SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012502870.1 NCBI__GCF_000020505.1:WP_012502870.1 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)

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)
40% identity, 100% coverage: 1:307/308 of query aligns to 1:291/291 of 4bjhB

query
sites
4bjhB

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active site: R47 (= R55), T48 (= T56), K75 (= K83), R97 (= R105), H126 (= H133), Q129 (= Q136)
binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S53), T46 (= T54), R47 (= R55), T48 (= T56), R97 (= R105), H126 (= H133), R159 (= R166), V160 (= V167), R213 (= R220), Q215 (= Q222), G251 (= G261)

3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
40% identity, 100% coverage: 1:307/308 of query aligns to 1:291/291 of 3d6nB

query
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3d6nB

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active site: R47 (= R55), T48 (= T56), K75 (= K83), R97 (= R105), H126 (= H133), Q129 (= Q136)
binding citrate anion: T48 (= T56), R97 (= R105), H126 (= H133), R159 (= R166), V160 (= V167), R213 (= R220), G251 (= G261)

6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
37% identity, 99% coverage: 1:306/308 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 (= S53), T49 (= T54), R50 (= R55), T51 (= T56), S75 (= S80), K78 (= K83), R100 (= R105), H127 (= H133), R160 (= R166), R210 (= R220), Q212 (= Q222), A253 (≠ G261)

3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
39% identity, 99% coverage: 1:306/308 of query aligns to 1:289/290 of 3r7lA

query
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3r7lA

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L

L

active site: R49 (= R55), T50 (= T56), K77 (= K83), R99 (= R105), H127 (= H133), Q130 (= Q136), L210 (= L219), P249 (= P260), G277 (= G294)
binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S53), T48 (= T54), R49 (= R55), T50 (= T56), S74 (= S80), K77 (= K83), R99 (= R105), H127 (= H133), R160 (= R166), 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)
39% identity, 99% coverage: 1:306/308 of query aligns to 1:289/304 of P05654

query
sites
P05654

M

M

N

K

H

H

L

L

T

T

G

T

L

M

F

S

G

E

L

L

P

S

A

T

S

E

T

E

L

I

V

K

E

D

L

L

D

Q

L

T

A

A

A

Q

G

E

Y

L

R

K

E

S

G

G

L

K

N

T

R

D

E

N

P

Q

E

-

T

-

F

-

A

-

P

-

L

-

L

L

S

T

N

G

R

K

R

F

I

A

A

A

L

N

V

L

F

F

E

E

N

P

S

S

T

T

R

R

T

T

R

R

F

F

S

S

F

F

E

E

L

V

A

A

A

E

R

K

H

K

L

L

G

G

A

M

G

N

T

V

L

L

S

N

F

L

T

D

A

G

A

T

S

S

S

T

S

S

V

V

S

Q

K

K

G

G

E

E

T

T

L

L

S

Y

D

D

T

T

I

I

R

R

N

T

L

L

E

E

A

S

M

I

K

G

V

V

D

D

A

V

F

C

V

V

L

I

R

R

H

H

P

S

S

E

S

D

G

E

A

Y

D

E

F

E

V

L

T

V

S

S

I

Q

T

V

N

N

R

I

P

P

V

I

I

L

N

N

A

A

G

G

D

D

G

G

T

C

H

G

E

Q

H

H

P

P

T

T

Q

Q

A

S

L

L

D

D

I

L

L

M

T

T

L

I

R

Y

S

E

Y

E

F

F

G

N

K

T

I

F

E

K

G

G

L

L

K

T

I

V

M

S

I

I

L

H

G

G

D

D

I

I

L

K

H

H

S

S

R

R

V

V

A

A

R

R

S

S

N

N

I

A

L

E

G

V

L

L

K

T

T

R

L

L

G

G

A

A

E

R

I

V

A

L

V

F

C

S

A

G

P

P

S

S

T

-

L

-

P

E

G

W

R

Q

I

D

D

E

Q

E

L

N

G

T

V

F

Q

G

V

T

F

Y

T

V

N

S

L

M

D

D

K

E

A

A

L

V

A

E

W

S

A

S

D

D

A

V

I

M

V

L

L

L

R

R

L

I

Q

Q

L

N

E

E

R

R

A

H

T

Q

G

S

G

A

Y

V

I

-

P

-

S

S

L

Q

E

E

E

G

Y

Y

S

L

A

N

G

K

Y

Y

G

G

L

L

T

T

D

V

E

E

K

R

F

A

D

E

R

R

L

M

K

K

R

R

L

H

M

A

P

I

V

I

L

M

H

H

P

P

G

A

P

P

I

V

N

N

R

R

E

G

I

V

E

E

I

I

S

D

N

D

M

S

V

L

A

V

D

E

R

S

I

-

Q

-

P

-

G

-

Y

-

S

E

S

K

S

S

M

R

L

I

M

F

E

K

Q

Q

V

M

T

K

N

N

G

G

V

V

A

F

V

I

R

R

M

M

A

A

V

V

L

I

H

Q

R

R

L

A

L

L

Sites not aligning to the query:

303 modified: Phosphoserine

3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
39% identity, 99% coverage: 1:306/308 of query aligns to 1:289/291 of 3r7fA

