SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_015799097.1 NCBI__GCF_000023265.1:WP_015799097.1 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)

6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
36% identity, 96% coverage: 5:302/310 of query aligns to 4:291/293 of 6pnzA

query
sites
6pnzA

F

L

L

L

G

S

V

M

E

E

Q

H

L

L

D

S

A

T

G

D

R

Q

L

I

G

Y

V

K

L

L

G

I

A

Q

R

K

V

A

D

S

E

Q

L

F

V

K

H

S

G

G

A

E

A

R

A

Q

S

L

R

P

C

N

L

F

E

E

G

G

R

K

R

Y

V

V

A

A

L

N

L

L

F

F

L

F

E

E

P

N

S
|
S

T
|
T

R
|
R

T
|
T

A

K

L

C

S

S

F

F

E

E

A

M

A

A

I

E

D

L

R

K

L

L

G

G

G

L

R

K

T

T

V

I

R

S

I

F

D

E

P

T

E

S

S

T

S

S

S
|
S

L

V

V

S

K
|
K

D

G

E

E

S

S

L

L

R

Y

D

D

T

T

L

C

R

K

V

T

L

L

A

E

A

S

Q

I

G

G

T

C

S

D

G

L

V

L

V

V

V

I

R
|
R

A

H

P

P

W

F

V

N

G

N

T

Y

A

Y

D

E

V

K

V

L

A

A

R

N

F

-

F

I

D

N

G

I

I

P

V

I

V

A

N

N

A

A

G

G

D

D

G

G

V

S

G

G

Q

Q

H
|
H

P

P

T

T

Q

Q

A

S

L

L

Q

L

D

D

V

L

C

M

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

Y

D

E

A

E

F

Y

G

G

A

Y

L

F

E

E

G

G

C

L

R

N

V

V

A

L

I

I

V

C

G

G

D

D

L

I

R

K

H

N

S

S

R
|
R

V

V

A

A

R

R

S

S

V

N

G

Y

R

H

L

S

L

L

A

K

S

A

V

L

G

G

A

A

E

N

V

V

V

M

G

F

V

N

A

S

P

P

R

N

E

A

W

W

S

I

L

D

D

D

P

-

K

-

A

S

L

L

G

E

A

A

V

P

G

Y

V

V

T

-

D

-

G

N

I

I

D

D

V

V

L

I

D

E

E

T

V

V

D

D

V

I

F

V

Y

M

M

L

L

L

R
|
R

I

I

Q
|
Q

H

H

E

E

R

R

V

H

G

G

A

L

N

A

E

E

R

E

V

T

D

R

L

F

S

A

G

A

-

D

Y

Y

R

H

A

Q

R

K

F

H

Q

G

L

L

S

N

G

E

H

V

R

R

L

Y

E

N

R

K

A

L

R

Q

P

E

D

H

A

A

V

I

V

V

L

M

H

H

P

P

G
x
A

P

P

V

V

N

N

R

R

G

G

V

V

E

E

L

I

D

Q

D

S

I

D

V

L

L

V

S

E

S

A

P

S

R

K

M

S

L

R

D

I

G

F

L

K

Q

Q

Y

M

A

E

Y

N

G

G

V

V

P

Y

T

L

R

R

V

M

A

A

V

V

L

I

E

D

A

E

L

L

binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S49), T49 (= T50), R50 (= R51), T51 (= T52), S75 (= S76), K78 (= K79), R100 (= R101), H127 (= H129), R160 (= R169), R210 (= R223), Q212 (= Q225), A253 (≠ G264)

3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
37% identity, 89% coverage: 25:300/310 of query aligns to 24:286/290 of 3r7lA

query
sites
3r7lA

E

E

L

L

V

K

H

S

G

G

A

K

A

T

A

D

S

N

R

Q

C

-

L

L

E

T

G

G

R

K

R

F

V

A

A

A

L

N

L

L

F

F

L

F

E

E

P

P

S
|
S

T
|
T

R
|
R

T
|
T

A

R

L

F

S

S

F

F

E

E

A

V

A

A

I

E

D

K

R

K

L

L

G

G

G

M

R

N

T

V

V

L

R

N

I

L

D

D

P

G

E

T

S

S

S

T

S
|
S

L

V

V

Q

K
|
K

D

G

E

E

S

T

L

L

R

Y

D

D

T

T

L

I

R

R

V

T

L

L

A

E

A

S

Q

I

G

G

T

V

S

D

G

V

V

C

V

V

V

I

R
|
R

A

H

P

S

W

E

V

D

G

E

T

Y

A

Y

D

E

V

E

V

L

A

V

R

S

F

Q

F

V

D

N

G

I

I

P

V

I

V

L

N

N

A

A

G

G

D

D

G

G

V

C

G

G

Q

Q

H
|
H

P

P

T

T

Q
|
Q

A

S

L

L

Q

L

D

D

V

L

C

M

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

Y

D

E

A

E

F

F

G

N

A

T

L

F

E

K

G

G

C

L

R

T

V

V

A

S

I

I

V

H

G

G

D

D

L

I

R

K

H

H

S

S

R
|
R

V

V

A

A

R

R

S

S

V

N

G

A

R

E

L

V

L

L

A

T

S

R

V

L

G

G

A

A

E

R

V

V

V

L

G

F

V

S

A

G

P

P

R

S

E

E

W

W

S

Q

L

D

D

E

P

E

K

N

A

T

L

F

G

G

A

T

V

Y

G

V

V

-

T

-

D

-

G

S

I

M

D

D

D

E

V

A

L

V

D

E

E

S

V

S

D

D

V

V

F

V

Y

M

M

L

L
|
L

R
|
R

I

I

Q
|
Q

H

N

E

E

R

R

V

-

G

-

A

H

N

Q

E

S

R

A

V

V

D

S

L

Q

S

E

G

G

Y

Y

R

L

A

N

R

K

F

Y

Q

G

L

L

S

T

G

V

H

E

R

R

L

A

E

E

R

R

A

M

R

K

P

R

D

H

A

A

V

I

L

M

H

H

P
|
P

G
x
A

P

P

V

V

N

N

R

R

G

G

V

V

E

E

L

I

D

D

I

S

V

L

L

V

S

E

S

S

P

E

R

K

M

S

L

R

D

I

G

F

L

K

Q

Q

Y

M

A

K

Y

N

G
|
G

V

V

P

F

T

I

R

R

V

M

A

A

V

V

L

I

E

Q

active site: R49 (= R51), T50 (= T52), K77 (= K79), R99 (= R101), H127 (= H129), Q130 (= Q132), L210 (= L222), P249 (= P263), G277 (= G291)
binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S49), T48 (= T50), R49 (= R51), T50 (= T52), S74 (= S76), K77 (= K79), R99 (= R101), H127 (= H129), R160 (= R169), R211 (= R223), Q213 (= Q225), A250 (≠ G264)

P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
37% identity, 85% coverage: 36:300/310 of query aligns to 34:286/304 of P05654

query
sites
P05654

L

L

E

T

G

G

R

K

R

F

V

A

A

A

L

N

L

L

F

F

L

F

E

E

P

P

S

S

T

T

R

R

T

T

A

R

L

F

S

S

F

F

E

E

A

V

A

A

I

E

D

K

R

K

L

L

G

G

G

M

R

N

T

V

V

L

R

N

I

L

D

D

P

G

E

T

S

S

S

T

S

S

L

V

V

Q

K

K

D

G

E

E

S

T

L

L

R

Y

D

D

T

T

L

I

R

R

V

T

L

L

A

E

A

S

Q

I

G

G

T

V

S

D

G

V

V

C

V

V

V

I

R

R

A

H

P

S

W

E

V

D

G

E

T

Y

A

Y

D

E

V

E

V

L

A

V

R

S

F

Q

F

V

D

N

G

I

I

P

V

I

V

L

N

N

A

A

G

G

D

D

G

G

V

C

G

G

Q

Q

H

H

P

P

T

T

Q

Q

A

S

L

L

Q

L

D

D

V

L

C

M

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

Y

D

E

A

E

F

F

G

N

A

T

L

F

E

K

G

G

C

L

R

T

V

V

A

S

I

I

V

H

G

G

D

D

L

I

R

K

H

H

S

S

R

R

V

V

A

A

R

R

S

S

V

N

G

A

R

E

L

V

L

L

A

T

S

R

V

L

G

G

A

A

E

R

V

V

V

L

G

F

V

S

A

G

P

P

R

S

E

E

W

W

S

Q

L

D

D

E

P

E

K

N

A

T

L

F

G

G

A

T

V

Y

G

V

V

-

T

-

D

-

G

S

I

M

D

D

D

E

V

A

L

V

D

E

E

S

V

S

D

D

V

V

F

V

Y

M

M

L

L

L

R

R

I

I

Q

Q

H

N

E

E

R

R

V

-

G

-

A

H

N

Q

E

S

R

A

V

V

D

S

L

Q

S

E

G

G

Y

Y

R

L

A

N

R

K

F

Y

Q

G

L

L

S

T

G

V

H

E

R

R

L

A

E

E

R

R

A

M

R

K

P

R

D

H

A

A

V

I

L

M

H

H

P

P

G

A

P

P

V

V

N

N

R

R

G

G

V

V

E

E

L

I

D

D

I

S

V

L

L

V

S

E

S

S

P

E

R

K

M

S

L

R

D

I

G

F

L

K

Q

Q

Y

M

A

K

Y

N

G

G

V

V

P

F

T

I

R

R

V

M

A

A

V

V

L

I

E

Q

Sites not aligning to the query:

