SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012674077.1 NCBI__GCF_000021545.1:WP_012674077.1 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.
44% identity, 100% coverage: 1:300/301 of query aligns to 1:292/293 of 6pnzA

query
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6pnzA

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binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S52), T49 (= T53), R50 (= R54), T51 (= T55), S75 (= S79), K78 (= K82), R100 (= R104), H127 (= H132), R160 (= R165), R210 (= R220), Q212 (= Q222), A253 (≠ G261)

3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
45% identity, 100% coverage: 1:300/301 of query aligns to 1:289/291 of 3r7fA

query
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active site: R49 (= R54), T50 (= T55), K77 (= K82), R99 (= R104), H127 (= H132), Q130 (= Q135), L210 (= L219), P249 (= P260), G277 (= G288)
binding phosphoric acid mono(formamide)ester: S47 (= S52), T48 (= T53), R49 (= R54), T50 (= T55), R99 (= R104), H127 (= H132), Q130 (= Q135), P249 (= P260), A250 (≠ G261)
binding phosphate ion: S11 (≠ E11), T12 (≠ K12), Q23 (≠ K23), K26 (= K31), E140 (= E145), R171 (≠ K176), K241 (= K252), H243 (≠ D254), K272 (≠ N283), K272 (≠ N283), K275 (≠ E286)

3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
45% identity, 100% coverage: 1:300/301 of query aligns to 1:289/291 of 3r7dA

query
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3r7dA

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active site: R49 (= R54), T50 (= T55), K77 (= K82), R99 (= R104), H127 (= H132), Q130 (= Q135), L210 (= L219), P249 (= P260), G277 (= G288)
binding phosphate ion: S11 (≠ E11), T12 (≠ K12), T73 (≠ S78), S74 (= S79), K77 (= K82), R171 (≠ K176)

3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
45% identity, 100% coverage: 1:300/301 of query aligns to 1:289/290 of 3r7lA

query
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3r7lA

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L

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active site: R49 (= R54), T50 (= T55), K77 (= K82), R99 (= R104), H127 (= H132), Q130 (= Q135), L210 (= L219), P249 (= P260), G277 (= G288)
binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S52), T48 (= T53), R49 (= R54), T50 (= T55), S74 (= S79), K77 (= K82), R99 (= R104), H127 (= H132), R160 (= R165), R211 (= R220), Q213 (= Q222), A250 (≠ G261)

P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
45% identity, 100% coverage: 1:300/301 of query aligns to 1:289/304 of P05654

query
sites
P05654

M

M

K

K

D

H

L

L

Y

T

S

T

V

M

N

S

Q

E

L

L

E

S

K

T

E

E

D

E

I

I

Q

K

K

D

I

L

F

L

Q

Q

L

T

A

A

K

Q

E

E

Y

-

K

-

E

-

R

-

F

-

L

L

K

K

G

S

E

G

K

K

K

T

F

D

N

N

D

Q

L

L

R

T

R

G

C

K

S

F

I

A

L

A

L

N

V

L

F

F

E

E

N

P

S

S

T

T

R

R

T

T

R

R

T

F

S

S

F

F

E

E

L

V

A

A

G

E

K

K

I

K

L

L

G

G

A

M

D

N

T

V

I

L

N

N

I

L

S

D

A

G

S

T

S

S

S

T

S

S

V

V

K

Q

K

K

G

G

E

E

T

T

L

L

Y

Y

D

D

T

T

V

I

K

R

T

T

L

L

E

E

A

S

L

I

N

G

S

V

D

D

F

V

I

C

V

V

I

I

R

R

H

H

N

S

M

E

S

D

G

E

A

Y

K

E

I

E

V

L

A

V

N

S

S

Q

V

V

K

N

S

I

H

P

V

I

V

L

N

N

A

A

G

G

D

D

G

G

T

C

N

G

E

Q

H

H

P

P

T

T

Q

Q

A

S

L

L

D

D

G

L

F

M

T

T

I

I

L

Y

E

E

K

E

K

F

G

N

S

T

L

F

E

K

G

G

L

L

K

T

I

V

A

S

I

I

V

H

G

G

D

D

I

I

L

K

H

H

S

S

R

R

V

V

A

A

R

R

S

S

D

N

I

A

K

E

L

V

F

L

K

T

K

R

L

L

G

G

A

A

E

R

V

V

T

L

L

F

C

S

G

G

P

P

M

S

T

E

M

W

L

-

P

-

R

Q

H

D

Y

E

E

E

A

N

L

T

G

F

A

G

D

T

Y

Y

I

V

T

S

T

M

D

D

I

-

K

-

E

E

A

A

V

V

K

E

N

S

K

S

D

D

V

V

I

M

F

L

L

L

R

R

I

I

Q

Q

L

N

E

E

R

R

Q

H

D

Q

K

S

P

A

F

V

F

-

S

-

T

S

L

Q

R

E

E

G

Y

Y

S

L

I

N

K

K

Y

Y

G

G

L

L

N

T

Q

V

E

E

L

R

L

A

K

E

I

R

L

M

K

K

P

R

D

H

T

A

V

I

I

I

M

M

H

H

P

P

G

A

P

P

V

V

N

N

R

R

G

G

V

V

E

E

I

I

Q

D

S

D

E

S

L

L

V

V

Y

E

S

S

S

E

K

K

S

S

L

R

I

I

L

F

N

K

Q

Q

V

M

E

K

N

N

G

G

L

V

F

F

I

I

R

R

M

M

A

A

V

V

Y

I

K

Q

Y

R

L

A

L

L

Sites not aligning to the query:

303 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)
42% identity, 100% coverage: 1:301/301 of query aligns to 1:291/291 of 4bjhB

