SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing BPHYT_RS29255 FitnessBrowser__BFirm:BPHYT_RS29255 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)

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)
41% identity, 83% coverage: 44:399/430 of query aligns to 1885:2222/2225 of P20054

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P20054

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Sites not aligning to the query:

1 modified: N-acetylmethionine

1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
41% identity, 72% coverage: 91:400/430 of query aligns to 7:306/307 of 1ml4A

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active site: R56 (= R140), T57 (= T141), K85 (= K169), R106 (= R190), H134 (= H218), Q137 (= Q221), T227 (= T316), P266 (= P355), G292 (= G386)
binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S138), T55 (= T139), R56 (= R140), T57 (= T141), R106 (= R190), H134 (= H218), R167 (= R255), T168 (= T256), R228 (= R317), L267 (= L356)

6yvbC Arabidopsis aspartate transcarbamoylase complex with carbamoyl phosphate (see paper)
42% identity, 74% coverage: 82:398/430 of query aligns to 7:321/324 of 6yvbC

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active site: R121 (= R190), H149 (= H218), Q152 (= Q221), T243 (= T316), P283 (= P355), G309 (= G386)
binding phosphoric acid mono(formamide)ester: S68 (= S138), T69 (= T139), R70 (= R140), T71 (= T141), R121 (= R190), H149 (= H218), Q152 (= Q221), P283 (= P355)

6ys6B Arabidopsis aspartate transcarbamoylase complex with pala (see paper)
43% identity, 70% coverage: 96:398/430 of query aligns to 14:309/312 of 6ys6B

query
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6ys6B

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P

P

R

R

D

-

S

-

R

-

P

-

G

-

A

L

N

D

D

E

L

I

S

T

V

A

D

D

L

V

N

D

H

A

D

D

S

P

R

R

L

A

A

A

I

Y

F

F

R

R

Q

Q

T

A

D

K

N

N

G
|
G

I

L

P

F

V

I

R

R

M

M

A

A

I

L

F

L

A

K

V

L

L

L

active site: R109 (= R190), H137 (= H218), Q140 (= Q221), T231 (= T316), P271 (= P355), G297 (= G386)
binding n-(phosphonacetyl)-l-aspartic acid: S85 (= S166), K88 (= K169)

6ypoA Arabidopsis aspartate transcarbamoylase bound to ump (see paper)
43% identity, 70% coverage: 96:398/430 of query aligns to 14:309/312 of 6ypoA