303 modified: Phosphoserine

3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
37% identity, 89% coverage: 25:300/310 of query aligns to 24:286/291 of 3r7fA

query
sites
3r7fA

E

E

L

L

V
x
K

H

S

G

G

A

K

A

T

A

D

S

N

R

Q

C

-

L

L

E

T

G

G

R

K

R

F

V

A

A

A

L

N

L

L

F

F

L

F

E

E

P

P

S
|
S

T
|
T

R
|
R

T
|
T

A

R

L

F

S

S

F

F

E

E

A

V

A

A

I

E

D

K

R

K

L

L

G

G

G

M

R

N

T

V

V

L

R

N

I

L

D

D

P

G

E

T

S

S

S

T

S

S

L

V

V

Q

K
|
K

D

G

E

E

S

T

L

L

R

Y

D

D

T

T

L

I

R

R

V

T

L

L

A

E

A

S

Q

I

G

G

T

V

S

D

G

V

V

C

V

V

V

I

R
|
R

A

H

P

S

W

E

V

D

G

E

T

Y

A

Y

D

E

V

E

V

L

A

V

R

S

F

Q

F

V

D

N

G

I

I

P

V

I

V

L

N

N

A

A

G

G

D

D

G

G

V

C

G

G

Q

Q

H
|
H

P

P

T

T

Q
|
Q

A

S

L

L

Q

L

D

D

V

L

C

M

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

Y

D
x
E

A

E

F

F

G

N

A

T

L

F

E

K

G

G

C

L

R

T

V

V

A

S

I

I

V

H

G

G

D

D

L

I

R

K

H

H

S

S

R

R

V

V

A

A

R

R

S

S

V

N

G

A

R

E

L

V

L

L

A

T

S
x
R

V

L

G

G

A

A

E

R

V

V

V

L

G

F

V

S

A

G

P

P

R

S

E

E

W

W

S

Q

L

D

D

E

P

E

K

N

A

T

L

F

G

G

A

T

V

Y

G

V

V

-

T

-

D

-

G

S

I

M

D

D

D

E

V

A

L

V

D

E

E

S

V

S

D

D

V

V

F

V

Y

M

M

L

L
|
L

R

R

I

I

Q

Q

H

N

E

E

R

R

V

-

G

-

A

H

N

Q

E

S

R

A

V

V

D

S

L

Q

S

E

G

G

Y

Y

R

L

A

N

R

K

F

Y

Q

G

L

L

S

T

G

V

H

E

R

R

L

A

E

E

R

R

A

M

R
x
K

P

R

D
x
H

A

A

V

I

L

M

H

H

P
|
P

G
x
A

P

P

V

V

N

N

R

R

G

G

V

V

E

E

L

I

D

D

I

S

V

L

L

V

S

E

S

S

P

E

R

K

M

S

L

R

D

I

G

F

L
x
K

Q

Q

Y

M

A
x
K

Y

N

G
|
G

V

V

P

F

T

I

R

R

V

M

A

A

V

V

L

I

E

Q

active site: R49 (= R51), T50 (= T52), K77 (= K79), R99 (= R101), H127 (= H129), Q130 (= Q132), L210 (= L222), P249 (= P263), G277 (= G291)
binding phosphoric acid mono(formamide)ester: S47 (= S49), T48 (= T50), R49 (= R51), T50 (= T52), R99 (= R101), H127 (= H129), Q130 (= Q132), P249 (= P263), A250 (≠ G264)
binding phosphate ion: K26 (≠ V27), E140 (≠ D149), R171 (≠ S180), K241 (≠ R255), H243 (≠ D257), K272 (≠ L286), K272 (≠ L286), K275 (≠ A289)

Sites not aligning to the query:

binding phosphate ion: 11, 12, 23

3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
37% identity, 89% coverage: 25:300/310 of query aligns to 24:286/291 of 3r7dA

query
sites
3r7dA

E

E

L

L

V

K

H

S

G

G

A

K

A

T

A

D

S

N

R

Q

C

-

L

L

E

T

G

G

R

K

R

F

V

A

A

A

L

N

L

L

F

F

L

F

E

E

P

P

S

S

T

T

R
|
R

T
|
T

A

R

L

F

S

S

F

F

E

E

A

V

A

A

I

E

D

K

R

K

L

L

G

G

G

M

R

N

T

V

V

L

R

N

I

L

D

D

P

G

E

T

S

S

S
x
T

S
|
S

L

V

V

Q

K
|
K

D

G

E

E

S

T

L

L

R

Y

D

D

T

T

L

I

R

R

V

T

L

L

A

E

A

S

Q

I

G

G

T

V

S

D

G

V

V

C

V

V

V

I

R
|
R

A

H

P

S

W

E

V

D

G

E

T

Y

A

Y

D

E

V

E

V

L

A

V

R

S

F

Q

F

V

D

N

G

I

I

P

V

I

V

L

N

N

A

A

G

G

D

D

G

G

V

C

G

G

Q

Q

H
|
H

P

P

T

T

Q
|
Q

A

S

L

L

Q

L

D

D

V

L

C

M

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

Y

D

E

A

E

F

F

G

N

A

T

L

F

E

K

G

G

C

L

R

T

V

V

A

S

I

I

V

H

G

G

D

D

L

I

R

K

H

H

S

S

R

R

V

V

A

A

R

R

S

S

V

N

G

A

R

E

L

V

L

L

A

T

S
x
R

V

L

G

G

A

A

E

R

V

V

V

L

G

F

V

S

A

G

P

P

R

S

E

E

W

W

S

Q

L

D

D

E

P

E

K

N

A

T

L

F

G

G

A

T

V

Y

G

V

V

-

T

-

D

-

G

S

I

M

D

D

D

E

V

A

L

V

D

E

E

S

V

S

D

D

V

V

F

V

Y

M

M

L

L
|
L

R

R

I

I

Q

Q

H

N

E

E

R

R

V

-

G

-

A

H

N

Q

E

S

R

A

V

V

D

S

L

Q

S

E

G

G

Y

Y

R

L

A

N

R

K

F

Y

Q

G

L

L

S

T

G

V

H

E

R

R

L

A

E

E

R

R

A

M

R

K

P

R

D

H

A

A

V

I

L

M

H

H

P
|
P

G

A

P

P

V

V

N

N

R

R

G

G

V

V

E

E

L

I

D

D

I

S

V

L

L

V

S

E

S

S

P

E

R

K

M

S

L

R

D

I

G

F

L

K

Q

Q

Y

M

A

K

Y

N

G
|
G

V

V

P

F

T

I

R

R

V

M

A

A

V

V

L

I

E

Q

active site: R49 (= R51), T50 (= T52), K77 (= K79), R99 (= R101), H127 (= H129), Q130 (= Q132), L210 (= L222), P249 (= P263), G277 (= G291)
binding phosphate ion: T73 (≠ S75), S74 (= S76), K77 (= K79), R171 (≠ S180)