query
sites
4bjhB

M

M

K

R

D

S

L

L

Y

I

S

S

V

S

N

L

Q

D

L

L

E

T

K

R

E

E

D

E

I

V

Q

E

K

E

I

I

F

L

Q

K

L

Y

A

A

K

K

E

E

Y

F

K

K

E

E

R

-

F

-

L

-

K

-

G

G

E

K

K

E

K

-

F

-

N

-

D

E

L

T

R

I

R

K

C

A

S

S

I

A

L

V

L

L

V

F

F

F

F

S

E

E

N

P

S
|
S

T
|
T

R
|
R

T
|
T

R

R

T

L

S

S

F

F

E

E

L

K

A

A

G

A

K

R

I

E

L

L

G

G

A

I

D

E

T

T

I

Y

N

L

I

V

S

S

A

G

S

S

S

E

S

S

V

T

K

V

K
|
K

G

G

E

E

T

S

L

F

Y

F

D

D

T

T

V

L

K

K

T

T

L

F

E

E

A

G

L

L

N

G

S

F

D

D

F

Y

I

V

V

V

I

F

R
|
R

H

V

N

P

M

F

S

V

G

F

A

F

A

P

-

Y

K

K

I

E

V

I

A

V

N

K

S

S

V

L

K

N

S

L

H

R

V

L

V

V

N

N

A

A

G

G

D

D

G

G

T

T

N

H

E

Q

H
|
H

P

P

T

S

Q
|
Q

A

G

L

L

L

I

D

D

G

F

F

F

T

T

I

I

L

K

E

E

K

H

K

F

G

G

S

E

L

V

E

K

G

D

L

L

K

R

I

V

A

L

I

Y

V

V

G

G

D

D

I

I

L

K

H

H

S

S

R
|
R

V
|
V

A

F

R

R

S

S

D

G

I

A

K

P

L

L

F

L

K

N

K

M

L

F

G

G

A

A

E

K

V

I

T

G

L

V

C

C

G

G

P

P

M

K

T

T

M

L

L

I

P

P

R

R

H

D

Y

V

E

E

A

V

L

F

G

K

A

V

D

D

Y

-

I

V

T

F

T

D

D

D

I

V

K

D

E

K

A

G

V

I

K

D

N

W

K

A

D

D

V

V

I

I

F

W

L

L

R
|
R

I

L

Q
|
Q

L

K

E

E

R

R

Q

Q

D

K

K

E

P

N

F

Y

F

I

S

P

T

S

L

E

R

S

E

S

Y

Y

S

F

I

K

K

Q

Y

F

G

G

L

L

N

T

Q

K

E

E

L

R

L

F

K

E

I

K

L

V

K

K

P

-

D

-

T

-

V

L

I

Y

M

M

H

H

P

P

G
|
G

P

P

V

V

N

N

R

R

G

N

V

V

E

D

I

I

Q

D

S

H

E

E

L

L

V

V

Y

Y

S

T

S

E

K

K

S

S

L

L

I

I

L

Q

N

E

Q

Q

V

V

E

K

N

N

G

G

L

I

F

P

I

V

R

R

M

K

A

A

V

I

Y

Y

K

K

Y

F

L

L

L

W

S

T

active site: R47 (= R54), T48 (= T55), K75 (= K82), R97 (= R104), H126 (= H132), Q129 (= Q135)
binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S52), T46 (= T53), R47 (= R54), T48 (= T55), R97 (= R104), H126 (= H132), R159 (= R165), V160 (= V166), R213 (= R220), Q215 (= Q222), G251 (= G261)

3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
42% identity, 100% coverage: 1:301/301 of query aligns to 1:291/291 of 3d6nB

query
sites
3d6nB

M

M

K

R

D

S

L

L

Y

I

S

S

V

S

N

L

Q

D

L

L

E

T

K

R

E

E

D

E

I

V

Q

E

K

E

I

I

F

L

Q

K

L

Y

A

A

K

K

E

E

Y

F

K

K

E

E

R

-

F

-

L

-

K

-

G

G

E

K

K

E

K

-

F

-

N

-

D

E

L

T

R

I

R

K

C

A

S

S

I

A

L

V

L

L

V

F

F

F

F

S

E

E

N

P

S

S

T

T

R
|
R

T
|
T

R

R

T

L

S

S

F

F

E

E

L

K

A

A

G

A

K

R

I

E

L

L

G

G

A

I

D

E

T

T

I

Y

N

L

I

V

S

S

A

G

S

S

S

E

S

S

V

T

K

V

K
|
K

G

G

E

E

T

S

L

F

Y

F

D

D

T

T

V

L

K

K

T

T

L

F

E

E

A

G

L

L

N

G

S

F

D

D

F

Y

I

V

V

V

I

F

R
|
R

H

V

N

P

M

F

S

V

G

F

A

F

A

P

-

Y

K

K

I

E

V

I

A

V

N

K

S

S

V

L

K

N

S

L

H

R

V

L

V

V

N

N

A

A

G

G

D

D

G

G

T

T

N

H

E

Q

H
|
H

P

P

T

S

Q
|
Q

A

G

L

L

L

I

D

D

G

F

F

F

T

T

I

I

L

K

E

E

K

H

K

F

G

G

S

E

L

V

E

K

G

D

L

L

K

R

I

V

A

L

I

Y

V

V

G

G

D

D

I

I

L

K

H

H

S

S

R
|
R

V
|
V

A

F

R

R

S

S

D

G

I

A

K

P

L

L

F

L

K

N

K

M

L

F

G

G

A

A

E

K

V

I

T

G

L

V

C

C

G

G

P

P

M

K

T

T

M

L

L

I

P

P

R

R

H

D

Y

V

E

E

A

V

L

F

G

K

A

V

D

D

Y

-

I

V

T

F

T

D

D

D

I

V

K

D

E

K

A

G

V

I

K

D

N

W

K

A

D

D

V

V

I

I

F

W

L

L

R
|
R

I

L

Q

Q

L

K

E

E

R

R

Q

Q

D

K

K

E

P

N

F

Y

F

I

S

P

T

S

L

E

R

S

E

S

Y

Y

S

F

I

K

K

Q

Y

F

G

G

L

L

N

T

Q

K

E

E

L

R

L

F

K

E

I

K

L

V

K

K

P

-

D

-

T

-

V

L

I

Y

M

M

H

H

P

P

G
|
G

P

P

V

V

N

N

R

R

G

N

V

V

E

D

I

I

Q

D

S

H

E

E

L

L

V

V

Y

Y

S

T

S

E

K

K

S

S

L

L

I

I

L

Q

N

E

Q

Q

V

V

E

K

N

N

G

G

L

I

F

P

I

V

R

R

M

K

A

A

V

I

Y

Y

K

K

Y

F

L

L

L

W

S

T

active site: R47 (= R54), T48 (= T55), K75 (= K82), R97 (= R104), H126 (= H132), Q129 (= Q135)
binding citrate anion: T48 (= T55), R97 (= R104), H126 (= H132), R159 (= R165), V160 (= V166), R213 (= R220), G251 (= G261)

8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
36% identity, 98% coverage: 6:301/301 of query aligns to 20:316/316 of 8bplA