query
sites
6ypoA

Q

Q

F

F

S

D

R

R

D

E

S

M

V

L

E

S

A

A

L

I

F

F

R

D

V

V

A

A

D

R

I

E

M

M

Q

E

P

K

I

I

A

E

R

K

R

S

K

S

I

Q

S

S

R

E

V

I

L

L

E

K

G

G

A

Y

V

L

L

M

G

A

N

T

L

L

F

F

F

Y

E

E

A

P

S

S

T

T

R
|
R

T
|
T

R

R

V

L

S

S

F

F

G

E

A

S

A

A

F

M

C

K

R

R

L

L

G

G

S

E

V

V

C

L

D

T

T

T

-

E

T

N

G

A

F

R

T

E

F

F

S

S

M

A

A

A

K

K

G

G

E

E

S

T

I

L

Y

E

D

D

T

T

S

I

R

R

V

T

M

V

S

E

G

G

Y

Y

V

S

D

D

A

I

L

I

V

V

I

M

R
|
R

H

H

P

F

E

E

Q

S

G

G

S

A

V

A

A

R

E

K

F

A

A

A

R

A

A

T

T

A

N

N

V

I

P

P

V

V

I

I

N

N

G

A

G

G

D

D

G

G

P

P

G

G

E

E

H
|
H

P

P

S

T

Q
|
Q

A

A

L

L

D

D

L

V

Y

Y

T

T

I

I

Q

Q

R

S

E

E

F

I

S

G

R

K

L

L

G

-

K

-

I

-

V

-

D

D

G

G

A

I

H

S

I

V

A

A

L

L

V

V

G

G

D

D

L

L

K

A

Y

N

G

G

R
|
R

T
|
T

V

V

H

R

S

S

L

L

V

A

K

Y

L

L

A

A

L

K

H

F

R

K

G

D

I

V

K

K

F

I

T

Y

L

F

I

V

S

S

P

P

P

E

M

I

L

V

E

K

M

M

P

K

S

D

Y

D

I

I

I

K

E

D

Q

Y

I

L

S

T

R

S

N

S

D

G

H

V

V

E

I

W

E

E

Q

E

T

S

D

D

L

L

T

M

T

E

G

V

L

A

R

S

G

K

A

C

D

D

V

V

Y

Y

A

Q

T
|
T

R
|
R

I

I

Q

Q

K

R

E

E

R

R

F

F

T

G

D

E

-

R

-

L

E

D

S

L

F

Y

E

E

G

A

Y

A

T

R

P

G

D

K

F

F

Q

I

I

V

N

D

Q

K

A

D

L

L

V

L

D

-

S

G

V

V

C

M

G

Q

A

K

D

K

T

A

L

I

I

I

M

M

H
|
H

P
|
P

L
|
L

P

P

R

R

D

-

S

-

R

-

P

-

G

-

A

L

N

D

D

E

L

I

S

T

V

A

D

D

L

V

N

D

H

A

D

D

S

P

R

R

L

A

A

A

I

Y

F

F

R

R

Q

Q

T

A

D

K

N

N

G
|
G

I

L

P

F

V

I

R

R

M

M

A

A

I

L

F

L

A

K

V

L

L

L

active site: R109 (= R190), H137 (= H218), Q140 (= Q221), T231 (= T316), P271 (= P355), G297 (= G386)
binding uridine-5'-monophosphate: R58 (= R140), T59 (= T141), R109 (= R190), H137 (= H218), R170 (= R255), T171 (= T256), R232 (= R317), H270 (= H354), P271 (= P355), L272 (= L356)

P49077 Aspartate carbamoyltransferase, chloroplastic; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
43% identity, 70% coverage: 96:398/430 of query aligns to 92:387/390 of P49077