query
sites
3r7fA

M

M

N

K

H

H

L

L

T

T

G

T

L

M

F

S

G

E

L

L

P
x
S

A
x
T

S

E

T

E

L

I

V

K

E

D

L

L

D

Q

L

T

A

A

A
x
Q

G

E

Y

L

R
x
K

E

S

G

G

L

K

N

T

R

D

E

N

P

Q

E

-

T

-

F

-

A

-

P

-

L

-

L

L

S

T

N

G

R

K

R

F

I

A

A

A

L

N

V

L

F

F

E

E

N

P

S
|
S

T
|
T

R
|
R

T
|
T

R

R

F

F

S

S

F

F

E

E

L

V

A

A

A

E

R

K

H

K

L

L

G

G

A

M

G

N

T

V

L

L

S

N

F

L

T

D

A

G

A

T

S

S

S

T

S

S

V

V

S

Q

K
|
K

G

G

E

E

T

T

L

L

S

Y

D

D

T

T

I

I

R

R

N

T

L

L

E

E

A

S

M

I

K

G

V

V

D

D

A

V

F

C

V

V

L

I

R
|
R

H

H

P

S

S

E

S

D

G

E

A

Y

D

E

F

E

V

L

T

V

S

S

I

Q

T

V

N

N

R

I

P

P

V

I

I

L

N

N

A

A

G

G

D

D

G

G

T

C

H

G

E

Q

H
|
H

P

P

T

T

Q
|
Q

A

S

L

L

D

D

I

L

L

M

T

T

L

I

R

Y

S
x
E

Y

E

F

F

G

N

K

T

I

F

E

K

G

G

L

L

K

T

I

V

M

S

I

I

L

H

G

G

D

D

I

I

L

K

H

H

S

S

R

R

V

V

A

A

R

R

S

S

N

N

I

A

L

E

G

V

L

L

K

T

T
x
R

L

L

G

G

A

A

E

R

I

V

A

L

V

F

C

S

A

G

P

P

S

S

T

-

L

-

P

E

G

W

R

Q

I

D

D

E

Q

E

L

N

G

T

V

F

Q

G

V

T

F

Y

T

V

N

S

L

M

D

D

K

E

A

A

L

V

A

E

W

S

A

S

D

D

A

V

I

M

V

L

L
|
L

R

R

L

I

Q

Q

L

N

E

E

R

R

A

H

T

Q

G

S

G

A

Y

V

I

-

P

-

S

S

L

Q

E

E

E

G

Y

Y

S

L

A

N

G

K

Y

Y

G

G

L

L

T

T

D

V

E

E

K

R

F

A

D

E

R

R

L

M

K
|
K

R

R

L
x
H

M

A

P

I

V

I

L

M

H

H

P
|
P

G
x
A

P

P

I

V

N

N

R

R

E

G

I

V

E

E

I

I

S

D

N

D

M

S

V

L

A

V

D

E

R

S

I

-

Q

-

P

-

G

-

Y

-

S

E

S

K

S

S

M

R

L

I

M

F

E
x
K

Q

Q

V

M

T
x
K

N

N

G
|
G

V

V

A

F

V

I

R

R

M

M

A

A

V

V

L

I

H

Q

R

R

L

A

L

L

active site: R49 (= R55), T50 (= T56), K77 (= K83), R99 (= R105), H127 (= H133), Q130 (= Q136), L210 (= L219), P249 (= P260), G277 (= G294)
binding phosphoric acid mono(formamide)ester: S47 (= S53), T48 (= T54), R49 (= R55), T50 (= T56), R99 (= R105), H127 (= H133), Q130 (= Q136), P249 (= P260), A250 (≠ G261)
binding phosphate ion: S11 (≠ P11), T12 (≠ A12), Q23 (≠ A23), K26 (≠ R26), E140 (≠ S146), R171 (≠ T177), K241 (= K252), H243 (≠ L254), K272 (≠ E289), K272 (≠ E289), K275 (≠ T292)

3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
39% identity, 99% coverage: 1:306/308 of query aligns to 1:289/291 of 3r7dA

query
sites
3r7dA

M

M

N

K

H

H

L

L

T

T

G

T

L

M

F

S

G

E

L

L

P
x
S

A
x
T

S

E

T

E

L

I

V

K

E

D

L

L

D

Q

L

T

A

A

A

Q

G

E

Y

L

R

K

E

S

G

G

L

K

N

T

R

D

E

N

P

Q

E

-

T

-

F

-

A

-

P

-

L

-

L

L

S

T

N

G

R

K

R

F

I

A

A

A

L

N

V

L

F

F

E

E

N

P

S

S

T

T

R
|
R

T
|
T

R

R

F

F

S

S

F

F

E

E

L

V

A

A

A

E

R

K

H

K

L

L

G

G

A

M

G

N

T

V

L

L

S

N

F

L

T

D

A

G

A

T

S

S

S
x
T

S
|
S

V

V

S

Q

K
|
K

G

G

E

E

T

T

L

L

S

Y

D

D

T

T

I

I

R

R

N

T

L

L

E

E

A

S

M

I

K

G

V

V

D

D

A

V

F

C

V

V

L

I

R
|
R

H

H

P

S

S

E

S

D

G

E

A

Y

D

E

F

E

V

L

T

V

S

S

I

Q

T

V

N

N

R

I

P

P

V

I

I

L

N

N

A

A

G

G

D

D

G

G

T

C

H

G

E

Q

H
|
H

P

P

T

T

Q
|
Q

A

S

L

L

D

D

I

L

L

M

T

T

L

I

R

Y

S

E

Y

E

F

F

G

N

K

T

I

F

E

K

G

G

L

L

K

T

I

V

M

S

I

I

L

H

G

G

D

D

I

I

L

K

H

H

S

S

R

R

V

V

A

A

R

R

S

S

N

N

I

A

L

E

G

V

L

L

K

T

T
x
R

L

L

G

G

A

A

E

R

I

V

A

L

V

F

C

S

A

G

P

P

S

S

T

-

L

-

P

E

G

W

R

Q

I

D

D

E

Q

E

L

N

G

T

V

F

Q

G

V

T

F

Y

T

V

N

S

L

M

D

D

K

E

A

A

L

V

A

E

W

S

A

S

D

D

A

V

I

M

V

L

L
|
L

R

R

L

I

Q

Q

L

N

E

E

R

R

A

H

T

Q

G

S

G

A

Y

V

I

-

P

-

S

S

L

Q

E

E

E

G

Y

Y

S

L

A

N

G

K

Y

Y

G

G

L

L

T

T

D

V

E

E

K

R

F

A

D

E

R

R

L

M

K

K

R

R

L

H

M

A

P

I

V

I

L

M

H

H

P
|
P

G

A

P

P

I

V

N

N

R

R

E

G

I

V

E

E

I

I

S

D

N

D

M

S

V

L

A

V

D

E

R

S

I

-

Q

-

P

-

G

-

Y

-

S

E

S

K

S

S

M

R

L

I

M

F

E

K

Q

Q

V

M

T

K

N

N

G
|
G

V

V

A

F

V

I

R

R

M

M

A

A

V

V

L

I

H

Q

R

R

L

A

L

L

active site: R49 (= R55), T50 (= T56), K77 (= K83), R99 (= R105), H127 (= H133), Q130 (= Q136), L210 (= L219), P249 (= P260), G277 (= G294)
binding phosphate ion: S11 (≠ P11), T12 (≠ A12), T73 (≠ S79), S74 (= S80), K77 (= K83), R171 (≠ T177)

1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
38% identity, 84% coverage: 45:302/308 of query aligns to 46:300/307 of 1ml4A