Sites not aligning to the query:

binding phosphate ion: 11, 12

P20054 Multifunctional protein pyr1-3; 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 Dictyostelium discoideum (Social amoeba)
36% identity, 91% coverage: 26:307/310 of query aligns to 1949:2224/2225 of P20054

query
sites
P20054

L

L

V

V

H

K

G

R

A

S

A

G

S

S

R

D

C

L

L

L

E

K

G

G

R

K

R

V

V

L

A

A

L

T

L

L

F

F

L

Y

E

E

P

P

S

S

T

T

R

R

T

T

A

Q

L

C

S

S

F

F

E

T

A

A

I

M

D

Q

R

R

L

L

G

G

R

S

T

V

V

V

R

T

I

V

D

D

P

N

E

V

S

S

L

V

V

A

K

K

D

G

E

E

S

S

L

I

R

A

D

D

T

T

L

I

R

Q

V

T

L

L

A

E

A

S

Q

Y

G

-

T

C

S

D

G

A

V

V

V

C

V

M

R

R

A

H

P

P

W

A

V

V

G

G

T

S

A

V

D

E

V

S

V

A

A

I

R

Q

F

V

F

A

D

K

G

K

I

P

V

I

N

N

A

A

G

G

D

D

G

G

V

V

G

G

Q

E

H

H

P

P

T

T

Q

Q

A

A

L

L

Q

L

D

D

V

V

C

F

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

R

D

E

A

E

F

L

G

G

A

T

L

V

E

N

G

G

C

L

R

T

V

I

A

T

I

V

V

V

G

G

D

D

L

L

R

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

V

L

G

V

R

R

L

L

A

A

S

N

V

Y

G

Q

A

V

E

K

V

I

V

N

G

Y

V

V

A

S

P

P

R

S

E

S

W

L

S

S

L

M

D

P

P

T

-

E

-

I

K

K

A

E

L

L

G

N

A

E

V

K

G

G

V

I

T

E

D

Q

-

K

-

E

-

Y

-

T

G

N

I

I

D

E

D

S

V

I

L

L

D

P

E

T

V

T

D

N

V

V

F

L

Y

Y

M

V

L

T

R

R

I

V

Q

Q

H

K

E

E

R

R

V

F

G

Q

A

S

N

I

E

E

R

-

V

-

D

E

L

Y

S

E

G

K

Y

V

R

K

A

D

R

S

F

F

Q

I

L

I

S

T

G

P

H

H

R

T

L

L

E

T

R

K

A

A

R

S

P

D

D

N

A

M

V

I

V

V

L

M

H

H

P

P

G

L

P

P

V

-

N

-

R

R

G

I

V

N

E

E

L

I

D

S

D

P

I

E

V

V

L

D

S

S

S

D

P

P

R

R

M

A

L

A

D

Y

G

F

L

R

Q

Q

Y

M

A

E

Y

N

G

G

V

L

P

Y

T

V

R

R

V

M

A

S

V

L

L

L

E

-

A

A

L

L

A

V

E

F

E

G

A

A

G

G

Sites not aligning to the query:

1 modified: N-acetylmethionine

5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
35% identity, 85% coverage: 36:299/310 of query aligns to 42:300/307 of 5g1nE

query
sites
5g1nE

L

L

E

K

G

G

R

K

R

V

V

M

A

A

L

S

L

M

F

F

L

Y

E

E

P

V

S
|
S

T
|
T

R
|
R

T
|
T

A

S

L

S

S

S

F

F

E

A

A

A

I

M

D

A

R

R

L

L

G

G

R

A

T

V

V

L

R

S

I

F

D

S

P

E

E

A

S

T

S

S

S
|
S

L

V

V

Q

K
|
K

D

G

E

E

S

S

L

L

R

A

D

D

T

S

L

V

R

Q

V

T

L

M

A

S

A

C

Q

Y

G

A

T

-

S

D

G

V

V

V

V

L

R
|
R

A

H

P

P

W

Q

V

P

G

G

T

A

A

V

D

E

V

L

V

A

A

A

R

K

F

H

F

C

D

R

G

R

I

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

V

V

G

G

Q

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

L

Q

L

D

D

V

I

C

F

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

R

D

E

A

E

F

L

G

G

A

T

L

V

E

N

G

G

C

M

R

T

V

I

A

T

I

M

V

V

G

G

D

D

L

L

R

K

H

H

S

G

R
|
R

V

T

A

V

R

H

S

S

V

L

G

A

R

C

L

L

A

T

S

Q

V

Y

G

R

A

V

E

S

V

L

V

R

G

Y

V

V

A

A

P

P

R

P

E

S

W

L

S

R

L

M

D

P

P

P

K

T

A

V

L

R

G

A

A

F

V

V

G

A

V

S

-

R

-

G

-

T

-

K

-

Q

-

E

T

F

D

E

G

S

I

I

D

E

V

A

L

L

D

P

E

D

V

T

D

D

V

V

F

L

Y

Y

M

M

L
x
T

R
|
R

I

I

Q
|
Q

H

K

E

E

R

R

V

F

G

G

A

S

N

T

E

Q

R

-

V

-

D

E

L

Y

S

E

G

A

Y

C

R

F

A

G

R

Q

F

F

Q

I

L

L

S

T

G

P

H

H

R

I

L

M

E

T

R

R

A

A

R

K

P

K

D

K

A

M

V

V

L

M

H

H

P
|
P

G
x
M

P

P

-

R

V

V

N

N

R

E

-

I

G

S

V

V

E

E

L

V

D

D

D

-

I

-

V

-

L

-

S

S

S

D

P

P

R

R

M

A

L

A

D

Y

G

F

L

R

Q

Q

Y

A

A

E

Y

N

G
|
G

V

M

P

Y

T

I

R

R

V

M

A

A

V

L

L

L

active site: R57 (= R51), T58 (= T52), K85 (= K79), R106 (= R101), H134 (= H129), Q137 (= Q132), T227 (≠ L222), P266 (= P263), G292 (= G291)
binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S49), T56 (= T50), R57 (= R51), T58 (= T52), S82 (= S76), K85 (= K79), R106 (= R101), H134 (= H129), R167 (= R169), R228 (= R223), Q230 (= Q225), M267 (≠ G264)

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)
36% identity, 85% coverage: 36:299/310 of query aligns to 1955:2213/2224 of P05990

query
sites
P05990

L

L

E

P

G

G

R

K

R

I

V

M

A

A

L

S

L

V

F

F

L

Y

E

E

P

V

S

S

T

T

R

R

T

T

A

Q

L

C

S

S

F

F

E

A

A

A

I

M

D

L

R

R

L

L

G

G

R

R

T

V

V

I

R

S

I

M

D

D

P

N

E

I

S

T

S

S

L

V

V

K

K

K

D

G

E

E

S

S

L

L

R

E

D

D

T

S

L

I

R

K

V

V

L

V

A

S

Q

Y

G

A

T

D

S

V

G

-

V

V

V

L

R

R

A

H

P

P

W

S

V

P

G

G

T

A

A

V

D

A

V

R

V

A

A

A

R

T

F

F

F

S

D

R

G

K

I

P

V

L

V

I

N

N

A

A

G

G

D

D

G

G

V

V

G

G

Q

E

H

H

P

P

T

T

Q

Q

A

A

L

L

Q

L

D

D

V

I

C

F

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

R

D

E

A

E

F

F

G

G

A

T

L

V

E

N

G

G

C

L

R

T

V

I

A

T

I

M

V

V

G

G

D

D

L

L

R

K

H

N

S

G

R

R

V

T

A

V

R

H

S

S

V

L

G

A

R

R

L

L

A

T

S

L

V

Y

G

N

A

V

E

N

V

L

V

Q

G

Y

V

V

A

A

P

P

R

N

E

S

W

L

S

Q

L

M

D

P

P

D

K

E

A

V

L

V

G

Q

A

F

V

V

-

H

-

Q

-

R

G

G

V

V

T

K

D

Q

-

L

-

F

-

A

-

R

G

D

I

L

D

K

D

N

V

V

L

L

D

P

E

D

V

T

D

D

V

V

F

L

Y

Y

M

M

L

T

R

R

I

I

Q

Q

H

R

E

E

R

R

V

F

G

D

A

N

N

V

E

E

R

-

V

-

D

D

L

Y

S

E

G

K

Y

C

R

C

A

G

R

H

F

L

Q

V

L

L

S

T

G

P

H

E

R

H

L

M

E

M

R

R

A

A

R

K

P

K

D

R

A

S

V

I

V

V

L

L

H

H

P

P

G

L

P

P

V

-

N

-

R

R

G

L

V

N

E

E

L

I

D

S

D

R

I

E

V

I

L

D

S

S

S

D

P

P

R

R

M

A

L

A

D

Y

G

F

L

R

Q

Q

Y

A

A

E

Y

Y

G

G

V

M

P

Y

T

I

R

R

V

M

A

A

V

L

L

L

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

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)
35% identity, 85% coverage: 36:299/310 of query aligns to 1960:2218/2225 of P08955