query
sites
P49077

Q

Q

F

F

S

D

R

R

D

E

S

M

V

L

E

S

A

A

L

I

F

F

R

D

V

V

A

A

D

R

I

E

M

M

Q

E

P

K

I

I

A

E

R

K

R

S

K

S

I

Q

S

S

R

E

V

I

L

L

E

K

G

G

A

Y

V

L

L

M

G

A

N

T

L

L

F

F

F

Y

E

E

A

P

S

S

T

T

R
|
R

T
|
T

R

R

V

L

S

S

F

F

G

E

A

S

A

A

F

M

C

K

R

R

L

L

G

G

S

E

V

V

C

L

D

T

T

T

-

E

T

N

G

A

F

R

T

E

F

F

S

S

M

A

A

A

K

K

G

G

E

E

S

T

I

L

Y

E

D

D

T

T

S

I

R

R

V

T

M

V

S

E

G

G

Y

Y

V

S

D

D

A

I

L

I

V

V

I

M

R
|
R

H

H

P

F

E

E

Q

S

G

G

S

A

V

A

A

R

E

K

F

A

A

A

R

A

A

T

T

A

N

N

V

I

P

P

V

V

I

I

N

N

G

A

G

G

D

D

G

G

P

P

G

G

E

E

H
|
H

P

P

S

T

Q

Q

A

A

L

L

D

D

L

V

Y

Y

T

T

I

I

Q

Q

R

S

E

E

F

I

S

G

R

K

L

L

G

-

K

-

I

-

V

-

D

D

G

G

A

I

H

S

I

V

A

A

L

L

V

V

G

G

D

D

L

L

K

A

Y

N

G

G

R
|
R

T

T

V

V

H

R

S

S

L

L

V

A

K

Y

L

L

A

A

L

K

H

F

R

K

G

D

I

V

K

K

F

I

T

Y

L

F

I

V

S

S

P

P

P

E

M

I

L

V

E

K

M

M

P

K

S

D

Y

D

I

I

I

K

E

D

Q

Y

I

L

S

T

R

S

N

S

D

G

H

V

V

E

I

W

E

E

Q

E

T

S

D

D

L

L

T

M

T

E

G

V

L

A

R

S

G

K

A

C

D

D

V

V

Y

Y

A

Q

T

T

R
|
R

I

I

Q

Q

K

R

E

E

R

R

F

F

T

G

D

E

-

R

-

L

E

D

S

L

F

Y

E

E

G

A

Y

A

T

R

P

G

D

K

F

Y

Q

I

I

V

N

D

Q

K

A

D

L

L

V

L

D

-

S

G

V

V

C

M

G

Q

A

K

D

K

T

A

L

I

I

I

M

M

H

H

P

P

L

L

P

P

R

R

D

-

S

-

R

-

P

-

G

-

A

L

N

D

D

E

L

I

S

T

V

A

D

D

L

V

N

D

H

A

D

D

S

P

R

R

L

A

A

A

I

Y

F

F

R

R

Q

Q

T

A

D

K

N

N

G

G

I

L

P

F

V

I

R

R

M

M

A

A

I

L

F

L

A

K

V

L

L

L

R136 (= R140) binding UMP
T137 (= T141) binding UMP
R187 (= R190) binding UMP
H215 (= H218) binding UMP
R248 (= R255) binding UMP
R310 (= R317) binding UMP

5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
41% identity, 72% coverage: 90:399/430 of query aligns to 7:305/307 of 5g1nE

query
sites
5g1nE

Q

H

L

I

L

L

S

S

V

V

D

Q

Q

Q

F

F

S

T

R

K

D

D

S

Q

V

M

E

S

A

H

L

L

F

F

R

N

V

V

A

A

D

H

I

T

M

L

Q

R

P

M

I

M

A

V

R

Q

R

K

R

E

K

R

I

S

S

L

R

D

V

I

L

L

E

K

G

G

A

K

V

V

L

M

G

A

N

S

L

M

F

F

F

Y

E

E

A

V

S
|
S

T
|
T

R
|
R

T
|
T

R

S

V

S

S

S

F

F

G

A

A

A

F

M

C

A

R

R

L

L

G

G

S

A

V

V

C

L

D

S

T

F

T

S

G

E

F

A

T

T

F

-

S

S

S
|
S

M

V

A

Q

K
|
K

G

G

E

E

S

S

I

L

Y

A

D

D

T

S

S

V

R

Q

V

T

M

M

S

S

G

C

Y

Y

V

A

D

D

A

V

L

V

V

V

I

L

R
|
R

H

H

P

P

E

Q

Q

P

G

G

S

A

V

V

A

E

E

L

F

A

A

A

R

K

A

H

T

C

N

R

V

R

P

P

V

V

I

I

N

N

G

A

G

G

D

D

G

G

P

V

G

G

E

E

H
|
H

P

P

S

T

Q
|
Q

A

A

L

L

D

D

L

I

Y

F

T

T

I

I

Q

R

R

E

E

E

F

L

S

G

R

-

L

-

G

-

K

-

I

T

V

V

D

N

G

G

A

M

H

T

I

I

A

T

L

M

V

V

G

G

D

D

L

L

K

K

Y

H

G

G

R
|
R

T

T

V

V

H

H

S

S

L

L

V

A

K

C

L

L

A

T

L

Q

H

Y

R

R

G

-

I

V

K

S

F

L

T

R

L

Y

I

V

S

A

P

P

M

S

L

L

E

R

M

M

P

P

S

P

Y

T

I

V

I

R

E

A

Q

F

I

V

S

A

R

S

N

R

D

G

H

T

V

K

I

Q

E

E

Q

E

T

F

T

E

D

S

L

I

T

E

G

A

L

L

R

P

G

D

A

T

D

D

V

V

V

L

Y

Y

A

M

T
|
T

R
|
R

I

I

Q
|
Q

K

K

E

E

R

R

F

F

-

G

T

S

D

T

E

Q

S

E

F

Y

E

E

G

A

Y

C

T

F

P

G

D

Q

F

F

Q

I

I

L

N

T

Q

P

A

H

L

I

V

M

D

-

S

T

V

R

C

A

G

K

A

K

D

K

T

M

L

V

I

V

M

M

H

H

P
|
P

L
x
M

P

P

R

R

D

-

S

-

R

-

P

-

G

-

A

V

N

N

D

E

L

I

S

S

V

V

D

E

L

V

N

D

H

S

D

D

S

P

R

R

L

A

A

A

I

Y

F

F

R

R

Q

Q

T

A

D

E

N

N

G
|
G

I

M

P

Y

V

I

R

R

M

M

A

A

I

L

F

L

A

A

V

T

L

V

L

L

G

G

active site: R57 (= R140), T58 (= T141), K85 (= K169), R106 (= R190), H134 (= H218), Q137 (= Q221), T227 (= T316), P266 (= P355), G292 (= G386)
binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S138), T56 (= T139), R57 (= R140), T58 (= T141), S82 (= S166), K85 (= K169), R106 (= R190), H134 (= H218), R167 (= R255), R228 (= R317), Q230 (= Q319), M267 (≠ L356)