query
sites
1ml4A

I

L

A

A

L

T

V

L

F

F

E

E

N

P

S
|
S

T
|
T

R
|
R

T
|
T

R

R

F

L

S

S

F

F

E

E

L

S

A

A

A

M

R

H

H

R

L

L

G

G

A

G

G

A

T

V

L

I

S

G

F

F

T

A

A

E

A

A

S

S

-

T

S

S

V

V

S

K

K
|
K

G

G

E

E

T

S

L

L

S

R

D

D

T

T

I

I

R

K

N

T

L

V

E

E

A

Q

M

Y

K

-

V

C

D

D

A

V

F

I

V

V

L

I

R
|
R

H

H

P

P

S

K

S

E

G

G

A

A

D

R

F

L

V

A

T

A

S

E

I

V

T

A

N

E

R

V

P

P

V

V

I

I

N

N

A

A

G

G

D

D

G

G

T

S

H

N

E

Q

H
|
H

P

P

T

T

Q
|
Q

A

T

L

L

D

D

I

L

L

Y

T

T

L

I

R

K

S

K

Y

E

F

F

G

G

K

R

I

I

E

D

G

G

L

L

K

K

I

I

M

G

I

L

L

L

G

G

D

D

I

L

L

K

H

Y

S

G

R
|
R

V
x
T

A

V

R

H

S

S

N

L

I

A

L

E

G

A

L

L

K

T

T

F

L

Y

G

D

A

V

E

E

I

L

A

Y

V

L

C

I

A

S

P

P

S

E

T

L

L

L

-

R

L

M

P

P

G

R

R

H

I

I

-

V

-

E

-

L

D

R

Q

E

L

K

G

G

V

M

Q

K

V

V

F

V

-

E

-

T

T

T

N

T

L

L

D

E

K

D

A

V

L

I

A

G

W

K

A

L

D

D

A

V

A

L

I

Y

V

V

L
x
T

R
|
R

L

I

Q

Q

L

K

E

E

R

R

A

-

T

-

G

-

Y

-

I

F

P

P

S

D

L

E

E

Q

E

E

Y

Y

-

L

-

K

-

V

S

K

A

G

G

S

Y

Y

G

Q

L

V

T

N

D

L

E

K

K

V

F

L

D

E

R

K

L

A

K

K

R

D

L

E

M

L

P

R

V

I

L

M

H

H

P
|
P

G
x
L

P

P

I

R

N

V

R

D

E

E

I

I

-

H

-

P

E

E

I

V

S

D

N

N

M

T

V

-

A

-

D

-

R

-

I

-

Q

-

P

-

G

-

Y

-

S

K

S

H

S

A

M

I

L

Y

M

F

E

R

Q

Q

V

V

T

F

N

N

G
|
G

V

V

A

P

V

V

R

R

M

M

A

A

V

L

L

L

active site: R56 (= R55), T57 (= T56), K85 (= K83), R106 (= R105), H134 (= H133), Q137 (= Q136), T227 (≠ L219), P266 (= P260), G292 (= G294)
binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S53), T55 (= T54), R56 (= R55), T57 (= T56), R106 (= R105), H134 (= H133), R167 (= R166), T168 (≠ V167), R228 (= R220), L267 (≠ G261)

5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
33% identity, 100% coverage: 2:308/308 of query aligns to 6:306/307 of 5g1nE

query
sites
5g1nE

N

Q

H

H

L

I

T

L

G

S

L

V

F

Q

G

Q

L

F

P

T

A

K

S

D

T

Q

L

M

V

S

E

H

L

L

L

F

D

N

L

V

A

A

A

H

G

T

Y

L

R

R

E

M

G

M

L

V

N

Q

R

K

E

E

P

R

E

S

T

L

F

-

A

-

P

D

L

I

L

L

S

K

N

G

R

K

R

V

I

M

A

A

L

S

V

M

F

F

F

Y

E

E

N

V

S
|
S

T
|
T

R
|
R

T
|
T

R

S

F

S

S

S

F

F

E

A

L

A

A

A

A

M

R

A

H

R

L

L

G

G

A

G

G

A

T

V

L

L

S

S

F

F

T

S

A

E

A

A

S

T

S

S

S
|
S

V

V

S

Q

K
|
K

G

G

E

E

T

S

L

L

S

A

D

D

T

S

I

V

R

Q

N

T

L

M

E

S

A

C

M

Y

K

-

V

A

D

D

A

V

F

V

V

V

L

L

R
|
R

H

H

P

P

S

Q

S

P

G

G

A

A

A

V

D

E

F

L

V

A

T

A

S

K

I

H

T

C

N

R

R

R

P

P

V

V

I

I

N

N

A

A

G

G

D

D

G

G

T

V

H

G

E

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

L

D

D

I

I

L

F

T

T

L

I

R

R

S

E

Y

E

F

L

G

G

K

T

I

V

E

N

G

G

L

M

K

T

I

I

M

T

I

M

L

V

G

G

D

D

I

L

L

K

H

H

S

G

R
|
R

V

T

A

V

R

H

S

S

N

L

I

A

L

C

G

L

L

L

K

T

T

Q

L

Y

G

R

A

V

E

S

I

L

A

R

V

Y

C

V

A

A

P

P

S

P

T

S

L

L

-

R

L

M

P

P

G

P

R

T

I

V

D

R

Q

A

L

F

-

V

-

A

-

S

-

R

-

G

-

T

G

K

V

Q

Q

E

V

E

F

F

T

E

N

S

L

I

D

E

K

E

A

A

L

L

A

P

W

D

A

T

D

D

A

V

A

L

I

Y

V

M

L
x
T

R
|
R

L

I

Q
|
Q

L

K

E

E

R

R

A

-

T

-

G

-

Y

-

I

F

P

G

S

S

L

T

E

Q

E

E

Y

Y

S

E

A

A

G

C

Y

F

G

G

-

Q

-

F

-

I

L

L

T

T

D

P

E

H

K

I

F

M

D

T

R

R

L

A

K

K

R

K

L

K

M

M

P

V

V

V

L

M

H

H

P
|
P

G
x
M

P

P

I

R

N

V

R

N

E

E

I

I

E

S

I

V

S

E

N

-

M

-

V

-

A

V

D

D

R

S

I

D

Q

P

P

R

P

A

G

A

Y

Y

S

-

M

-

L

-

M

F

E

R

Q

Q

V

A

T

E

N

N

G
|
G

V

M

A

Y

V

I

R

R

M

M

A

A

V

L

L

L

H

A

R

T

L

V

L

L

A

G

K

R

active site: R57 (= R55), T58 (= T56), K85 (= K83), R106 (= R105), H134 (= H133), Q137 (= Q136), T227 (≠ L219), P266 (= P260), G292 (= G294)
binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S53), T56 (= T54), R57 (= R55), T58 (= T56), S82 (= S80), K85 (= K83), R106 (= R105), H134 (= H133), R167 (= R166), R228 (= R220), Q230 (= Q222), M267 (≠ 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)
36% identity, 88% coverage: 39:308/308 of query aligns to 1959:2224/2225 of P27708

