P

N

-

I

N

N

P

N

V

I

T

T

T

Y

T

C

R

R

Y

N

H

F

S

S

-

S

-

A

-

M

-

D

L

L

V

Y

I

S

E

N

Q

Y

S

K

T

L

L

M

P

N

E

E

C

C

L

L

-

F

-

E

-

N

-

I

-

K

-

S

E

D

I

I

T

T

A

T

W

V

T

W

Q

M

D
x
N

A
x
H

N
|
N

G
x
D

E

E

L

V

D

T

E

K

I

I

-

P

-

E

-

N

-

F

-

Y

-

L

-

V

-

S

-

E

-

N

-

C

-

L

-

I

M

C

G

S

V

I

R

Y

H

N

K

K

T

E

L

Y

P

N

I

I

E

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

S

V

I

Y

L

E

T

S

D

L

Q

D

G

G

H

E

Q

L

M

M

L

F

R

Y

N

N

F

F

active site: G52 (= G52), A83 (≠ C79), Y84 (≠ L80), H197 (= H173), E199 (= E175)
binding glutamine: Q87 (= Q83), N158 (≠ D149), H159 (≠ A150), N160 (= N151), D161 (≠ G152), H197 (= H173)

Sites not aligning to the query:

active site: 255, 393

P07259 Multifunctional protein URA2; Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase; CPSase-ATCase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
29% identity, 85% coverage: 13:176/194 of query aligns to 238:389/2214 of P07259

query
sites
P07259

Y

Y

N

N

I

Q

V

I

Q

R

Y

C

F

F

G

I

E

K

L

R

G

G

Q

V

H

E

V

L

E

K

V

V

F

V

-

P

R

W

N

N

D

Y

Q

D

I

F

T

T

I

K

E

E

G

D

I

Y

E

D

A

G

L

L

N

-

P

-

K

-

Y

-

L

-

V

F

I

I

S

S

P

N

G

G

P

P

C

G

T

D

P

P

A

S

E

V

A

L

G

D

I

D

S

L

V

S

A

Q

A

R

I

L

Q

S

Y

N

F

V

-

L

-

E

A

A

G

K

K

K

I

T

P

P

I

V

M

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

L

I

I

G

A

Q

R

A

A

F

A

G

G

G

A

H

S

V

T

I

L

R

K

A

L

K

K

E

F

V

G

M

N

H

R

G

G

K

H

T

N

S

I

P

P

V

C

Y

T

H

S

Q

T

D

I

T

S

G

G

M

R

F

C

A

-

N

-

L

-

P

-

N

-

P

-

V

Y

T

I

T

T

T

S

R

Q

Y

N

H

H

S

G

L

F

V

A

I

V

E

D

Q

V

S

D

T

T

L

L

P

-

E

-

C

-

L

-

E

-

I

T

T

S

A

G

W

W

T

K

Q

P

-

L

-

F

-

V

D

N

A

A

N

N

G

D

E

D

L

S

D

N

E

E

I

-

M

-

G

G

V

I

R

Y

H

H

K

S

T

E

L

L

P

P

I

Y

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

S

Sites not aligning to the query:

1857 modified: Phosphoserine; by PKA

Query Sequence

>WP_019557133.1 NCBI__GCF_000381085.1:WP_019557133.1
MLLMIDNYDSFTYNIVQYFGELGQHVEVFRNDQITIEGIEALNPKYLVISPGPCTPAEAG
ISVAAIQYFAGKIPIMGVCLGHQSIGQAFGGHVIRAKEVMHGKTSPVYHQDTGMFANLPN
PVTTTRYHSLVIEQSTLPECLEITAWTQDANGELDEIMGVRHKTLPIEGVQFHPESILTD
QGHQMLRNFLEQNA

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