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)
41% identity, 72% coverage: 90:399/430 of query aligns to 1925:2223/2225 of P08955

query
sites
P08955

Q

H

L

I

L

L

S

S

V

V

D

K

Q

Q

F

F

S

T

R

K

D

D

S

Q

V

M

E

S

A

H

L

L

F

F

R

N

V

V

A

A

D

H

I

T

M

L

Q

R

P

M

I

M

A

V

R

Q

R

K

R

E

K

R

I

S

S

L

R

D

V

I

L

L

E

K

G

G

A

K

V

V

L

M

G

A

N

S

L

M

F

F

F

Y

E

E

A

V

S

S

T

T

R

R

T

T

R

S

V

S

S

S

F

F

G

A

A

A

F

M

C

A

R

R

L

L

G

G

S

A

V

V

C

L

D

S

T

F

T

S

G

E

F

A

T

T

F

-

S

S

M

V

A

Q

K

K

G

G

E

E

S

S

I

L

Y

A

D

D

T

S

S

V

R

Q

V

T

M

M

S

S

G

C

Y

Y

V

A

D

D

A

V

L

V

V

V

I

L

R

R

H

H

P

P

E

Q

Q

P

G

G

S

A

V

V

A

E

E

L

F

A

A

A

R

K

A

H

T

C

N

R

V

R

P

P

V

V

I

I

N

N

G

A

G

G

D

D

G

G

P

V

G

G

E

E

H

H

P

P

S

T

Q

Q

A

A

L

L

D

D

L

I

Y

F

T

T

I

I

Q

R

R

E

E

E

F

L

S

G

R

-

L

-

G

-

K

-

I

T

V

V

D

N

G

G

A

M

H

T

I

I

A

T

L

M

V

V

G

G

D

D

L

L

K

K

Y

H

G

G

R

R

T

T

V

V

H

H

S

S

L

L

V

A

K

C

L

L

A

T

L

Q

H

Y

R

R

G

-

I

V

K

S

F

L

T

R

L

Y

I

V

S

A

P

P

M

S

L

L

E

R

M

M

P

P

S

P

Y

S

I

V

I

W

E

D

Q

F

I

V

S

A

R

S

N

R

D

G

H

T

V

K

I

Q

E

E

Q

E

T

F

T

E

D

S

L

I

T

E

G

A

L

L

R

P

G

D

A

T

D

D

V

V

V

L

Y

Y

A

M

T

T

R

R

I

I

Q

Q

K

K

E

E

R

R

F

F

-

G

T

S

D

T

E

Q

S

E

F

Y

E

E

G

A

Y

C

T

F

P

G

D

Q

F

F

Q

I

I

L

N

T

Q

P

A

H

L

I

V

M

D

T

S

R

V

A

C

-

G

K

A

K

D

K

T

M

L

V

I

V

M

M

H

H

P

P

L

M

P

P

R

R

D

-

S

-

R

-

P

-

G

-

A

V

N

N

D

E

L

I

S

S

V

V

D

E

L

V

N

D

H

S

D

D

S

P

R

R

L

A

A

A

I

Y

F

F

R

R

Q

Q

T

A

D

E

N

N

G

G

I

M

P

Y

V

I

R

R

M

M

A

A

I

L

F

L

A

A

V

T

L

V

L

L

G

G

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.