query
sites
P27708

L
x
I

L
|
L

S
x
K

N
x
G

R
x
K

R
x
V

I
x
M

A
|
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

F
x
S

S
|
S

F
|
F

E
x
A

L
x
A

A
|
A

A
x
M

R
x
A

H
x
R

L
|
L

G
|
G

A
x
G

G
x
A

T
x
V

L
|
L

S
|
S

F
|
F

T
x
S

A
x
E

A
|
A

S
x
T

S
|
S

V
|
V

S
x
Q

K
|
K

G
|
G

E
|
E

T
x
S

L
|
L

S
x
A

D
|
D

T
x
S

I
x
V

R
x
Q

N
x
T

L
x
M

E
x
S

A
x
C

M
x
Y

K

-

V
x
A

D
|
D

A
x
V

F
x
V

V
|
V

L
|
L

R
|
R

H
|
H

P
|
P

S
x
Q

S
x
P

G
|
G

A
|
A

A
x
V

D
x
E

F
x
L

V
x
A

T
x
A

S
x
K

I
x
H

T
x
C

N
x
R

R
|
R

P
|
P

V
|
V

I
|
I

N
|
N

A
|
A

G
|
G

D
|
D

G
|
G

T
x
V

H
x
G

E
|
E

H
|
H

P
|
P

T
|
T

Q
|
Q

A
|
A

L
|
L

D
|
D

I
|
I

L
x
F

T
|
T

L
x
I

R
|
R

S
x
E

Y
x
E

F
x
L

G
|
G

K
x
T

I
x
V

E
x
N

G
|
G

L
x
M

K
x
T

I
|
I

M
x
T

I
x
M

L
x
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

N
x
L

I
x
A

L
x
C

G
x
L

L
|
L

K
x
T

T
x
Q

L
x
Y

G
x
R

A
x
V

E
x
S

I
x
L

A
x
R

V
x
Y

C
x
V

A
|
A

P
|
P

S
x
P

T
x
S

L
|
L

-
x
R

L
x
M

P
|
P

G
x
P

R
x
T

I
x
V

D
x
R

Q
x
A

L
x
F

-
x
V

-
x
A

-
x
S

-
x
R

-
x
G

-
x
T

G
x
K

V
x
Q

Q
x
E

V
x
E

F
|
F

T
x
E

N
x
S

L
x
I

D
x
E

K
x
E

A
|
A

L
|
L

A
x
P

W
x
D

A
x
T

D
|
D

A
x
V

A
x
L

I
x
Y

V
x
M

L
x
T

R
|
R

L
x
I

Q
|
Q

L
x
K

E
|
E

R
|
R

A

-

T

-

G

-

Y

-

I
x
F

P
x
G

S
|
S

L
x
T

E
x
Q

E
|
E

Y
|
Y

S
x
E

A
|
A

G
x
C

Y
x
F

G
|
G

-
x
Q

-
x
F

-
x
I

L
|
L

T
|
T

D
x
P

E
x
H

K
x
I

F
x
M

D
x
T

R
|
R

L
x
A

K
|
K

R
x
K

L
x
K

M
|
M

P
x
V

V
|
V

L
x
M

H
|
H

P
|
P

G
x
M

P
|
P

I
x
R

N
x
V

R
x
N

E
|
E

I
|
I

E
x
S

I
x
V

S
x
E

N
x
V

M
x
D

V
x
S

A
x
D

D
x
P

R
|
R

I

-

Q

-

P

-

G

-

Y

-

S

-

S
x
A

M
x
A

L
x
Y

M
x
F

E
x
R

Q
|
Q

V
x
A

T
x
E

N
|
N

G
|
G

V
x
M

A
x
Y

V
x
I

R
|
R

M
|
M

A
|
A

V
x
L

L
|
L

H
x
A

R
x
T

L
x
V

L
|
L

A
x
G

K
x
R

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 ; binding ; H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
1473 binding ; H→A: No zinc-binding and no catalytic activity.
1475 binding
1505 binding
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 ; H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
1613 binding ; C→S: Reduces dihydroorotase activity.
1614 binding ; H→A: Abolishes dihydroorotase activity.
1637 binding ; E→T: Abolishes dihydroorotase activity.
1642 H→N: 11.5% of wild-type catalytic activity.
1661 binding
1686 binding ; D→N: Abolishes dihydroorotase activity.
1690 binding ; H→N: 3% of wild-type catalytic activity.
1702 binding
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)
36% identity, 88% coverage: 39:308/308 of query aligns to 1959:2224/2225 of P08955

query
sites
P08955

L

I

L

L

S

K

N

G

R

K

R

V

I

M

A

A

L

S

V

M

F

F

F

Y

E

E

N

V

S

S

T

T

R

R

T

T

R

S

F

S

S

S

F

F

E

A

L

A

A

A

A

M

R

A

H

R

L

L

G

G

A

G

G

A

T

V

L

L

S

S

F

F

T

S

A

E

A

A

S

T

S

S

V

V

S

Q

K

K

G

G

E

E

T

S

L

L

S

A

D

D

T

S

I

V

R

Q

N

T

L

M

E

S

A

C

M

Y

K

-

V

A

D

D

A

V

F

V

V

V

L

L

R

R

H

H

P

P

S

Q

S

P

G

G

A

A

A

V

D

E

F

L

V

A

T

A

S

K

I

H

T

C

N

R

R

R

P

P

V

V

I

I

N

N

A

A

G

G

D

D

G

G

T

V

H

G

E

E

H

H

P

P

T

T

Q

Q

A

A

L

L

D

D

I

I

L

F

T

T

L

I

R

R

S

E

Y

E

F

L

G

G

K

T

I

V

E

N

G

G

L

M

K

T

I

I

M

T

I

M

L

V

G

G

D

D

I

L

L

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

N

L

I

A

L

C

G

L

L

L

K

T

T

Q

L

Y

G

R

A

V

E

S

I

L

A

R

V

Y

C

V

A

A

P

P

S

P

T

S

L

L

-

R

L

M

P

P

G

P

R

S

I

V

D

W

Q

D

L

F

-

V

-

A

-

S

-

R

-

G

-

T

G

K

V

Q

Q

E

V

E

F

F

T

E

N

S

L

I

D

E

K

E

A

A

L

L

A

P

W

D

A

T

D

D

A

V

A

L

I

Y

V

M

L

T

R

R

L

I

Q

Q

L

K

E

E

R

R

A

-

T

-

G

-

Y

-

I

F

P

G

S

S

L

T

E

Q

E

E

Y

Y

S

E

A

A

G

C

Y

F

G

G

-

Q

-

F

-

I

L

L

T

T

D

P

E

H

K

I

F

M

D

T

R

R

L

A

K

K

R

K

L

K

M

M

P

V

V

V

L

M

H

H

P

P

G

M

P

P

I

R

N

V

R

N

E

E

I

I

E

S

I

V

S

E

N

V

M

D

V

S

A

D

D

P

R

R

I

-

Q

-

P

-

G

-

Y

-

S

-

S

A

M

A

L

Y

M

F

E

R

Q

Q

V

A

T

E

N

N

G

G

V

M

A

Y

V

I

R

R

M

M

A

A

V

L

L

L

H

A

R

T

L

V

L

L

A

G

K

R

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.

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, 86% coverage: 39:302/308 of query aligns to 1958:2217/2225 of P20054

query
sites
P20054

L

L

S

K

N

G

R

K

R

V

I

L

A

A

L

T

V

L

F

F

F

Y

E

E

N

P

S

S

T

T

R

R

T

T

R

Q

F

C

S

S

F

F

E

T

L

A

A

A

A

M

R

Q

H

R

L

L

G

G

A

G

G

S

T

V

L

V

S

T

F

V

T

D

A

N

A

V

S

S

V

V

S

A

K

K

G

G

E

E

T

S

L

I

S

A

D

D

T

T

I

I

R

Q

N

T

L

L

E

E

A

S

M

Y

K

-

V

C

D

D

A

A

F

V

V

C

L

M

R

R

H

H

P

P

S

A

S

V

G

G

A

S

A

V

D

E

F

S

V

A

T

I

S

Q

I

V

T

A

N

K

R

K

P

P

V

I

I

I

N

N

A

A

G

G

D

D

G

G

T

V

H

G

E

E

H

H

P

P

T

T

Q

Q

A

A

L

L

D

D

I

V

L

F

T

T

L

I

R

R

S

E

Y

E

F

L

G

G

K

T

I

V

E

N

G

G

L

L

K

T

I

I

M

T

I

V

L

V

G

G

D

D

I

L

L

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

N

L

I

V

L

R

G

L

L

L

K

A

T

N

L

Y

G

Q

A

V

E

K

I

I

A

N

V

Y

C

V

A

S

P

P

S

S

T

S

L

L

-

S

L

M

P

P

G

T

R

E

I

I

-

I

-

K

-

E

-

L

D

N

Q

E

L

K

G

G

V

I

Q

E

V

Q

-

K

-

E

F

Y

T

T

N

N

L

I

D

E

K

S

A

I

L

L

A

P

W

T

A

T

D

N

A

V

A

L

I

Y

V

V

L

T

R

R

L

V

Q

Q

L

K

E

E

R

R

A

-

T

-

G

-

Y

-

I

F

P

Q

S

S

L

I

E

E

Y

Y

S

E

A

K

-

V

-

K

-

D

G

S

Y

F

G

I

L

I

T

T

D

P

E

H

K

T

F

L

D

T

R

K

L

A

K

S

R

D

L

N

M

M

P

I

V

V

L

M

H

H

P

P

G

L

P

P

I

-

N

-

R

R

E

I

I

N

E

E

I

I

S

S

N

P

M

E

V

V

A

-

D

D

R

S

I

D

Q

P

P

R

P

A

G

A

Y

Y

S

-

M

-

L

-

M

F

E

R

Q

Q

V

M

T

E

N

N

G

G

V

L

A

Y

V

V

R

R

M

M

A

S

V

L

L

L

Sites not aligning to the query:

1 modified: N-acetylmethionine

4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
35% identity, 99% coverage: 1:306/308 of query aligns to 1:300/304 of 4eknB

query
sites
4eknB

M

M

N

K

H

H

L

L

T

I

G

S

L

M

F

K

G

D

L

I

P

G

A

K

S

E

T

E

L

I

V

L

E

E

L

I

L

L

D

D

L

E

A

A

A

R

G

K

Y

M

R

E

E

E

G

L

L

L

N

N

-

T

R

K

E

R

P

P

E

-

T

-

F

-

A

L

P

K

L

L

S

E

N

G

R

K

R

I

I

L

A

A

L

T

V

V

F

F

F

Y

E

E

N

P

S

S

T

T

R

R

T

T

R

R

F

L

S

S

F

F

E

E

L

T

A

A

A

M

R

K

H

R

L

L

G

G

A

G

G

E

T

V

L

I

S

T

F

M

T

T

A

D

-

L

A

K

S

S

V

V

S

A

K

K

G

G

E

E

T

S

L

L

S

I

D

D

T

T

I

I

R

R

N

V

L

I

E

S

A

G

M

Y

K

-

V

A

D

D

A

I

F

I

V

V

L

L

R

R

H

H

P

P

S

S

S

E

G

G

A

A

D

R

F

L

V

A

T

S

S

E

I

Y

T

S

N

Q

R

V

P

P

V

I

I

I

N

N

A

A

G

G

D

D

G

G

T

S

H

N

E

Q

H

H

P

P

T

T

Q

Q

A

T

L

L

D

D

I

L

L

Y

T

T

L

I

R

M

S

R

Y

E

F

I

G

G

K

R

I

I

E

D

G

G

L

I

K

K

I

I

M

A

I

F

L

V

G

G

D

D

I

L

L

K

H

Y

S
x
G

R
|
R

V
x
T

A

V

R

H

S

S

N

L

I

V

L

Y

G

A

L

L

K

S

T

L

L

F

-

E

G

N

A

V

E

E

I

M

A

Y

V

F

C

V

A

S

P

P

S

K

T

E

L

L

-

R

L

L

P

P

G

K

R

D

-

I

I

I

D

E

Q

D

L

L

G

K

V

A

Q

K

V

N

F

I

T

K

N

F

L

Y

D

E

K

K

A

E

-

S

-

L

-

D

-

L

L

D

A

D

W

D

A

I

D

D

A

V

A

L

I

Y

V

V

L
x
T

R
|
R

L

I

Q

Q

L

K

E

E

R

R

A

-

T

-

G

-

Y

-

I

F

P

P

S

D

L

P

E

N

E

E

Y

Y

-

E

-

K

-

V

S

K

A

G

G

S

Y

Y

G

K

L

I

T

K

D

R

E

E

K

Y

F

V

D

E

R

G

L

K

K

K

R

F

L

I

M

-

P

-

V

I

L

M

H

H

P
|
P

G

L

P

P

I

-

N

-

R

R

E

V

I

D

E

E

I

I

S

D

N

Y

M

D

V

V

A

D

D

D

R

L

I

P

Q

Q

P

A

P

K

G

Y

Y

F

S

K

S

Q

S

S

M

F

L

Y

M

-

E

-

Q

-

V

-

T

-

N

-

G
|
G

V

I

A

P

V

V

R

R

M

M

A

A

V

I

L

L

H

K

R

K

L

L

L

I

active site: T225 (≠ L219), P262 (= P260), G288 (= G294)
binding sulfate ion: G163 (≠ S165), R164 (= R166), T165 (≠ V167), R226 (= R220)

5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
32% identity, 100% coverage: 2:308/308 of query aligns to 3:291/292 of 5g1pA

query
sites
5g1pA

N

Q

H

H

L

I

T

L

G

S

L

V

F

Q

G

Q

L

F

P

T

A

K

S

D

T

Q

L

M

V

S

E

H

L

L

L

F

D

N

L

V

A

A

A

H

G

T

Y

L

R

R

E

M

G

M

L

V

N

Q

R

K

E

E

P

R

E

S

T

L

F

-

A

-

P

D

L

I

L

L

S

K

N

G

R

K

R

V

I

M

A

A

L

S

V

M

F

F

F

Y

E

E

N

V

S
|
S

T
|
T

R
|
R

T
|
T

R

S

F

S

S

S

F

F

E

A

L

A

A

A

A

M

R

A

H

R

L

L

G

G

A

G

G

A

T

V

L

L

S

S

F

F

T

S

A

E

A

A

S

T

S

S

V

V

S

Q

K
|
K

G

G

E

E

T

S

L

L

S

A

D

D

T

S

I

V

R

Q

N

T

L

M

E

S

A

C

M

Y

K

-

V

A

D

D

A

V

F

V

V

V

L

L

R
|
R

H

H

P

P

S

Q

S

P

G

G

A

A

A

V

D

E

F

L

V

A

T

A

S

K

I

H

T

C

N

R

R

R

P

P

V

V

I

I

N

N

A

A

G

G

D

D

G

G

T

V

H

G

E

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

L

D

D

I

I

L

F

T

T

L

I

R

R

S

E

Y

E

F

L

G

G

K

T

I

V

E

N

G

G

L

M

K

T

I

I

M

T

I

M

L

V

G

G

D

D

I

L

L

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

N

L

I

A

L

C

G

L

L

L

K

T

T

Q

L

Y

G

R

A

V

E

S

I

L

A

R

V

Y

C

V

A

A

P

P

S

P

T

S

L

L

-

R

L

M

P

P

G

P

R

T

I

V

D

R

Q

A

L

F

-

V

-

A

-

S

-

G

-

T

G

K

V

Q

Q

E

V

E

F

F

T

E

N

S

L

I

D

E

K

E

A

A

L

L

A

P

W

D

A

T

D

D

A

V

A

L

I

Y

V

M

L
x
T

R

R

L

I

Q

Q

L

K

E

E

R

R

A

F

T

Q

G

-

Y

-

I

-

P

-

S

-

L

-

E

-

Y

-

S

-

A

-

G

-

Y

F

G

I

L

L

T

T

D

P

E

H

K

I

F

M

D

T

R

R

L

A

K

K

R

K

L

K

M

M

P

V

V

V

L

M

H

H

P
|
P

G
x
M

P

P

I

R

N

V

R

N

E

E

I

I

E

S

I

V

S

E

N

-

M

-

V

-

A

V

D

D

R

S

I

D

Q

P

P

R

P

A

G

A

Y

Y

S

-

M

-

L

-

M

F

E

R

Q

Q

V

A

T

E

N

N

G
|
G

V

M

A

Y

V

I

R

R

M

M

A

A

V

L

L

L

H

A

R

T

L

V

L

L

A

G

K

R

active site: R54 (= R55), T55 (= T56), K82 (= K83), R103 (= R105), H131 (= H133), Q134 (= Q136), T223 (≠ L219), P251 (= P260), G277 (= G294)
binding phosphoric acid mono(formamide)ester: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R103 (= R105), Q134 (= Q136), M252 (≠ G261)