query
sites
8bplA

S

S

V

V

N

T

Q

Q

L

F

E

T

K

R

E

A

D

D

I

L

Q

H

K

L

I

L

F

F

Q

Q

L

I

A

A

K

Q

E

E

Y

M

K

R

E

-

R

L

F

G

L

V

K

Q

G

R

E

E

K

G

K

V

F

L

N

D

D

I

L

L

R

R

R

G

C

K

S

V

I

L

L

C

L

T

V

L

F

F

F

Y

E

E

N

P

S
|
S

T
|
T

R
|
R

T
|
T

R

S

T

A

S

S

F

F

E

D

L

A

A

A

G

M

K

Q

I

R

L

L

G

G

A

G

D

R

T

T

I

I

N

P

I

I

S

Q

A

T

S

S

S

T

S

S

V

V

K

Q

K

K

G

G

E

E

T

T

L

L

Y

Q

D

D

T

T

V

L

K

R

T

T

L

L

E

-

A

A

L

C

N

Y

S

S

D

D

F

A

I

I

V

V

I

L

R
|
R

H

H

N

P

M

D

S

E

G

K

A

C

A

V

K

D

I

V

V

A

A

K

N

K

S

Y

V

C

K

P

S

V

H

P

V

V

V

I

N

N

A

G

G

G

D

N

G

G

T

S

N

K

E

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

F

L

L

D

D

G

L

F

F

T

T

I

I

L

R

E

E

K

E

K

L

G

G

S

T

L

M

E

Q

G

G

L

L

K

T

I

I

A

T

I

F

V

V

G

G

D

D

I

L

L

L

H

Y

S

G

R

R

V

P

A

V

R

H

S

S

D

L

I

V

K

Y

L

L

F

L

K

R

K

H

L

Y

G

Q

A

V

E

K

V

V

T

Q

L

L

C

V

G

S

P

P

M

K

T

A

M

L

-

R

L

L

P

P

R

P

-

A

-

V

H

R

Y

Q

E

Q

A

L

L

V

G

D

A

A

D

G

Y

Q

I

L

T

L

T

C

D

E

-

S

-

E

-

A

-

L

I

T

K

P

E

E

A

I

V

L

K

G

N

R

K

T

D

D

V

V

V

L

I

Y

F

C

L

T

R

R

I

V

Q

Q

L

K

E

E

R

R

Q

-

D

-

K

-

P

-

F

-

F

F

S

P

T

S

L

L

R

A

E

E

Y

F

S

E

I

A

-

V

-

K

-

D

K

S

Y

Y

G

R

L

I

N

D

Q

Y

E

S

L

T

L

L

K

K

I

Y

L

A

K

K

P

P

D

T

T

T

V

V

I

V

M

M

H

H

P

P

G
x
L

P

P

V

R

N

N

R

E

G

-

V

-

E

E

I

V

Q

A

S

E

E

E

L

V

V

D

Y

F

S

D

S

Q

K

R

S

A

L

A

I

Y

L

F

N

R

Q

Q

V

M

E

C

N

Y

G

G

L

L

F

Y

I

C

R

R

M

M

A

A

V

L

Y

L

K

A

Y

L

L

V

L

M

S

S

binding phosphoric acid mono(formamide)ester: S65 (= S52), T66 (= T53), R67 (= R54), T68 (= T55), R116 (= R104), H144 (= H132), Q147 (= Q135), L278 (≠ G261)

5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
34% identity, 99% coverage: 2:300/301 of query aligns to 6:304/307 of 5g1nE

query
sites
5g1nE

K

Q

D

H

L

I

Y

L

S

S

V

V

N

Q

Q

Q

L

F

E

T

K

K

E

D

D

Q

I

M

Q

S

K

H

I

L

F

F

Q

N

L

V

A

A

K

H

E

T

Y

L

K

R

E

-

R

M

F

M

L

V

K

Q

G

K

E

E

K

R

K

S

F

L

N

D

D

I

L

L

R

K

R

G

C

K

S

V

I

M

L

A

L

S

V

M

F

F

F

Y

E

E

N

V

S
|
S

T
|
T

R
|
R

T
|
T

R

S

T

S

S

S

F

F

E

A

L

A

A

A

G

M

K

A

I

R

L

L

G

G

A

G

D

A

T

V

I

L

N

S

I

F

S

S

A

E

S

A

S

T

S

S

S
|
S

V

V

K

Q

K
|
K

G

G

E

E

T

S

L

L

Y

A

D

D

T

S

V

V

K

Q

T

T

L

M

E

S

A

C

L

Y

N

-

S

A

D

D

F

V

I

V

V

V

I

L

R
|
R

H

H

N

P

M

Q

S

P

G

G

A

A

A

V

K

E

I

L

V

A

A

A

N

K

S

H

V

C

K

R

S

R

H

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

T

V

N

G

E

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

L

D

D

G

I

F

F

T

T

I

I

L

R

E

E

K

E

K

L

G

G

S

T

L

V

E

N

G

G

L

M

K

T

I

I

A

T

I

M

V

V

G

G

D

D

I

L

L

K

H

H

S

G

R
|
R

V

T

A

V

R

H

S

S

D

L

I

A

K

C

L

L

F

L

K

T

K

Q

L

Y

G

R

A

V

E

S

V

L

T

R

L

Y

C

V

G

A

P

P

M

P

T

S

M

L

-

R

L

M

P

P

R

P

H

T

Y

V

E

R

A

A

L

F

G

V

A

A

D

S

Y

R

I

G

T

T

-

K

-

Q

-

E

-

F

T

E

D

S

I

I

K

E

E

E

A

A

V

L

K

P

N

D

K

T

D

D

V

V

V

L

I

Y

F

M

L
x
T

R
|
R

I

I

Q
|
Q

L

K

E

E

R

R

Q

-

D

-

K

-

P

-

F

-

F

F

S

G

T

S

L

T

R

Q

E

E

Y

Y

S

E

I

A

K

C

Y

F

G

G

-

Q

-

F

-

I

L

L

N

T

Q

P

E

H

L

I

L

M

K

T

I

R

L

A

K

K

P

K

D

K

T

M

V

V

I

V

M

M

H

H

P
|
P

G
x
M

P

P

V

-

N

-

R

R

G

V

V

N

E

E

I

I

Q

S

S

V

E

E

L

V

V

D

Y

S

S

D

S

P

K

R

S

A

L

A

I

Y

L

F

N

R

Q

Q

V

A

E

E

N

N

G
|
G

L

M

F

Y

I

I

R

R

M

M

A

A

V

L

Y

L

K

A

Y

T

L

V

L

L

active site: R57 (= R54), T58 (= T55), K85 (= K82), R106 (= R104), H134 (= H132), Q137 (= Q135), T227 (≠ L219), P266 (= P260), G292 (= G288)
binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S52), T56 (= T53), R57 (= R54), T58 (= T55), S82 (= S79), K85 (= K82), R106 (= R104), H134 (= H132), R167 (= R165), R228 (= R220), Q230 (= Q222), M267 (≠ G261)

1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
39% identity, 100% coverage: 2:301/301 of query aligns to 5:305/307 of 1ml4A