query
sites
P08955

L

L

E

K

G

G

R

K

R

V

V

M

A

A

L

S

L

M

F

F

L

Y

E

E

P

V

S

S

T

T

R

R

T

T

A

S

L

S

S

S

F

F

E

A

A

A

I

M

D

A

R

R

L

L

G

G

R

A

T

V

V

L

R

S

I

F

D

S

P

E

E

A

S

T

S

S

L

V

V

Q

K

K

D

G

E

E

S

S

L

L

R

A

D

D

T

S

L

V

R

Q

V

T

L

M

A

S

A

C

Q

Y

G

A

T

D

S

V

G

-

V

V

V

L

R

R

A

H

P

P

W

Q

V

P

G

G

T

A

A

V

D

E

V

L

V

A

A

A

R

K

F

H

F

C

D

R

G

R

I

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

V

V

G

G

Q

E

H

H

P

P

T

T

Q

Q

A

A

L

L

Q

L

D

D

V

I

C

F

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

R

D

E

A

E

F

L

G

G

A

T

L

V

E

N

G

G

C

M

R

T

V

I

A

T

I

M

V

V

G

G

D

D

L

L

R

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

V

L

G

A

R

C

L

L

A

T

S

Q

V

Y

G

R

A

V

E

S

V

L

V

R

G

Y

V

V

A

A

P

P

R

P

E

S

W

L

S

R

L

M

D

P

P

P

K

S

A

V

L

W

G

D

A

F

V

V

G

A

V

S

-

R

-

G

-

T

-

K

-

Q

-

E

T

F

D

E

G

S

I

I

D

E

V

A

L

L

D

P

E

D

V

T

D

D

V

V

F

L

Y

Y

M

M

L

T

R

R

I

I

Q

Q

H

K

E

E

R

R

V

F

G

G

A

S

N

T

E

Q

R

E

V

Y

D

E

L

-

S

-

G

A

Y

C

R

F

A

G

R

Q

F

F

Q

I

L

L

S

T

G

P

H

H

R

I

L

M

E

T

R

R

A

A

R

K

P

K

D

K

A

M

V

V

L

M

H

H

P

P

G

M

P

P

-

R

V

V

N

N

R

E

-

I

G

S

V

V

E

E

L

V

D

D

D

-

I

-

V

-

L

-

S

S

S

D

P

P

R

R

M

A

L

A

D

Y

G

F

L

R

Q

Q

Y

A

A

E

Y

N

G

G

V

M

P

Y

T

I

R

R

V

M

A

A

V

L

L

L

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.

P27708 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 Homo sapiens (Human) (see 7 papers)
35% identity, 85% coverage: 36:299/310 of query aligns to 1960:2218/2225 of P27708

query
sites
P27708

L
|
L

E
x
K

G
|
G

R
x
K

R
x
V

V
x
M

A
|
A

L
x
S

L
x
M

F
|
F

L
x
Y

E
|
E

P
x
V

S
|
S

T
|
T

R
|
R

T
|
T

A
x
S

L
x
S

S
|
S

F
|
F

E
x
A

A
|
A

I
x
M

D
x
A

R
|
R

L
|
L

G
|
G

R
x
A

T
x
V

V
x
L

R
x
S

I
x
F

D
x
S

P
x
E

E
x
A

S
x
T

S
|
S

L
x
V

V
x
Q

K
|
K

D
x
G

E
|
E

S
|
S

L
|
L

R
x
A

D
|
D

T
x
S

L
x
V

R
x
Q

V
x
T

L
x
M

A
x
S

A
x
C

Q
x
Y

G
x
A

T
x
D

S
x
V

G

-

V
|
V

V
x
L

R
|
R

A
x
H

P
|
P

W
x
Q

V
x
P

G
|
G

T
x
A

A
x
V

D
x
E

V
x
L

V
x
A

A
|
A

R
x
K

F
x
H

F
x
C

D
x
R

G
x
R

I
x
P

V
|
V

V
x
I

N
|
N

A
|
A

G
|
G

D
|
D

G
|
G

V
|
V

G
|
G

Q
x
E

H
|
H

P
|
P

T
|
T

Q
|
Q

A
|
A

L
|
L

Q
x
L

D
|
D

V
x
I

C
x
F

V
x
T

L
x
I

A

-

R

-

T

-

R

-

G

-

R

-

A
x
R

D
x
E

A
x
E

F
x
L

G
|
G

A
x
T

L
x
V

E
x
N

G
|
G

C
x
M

R
x
T

V
x
I

A
x
T

I
x
M

V
|
V

G
|
G

D
|
D

L
|
L

R
x
K

H
|
H

S
x
G

R
|
R

V
x
T

A
x
V

R
x
H

S
|
S

V
x
L

G
x
A

R
x
C

L
|
L

A
x
T

S
x
Q

V
x
Y

G
x
R

A
x
V

E
x
S

V
x
L

V
x
R

G
x
Y

V
|
V

A
|
A

P
|
P

R
x
P

E
x
S

W
x
L

S
x
R

L
x
M

D
x
P

P
|
P

K
x
T

A
x
V

L
x
R

G
x
A

A
x
F

V
|
V

G
x
A

V
x
S

-
x
R

-
x
G

-
x
T

-
x
K

-
x
Q

-
x
E

T
x
F

D
x
E

G
x
S

I
|
I

D
x
E

V
x
A

L
|
L

D
x
P

E
x
D

V
x
T

D
|
D

V
|
V

F
x
L

Y
|
Y

M
|
M

L
x
T

R
|
R

I
|
I

Q
|
Q

H
x
K

E
|
E

R
|
R

V
x
F

G
|
G

A
x
S

N
x
T

E
x
Q

R
x
E

V
x
Y

D
x
E

L

-

S

-

G
x
A

Y
x
C

R
x
F

A
x
G

R
x
Q

F
|
F

Q
x
I

L
|
L

S
x
T

G
x
P

H
|
H

R
x
I

L
x
M

E
x
T

R
|
R

A
|
A

R
x
K

P
x
K

D
x
K

A
x
M

V
|
V

L
x
M

H
|
H

P
|
P

G
x
M

P
|
P

-
x
R

V
|
V

N
|
N

R
x
E

-
x
I

G
x
S

V
|
V

E
|
E

L
x
V

D
|
D

D

-

I

-

V

-

L

-

S
|
S

S
x
D

P
|
P

R
|
R

M
x
A

L
x
A

D
x
Y

G
x
F

L
x
R

Q
|
Q

Y
x
A

A
x
E

Y
x
N

G
|
G

V
x
M

P
x
Y

T
x
I

R
|
R

V
x
M

A
|
A

V
x
L

L
|
L

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylalanine
33 M → R: in DEE50; uncertain significance; dbSNP:rs751610198
177 R → Q: in a colorectal cancer sample; somatic mutation; dbSNP:rs374122292
456 modified: Phosphothreonine; by MAPK1
735 Y → C: in a colorectal cancer sample; somatic mutation
1406 modified: Phosphoserine; by PKA
1471 binding Zn(2+); binding Zn(2+); H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
1473 binding Zn(2+); H→A: No zinc-binding and no catalytic activity.
1475 binding (S)-dihydroorotate
1505 binding (S)-dihydroorotate
1512 D→N: No change in catalytic activity.
1556 binding via carbamate group; binding via carbamate group; modified: N6-carboxylysine
1562 T→A: Abolishes dihydroorotase activity.
1563 F→A: Abolishes dihydroorotase activity.
1590 binding Zn(2+); H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
1613 binding Zn(2+); C→S: Reduces dihydroorotase activity.
1614 binding Zn(2+); H→A: Abolishes dihydroorotase activity.
1637 binding Zn(2+); E→T: Abolishes dihydroorotase activity.
1642 H→N: 11.5% of wild-type catalytic activity.
1661 binding (S)-dihydroorotate
1686 binding Zn(2+); D→N: Abolishes dihydroorotase activity.
1690 binding (S)-dihydroorotate; H→N: 3% of wild-type catalytic activity.
1702 binding (S)-dihydroorotate
1789:2225 natural variant: Missing (in DEE50; uncertain significance)
1859 modified: Phosphoserine; by RPS6KB1 and PKA
1873 modified: Phosphoserine; by PKC; in vitro; S→A: Abolishes PMA-induced Thr-456 phosphorylation.
1900 modified: Phosphoserine