8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
34% identity, 93% coverage: 18:302/308 of query aligns to 32:311/316 of 8bplA

query
sites
8bplA

L

L

L

F

D

Q

L

I

A

A

A

Q

G

E

Y

M

R

R

E

L

G

G

L

V

N

Q

R

R

E

E

P

-

E

-

T

G

F

V

A

L

P

D

L

I

L

L

S

R

N

G

R

K

R

V

I

L

A

C

L

T

V

L

F

F

F

Y

E

E

N

P

S
|
S

T
|
T

R
|
R

T
|
T

R

S

F

A

S

S

F

F

E

D

L

A

A

A

A

M

R

Q

H

R

L

L

G

G

A

G

G

R

T

T

L

I

S

P

F

I

T

Q

A

T

A

S

S

T

S

S

V

V

S

Q

K

K

G

G

E

E

T

T

L

L

S

Q

D

D

T

T

I

L

R

R

N

T

L

L

E

-

A

A

M

C

K

Y

V

S

D

D

A

A

F

I

V

V

L

L

R
|
R

H

H

P

P

S

D

S

E

G

K

A

C

A

V

D

D

F

V

V

A

T

K

S

K

I

Y

T

C

N

P

R

V

P

P

V

V

I

I

N

N

A

G

G

G

D

N

G

G

T

S

H

K

E

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

F

L

L

D

D

I

L

L

F

T

T

L

I

R

R

S

E

Y

E

F

L

G

G

K

T

I

M

E

Q

G

G

L

L

K

T

I

I

M

T

I

F

L

V

G

G

D

D

I

L

L

L

H

Y

S

G

R

R

V

P

A

V

R

H

S

S

N

L

I

V

L

Y

G

L

L

L

K

R

T

H

L

Y

G

Q

A

V

E

K

I

V

A

Q

V

L

C

V

A

S

P

P

S

K

T

A

L

L

-

R

L

L

P

P

G

P

R

A

I

V

D

R

Q

Q

L

Q

G

L

V

V

-

D

-

A

-

G

Q

Q

V

L

F

L

T

C

N

E

L

S

D

E

-

A

-

L

-

T

-

P

K

E

A

I

L

L

A

G

W

R

A

T

D

D

A

V

A

L

I

Y

V

C

L

T

R

R

L

V

Q

Q

L

K

E

E

R

R

A

-

T

-

G

-

Y

-

I

F

P

P

S

S

L

L

E

A

E

E

Y

F

S

E

A

A

G

V

Y

K

G

D

L

S

T

Y

D

R

E

I

K

D

F

Y

D

S

R

T

L

L

K

K

R

Y

L

A

M

K

P

P

-

T

-

V

V

V

L

M

H

H

P

P

G
x
L

P

P

I

R

N

N

R

E

E

E

I

V

E

A

I

E

S

E

N

-

M

-

V

-

A

V

D

D

R

F

I

D

Q

Q

P

R

P

A

G

A

Y

Y

S

-

M

-

L

-

M

F

E

R

Q

Q

V

M

T

C

N

Y

G

G

V

L

A

Y

V

C

R

R

M

M

A

A

V

L

L

L

binding phosphoric acid mono(formamide)ester: S65 (= S53), T66 (= T54), R67 (= R55), T68 (= T56), R116 (= R105), H144 (= H133), Q147 (= Q136), L278 (≠ G261)

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)
37% identity, 86% coverage: 39:302/308 of query aligns to 1954:2213/2224 of P05990

query
sites
P05990

L

L

S

P

N

G

R

K

R

I

I

M

A

A

L

S

V

V

F

F

F

Y

E

E

N

V

S

S

T

T

R

R

T

T

R

Q

F

C

S

S

F

F

E

A

L

A

A

A

A

M

R

L

H

R

L

L

G

G

A

G

G

R

T

V

L

I

S

S

F

M

T

D

A

N

A

I

S

T

S

S

V

V

S

K

K

K

G

G

E

E

T

S

L

L

S

E

D

D

T

S

I

I

R

K

N

V

L

V

E

S

A

S

M

Y

K

-

V

A

D

D

A

V

F

V

V

V

L

L

R

R

H

H

P

P

S

S

S

P

G

G

A

A

A

V

D

A

F

R

V

A

T

A

S

T

I

F

T

S

N

R

R

K

P

P

V

L

I

I

N

N

A

A

G

G

D

D

G

G

T

V

H

G

E

E

H

H

P

P

T

T

Q

Q

A

A

L

L

D

D

I

I

L

F

T

T

L

I

R

R

S

E

Y

E

F

F

G

G

K

T

I

V

E

N

G

G

L

L

K

T

I

I

M

T

I

M

L

V

G

G

D

D

I

L

L

K

H

N

S

G

R

R

V

T

A

V

R

H

S

S

N

L

I

A

L

R

G

L

L

L

K

T

T

L

L

Y

G

N

A

V

E

N

I

L

A

Q

V

Y

C

V

A

A

P

P

S

N

T

S

L

L

-

Q

L

M

P

P

G

D

R

E

I

V

D

V

Q

Q

L

F

-

V

-

H

-

Q

-

R

G

G

V

V

-

K

Q

Q

V

L

F

F

T

A

-

R

N

D

L

L

D

K

K

N

A

V

L

L

A

P

W

D

A

T

D

D

A

V

A

L

I

Y

V

M

L

T

R

R

L

I

Q

Q

L

R

E

E

R

R

A

-

T

-

G

-

Y

-

I

F

P

D

S

N

L

V

E

E

E

D

Y

Y

S

E

A

K

G

C

Y

C

G

G

-

H

-

L

-

V

L

L

T

T

D

P

E

E

K

H

F

M

D

M

R

R

L

A

K

K

R

K

L

R

M

S

P

I

V

V

L

L

H

H

P

P

G

L

P

P

-

R

-

L

-

N

-

E

I

I

N

S

R

R

E

E

I

I

E

D

I

S

S

D

N

P

M

R

V

A

A

A

D

-

R

-

I

-

Q

-

P

-

G

-

Y

-

S

-

M

-

L

Y

M

F

E

R

Q

Q

V

A

T

E

N

Y

G

G

V

M

A

Y

V

I

R

R

M

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

2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
36% identity, 92% coverage: 21:302/308 of query aligns to 24:300/310 of 2hseA