4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
41% identity, 72% coverage: 90:398/430 of query aligns to 3:300/304 of 4eknB

query
sites
4eknB

Q

H

L

L

L

I

S

S

V

M

D

K

Q

D

F

I

S

G

R

K

D

E

S

E

V

I

E

L

A

E

L

I

F

L

R

D

V

E

A

A

D

R

I

K

M

M

Q

E

P

E

I

L

A

L

R

N

R

T

R

K

K

R

I

P

S

L

R

K

V

L

L

L

E

E

G

G

A

K

V

I

L

L

G

A

N

T

L

V

F

F

F

Y

E

E

A

P

S

S

T

T

R

R

T

T

R

R

V

L

S

S

F

F

G

E

A

T

A

A

F

M

C

K

R

R

L

L

G

G

S

E

V

V

C

I

D

T

T

M

T

T

G

D

F

L

T

K

F

S

S

S

M

V

A

A

K

K

G

G

E

E

S

S

I

L

Y

I

D

D

T

T

S

I

R

R

V

V

M

I

S

S

G

G

Y

Y

V

A

D

D

A

I

L

I

V

V

I

L

R

R

H

H

P

P

E

S

Q

E

G

G

S

A

V

A

A

R

E

L

F

A

A

S

R

E

A

Y

T

S

N

Q

V

V

P

P

V

I

I

I

N

N

G

A

G

G

D

D

G

G

P

S

G

N

E

Q

H

H

P

P

S

T

Q

Q

A

T

L

L

D

D

L

L

Y

Y

T

T

I

I

Q

M

R

R

E

E

F

I

S

G

R

R

L

-

G

-

K

-

I

-

V

I

D

D

G

G

A

I

H

K

I

I

A

A

L

F

V

V

G

G

D

D

L

L

K

K

Y

Y

G
|
G

R
|
R

T
|
T

V

V

H

H

S

S

L

L

V

V

K

Y

L

A

L

L

A

S

L

L

H

F

R

E

G

N

I

V

K

E

F

M

T

Y

L

F

I

V

S

S

P

P

P

K

M

E

L

L

E

R

M

L

P

P

S

K

Y

D

I

I

E

E

Q

D

I

L

S

K

R

A

N

K

D

N

H

I

V

K

I

F

E

Y

Q

E

T

K

T

E

D

S

L

L

T

D

G

L

L

D

R

D

G

D

A

I

D

D

V

V

V

L

Y

Y

A

V

T
|
T

R
|
R

I

I

Q

Q

K

K

E

E

R

R

F

F

T

P

D

D

-

P

E

N

S

E

F

Y

E

E

G

K

Y

V

T

K

P

G

D

S

F

Y

Q

K

I

I

N

K

Q

R

A

E

L

Y

V

V

D

E

S

-

V

-

C

-

G

G

A

K

D

K

T

F

L

I

I

I

M

M

H

H

P
|
P

L

L

P

P

R

R

D

-

S

-

R

-

P

-

G

-

A

V

N

D

D

E

L

I

S

D

V

Y

D

D

L

V

N

D

H

D

D

L

S

P

R

Q

L

A

A

K

I

Y

F

F

R

K

Q

Q

T

S

D

F

N

Y

G
|
G

I

I

P

P

V

V

R

R

M

M

A

A

I

I

F

L

A

K

V

K

L

L

L

I

active site: T225 (= T316), P262 (= P355), G288 (= G386)
binding sulfate ion: G163 (= G254), R164 (= R255), T165 (= T256), R226 (= R317)

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)
41% identity, 72% coverage: 90:399/430 of query aligns to 1925:2223/2225 of P27708