4bjhB Crystal structure of the aquifex reactor complex formed by dihydroorotase (h180a, h232a) with dihydroorotate and aspartate transcarbamoylase with n-(phosphonacetyl)-l-aspartate (pala) (see paper)
36% identity, 84% coverage: 43:302/310 of query aligns to 39:289/291 of 4bjhB

query
sites
4bjhB

L

L

L

F

F

F

L

S

E

E

P

P

S
|
S

T
|
T

R
|
R

T
|
T

A

R

L

L

S

S

F

F

E

E

A

K

A

A

I

A

D

R

R

E

L

L

G

G

G

I

R

E

T

T

V

Y

R

L

I

V

D

S

P

G

E

S

S

E

S

S

L

T

V

V

K
|
K

D

G

E

E

S

S

L

F

R

F

D

D

T

T

L

L

R

K

V

T

L

F

A

E

A

G

Q

L

G

G

T

F

S

D

-

Y

G

V

V

V

V

F

V
x
R

R

V

A

P

P

F

W

V

V

F

G

F

T

P

A

Y

D

K

V

E

V

I

A

V

R

K

F

S

F

L

D

N

G

L

I

R

V

L

V

V

N

N

A

A

G

G

D

D

G

G

V

T

G

H

Q

Q

H
|
H

P

P

T

S

Q
|
Q

A

G

L

L

Q

I

D

D

V

F

C

F

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

K

D

E

A

H

F

F

G

G

A

E

L

V

E

K

G

D

C

L

R

R

V

V

A

L

I

Y

V

V

G

G

D

D

L

I

R

K

H

H

S

S

R
|
R

V
|
V

A

F

R

R

S

S

V

G

G

A

R

P

L

L

A

N

S

M

V

F

G

G

A

A

E

K

V

I

V

G

G

V

V

C

A

G

P

P

R

K

E

-

W

-

S

T

L

L

D

I

P

P

K

R

-

D

-

V

A

E

L

V

G

F

A

K

V

V

G

D

V

V

T

F

D

D

G

D

I

V

D

D

D

K

V

G

L

I

D

D

E

W

V

A

D

D

V

V

F

V

Y

I

M

W

L

L

R
|
R

I

L

Q
|
Q

H

K

E

E

R

R

V

Q

G

K

A

E

N

N

E

Y

R

I

V

P

D

S

L

E

S

S

G

S

Y

Y

R

F

A

K

R

Q

F

F

Q

G

L

L

S

T

G

K

H

E

R

R

L

F

E

E

R

K

A

V

R

K

P

-

D

-

A

-

V

L

V

Y

L

M

H

H

P

P

G
|
G

P

P

V

V

N

N

R

R

G

N

V

V

E

D

L

I

D

D

D

H

I

E

V

L

L

V

S

Y

S

T

P

E

R

K

M

S

L

L

D

I

G

Q

L

E

Q

Q

Y

V

A

K

Y

N

G

G

V

I

P

P

T

V

R

R

V

K

A

A

V

I

L

Y

E

K

A

F

L

L

active site: R47 (= R51), T48 (= T52), K75 (= K79), R97 (≠ V100), H126 (= H129), Q129 (= Q132)
binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S49), T46 (= T50), R47 (= R51), T48 (= T52), R97 (≠ V100), H126 (= H129), R159 (= R169), V160 (= V170), R213 (= R223), Q215 (= Q225), G251 (= G264)

3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
36% identity, 84% coverage: 43:302/310 of query aligns to 39:289/291 of 3d6nB

query
sites
3d6nB

L

L

L

F

F

F

L

S

E

E

P

P

S

S

T

T

R
|
R

T
|
T

A

R

L

L

S

S

F

F

E

E

A

K

A

A

I

A

D

R

R

E

L

L

G

G

G

I

R

E

T

T

V

Y

R

L

I

V

D

S

P

G

E

S

S

E

S

S

L

T

V

V

K
|
K

D

G

E

E

S

S

L

F

R

F

D

D

T

T

L

L

R

K

V

T

L

F

A

E

A

G

Q

L

G

G

T

F

S

D

-

Y

G

V

V

V

V

F

V
x
R

R

V

A

P

P

F

W

V

V

F

G

F

T

P

A

Y

D

K

V

E

V

I

A

V

R

K

F

S

F

L

D

N

G

L

I

R

V

L

V

V

N

N

A

A

G

G

D

D

G

G

V

T

G

H

Q

Q

H
|
H

P

P

T

S

Q
|
Q

A

G

L

L

Q

I

D

D

V

F

C

F

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

K

D

E

A

H

F

F

G

G

A

E

L

V

E

K

G

D

C

L

R

R

V

V

A

L

I

Y

V

V

G

G

D

D

L

I

R

K

H

H

S

S

R
|
R

V
|
V

A

F

R

R

S

S

V

G

G

A

R

P

L

L

A

N

S

M

V

F

G

G

A

A

E

K

V

I

V

G

G

V

V

C

A

G

P

P

R

K

E

-

W

-

S

T

L

L

D

I

P

P

K

R

-

D

-

V

A

E

L

V

G

F

A

K

V

V

G

D

V

V

T

F

D

D

G

D

I

V

D

D

D

K

V

G

L

I

D

D

E

W

V

A

D

D

V

V

F

V

Y

I

M

W

L

L

R
|
R

I

L

Q

Q

H

K

E

E

R

R

V

Q

G

K

A

E

N

N

E

Y

R

I

V

P

D

S

L

E

S

S

G

S

Y

Y

R

F

A

K

R

Q

F

F

Q

G

L

L

S

T

G

K

H

E

R

R

L

F

E

E

R

K

A

V

R

K

P

-

D

-

A

-

V

L

V

Y

L

M

H

H

P

P

G
|
G

P

P

V

V

N

N

R

R

G

N

V

V

E

D

L

I

D

D

D

H

I

E

V

L

L

V

S

Y

S

T

P

E

R

K

M

S

L

L

D

I

G

Q

L

E

Q

Q

Y

V

A

K

Y

N

G

G

V

I

P

P

T

V

R

R

V

K

A

A

V

I

L

Y

E

K

A

F

L

L

active site: R47 (= R51), T48 (= T52), K75 (= K79), R97 (≠ V100), H126 (= H129), Q129 (= Q132)
binding citrate anion: T48 (= T52), R97 (≠ V100), H126 (= H129), R159 (= R169), V160 (= V170), R213 (= R223), G251 (= G264)

5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
36% identity, 85% coverage: 36:299/310 of query aligns to 39:285/292 of 5g1pA