query
sites
2hseA

L

L

A

A

A

T

G

A

Y

A

R

K

E

L

G

K

L

A

N

N

R

P

E

Q

P

P

E

E

T

-

F

-

A

-

P

-

L

L

S

K

N

H

R

K

R

V

I

I

A

A

L

S

V

C

F

F

E

E

N

A

S
|
S

T
|
T

R
|
R

T
|
T

R

R

F

L

S
|
S

F

F

E

E

L

T

A

S

A

M

R

H

H

R

L

L

G

G

A

A

G

S

T

V

L

V

S

G

F

F

T

S

-

D

-

S

A

A

A

N

S

T

S

S

S

L

V

G

S

K

K
|
K

G

G

E

E

T

T

L

L

S

A

D

D

T

T

I

I

R

-

N

S

L

V

E

I

A

S

M

T

K

Y

V

V

D

D

A

A

F

I

V

V

L

M

R
|
R

H

H

P

P

S

Q

S

E

G

G

A

A

D

R

F

L

V

A

T

T

S

E

I

F

T

S

-

G

N

N

R

V

P

P

V

V

I

L

N

N

A

A

G

G

D

D

G

G

T

S

H

N

E

Q

H
|
H

P

P

T

T

Q
|
Q

A

T

L

L

D

D

I

L

L

F

T

T

L

I

R

Q

S

E

Y

T

F

Q

G

G

K

R

I

L

E

D

G

N

L

L

K

H

I

V

M

A

I

M

L

V

G

G

D

D

I

L

L

K

H

Y

S

G

R
|
R

V

T

A

V

R

H

S

S

N

L

I

T

L

Q

G

A

L

L

-

A

K

K

T

F

L

D

G

G

A

N

E

R

I

F

A

Y

V

F

C

I

A

A

P

P

S

D

T

A

L

L

-

A

L

M

P

P

G

Q

R

Y

I

I

-

L

-

D

-

M

-

L

D

D

Q

E

L

K

G

G

V

I

-

A

-

W

Q

S

V

L

F

H

T

S

N

S

L

I

D

E

K

E

A

V

L

M

A

A

W

E

A

V

D

D

A

I

A

L

I

Y

V

M

L
x
T

R
|
R

L

V

Q
|
Q

L

K

E

E

R

R

A

L

T

A

G

-

Y

-

I

-

P

P

S

S

L

-

E

-

E

E

Y

Y

S

A

-

N

-

V

-

K

A

A

G

Q

Y

F

G

V

L

L

T

R

D

A

E

S

K

D

F

L

D

H

R

N

L

A

K

K

R

A

L

N

M

M

P

K

V

V

L

L

H

H

P
|
P

G
x
L

P
|
P

I

-

N

-

R

R

E

V

I

D

E

E

I

I

S

A

N

T

M

D

V

V

A

-

D

D

R

K

I

T

Q

P

P

H

P

A

G

W

Y

Y

S

-

M

-

L

-

M

F

E

Q

Q

Q

V
x
A

T

G

N

N

G
|
G

V

I

A

F

V

A

R
|
R

M

Q

A

A

V

L

L

L

active site: R54 (= R55), T55 (= T56), K84 (= K83), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (≠ L219), P266 (= P260), G292 (= G294)
binding aspartic acid: R54 (= R55), T55 (= T56), S58 (= S59), R105 (= R105), H134 (= H133), Q137 (= Q136), R167 (= R166), R229 (= R220), Q231 (= Q222), L267 (≠ G261), P268 (= P262), A289 (≠ V291), R296 (= R298)
binding phosphonoacetamide: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R105), L267 (≠ G261)

2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
36% identity, 92% coverage: 21:302/308 of query aligns to 24:300/310 of 2a0fA

query
sites
2a0fA

L

L

A

A

A

T

G

A

Y

A

R

K

E

L

G

K

L

A

N

N

R

P

E

Q

P

P

E

E

T

-

F

-

A

-

P

-

L

L

S

K

N

H

R

K

R

V

I

I

A

A

L

S

V

C

F

F

E

E

N

A

S

S

T

T

R
|
R

T
|
T

R

R

F

L

S

S

F

F

E

E

L

T

A

S

A

M

R

H

H

R

L

L

G

G

A

A

G

S

T

V

L

V

S

G

F

F

T

S

-

D

-

S

A

A

A

N

S

T

S

S

S

L

V

G

S

K

K
|
K

G

G

E

E

T

T

L

L

S

A

D

D

T

T

I

I

R

-

N

S

L

V

E

I

A

S

M

T

K

Y

V

V

D

D

A

A

F

I

V

V

L

M

R
|
R

H

H

P

P

S

Q

S

E

G

G

A

A

D

R

F

L

V

A

T

T

S

E

I

F

T

S

-

G

N

N

R

V

P

P

V

V

I

L

N

N

A

A

G

G

D

D

G

G

T

S

H

N

E

Q

H
|
H

P

P

T

T

Q
|
Q

A

T

L

L

D

D

I

L

L

F

T

T

L

I

R

Q

S

E

Y

T

F

Q

G

G

K

R

I

L

E

D

G

N

L

L

K

H

I

V

M

A

I

M

L

V

G

G

D

D

I

L

L

K

H

Y

S

G

R

R

V

T

A

V

R

H

S

S

N

L

I

T

L

Q

G

A

L

L

-

A

K

K

T

F

L

D

G

G

A

N

E

R

I

F

A

Y

V

F

C

I

A

A

P

P

S

D

T

A

L

L

-

A

L

M

P

P

G

Q

R

Y

I

I

-

L

-

D

-

M

-

L

D

D

Q

E

L

K

G

G

V

I

-

A

-

W

Q

S

V

L

F

H

T

S

N

S

L

I

D

E

K

E

A

V

L

M

A

A

W

E

A

V

D

D

A

I

A

L

I

Y

V

M

L
x
T

R

R

L

V

Q

Q

L

K

E

E

R

R

A

L

T

A

G

-

Y

-

I

-

P

P

S

S

L

-

E

-

E

E

Y

Y

S

A

-

N

-

V

-

K

A

A

G

Q

Y

F

G

V

L

L

T

R

D

A

E

S

K

D

F

L

D

H

R

N

L

A

K

K

R

A

L

N

M

M

P

K

V

V

L

L

H

H

P
|
P

G
x
L

P

P

I

-

N

-

R

R

E

V

I

D

E

E

I

I

S

A

N

T

M

D

V

V

A

-

D

D

R

K

I

T

Q

P

P

H

P

A

G

W

Y

Y

S

-

M

-

L

-

M

F

E

Q

Q

Q

V

A

T

G

N

N

G
|
G

V

I

A

F

V

A

R

R

M

Q

A

A

V

L

L

L

active site: R54 (= R55), T55 (= T56), K84 (= K83), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (≠ L219), P266 (= P260), G292 (= G294)
binding phosphonoacetamide: R54 (= R55), T55 (= T56), H134 (= H133), Q137 (= Q136), L267 (≠ G261)