query
sites
1ml4A

K

R

D

D

L

V

Y

I

S

S

V

I

N

R

Q

D

L

F

E

S

K

K

E

E

D

D

I

I

Q

E

K

T

I

V

F

L

Q

A

L

T

A

A

K

-

E

E

Y

R

K

L

E

E

R

R

F

E

L

L

K

K

G

E

E

K

K

G

K

Q

F

L

N

E

D

Y

L

A

R

K

R

G

C

K

S

I

I

L

L

A

L

T

V

L

F

F

E

E

N

P

S
|
S

T
|
T

R
|
R

T
|
T

R

R

T

L

S

S

F

F

E

E

L

S

A

A

G

M

K

H

I

R

L

L

G

G

A

G

D

A

T

V

I

I

N

G

I

F

S

A

-

E

A

A

S

S

S

T

S

S

V

V

K

K

K
|
K

G

G

E

E

T

S

L

L

Y

R

D

D

T

T

V

I

K

K

T

T

L

V

E

E

A

Q

L

Y

N

-

S

C

D

D

F

V

I

I

V

V

I

I

R
|
R

H

H

N

P

M

K

S

E

G

G

A

A

K

R

I

L

V

A

A

A

N

E

S

V

V

A

K

E

S

V

H

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

T

S

N

N

E

Q

H
|
H

P

P

T

T

Q
|
Q

A

T

L

L

D

D

G

L

F

Y

T

T

I

I

L

K

E

K

K

E

K

F

G

G

S

R

L

I

E

D

G

G

L

L

K

K

I

I

A

G

I

L

V

L

G

G

D

D

I

L

L

K

H

Y

S

G

R
|
R

V
x
T

A

V

R

H

S

S

D

L

I

A

K

E

L

A

F

L

K

T

K

F

L

Y

G

D

A

V

E

E

V

L

T

Y

L

L

C

I

G

S

P

P

-

E

M

L

T

L

M

R

L

M

P

P

R

R

H

H

-

I

Y

V

E

E

A

E

L

L

-

R

-

E

-

K

G

G

A

M

D

K

Y

V

I

V

-

E

T

T

D

T

I

L

K

E

E

D

A

V

V

I

K

G

N

K

K

L

D

D

V

V

V

L

I

Y

F

V

L
x
T

R
|
R

I

I

Q

Q

L

K

E

E

R

R

Q

-

D

-

K

-

P

-

F

-

F

F

S

P

T

D

L

E

R

Q

E

E

Y

Y

-

L

S

K

I

V

K

K

-

G

-

S

Y

Y

G

Q

L

V

N

N

Q

L

E

K

L

V

L

L

K

E

I

K

L

A

K

K

P

D

D

E

T

L

V

R

I

I

M

M

H

H

P
|
P

G
x
L

P

P

V

-

N

-

R

R

G

V

V

D

E

E

I

I

Q

H

S

P

E

E

L

V

V

D

Y

N

S

T

S

K

K

H

S

A

L

I

I

Y

L

F

N

R

Q

Q

V

V

E

F

N

N

G
|
G

L

V

F

P

I

V

R

R

M

M

A

A

V

L

Y

L

K

A

Y

L

L

V

L

L

S

G

active site: R56 (= R54), T57 (= T55), K85 (= K82), R106 (= R104), H134 (= H132), Q137 (= Q135), T227 (≠ L219), P266 (= P260), G292 (= G288)
binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S52), T55 (= T53), R56 (= R54), T57 (= T55), R106 (= R104), H134 (= H132), R167 (= R165), T168 (≠ V166), R228 (= R220), L267 (≠ G261)

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)
34% identity, 99% coverage: 2:300/301 of query aligns to 1924:2222/2225 of P27708

query
sites
P27708

K
x
Q

D
x
H

L
x
I

Y
x
L

S
|
S

V
|
V

N
x
Q

Q
|
Q

L
x
F

E
x
T

K
|
K

E
x
D

D
x
Q

I
x
M

Q
x
S

K
x
H

I
x
L

F
|
F

Q
x
N

L
x
V

A
|
A

K
x
H

E
x
T

Y
x
L

K
x
R

E

-

R
x
M

F
x
M

L
x
V

K
x
Q

G
x
K

E
|
E

K
x
R

K
x
S

F
x
L

N
x
D

D
x
I

L
|
L

R
x
K

R
x
G

C
x
K

S
x
V

I
x
M

L
x
A

L
x
S

V
x
M

F
|
F

F
x
Y

E
|
E

N
x
V

S
|
S

T
|
T

R
|
R

T
|
T

R
x
S

T
x
S

S
|
S

F
|
F

E
x
A

L
x
A

A
|
A

G
x
M

K
x
A

I
x
R

L
|
L

G
|
G

A
x
G

D
x
A

T
x
V

I
x
L

N
x
S

I
x
F

S
|
S

A
x
E

S
x
A

S
x
T

S
|
S

V
|
V

K
x
Q

K
|
K

G
|
G

E
|
E

T
x
S

L
|
L

Y
x
A

D
|
D

T
x
S

V
|
V

K
x
Q

T
|
T

L
x
M

E
x
S

A
x
C

L
x
Y

N

-

S
x
A

D
|
D

F
x
V

I
x
V

V
|
V

I
x
L

R
|
R

H
|
H

N
x
P

M
x
Q

S
x
P

G
|
G

A
|
A

A
x
V

K
x
E

I
x
L

V
x
A

A
|
A

N
x
K

S
x
H

V
x
C

K
x
R

S
x
R

H
x
P

V
|
V

V
x
I

N
|
N

A
|
A

G
|
G

D
|
D

G
|
G

T
x
V

N
x
G

E
|
E

H
|
H

P
|
P

T
|
T

Q
|
Q

A
|
A

L
|
L

D
|
D

G
x
I

F
|
F

T
|
T

I
|
I

L
x
R

E
|
E

K
x
E

K
x
L

G
|
G

S
x
T

L
x
V

E
x
N

G
|
G

L
x
M

K
x
T

I
|
I

A
x
T

I
x
M

V
|
V

G
|
G

D
|
D

I
x
L

L
x
K

H
|
H

S
x
G

R
|
R

V
x
T

A
x
V

R
x
H

S
|
S

D
x
L

I
x
A

K
x
C

L
|
L

F
x
L

K
x
T

K
x
Q

L
x
Y

G
x
R

A
x
V

E
x
S

V
x
L

T
x
R

L
x
Y

C
x
V

G
x
A

P
|
P

M
x
P

T
x
S

M
x
L

-
x
R

L
x
M

P
|
P

R
x
P

H
x
T

Y
x
V

E
x
R

A
|
A

L
x
F

G
x
V

A
|
A

D
x
S

Y
x
R

I
x
G

T
|
T

T
x
K

-
x
Q

-
x
E

-
x
F

-
x
E

D
x
S

I
|
I

K
x
E

E
|
E

A
|
A

V
x
L

K
x
P

N
x
D

K
x
T

D
|
D

V
|
V

V
x
L

I
x
Y

F
x
M

L
x
T

R
|
R

I
|
I

Q
|
Q

L
x
K

E
|
E

R
|
R

Q

-

D

-

K

-

P

-

F

-

F
|
F

S
x
G

T
x
S

L
x
T

R
x
Q

E
|
E

Y
|
Y

S
x
E

I
x
A

K
x
C

Y
x
F

G
|
G

-
x
Q

-
x
F

-
x
I

L
|
L

N
x
T

Q
x
P

E
x
H

L
x
I

L
x
M

K
x
T

I
x
R

L
x
A

K
|
K

P
x
K

D
x
K

T
x
M

V
|
V

I
x
V

M
|
M

H
|
H

P
|
P

G
x
M

P
|
P

V

-

N

-

R
|
R

G
x
V

V
x
N

E
|
E

I
|
I

Q
x
S

S
x
V

E
|
E

L
x
V

V
x
D

Y
x
S

S
x
D

S
x
P

K
x
R

S
x
A

L
x
A

I
x
Y

L
x
F

N
x
R

Q
|
Q

V
x
A

E
|
E

N
|
N

G
|
G

L
x
M

F
x
Y

I
|
I

R
|
R

M
|
M

A
|
A

V
x
L

Y
x
L

K
x
A

Y
x
T

L
x
V

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

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)
33% identity, 99% coverage: 2:300/301 of query aligns to 1924:2222/2225 of P08955