query
sites
5g1pA

L

L

E

K

G

G

R

K

R

V

V

M

A

A

L

S

L

M

F

F

L

Y

E

E

P

V

S
|
S

T
|
T

R
|
R

T
|
T

A

S

L

S

S

S

F

F

E

A

A

A

I

M

D

A

R

R

L

L

G

G

R

A

T

V

V

L

R

S

I

F

D

S

P

E

E

A

S

T

S

S

L

V

V

Q

K
|
K

D

G

E

E

S

S

L

L

R

A

D

D

T

S

L

V

R

Q

V

T

L

M

A

S

A

C

Q

Y

G

A

T

-

S

D

G

V

V

V

V

L

R
|
R

A

H

P

P

W

Q

V

P

G

G

T

A

A

V

D

E

V

L

V

A

A

A

R

K

F

H

F

C

D

R

G

R

I

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

V

V

G

G

Q

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

L

Q

L

D

D

V

I

C

F

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

R

D

E

A

E

F

L

G

G

A

T

L

V

E

N

G

G

C

M

R

T

V

I

A

T

I

M

V

V

G

G

D

D

L

L

R

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

V

L

G

A

R

C

L

L

A

T

S

Q

V

Y

G

R

A

V

E

S

V

L

V

R

G

Y

V

V

A

A

P

P

R

P

E

S

W

L

S

R

L

M

D

P

P

P

-

T

-

V

K

R

A

A

L

F

G

V

A

A

V

S

G

G

V

T

T

K

-

Q

-

E

-

F

D

E

G

S

I

I

D

E

V

A

L

L

D

P

E

D

V

T

D

D

V

V

F

L

Y

Y

M

M

L
x
T

R

R

I

I

Q

Q

H

K

E

E

R

R

V

F

G

-

A

-

N

-

E

-

R

-

V

-

D

-

L

-

S

-

G

-

Y

-

R

-

A

-

R

Q

F

F

Q

I

L

L

S

T

G

P

H

H

R

I

L

M

E

T

R

R

A

A

R

K

P

K

D

K

A

M

V

V

L

M

H

H

P
|
P

G
x
M

P

P

-

R

V

V

N

N

R

E

-

I

G

S

V

V

E

E

L

V

D

D

D

-

I

-

V

-

L

-

S

S

S

D

P

P

R

R

M

A

L

A

D

Y

G

F

L

R

Q

Q

Y

A

A

E

Y

N

G
|
G

V

M

P

Y

T

I

R

R

V

M

A

A

V

L

L

L

active site: R54 (= R51), T55 (= T52), K82 (= K79), R103 (= R101), H131 (= H129), Q134 (= Q132), T223 (≠ L222), P251 (= P263), G277 (= G291)
binding phosphoric acid mono(formamide)ester: S52 (= S49), T53 (= T50), R54 (= R51), T55 (= T52), R103 (= R101), Q134 (= Q132), M252 (≠ G264)

7zstB Crystal structure of truncated aspartate transcarbamoylase from plasmodium falciparum in complex with fla-01 (see paper)
30% identity, 93% coverage: 12:299/310 of query aligns to 23:319/329 of 7zstB

query
sites
7zstB

D

D

A

E

G

E

R

L

L

L

G

A

V

I

L

L

-

Y

-

T

G

S

A

K

R

Q

V

F

D

E

E

K

L

I

V

L

H

K

G

N

A

N

A

E

A

D

S

S

R

K

C

Y

L

L

E

E

G

N

R

K

R

V

V

F

A

C

L

S

L

V

F

F

L

L

E

E

P

P

S
|
S

T

T

R
|
R

T
|
T

A

R

L

C

S

S

F

F

E

D

A

A

I

I

D

L

R

K

L

L

G

G

G

S

R

K

T

V

V

L

R

N

I

I

-

T

D

D

P

M

E

N

S

S

S

T

S

S

L

F

V

Y

K

K

D

G

E

E

S

T

L

V

R

E

D

D

T

A

L

F

R

K

V

I

L

L

A

S

A

T

Q

Y

G

-

T

V

S

D

G

G

V

I

V

Y

R
|
R

A

D

P

P

W

S

V

K

G

K

T

N

A

V

D

D

V

I

V

A

A

V

R

S

F

S

D

S

G

K

I

P

V

I

N

N

A

A

G

G

D

N

G

G

V

T

G

G

Q

E

H

H

P

P

T

T

Q

Q

A

S

L

L

Q

L

D

D

V

F

C

Y

V

T

L

I

A

H

R

N

T

Y

R

F

G

P

G

F

R

I

A

L

D

D

A

R

F

-

G

N

A

I

L

N

E

K

G

K

C

L

R

N

V

I

A

A

I

F

V

V

G

G

D

D

L

L

R

K

H

N

S

G

R

R

V

T

A

V

R

H

S

S

V

L

G

S

R

K

L

L

A

S

S

R

V

Y

G

N

A

V

E

S

V

F

V

N

G

F

V

V

A

S

P

C

R

K

E

S

W

L

S

N

L

I

D

-

P

P

K

K

A

D

L

I

-

V

-

N

-

T

-

I

-

T

-

Y

-

N

-

L

-

K

-

N

-

F

-

Y

-

S

-

D

G

D

A

S

V

I

G

K

V

Y

T

F

D

D

G

N

I

L

D

E

V

G

L

L

D

E

E

D

V

V

D

H

V

I

F

I

Y

Y

M

M

L

T

R
|
R

I

I

Q

Q

H

K

E

E

R

R

V

F

G

-

A

-

N

-

E

-

R

-

V

T

D

D

L

V

S

D

G

E

Y

Y

R

N

A

N

R

A

F

F

Q

I

L

L

S

S

G

N

H

K

R

T

L

L

E

E

R

N

A

T

R

R

P

D

D

D

A

T

V

K

V

I

L

L

H

H

P

P

G

L

P

P

-

R

V

V

N

N

R

E

-

I

G

K

V

V

E

E

L

V

D

D

D

-

I

-

V

-

L

-

S

S

S

N

P

P

R

K

M

S

L

V

D

Y

G

F

L

T

Q

Q

Y

A

A

E

Y

N

G

G

V

L

P

Y

T

V

R

R

V

M

A

A

V

L

L

L

binding 2-azanyl-~{N}-(2-methoxyethyl)-5-phenyl-thiophene-3-carboxamide: S62 (= S49), R64 (= R51), T65 (= T52), R114 (= R101), R250 (= R223)

4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
35% identity, 96% coverage: 8:305/310 of query aligns to 16:302/304 of 4eknB

query
sites
4eknB

V

L

E

E

Q

I

L

L

D

D

A

E

G

A

R

R

L

-

G

-

V

-

L

-

G

-

A

-

R

K

V

M

D

E

E

E

L

L

V

L

H

N

G

T

A

K

A

R

A

P

S

L

R

K

C

L

L

L

E

E

G

G

R

K

R

I

V

L

A

A

L

T

L

V

F

F

L

Y

E

E

P

P

S

S

T

T

R

R

T

T

A

R

L

L

S

S

F

F

E

E

A

T

A

A

I

M

D

K

R

R

L

L

G

G

R

E

T

V

V

I

R

T

I

M

-

T

D

D

P

L

E

K

S

S

L

V

V

A

K

K

D

G

E

E

S

S

L

L

R

I

D

D

T

T

L

I

R

R

V

V

L

I

A

S

A

G

Q

Y

G

A

T

-

S

D

G

I

V

I

V

V

V

L

R

R

A

H

P

P

W

S

V

E

G

G

T

A

A

A

D

R

V

L

V

A

A

S

R

E

F

Y

F

S

D

Q

G

V

I

P

V

I

N

N

A

A

G

G

D

D

G

G

V

S

G

N

Q

Q

H

H

P

P

T

T

Q

Q

A

T

L

L

Q

L

D

D

V

L

C

Y

V

T

L

I

A

M

R

R

T

-

R

-

G

-

R

-

A

-

D

-

A

E

F

I

G

G

A

R

L

I

E

D

G

G

C

I

R

K

V

I

A

A

I

F

V

V

G

G

D

D

L

L

R

K

H

Y

S
x
G

R
|
R

V
x
T

A

V

R

H

S

S

V

L

G

V

R

Y

L

A

L

L

A

S

S

L

V

F

-

E

G

N

A

V

E

E

V

M

V

Y

G

F

V

V

A

S

P

P

R

K

E

E

W

L

S

R

L

L

D

-

P

P

K

K

-

D

-

I

-

E

A

D

L

L

G

K

A

A

V

K

G

N

V

I

-

K

-

F

-

Y

-

E

T

K

D

E

G

S

I

L

D

D

V

L

L

D

D

D

E

D

V

I

D

D

V

V

F

L

Y

Y

M

V

L
x
T

R
|
R

I

I

Q

Q

H

K

E

E

R

R

V

F

-

P

-

D

-

P

G

N

A

E

N

Y

E

E

R

K

V

V

D

K

L

G

S

S

G

Y

Y

K

R

I

A

K

R

R

F

E

Q

Y

L

V

S

E

G

G

H

K

R

K

L

F

E

-

R

-

A

-

R

-

P

-

D

-

A

-

V

I

L

M

H

H

P
|
P

G

L

P

P

V

-

N

-

R

R

G

V

V

D

E

E

L

I

D

D

D

Y

I

D

V

V

L

D

S

D

S

L

P

P

R

Q

M

A

L

K

D

Y

G

F

L

K

Q

Q

Y

S

A

F

Y

Y

G
|
G

V

I

P

P

T

V

R

R

V

M

A

A

V

I

L

L

E

K

A

K

L

L

A

I

E

E

E

D

active site: T225 (≠ L222), P262 (= P263), G288 (= G291)
binding sulfate ion: G163 (≠ S168), R164 (= R169), T165 (≠ V170), R226 (= R223)