query
sites
P27708

Q
x
H

L
x
I

L
|
L

S
|
S

V
|
V

D
x
Q

Q
|
Q

F
|
F

S
x
T

R
x
K

D
|
D

S
x
Q

V
x
M

E
x
S

A
x
H

L
|
L

F
|
F

R
x
N

V
|
V

A
|
A

D
x
H

I
x
T

M
x
L

Q
x
R

P
x
M

I
x
M

A
x
V

R
x
Q

R
x
K

R
x
E

K
x
R

I
x
S

S
x
L

R
x
D

V
x
I

L
|
L

E
x
K

G
|
G

A
x
K

V
|
V

L
x
M

G
x
A

N
x
S

L
x
M

F
|
F

F
x
Y

E
|
E

A
x
V

S
|
S

T
|
T

R
|
R

T
|
T

R
x
S

V
x
S

S
|
S

F
|
F

G
x
A

A
|
A

F
x
M

C
x
A

R
|
R

L
|
L

G
|
G

S
x
A

V
|
V

C
x
L

D
x
S

T
x
F

T
x
S

G
x
E

F
x
A

T
|
T

F

-

S
|
S

M
x
V

A
x
Q

K
|
K

G
|
G

E
|
E

S
|
S

I
x
L

Y
x
A

D
|
D

T
x
S

S
x
V

R
x
Q

V
x
T

M
|
M

S
|
S

G
x
C

Y
|
Y

V
x
A

D
|
D

A
x
V

L
x
V

V
|
V

I
x
L

R
|
R

H
|
H

P
|
P

E
x
Q

Q
x
P

G
|
G

S
x
A

V
|
V

A
x
E

E
x
L

F
x
A

A
|
A

R
x
K

A
x
H

T
x
C

N
x
R

V
x
R

P
|
P

V
|
V

I
|
I

N
|
N

G
x
A

G
|
G

D
|
D

G
|
G

P
x
V

G
|
G

E
|
E

H
|
H

P
|
P

S
x
T

Q
|
Q

A
|
A

L
|
L

D
|
D

L
x
I

Y
x
F

T
|
T

I
|
I

Q
x
R

R
x
E

E
|
E

F
x
L

S
x
G

R

-

L

-

G

-

K

-

I
x
T

V
|
V

D
x
N

G
|
G

A
x
M

H
x
T

I
|
I

A
x
T

L
x
M

V
|
V

G
|
G

D
|
D

L
|
L

K
|
K

Y
x
H

G
|
G

R
|
R

T
|
T

V
|
V

H
|
H

S
|
S

L
|
L

V
x
A

K
x
C

L
|
L

A
x
T

L
x
Q

H
x
Y

R
|
R

G

-

I
x
V

K
x
S

F
x
L

T
x
R

L
x
Y

I
x
V

S
x
A

P
|
P

M
x
S

L
|
L

E
x
R

M
|
M

P
|
P

S
x
P

Y
x
T

I
x
V

I
x
R

E
x
A

Q
x
F

I
x
V

S
x
A

R
x
S

N
x
R

D
x
G

H
x
T

V
x
K

I
x
Q

E
|
E

Q
x
E

T
x
F

T
x
E

D
x
S

L
x
I

T
x
E

G
x
A

L
|
L

R
x
P

G
x
D

A
x
T

D
|
D

V
|
V

V
x
L

Y
|
Y

A
x
M

T
|
T

R
|
R

I
|
I

Q
|
Q

K
|
K

E
|
E

R
|
R

F
|
F

-
x
G

T
x
S

D
x
T

E
x
Q

S
x
E

F
x
Y

E
|
E

G
x
A

Y
x
C

T
x
F

P
x
G

D
x
Q

F
|
F

Q
x
I

I
x
L

N
x
T

Q
x
P

A
x
H

L
x
I

V
x
M

D
x
T

S
x
R

V
x
A

C

-

G
x
K

A
x
K

D
x
K

T
x
M

L
x
V

I
x
V

M
|
M

H
|
H

P
|
P

L
x
M

P
|
P

R
|
R

D

-

S

-

R

-

P

-

G

-

A
x
V

N
|
N

D
x
E

L
x
I

S
|
S

V
|
V

D
x
E

L
x
V

N
x
D

H
x
S

D
|
D

S
x
P

R
|
R

L
x
A

A
|
A

I
x
Y

F
|
F

R
|
R

Q
|
Q

T
x
A

D
x
E

N
|
N

G
|
G

I
x
M

P
x
Y

V
x
I

R
|
R

M
|
M

A
|
A

I
x
L

F
x
L

A
|
A

V
x
T

L
x
V

L
|
L

G
|
G

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

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)
42% identity, 72% coverage: 90:399/430 of query aligns to 1878:2194/2198 of Q18990