query
sites
P08955

K

Q

D

H

L

I

Y

L

S

S

V

V

N

K

Q

Q

L

F

E

T

K

K

E

D

D

Q

I

M

Q

S

K

H

I

L

F

F

Q

N

L

V

A

A

K

H

E

T

Y

L

K

R

E

-

R

M

F

M

L

V

K

Q

G

K

E

E

K

R

K

S

F

L

N

D

D

I

L

L

R

K

R

G

C

K

S

V

I

M

L

A

L

S

V

M

F

F

F

Y

E

E

N

V

S

S

T

T

R

R

T

T

R

S

T

S

S

S

F

F

E

A

L

A

A

A

G

M

K

A

I

R

L

L

G

G

A

G

D

A

T

V

I

L

N

S

I

F

S

S

A

E

S

A

S

T

S

S

V

V

K

Q

K

K

G

G

E

E

T

S

L

L

Y

A

D

D

T

S

V

V

K

Q

T

T

L

M

E

S

A

C

L

Y

N

-

S

A

D

D

F

V

I

V

V

V

I

L

R

R

H

H

N

P

M

Q

S

P

G

G

A

A

A

V

K

E

I

L

V

A

A

A

N

K

S

H

V

C

K

R

S

R

H

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

T

V

N

G

E

E

H

H

P

P

T

T

Q

Q

A

A

L

L

D

D

G

I

F

F

T

T

I

I

L

R

E

E

K

E

K

L

G

G

S

T

L

V

E

N

G

G

L

M

K

T

I

I

A

T

I

M

V

V

G

G

D

D

I

L

L

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

D

L

I

A

K

C

L

L

F

L

K

T

K

Q

L

Y

G

R

A

V

E

S

V

L

T

R

L

Y

C

V

G

A

P

P

-

P

-

S

M

L

T

R

M

M

L

P

P

P

R

S

H

V

Y

W

E

D

A

F

L

V

G

A

A

S

D

R

Y

G

I

T

T

K

T

Q

D

E

-

E

-

F

-

E

-

S

I

I

K

E

E

E

A

A

V

L

K

P

N

D

K

T

D

D

V

V

V

L

I

Y

F

M

L

T

R

R

I

I

Q

Q

L

K

E

E

R

R

Q

-

D

-

K

-

P

-

F

-

F

F

S

G

T

S

L

T

R

Q

E

E

Y

Y

S

E

I

A

K

C

Y

F

G

G

-

Q

-

F

-

I

L

L

N

T

Q

P

E

H

L

I

L

M

K

T

I

R

L

A

K

K

P

K

D

K

T

M

V

V

I

V

M

M

H

H

P

P

G

M

P

P

V

-

N

-

R

R

G

V

V

N

E

E

I

I

Q

S

S

V

E

E

L

V

V

D

Y

S

S

D

S

P

K

R

S

A

L

A

I

Y

L

F

N

R

Q

Q

V

A

E

E

N

N

G

G

L

M

F

Y

I

I

R

R

M

M

A

A

V

L

Y

L

K

A

Y

T

L

V

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.

5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
33% identity, 99% coverage: 2:300/301 of query aligns to 3:289/292 of 5g1pA

query
sites
5g1pA

K

Q

D

H

L

I

Y

L

S

S

V

V

N

Q

Q

Q

L

F

E

T

K

K

E

D

D

Q

I

M

Q

S

K

H

I

L

F

F

Q

N

L

V

A

A

K

H

E

T

Y

L

K

R

E

-

R

M

F

M

L

V

K

Q

G

K

E

E

K

R

K

S

F

L

N

D

D

I

L

L

R

K

R

G

C

K

S

V

I

M

L

A

L

S

V

M

F

F

F

Y

E

E

N

V

S
|
S

T
|
T

R
|
R

T
|
T

R

S

T

S

S

S

F

F

E

A

L

A

A

A

G

M

K

A

I

R

L

L

G

G

A

G

D

A

T

V

I

L

N

S

I

F

S

S

A

E

S

A

S

T

S

S

V

V

K

Q

K
|
K

G

G

E

E

T

S

L

L

Y

A

D

D

T

S

V

V

K

Q

T

T

L

M

E

S

A

C

L

Y

N

-

S

A

D

D

F

V

I

V

V

V

I

L

R
|
R

H

H

N

P

M

Q

S

P

G

G

A

A

A

V

K

E

I

L

V

A

A

A

N

K

S

H

V

C

K

R

S

R

H

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

T

V

N

G

E

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

L

D

D

G

I

F

F

T

T

I

I

L

R

E

E

K

E

K

L

G

G

S

T

L

V

E

N

G

G

L

M

K

T

I

I

A

T

I

M

V

V

G

G

D

D

I

L

L

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

D

L

I

A

K

C

L

L

F

L

K

T

K

Q

L

Y

G

R

A

V

E

S

V

L

T

R

L

Y

C

V

G

A

P

P

M

P

T

S

M

L

-

R

L

M

P

P

R

P

H

T

Y

V

E

R

A

A

L

F

G

V

A

A

D

S

Y

G

I

T

T

K

T

Q

D

E

-

E

-

F

-

E

-

S

I

I

K

E

E

E

A

A

V

L

K

P

N

D

K

T

D

D

V

V

V

L

I

Y

F

M

L
x
T

R

R

I

I

Q

Q

L

K

E

E

R

R

Q

-

D

-

K

-

P

-

F

-

S

-

T

-

L

-

R

-

E

-

Y

-

S

-

I

F

K

Q

Y

F

G

I

L

L

N

T

Q

P

E

H

L

I

L

M

K

T

I

R

L

A

K

K

P

K

D

K

T

M

V

V

I

V

M

M

H

H

P
|
P

G
x
M

P

P

V

-

N

-

R

R

G

V

V

N

E

E

I

I

Q

S

S

V

E

E

L

V

V

D

Y

S

S

D

S

P

K

R

S

A

L

A

I

Y

L

F

N

R

Q

Q

V

A

E

E

N

N

G
|
G

L

M

F

Y

I

I

R

R

M

M

A

A

V

L

Y

L

K

A

Y

T

L

V

L

L

active site: R54 (= R54), T55 (= T55), K82 (= K82), R103 (= R104), H131 (= H132), Q134 (= Q135), T223 (≠ L219), P251 (= P260), G277 (= G288)
binding phosphoric acid mono(formamide)ester: S52 (= S52), T53 (= T53), R54 (= R54), T55 (= T55), R103 (= R104), Q134 (= Q135), M252 (≠ G261)

P49077 Aspartate carbamoyltransferase, chloroplastic; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
37% identity, 100% coverage: 1:300/301 of query aligns to 84:387/390 of P49077