P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
36% identity, 92% coverage: 21:302/308 of query aligns to 25:301/311 of P0A786

query
sites
P0A786

L

L

A

A

A

T

G

A

Y

A

R

K

E

L

G

K

L

A

N

N

R

P

E

Q

P

P

E

E

T

-

F

-

A

-

P

-

L

L

S

K

N

H

R

K

R

V

I

I

A

A

L

S

V

C

F

F

E

E

N

A

S

S

T

T

R
|
R

T
|
T

R

R

F

L

S

S

F

F

E

E

L

T

A

S

A

M

R

H

H

R

L

L

G

G

A

A

G

S

T

V

L

V

S

G

F

F

T

S

-

D

-

S

A

A

A

N

S

T

S

S

S

L

V

G

S

K

K

K

G

G

E

E

T

T

L

L

S

A

D

D

T

T

I

I

R

-

N

S

L

V

E

I

A

S

M

T

K

Y

V

V

D

D

A

A

F

I

V

V

L

M

R
|
R

H

H

P

P

S

Q

S

E

G

G

A

A

D

R

F

L

V

A

T

T

S

E

I

F

T

S

-

G

N

N

R

V

P

P

V

V

I

L

N

N

A

A

G

G

D

D

G

G

T

S

H

N

E

Q

H
|
H

P

P

T

T

Q
|
Q

A

T

L

L

D

D

I

L

L

F

T

T

L

I

R

Q

S

E

Y

T

F

Q

G

G

K

R

I

L

E

D

G

N

L

L

K

H

I

V

M

A

I

M

L

V

G

G

D

D

I

L

L

K

H

Y

S

G

R

R

V

T

A

V

R

H

S

S

N

L

I

T

L

Q

G

A

L

L

-

A

K

K

T

F

L

D

G

G

A

N

E

R

I

F

A

Y

V

F

C

I

A

A

P

P

S

D

T

A

L

L

-

A

L

M

P

P

G

Q

R

Y

I

I

-

L

-

D

-

M

-

L

D

D

Q

E

L

K

G

G

V

I

-

A

-

W

Q

S

V

L

F

H

T

S

N

S

L

I

D

E

K

E

A

V

L

M

A

A

W

E

A

V

D

D

A

I

A

L

I

Y

V

M

L

T

R

R

L

V

Q

Q

L

K

E

E

R

R

A

L

T

D

G

-

Y

-

I

-

P

P

S

S

L

-

E

-

E

E

Y

Y

S

A

-

N

-

V

-

K

A

A

G

Q

Y

F

G

V

L

L

T

R

D

A

E

S

K

D

F

L

D

H

R

N

L

A

K

K

R

A

L

N

M

M

P

K

V

V

L

L

H

H

P

P

G
x
L

P
|
P

I

-

N

-

R

R

E

V

I

D

E

E

I

I

S

A

N

T

M

D

V

V

A

-

D

D

R

K

I

T

Q

P

P

H

P

A

G

W

Y

Y

S

-

M

-

L

-

M

F

E

Q

Q

Q

V

A

T

G

N

N

G

G

V

I

A

F

V

A

R

R

M

Q

A

A

V

L

L

L

R55 (= R55) binding
T56 (= T56) binding
R106 (= R105) binding
H135 (= H133) binding
Q138 (= Q136) binding
L268 (≠ G261) binding
P269 (= P262) binding

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
36% identity, 92% coverage: 21:302/308 of query aligns to 24:300/310 of 2ipoA

query
sites
2ipoA

L

L

A

A

A

T

G

A

Y

A

R

K

E

L

G

K

L

A

N

N

R

P

E

Q

P

P

E

E

T

-

F

-

A

-

P

-

L

L

S

K

N

H

R

K

R

V

I

I

A

A

L

S

V

C

F

F

E

E

N

A

S
|
S

T
|
T

R
|
R

T
|
T

R

R

F

L

S

S

F

F

E

E

L

T

A

S

A

M

R

H

H

R

L

L

G

G

A

A

G

S

T

V

L

V

S

G

F

F

T

S

-

D

-

S

A

A

A

N

S

T

S

S

S

L

V

G

S

K

K
|
K

G

G

E

E

T

T

L

L

S

A

D

D

T

T

I

I

R

-

N

S

L

V

E

I

A

S

M

T

K

Y

V

V

D

D

A

A

F

I

V

V

L

M

R
|
R

H

H

P

P

S

Q

S

E

G

G

A

A

D

R

F

L

V

A

T

T

S

E

I

F

T

S

-

G

N

N

R

V

P

P

V

V

I

L

N

N

A

A

G

G

D

D

G

G

T

S

H

N

E

Q

H
|
H

P

P

T

T

Q
|
Q

A

T

L

L

D

D

I

L

L

F

T

T

L

I

R

Q

S

E

Y

T

F

Q

G

G

K

R

I

L

E

D

G

N

L

L

K

H

I

V

M

A

I

M

L

V

G

G

D

D

I

L

L

K

H

Y

S

G

R
|
R

V
x
T

A

V

R

H

S

S

N

L

I

T

L

Q

G

A

L

L

-

A

K

K

T

F

L

D

G

G

A

N

E

R

I

F

A

Y

V

F

C

I

A

A

P

P

S

D

T

A

L

L

-

A

L

M

P

P

G

Q

R

Y

I

I

-

L

-

D

-

M

-

L

D

D

Q

E

L

K

G

G

V

I

-

A

-

W

Q

S

V

L

F

H

T

S

N

S

L

I

D

E

K

E

A

V

L

M

A

A

W

E

A

V

D

D

A

I

A

L

I

Y

V

M

L
x
T

R
|
R

L

V

Q

Q

L

K

E

E

R

R

A

L

T

D

G

-

Y

-

I

-

P

P

S

S

L

-

E

-

E

E

Y

Y

S

A

-

N

-

V

-

K

A

A

G

Q

Y

F

G

V

L

L

T

R

D

A

E

S

K

D

F

L

D

H

R

N

L

A

K

K

R

A

L

N

M

M

P

K

V

V

L

L

H

H

P
|
P

G
x
L

P

P

I

-

N

-

R

R

E

V

I

D

E

E

I

I

S

A

N

T

M

D

V

V

A

-

D

D

R

K

I

T

Q

P

P

H

P

A

G

W

Y

Y

S

-

M

-

L

-

M

F

E

Q

Q

Q

V

A

T

G

N

N

G
|
G

V

I

A

F

V

A

R

R

M

Q

A

A

V

L

L

L

active site: R54 (= R55), T55 (= T56), K84 (= K83), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (≠ L219), P266 (= P260), G292 (= G294)
binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R105), H134 (= H133), R167 (= R166), T168 (≠ V167), R229 (= R220), L267 (≠ G261)

Query Sequence

>WP_012502870.1 NCBI__GCF_000020505.1:WP_012502870.1
MNHLTGLFGLPASTLVELLDLAAGYREGLNREPETFAPLLSNRRIALVFFENSTRTRFSF
ELAARHLGAGTLSFTAASSSVSKGETLSDTIRNLEAMKVDAFVLRHPSSGAADFVTSITN
RPVINAGDGTHEHPTQALLDILTLRSYFGKIEGLKIMILGDILHSRVARSNILGLKTLGA
EIAVCAPSTLLPGRIDQLGVQVFTNLDKALAWADAAIVLRLQLERATGGYIPSLEEYSAG
YGLTDEKFDRLKRLMPVLHPGPINREIEISNMVADRIQPPGYSSSMLMEQVTNGVAVRMA
VLHRLLAK

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