7zidB Crystal structure of truncated aspartate transcarbamoylase from plasmodium falciparum in complex with bda-14 (see paper)
29% identity, 93% coverage: 12:299/310 of query aligns to 22:321/331 of 7zidB

query
sites
7zidB

D

D

A

E

G

E

R

L

L

L

G

A

V

I

L

L

-

Y

-

T

G

S

A

K

R

Q

V

F

D

E

E

K

L

I

V

L

H

K

G

N

A

N

A

E

A

D

S

S

R

K

C

Y

L

L

E

E

G

N

R

K

R

V

V

F

A

C

L

S

L

V

F

F

L

L

E

E

P

P

S
|
S

T
|
T

R
|
R

T
|
T

A

R

L

C

S

S

F

F

E

D

A

A

I

I

D

L

R

K

L

L

G

G

G

S

R

K

T

V

V

L

R

N

I

I

-

T

D

D

P

M

E

N

S

S

S

T

S

S

L

F

V

Y

K

K

D

G

E

E

S

T

L

V

R

E

D

D

T

A

L

F

R

K

V

I

L

L

A

S

A

T

Q

Y

G

-

T

V

S

D

G

G

V

I

V

Y

R

R

A

D

P

P

W

S

V

K

G

K

T

N

A

V

D

D

V

I

V

A

A

V

R

S

F

S

D

S

G

K

I

P

V

I

N

N

A

A

G

G

D

N

G

G

V

T

G

G

Q

E

H

H

P

P

T

T

Q
|
Q

A

S

L

L

Q

L

D

D

V

F

C

Y

V

T

L

I

A

H

R

N

T

Y

R

F

G

P

G

F

R

I

A

L

D

D

A

R

F

-

G

N

A

I

L

N

E

K

G

K

C

L

R

N

V

I

A

A

I

F

V

V

G

G

D

D

L

L

R

K

H

N

S

G

R

R

V

T

A

V

R

H

S

S

V

L

G

S

R

K

L

L

A

S

S

R

V

Y

G

N

A

V

E

S

V

F

V

N

G

F

V

V

A

S

P

C

R

K

E

S

W

L

S

N

L

I

D

-

P

P

K

K

A

D

L

I

-

V

-

N

-

T

-

I

-

T

-

Y

-

N

-

L

-

K

-

N

-

F

-

Y

-

S

-

D

G

D

A

S

V

I

G

K

V

Y

T

F

D

D

G

N

I

L

D

E

V

G

L

L

D

E

E

D

V

V

D

H

V

I

F

I

Y

Y

M

M

L

T

R
|
R

I

I

Q
|
Q

H

K

E
|
E

R

R

V

F

G

T

A

D

N

V

E

D

R

-

V

-

D

E

L

Y

S

N

G

Q

Y

Y

R

K

A

N

R

A

F

F

Q

I

L

L

S

S

G

N

H

K

R

T

L

L

E

E

R

N

A

T

R

R

P

D

D

D

A

T

V

K

V

I

L

L

H

H

P

P

G

L

P

P

-

R

V

V

N

N

R

E

-

I

G

K

V

V

E

E

L

V

D

D

D

-

I

-

V

-

L

-

S

S

S

N

P

P

R

K

M

S

L

V

D

Y

G

F

L

T

Q

Q

Y

A

A

E

Y

N

G

G

V

L

P

Y

T

V

R

R

V

M

A

A

V

L

L

L

binding tert-butyl N-[3-(2-hydroxyethylcarbamoyl)-5-phenyl-thiophen-2-yl]carbamate: S61 (= S49), T62 (= T50), R63 (= R51), T64 (= T52), Q144 (= Q132), R249 (= R223), Q251 (= Q225), E253 (= E227)

1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
34% identity, 85% coverage: 37:299/310 of query aligns to 42:300/307 of 1ml4A

query
sites
1ml4A

E

K

G

G

R

K

R

I

V

L

A

A

L

T

L

L

F

F

L

F

E

E

P

P

S
|
S

T
|
T

R
|
R

T
|
T

A

R

L

L

S

S

F

F

E

E

A

S

A

A

I

M

D

H

R

R

L

L

G

G

R

A

T

V

V

I

R

G

I

F

-

A

D

E

P

A

E

S

S

T

S

S

L

V

V

K

K
|
K

D

G

E

E

S

S

L

L

R

R

D

D

T

T

L

I

R

K

V

T

L

V

A

-

A

E

Q

Q

G

Y

T

C

S

D

G

V

V

I

V

V

V

I

R
|
R

A

H

P

P

W

K

V

E

G

G

T

A

A

A

D

R

V

L

V

A

A

A

R

E

F

V

F

A

D

E

G

V

I

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

V

S

G

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

A

T

L

L

Q

L

D

D

V

L

C

Y

V

T

L

I

A

K

R

K

T

-

R

-

G

-

R

-

A

-

D

-

A

E

F

F

G

G

A

R

L

I

E

D

G

G

C

L

R

K

V

I

A

G

I

L

V

L

G

G

D

D

L

L

R

K

H

Y

S

G

R
|
R

V
x
T

A

V

R

H

S

S

V

L

G

A

R

E

L

A

L

L

A

T

S

F

V

Y

G

D

A

V

E

E

V

L

V

Y

G

L

V

I

A

S

P

P

R

E

E

L

W

L

-

R

-

M

-

P

-

R

-

H

-

I

-

V

-

E

S

E

L

L

D

R

P

E

K

K

A

G

L

M

G

K

A

V

V

V

G

E

V

T

T

T

D

-

G

T

I

L

D

E

D

D

V

V

L

I

D

G

E

K

V

L

D

D

V

V

F

L

Y

Y

M

V

L
x
T

R
|
R

I

I

Q

Q

H

K

E

E

R

R

V

F

-

P

G

D

A

E

N

Q

E

E

R

Y

V

L

D

K

L

V

S

K

G

G

Y

-

R

-

A

-

R

S

F

Y

Q

Q

L

V

S

N

G

L

H

K

R

V

L

L

E

E

R

K

A

A

R

K

P

D

D

E

A

L

V

R

V

I

L

M

H

H

P
|
P

G
x
L

P

P

V

-

N

-

R

R

G

V

V

D

E

E

L

I

D

H

D

P

I

E

V

V

L

D

S

N

S

T

P

K

R

H

M

A

L

I

D

Y

G

F

L

R

Q

Q

Y

V

A

F

Y

N

G
|
G

V

V

P

P

T

V

R

R

V

M

A

A

V

L

L

L

active site: R56 (= R51), T57 (= T52), K85 (= K79), R106 (= R101), H134 (= H129), Q137 (= Q132), T227 (≠ L222), P266 (= P263), G292 (= G291)
binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S49), T55 (= T50), R56 (= R51), T57 (= T52), R106 (= R101), H134 (= H129), R167 (= R169), T168 (≠ V170), R228 (= R223), L267 (≠ G264)

Q09794 Multifunctional protein ura1; 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 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 85% coverage: 38:299/310 of query aligns to 1975:2233/2244 of Q09794

query
sites
Q09794

G

G

R

K

R

L

V

L

A

C

L

T

L

M

F

F

L

F

E

E

P

P

S

S

T

T

R

R

T

T

A

S

L

S

S

S

F

F

E

D

A

A

I

M

D

Q

R

R

L

L

G

G

R

K

T

V

V

V

R

A

I

V

D

T

P

A

E

S

S

A

S

S

L

V

V

N

K

K

D

G

E

E

S

S

L

L

R

A

D

D

T

T

L

I

R

R

V

T

L

L

A

G

A

C

Q

Y

G

G

T

D

S

A

G

-

V

I

V

V

V

L

R

R

A

H

P

P

W

S

V

I

G

E

T

S

A

A

D

R

V

I

V

A

A

A

R

N

F

F

F

S

D

P

G

V

I

P

V

I

N

N

A

G

G

G

D

N

G

G

V

S

G

K

Q

E

H

H

P

P

T

T

Q

Q

A

A

L

F

Q

L

D

D

V

L

C

Y

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

R

D

E

A

E

F

L

G

G

A

S

L

V

E

N

G

G

C

L

R

T

V

I

A

T

I

F

V

I

G

G

D

D

L

L

R

K

H

Y

S

G

R

R

V

T

A

V

R

H

S

S

V

L

G

A

R

R

L

L

A

A

S

F

V

W

G

H

A

V

E

E

V

L

V

H

G

L

V

V

A

S

P

P

R

E

E

Q

W

L

S

A

L

L

-

P

-

D

-

V

-

K

-

D

D

D

P

I

K

R

A

A

-

N

-

G

L

L

G

N

A

F

V

I

G

E

V

H

T

R

D

E

G

L

I

T

D

K

D

E

V

V

L

V

D

A

E

Q

V

S

D

D

V

V

F

L

Y

Y

M

C

L

T

R

R

I

V

Q

Q

H

K

E

E

R

R

V

F

G

A

A

S

N

V

E

D

R

-

V

-

D

E

L

Y

S

E

G

K

Y

L

R

K

A

D

R

S

F

F

Q

I

L

V

S

D

G

N

H

S

R

V

L

L

E

A

R

S

A

A

R

K

P

S

D

H

A

C

V

I

V

V

L

M

H

H

P

P

G

L

P

P

V

R

N

N

R

R

G

E

V

I

E

S

L

-

D

E

I

V

V

D

L

F

S

D

S

Q

P

R

R

R

M

A

L

A

D

Y

G

F

L

R

Q

Q

Y

M

A

R

Y

Y

G

G

V

L

P

Y

T

I

R

R

V

M

A

A

V

L

L

L

Sites not aligning to the query:

1119 modified: Phosphoserine
1881 modified: Phosphoserine
1885 modified: Phosphoserine

8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
33% identity, 85% coverage: 36:299/310 of query aligns to 52:311/316 of 8bplA

query
sites
8bplA

L

L

E

R

G

G

R

K

R

V

V

L

A

C

L

T

L

L

F

F

L

Y

E

E

P

P

S
|
S

T
|
T

R
|
R

T
|
T

A

S

L

A

S

S

F

F

E

D

A

A

I

M

D

Q

R

R

L

L

G

G

R

R

T

T

V

I

R

P

I

I

D

Q

P

T

E

S

S

T

S

S

L

V

V

Q

K

K

D

G

E

E

S

T

L

L

R

Q

D

D

T

T

L

L

R

R

V

T

L

L

A

A

A

C

Q

Y

G

-

T

S

S

D

G

A

V

I

V

V

V

L

R
|
R

A

H

P

P

W

D

V

E

G

K

T

C

A

V

D

D

V

V

V

A

A

K

R

K

F

Y

F

C

D

P

G

V

I

P

V

V

V

I

N

N

A

G

G

G

D

N

G

G

V

S

G

K

Q

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

F

Q

L

D

D

V

L

C

F

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

R

D

E

A

E

F

L

G

G

A

T

L

M

E

Q

G

G

C

L

R

T

V

I

A

T

I

F

V

V

G

G

D

D

L

L

R

L

H

Y

S

G

R

R

V

P

A

V

R

H

S

S

V

L

G

V

R

Y

L

L

A

R

S

H

V

Y

G

Q

A

V

E

K

V

V

V

Q

G

L

V

V

A

S

P

P

R

K

E

A

W

L

S

R

L

L

D

-

P

P

K

P

A

A

L

V

G

R

A

Q

V

Q

G

L

V

V

T

D

D

A

G

G

-

Q

-

L

-

C

-

E

-

S

-

E

-

A

-

L

I

T

D

P

D

E

V

I

L

L

D

G

E

R

V

T

D

D

V

V

F

L

Y

Y

M

C

L

T

R

R

I

V

Q

Q

H

K

E

E

R

R

V

F

G

P

A

S

N

-

E

-

R

L

V

A

D

E

L

F

S

E

G

A

Y

V

R

K

A

D

R

S

F

Y

Q

R

L

I

S

D

G

Y

H

S

R

T

L

L

E

K

R

Y

A

A

R

K

P

P

D

T

A

T

V

V

L

M

H

H

P

P

G
x
L

P

P

V

R

N

N

R

E

G

-

V

-

E

E

L

V

D

A

D

E

I

E

V

V

L

D

S

F

S

D

P

Q

R

R

M

A

L

A

D

Y

G

F

L

R

Q

Q

Y

M

A

C

Y

Y

G

G

V

L

P

Y

T

C

R

R

V

M

A

A

V

L

L

L

binding phosphoric acid mono(formamide)ester: S65 (= S49), T66 (= T50), R67 (= R51), T68 (= T52), R116 (= R101), H144 (= H129), Q147 (= Q132), L278 (≠ G264)

6ys6B Arabidopsis aspartate transcarbamoylase complex with pala (see paper)
36% identity, 92% coverage: 23:308/310 of query aligns to 30:312/312 of 6ys6B

query
sites
6ys6B

V

M

D

E

E

K

L

I

V

E

H

K

G

S

A

S

A

Q

S

S

R

E

C

I

L

L

E

K

G

G

R

Y

R

L

V

M

A

A

L

T

L

L

F

F

L

Y

E

E

P

P

S

S

T

T

R

R

T

T

A

R

L

L

S

S

F

F

E

E

A

S

A

A

I

M

D

K

R

R

L

L

G

G

R

E

T

V

V

L

R

T

I

T

D

E

P

N

-

A

-

R

E

E

S

F

S

S

S
|
S

L

A

V

A

K
|
K

D

G

E

E

S

T

L

L

R

E

D

D

T

T

L

I

R

R

V

T

L

V

A

-

Q

E

G

G

T

Y

S

S

G

D

V

I

V

V

-

M

R
|
R

A

H

P

F

W

E

V

S

G

G

T

A

A

A

D

R

V

K

V

A

A

A

R

A

F

T

F

A

D

N

G

I

I

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

V

P

G

G

Q

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

L

Q

L

D

D

V

V

C

Y

V

T

L

I

A

-

R

-

T

-

R

-

G

-

R

-

A

Q

D

S

A

E

F

I

G

G

A

K

L

L

E

D

G

G

C

I

R

S

V

V

A

A

I

L

V

V

G

G

D

D

L

L

R

A

H

N

S

G

R

R

V

T

A

V

R

R

S

S

V

L

G

A

R

Y

L

L

A

A

S

K

V

F

G

K

-

D

A

V

E

K

V

I

V

Y

G

F

V

V

A

S

P

P

R

E

E

I

W

V

S

K

L

M

D

K

-

D

-

I

P

K

K

D

A

Y

L

L

G

T

A

S

V

S

G

G

V

V

-

E

-

W

-

E

T

S

D

S

G

D

I

L

D

M

D

E

V

V

L

A

D

S

E

K

V

C

D

D

V

V

F

V

Y

Y

M

Q

L
x
T

R

R

I

I

Q

Q

H

R

E

E

R

R

V

F

G

G

A

-

N

-

E

E

R

R

V

L

D

D

L

L

-

Y

S

E

G

A

Y

A

R

R

A

G

R

K

F

F

Q

I

L

V

S

D

G

K

H

D

R

L

L

L

E

G

R

V

A

M

R

Q

P

K

D

K

A

A

V

I

L

M

H

H

P
|
P

G

L

P

P

V

-

N

-

R

-

G

-

V

-

E

R

L

L

D

D

D

E

I

I

-

T

-

A

-

D

V

V

L

D

S

A

S

D

P

P

R

R

M

A

L

A

D

Y

G

F

L

R

Q

Q

Y

A

A

K

Y

N

G
|
G

V

L

P

F

T

I

R

R

V

M

A

A

V

L

L

L

E

K

A

L

L

L

A

L

E

-

A

V

G

G

W

W

active site: R109 (= R101), H137 (= H129), Q140 (= Q132), T231 (≠ L222), P271 (= P263), G297 (= G291)
binding n-(phosphonacetyl)-l-aspartic acid: S85 (= S76), K88 (= K79)

Query Sequence

>WP_015799097.1 NCBI__GCF_000023265.1:WP_015799097.1
MSATFLGVEQLDAGRLGVLGARVDELVHGAAASRCLEGRRVALLFLEPSTRTALSFEAAI
DRLGGRTVRIDPESSSLVKDESLRDTLRVLAAQGTSGVVVRAPWVGTADVVARFFDGIVV
NAGDGVGQHPTQALQDVCVLARTRGGRADAFGALEGCRVAIVGDLRHSRVARSVGRLLAS
VGAEVVGVAPREWSLDPKALGAVGVTDGIDDVLDEVDVFYMLRIQHERVGANERVDLSGY
RARFQLSGHRLERARPDAVVLHPGPVNRGVELDDIVLSSPRMLDGLQYAYGVPTRVAVLE
ALAEEAGWGL

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