query
sites
P49077

M

L

K

S

D

D

L

V

Y

I

S

E

V

G

N

K

Q

Q

L

F

E

D

K

R

E

E

D

M

I

L

Q

S

K

A

I

I

F

F

Q

D

L

V

A

A

K

R

E

E

Y

M

K

-

E

E

R

K

F

I

L

E

K

K

G

S

E

S

K

S

K

Q

F

S

N

E

D

I

L

L

R

K

R

G

C

Y

S

L

I

M

L

A

L

T

V

L

F

F

F

Y

E

E

N

P

S

S

T

T

R
|
R

T
|
T

R

R

T

L

S

S

F

F

E

E

L

S

A

A

G

M

K

K

I

R

L

L

G

G

A

G

D

E

T

V

I

L

N

T

I

T

S

E

A

N

S

A

S

R

-

E

-

F

S

S

V

A

K

A

K

K

G

G

E

E

T

T

L

L

Y

E

D

D

T

T

V

I

K

R

T

T

L

V

E

E

A

G

L

Y

N

-

S

S

D

D

F

I

I

I

V

V

I

M

R
|
R

H

H

N

F

M

E

S

S

G

G

A

A

K

R

I

K

V

A

A

A

N

A

S

T

V

A

K

N

S

I

H

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

T

P

N

G

E

E

H
|
H

P

P

T

T

Q

Q

A

A

L

L

D

D

G

V

F

Y

T

T

I

I

L

Q

E

S

K

E

K

I

G

G

S

K

L

L

E

D

G

G

L

I

K

S

I

V

A

A

I

L

V

V

G

G

D

D

I

L

L

A

H

N

S

G

R
|
R

V

T

A

V

R

R

S

S

D

L

I

A

K

Y

L

L

F

L

K

A

K

K

L

F

-

K

G

D

A

V

E

K

V

I

T

Y

L

F

C

V

G

S

P

P

M

E

T

I

M

V

-

K

-

M

-

K

-

D

L

I

P

K

R

D

H

Y

Y

L

E

T

A

S

L

S

G

G

A

V

D

E

Y

W

-

E

I

E

T

S

D

D

I

L

K

M

E

E

A

V

V

A

K

S

N

K

K

C

D

D

V

V

I

Y

F

Q

L

T

R
|
R

I

I

Q

Q

L

R

E

E

R

R

Q

-

D

-

K

-

P

-

F

F

F

G

S

E

T

R

L

L

R

D

E

L

Y

Y

S

E

I

A

-

A

-

R

-

G

K

K

Y

Y

G

I

L

V

N

D

Q

K

E

D

L

L

K

G

I

V

L

M

K

Q

P

K

D

K

T

A

V

I

I

I

M

M

H

H

P

P

G

L

P

P

V

-

N

-

R

R

G

L

V

D

E

E

I

I

Q

T

S

A

E

D

L

V

V

D

Y

A

S

D

S

P

K

R

S

A

L

A

I

Y

L

F

N

R

Q

Q

V

A

E

K

N

N

G

G

L

L

F

F

I

I

R

R

M

M

A

A

V

L

Y

L

K

K

Y

L

L

L

R136 (= R54) binding UMP
T137 (= T55) binding UMP
R187 (= R104) binding UMP
H215 (= H132) binding UMP
R248 (= R165) binding UMP
R310 (= R220) binding UMP

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)
37% identity, 99% coverage: 2:300/301 of query aligns to 1877:2193/2198 of Q18990

query
sites
Q18990

K

K

D

N

L

C

Y

I

S

S

V

V

N

K

Q

H

L

L

E

D

K

K

E

G

D

Q

I

I

Q

N

K

R

I

I

F

F

Q

E

L

L

A

A

K

D

E

R

Y

Y

K

K

E

H

R

D

F

V

L

E

K

K

G

G

E

H

K

P

K

L

F

T

N

H

D

I

L

L

R

N

R

G

C

K

S

V

I

L

L

V

L

N

V

L

F

F

F

Y

E

E

N

V

S

S

T

T

R

R

T

T

R

S

T

C

S

S

F

F

E

S

L

A

A

A

G

M

K

Q

I

R

L

L

G

G

A

G

D

S

T

V

I

I

N

S

I

V

S

D

A

S

S

Q

S

S

V

V

K

Q

K

K

G

G

E

E

T

T

L

L

Y

E

D

D

T

T

V

V

K

Q

T

V

L

L

E

G

A

S

L

Y

N

-

S

G

D

D

F

I

I

L

V

V

I

L

R

R

H

S

N

N

M

E

S

N

G

G

A

A

K

D

I

R

V

A

A

A

N

R

S

V

V

C

K

D

S

Q

H

P

V

V

V

I

N

N

A

G

G

G

D

D

G

G

T

T

N

G

E

E

H

H

P

P

T

T

Q

Q

A

A

L

L

D

D

G

V

F

Y

T

T

I

I

L

R

E

Q

K

E

K

M

G

G

S

T

L

V

E

N

G

G

L

L

K

T

I

I

A

A

I

L

V

V

G

G

D

D

I

L

L

K

H

N

S

G

R

R

V

T

A

V

R

H

S

S

D

L

I

A

K

K

L

L

F

L

K

-

K

C

L

L

G

Y

A

K

E

D

V

I

T

T

L

L

-

H

-

Y

C

V

G

A

P

P

M

S

T

T

M

E

L

L

P

E

R

M

H

P

Y

Q

E

E

A

V

L

L

G

-

A

-

D

D

Y

Y

I

V

T

S

-

S

-

K

-

S

-

N

-

F

-

V

-

Q

-

K

-

F

T

T

D

S

I

L

K

A

E

E

A

G

V

I

K

N

N

H

K

V

D

D

V

V

I

Y

F

V

L

T

R

R

I

I

Q

Q

L

K

E

E

R

R

Q

-

D

-

K

-

P

-

F

-

F

F

S

S

T

S

L

P

R

D

E

E

Y

Y

S

N

I

K

K

V

Y

K

G

G

-

S

-

Y

-

V

-

I

-

N

-

A

-

K

-

L

L

L

N

N

Q

E

E

A

L

A

L

R

K

D

I

V

L

E

K

E

P

P

D

S

T

S

-

L

-

V

-

P

-

A

-

R

-

S

-

L

-

P

V

I

I

V

M

M

H

H

P

P

G

L

P

P

V

-

N

-

R

R

G

V

V

D

E

E

I

I

Q

A

S

V

E

E

L

L

V

D

Y

H

S

D

S

E

K

R

S

A

L

A

I

Y

L

F

N

R

Q

Q

V

A

E

K

N

N

G

G

L

V

F

F

I

V

R

R

M

M

A

S

V

I

Y

L

K

S

Y

L

L

L

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.

6ys6B Arabidopsis aspartate transcarbamoylase complex with pala (see paper)
36% identity, 100% coverage: 1:300/301 of query aligns to 6:309/312 of 6ys6B

query
sites
6ys6B

M

L

K

S

D

D

L

V

Y

I

S

E

V

G

N

K

Q

Q

L

F

E

D

K

R

E

E

D

M

I

L

Q

S

K

A

I

I

F

F

Q

D

L

V

A

A

K

R

E

E

Y

M

K

-

E

E

R

K

F

I

L

E

K

K

G

S

E

S

K

S

K

Q

F

S

N

E

D

I

L

L

R

K

R

G

C

Y

S

L

I

M

L

A

L

T

V

L

F

F

F

Y

E

E

N

P

S

S

T

T

R

R

T

T

R

R

T

L

S

S

F

F

E

E

L

S

A

A

G

M

K

K

I

R

L

L

G

G

A

G

D

E

T

V

I

L

N

T

I

T

S

E

A

N

S

A

S

R

-

E

-

F

S

S

S
|
S

V

A

K

A

K
|
K

G

G

E

E

T

T

L

L

Y

E

D

D

T

T

V

I

K

R

T

T

L

V

E

E

A

G

L

Y

N

-

S

S

D

D

F

I

I

I

V

V

I

M

R
|
R

H

H

N

F

M

E

S

S

G

G

A

A

K

R

I

K

V

A

A

A

N

A

S

T

V

A

K

N

S

I

H

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

T

P

N

G

E

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

L

D

D

G

V

F

Y

T

T

I

I

L

Q

E

S

K

E

K

I

G

G

S

K

L

L

E

D

G

G

L

I

K

S

I

V

A

A

I

L

V

V

G

G

D

D

I

L

L

A

H

N

S

G

R

R

V

T

A

V

R

R

S

S

D

L

I

A

K

Y

L

L

F

L

K

A

K

K

L

F

-

K

G

D

A

V

E

K

V

I

T

Y

L

F

C

V

G

S

P

P

M

E

T

I

M

V

-

K

-

M

-

K

-

D

L

I

P

K

R

D

H

Y

Y

L

E

T

A

S

L

S

G

G

A

V

D

E

Y

W

-

E

I

E

T

S

D

D

I

L

K

M

E

E

A

V

V

A

K

S

N

K

K

C

D

D

V

V

I

Y

F

Q

L
x
T

R

R

I

I

Q

Q

L

R

E

E

R

R

Q

-

D

-

K

-

P

-

F

F

F

G

S

E

T

R

L

L

R

D

E

L

Y

Y

S

E

I

A

K

A

Y

R

G

G

-

K

-

F

-

I

L

V

N

D

Q

K

E

D

L

L

K

G

I

V

L

M

K

Q

P

K

D

K

T

A

V

I

I

I

M

M

H

H

P
|
P

G

L

P

P

V

-

N

-

R

R

G

L

V

D

E

E

I

I

Q

T

S

A

E

D

L

V

V

D

Y

A

S

D

S

P

K

R

S

A

L

A

I

Y

L

F

N

R

Q

Q

V

A

E

K

N

N

G
|
G

L

L

F

F

I

I

R

R

M

M

A

A

V

L

Y

L

K

K

Y

L

L

L

active site: R109 (= R104), H137 (= H132), Q140 (= Q135), T231 (≠ L219), P271 (= P260), G297 (= G288)
binding n-(phosphonacetyl)-l-aspartic acid: S85 (= S79), K88 (= K82)

6ypoA Arabidopsis aspartate transcarbamoylase bound to ump (see paper)
36% identity, 100% coverage: 1:300/301 of query aligns to 6:309/312 of 6ypoA

query
sites
6ypoA

M

L

K

S

D

D

L

V

Y

I

S

E

V

G

N

K

Q

Q

L

F

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K

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E

E

D

M

I

L

Q

S

K

A

I

I

F

F

Q

D

L

V

A

A

K

R

E

E

Y

M

K

-

E

E

R

K

F

I

L

E

K

K

G

S

E

S

K

S

K

Q

F

S

N

E

D

I

L

L

R

K

R

G

C

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S

L

I

M

L

A

L

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V

L

F

F

F

Y

E

E

N

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T

R
|
R

T
|
T

R

R

T

L

S

S

F

F

E

E

L

S

A

A

G

M

K

K

I

R

L

L

G

G

A

G

D

E

T

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I

L

N

T

I

T

S

E

A

N

S

A

S

R

-

E

-

F

S

S

V

A

K

A

K

K

G

G

E

E

T

T

L

L

Y

E

D

D

T

T

V

I

K

R

T

T

L

V

E

E

A

G

L

Y

N

-

S

S

D

D

F

I

I

I

V

V

I

M

R
|
R

H

H

N

F

M

E

S

S

G

G

A

A

K

R

I

K

V

A

A

A

N

A

S

T

V

A

K

N

S

I

H

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

T

P

N

G

E

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

L

D

D

G

V

F

Y

T

T

I

I

L

Q

E

S

K

E

K

I

G

G

S

K

L

L

E

D

G

G

L

I

K

S

I

V

A

A

I

L

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V

G

G

D

D

I

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L

A

H

N

S

G

R
|
R

V
x
T

A

V

R

R

S

S

D

L

I

A

K

Y

L

L

F

L

K

A

K

K

L

F

-

K

G

D

A

V

E

K

V

I

T

Y

L

F

C

V

G

S

P

P

M

E

T

I

M

V

-

K

-

M

-

K

-

D

L

I

P

K

R

D

H

Y

Y

L

E

T

A

S

L

S

G

G

A

V

D

E

Y

W

-

E

I

E

T

S

D

D

I

L

K

M

E

E

A

V

V

A

K

S

N

K

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C

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D

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V

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Q

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x
T

R
|
R

I

I

Q

Q

L

R

E

E

R

R

Q

-

D

-

K

-

P

-

F

F

F

G

S

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T

R

L

L

R

D

E

L

Y

Y

S

E

I

A

K

A

Y

R

G

G

-

K

-

F

-

I

L

V

N

D

Q

K

E

D

L

L

K

G

I

V

L

M

K

Q

P

K

D

K

T

A

V

I

I

I

M

M

H
|
H

P
|
P

G
x
L

P

P

V

-

N

-

R

R

G

L

V

D

E

E

I

I

Q

T

S

A

E

D

L

V

V

D

Y

A

S

D

S

P

K

R

S

A

L

A

I

Y

L

F

N

R

Q

Q

V

A

E

K

N

N

G
|
G

L

L

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F

I

I

R

R

M

M

A

A

V

L

Y

L

K

K

Y

L

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L

active site: R109 (= R104), H137 (= H132), Q140 (= Q135), T231 (≠ L219), P271 (= P260), G297 (= G288)
binding uridine-5'-monophosphate: R58 (= R54), T59 (= T55), R109 (= R104), H137 (= H132), R170 (= R165), T171 (≠ V166), R232 (= R220), H270 (= H259), P271 (= P260), L272 (≠ G261)

6yvbC Arabidopsis aspartate transcarbamoylase complex with carbamoyl phosphate (see paper)
36% identity, 100% coverage: 1:300/301 of query aligns to 18:321/324 of 6yvbC

query
sites
6yvbC

M

L

K

S

D

D

L

V

Y

I

S

E

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G

N

K

Q

Q

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F

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M

I

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Q

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K

A

I

I

F

F

Q

D

L

V

A

A

K

R

E

E

Y

M

K

-

E

E

R

K

F

I

L

E

K

K

G

S

E

S

K

S

K

Q

F

S

N

E

D

I

L

L

R

K

R

G

C

Y

S

L

I

M

L

A

L

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V

L

F

F

F

Y

E

E

N

P

S
|
S

T
|
T

R
|
R

T
|
T

R

R

T

L

S

S

F

F

E

E

L

S

A

A

G

M

K

K

I

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L

L

G

G

A

G

D

E

T

V

I

L

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T

I

T

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E

A

N

S

A

S

R

-

E

-

F

S

S

V

A

K

A

K

K

G

G

E

E

T

T

L

L

Y

E

D

D

T

T

V

I

K

R

T

T

L

V

E

E

A

G

L

Y

N

-

S

S

D

D

F

I

I

I

V

V

I

M

R
|
R

H

H

N

F

M

E

S

S

G

G

A

A

K

R

I

K

V

A

A

A

N

A

S

T

V

A

K

N

S

I

H

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

T

P

N

G

E

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

L

D

D

G

V

F

Y

T

T

I

I

L

Q

E

S

K

E

K

I

G

G

S

K

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L

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D

G

G

L

I

K

S

I

V

A

A

I

L

V

V

G

G

D

D

I

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L

A

H

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S

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R

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T

A

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S

D

L

I

A

K

Y

L

L

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L

K

A

K

K

L

F

-

K

G

D

A

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E

K

V

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T

Y

L

F

C

V

G

S

P

P

M

E

T

I

M

V

-

K

-

M

-

K

-

D

L

I

P

K

R

D

H

Y

Y

L

E

T

A

S

L

S

G

G

A

V

D

E

Y

W

-

E

I

E

T

S

D

D

I

L

K

M

E

E

A

V

V

A

K

S

N

K

K

C

D

D

V

V

I

Y

F

Q

L
x
T

R

R

I

I

Q

Q

L

R

E

E

R

R

Q

-

D

-

K

-

P

-

F

F

F

G

S

E

T

R

L

L

R

D

E

L

Y

Y

S

E

I

A

K

A

Y

R

G

G

-

K

-

F

-

I

L

V

N

D

Q

K

E

D

L

L

K

G

I

V

L

M

K

Q

P

K

D

K

T

A

V

I

I

I

M

M

H

H

P
|
P

G

L

P

P

V

-

N

-

R

R

G

L

V

D

E

E

I

I

Q

T

S

A

E

D

L

V

V

D

Y

A

S

D

S

P

K

R

S

A

L

A

I

Y

L

F

N

R

Q

Q

V

A

E

K

N

N

G
|
G

L

L

F

F

I

I

R

R

M

M

A

A

V

L

Y

L

K

K

Y

L

L

L

active site: R121 (= R104), H149 (= H132), Q152 (= Q135), T243 (≠ L219), P283 (= P260), G309 (= G288)
binding phosphoric acid mono(formamide)ester: S68 (= S52), T69 (= T53), R70 (= R54), T71 (= T55), R121 (= R104), H149 (= H132), Q152 (= Q135), P283 (= P260)

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)
35% identity, 98% coverage: 2:295/301 of query aligns to 1937:2232/2244 of Q09794

query
sites
Q09794

K

K

D

H

L

I

Y

I

S

S

V

V

N

H

Q

Q

L

V

E

T

K

R

E

S

D

D

I

L

Q

H

K

V

I

L

F

F

Q

A

L

I

A

A

K

-

E

-

Y

H

K

Q

E

M

R

R

F

I

L

I

K

V

G

E

E

R

K

Q

K

G

F

V

N

I

D

D

L

L

R

C

R

Y

C

G

S

K

I

L

L

L

L

C

-

T

V

M

F

F

E

E

N

P

S

S

T

T

R

R

T

T

R

S

T

S

S

S

F

F

E

D

L

A

A

A

G

M

K

Q

I

R

L

L

G

G

A

G

D

K

T

V

I

V

N

A

I

V

S

T

A

A

S

S

S

A

S

S

V

V

K

N

K

K

G

G

E

E

T

S

L

L

Y

A

D

D

T

T

V

I

K

R

T

T

L

L

E

-

A

G

L

C

N

Y

S

G

D

D

F

A

I

I

V

V

I

L

R

R

H

H

N

P

M

S

S

I

G

E

A

S

A

A

K

R

I

I

V

A

A

A

N

N

S

F

V

S

K

P

S

V

H

P

V

I

N

N

A

G

G

G

D

N

G

G

T

S

N

K

E

E

H

H

P

P

T

T

Q

Q

A

A

L

F

L

L

D

D

G

L

F

Y

T

T

I

I

L

R

E

E

K

E

K

L

G

G

S

S

L

V

E

N

G

G

L

L

K

T

I

I

A

T

I

F

V

I

G

G

D

D

I

L

L

K

H

Y

S

G

R

R

V

T

A

V

R

H

S

S

D

L

I

A

K

R

L

L

F

L

K

A

K

F

L

W

G

H

A

V

E

E

V

L

T

H

L

L

C

V

G

S

P

P

M

E

T

Q

M

L

-

A

L

L

P

P

R

D

H

D

Y

V

E

K

-

D

-

I

-

R

A

A

L

N

G

G

A

L

D

N

Y

F

I

I

T

E

T

H

D

R

-

E

-

L

I

T

K

K

E

E

A

V

V

V

K

A

N

Q

K

S

D

D

V

V

V

L

I

Y

F

C

L

T

R

R

I

V

Q

Q

L

K

E

E

R

R

Q

-

D

-

K

-

P

-

F

-

F

F

S

A

T

S

L

V

R

D

E

E

Y

Y

S

E

-

K

-

L

-

K

I

D

K

S

Y

F

G

I

L

V

N

D

Q

N

E

S

L

V

L

L

K

A

I

S

L

A

K

K

P

S

D

H

T

C

V

I

I

V

M

M

H

H

P

P

G

L

P

P

V

R

N

N

R

R

G

-

V

-

E

E

I

I

Q

S

S

E

E

E

L

V

V

D

Y

F

S

D

S

Q

-

R

K

R

S

A

L

A

I

Y

L

F

N

R

Q

Q

V

M

E

R

N

Y

G

G

L

L

F

Y

I

I

R

R

M

M

A

A

V

L

Sites not aligning to the query:

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

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)
34% identity, 98% coverage: 2:295/301 of query aligns to 1911:2205/2214 of P07259

query
sites
P07259

K

R

D

H

L

I

Y

L

S

S

V

I

N

K

Q

Q

L

F

E

K

K

R

E

S

D

D

I

F

Q

H

K

V

I

L

F

F

Q

A

L

V

A

A

K

Q

E

E

Y

L

K

R

E

A

R

A

F

V

L

A

K

R

G

-

E

E

K

G

K

V

F

L

N

D

D

L

L

M

R

K

R

G

C

H

S

V

I

I

L

T

V

I

F

F

E

E

N

P

S

S

T

T

R

R

T

T

R

C

T

S

S

S

F

F

E

I

L

A

A

A

G

M

K

E

I

R

L

L

G

G

A

G

D

R

T

I

I

V

N

N

I

V

S

N

A

P

S

L

S

V

S

S

V

V

K

K

G

G

E

E

T

T

L

L

Y

Q

D

D

T

T

V

I

K

R

T

T

L

L

E

-

A

A

L

C

N

Y

S

S

D

D

F

A

I

I

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Sites not aligning to the query:

1857 modified: Phosphoserine; by PKA

Query Sequence

>WP_012674077.1 NCBI__GCF_000021545.1:WP_012674077.1
MKDLYSVNQLEKEDIQKIFQLAKEYKERFLKGEKKFNDLRRCSILLVFFENSTRTRTSFE
LAGKILGADTINISASSSSVKKGETLYDTVKTLEALNSDFIVIRHNMSGAAKIVANSVKS
HVVNAGDGTNEHPTQALLDGFTILEKKGSLEGLKIAIVGDILHSRVARSDIKLFKKLGAE
VTLCGPMTMLPRHYEALGADYITTDIKEAVKNKDVVIFLRIQLERQDKPFFSTLREYSIK
YGLNQELLKILKPDTVIMHPGPVNRGVEIQSELVYSSKSLILNQVENGLFIRMAVYKYLL
S

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