query
sites
Q18990

Q

N

L

C

L

I

S

S

V

V

D

K

Q

H

F

L

S

D

R

K

D

G

S

Q

V

I

E

N

A

R

L

I

F

F

R

E

V

L

A

A

D

D

-

R

I

Y

M

K

Q

H

P

D

I

V

A

E

R

K

R

G

R

H

K

P

I

L

S

T

R

H

V

I

L

L

E

N

G

G

A

K

V

V

L

L

G

V

N

N

L

L

F

F

F

Y

E

E

A

V

S

S

T

T

R

R

T

T

R

S

V

C

S

S

F

F

G

S

A

A

F

M

C

Q

R

R

L

L

G

G

S

S

V

V

C

-

D

I

T

S

T

V

G

D

F

S

T

Q

F

S

S

S

M

V

A

Q

K

K

G

G

E

E

S

T

I

L

Y

E

D

D

T

T

S

V

R

Q

V

V

M

L

S

G

G

S

Y

Y

V

G

D

D

A

I

L

L

V

V

I

L

R

R

H

S

P

N

E

E

Q

N

G

G

S

A

V

A

A

D

E

R

F

A

A

A

R

R

A

V

T

C

N

D

V

Q

P

P

V

V

I

I

N

N

G

G

D

D

G

G

P

T

G

G

E

E

H

H

P

P

S

T

Q

Q

A

A

L

L

D

D

L

V

Y

Y

T

T

I

I

Q

R

R

Q

E

E

F

M

S

G

R

-

L

-

G

-

K

-

I

T

V

V

D

N

G

G

A

L

H

T

I

I

A

A

L

L

V

V

G

G

D

D

L

L

K

K

Y

N

G

G

R

R

T

T

V

V

H

H

S

S

L

L

V

A

K

K

L

L

A

C

L

L

H

Y

R

K

G

D

I

I

K

T

F

L

T

H

L

Y

I

V

S

A

P

P

P

S

M

T

-

E

L

L

E

E

M

M

P

P

S

Q

Y

E

I

V

I

L

E

D

Q

Y

I

V

-

S

S

S

R

K

N

S

D

N

H

F

V

V

I

Q

E

K

Q

K

T

F

T

T

D

S

L

L

T

A

T

E

G

G

L

I

R

N

G

H

A

V

D

D

V

V

Y

Y

A

V

T

T

R

R

I

I

Q

Q

K

K

E

E

R

R

F

F

T

S

D

S

-

P

E

D

S

E

F

Y

E

N

G

K

Y

V

T

K

P

G

D

S

F

Y

Q

V

I

I

N

N

Q

A

A

K

L

L

V

L

D

N

S

E

-

A

-

R

-

D

-

V

-

E

-

P

-

S

-

L

V

L

C

V

G

P

A

A

D

R

T

S

L

L

-

P

-

I

I

V

M

M

H

H

P

P

L

L

P

P

R

R

D

-

S

-

R

-

P

-

G

-

A

V

N

D

D

E

L

I

S

A

V

V

D

E

L

L

N

D

H

H

D

D

S

E

R

R

L

A

A

A

I

Y

F

F

R

R

Q

Q

T

A

D

K

N

N

G

G

I

V

P

F

V

V

R

R

M

M

A

S

I

I

F

L

A

S

V

L

L

L

G

G

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.

5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
40% identity, 72% coverage: 90:399/430 of query aligns to 4:290/292 of 5g1pA

query
sites
5g1pA

Q

H

L

I

L

L

S

S

V

V

D

Q

Q

Q

F

F

S

T

R

K

D

D

S

Q

V

M

E

S

A

H

L

L

F

F

R

N

V

V

A

A

D

H

I

T

M

L

Q

R

P

M

I

M

A

V

R

Q

R

K

R

E

K

R

I

S

S

L

R

D

V

I

L

L

E

K

G

G

A

K

V

V

L

M

G

A

N

S

L

M

F

F

F

Y

E

E

A

V

S
|
S

T
|
T

R
|
R

T
|
T

R

S

V

S

S

S

F

F

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A

A

A

F

M

C

A

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R

L

L

G

G

S

A

V

V

C

L

D

S

T

F

T

S

G

E

F

A

T

T

F

-

S

S

M

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K
|
K

G

G

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S

S

I

L

Y

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D

D

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S

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M

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Y

Y

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D

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|
R

H

H

P

P

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Q

Q

P

G

G

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A

V

V

A

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E

L

F

A

A

A

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K

A

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N

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P

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V

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I

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N

G

A

G

G

D

D

G

G

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G

G

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E

H
|
H

P

P

S

T

Q
|
Q

A

A

L

L

D

D

L

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Y

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|
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M

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N

N

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F

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|
G

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P

Y

V

I

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M

A

A

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L

F

L

A

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T

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V

L

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G

G

active site: R54 (= R140), T55 (= T141), K82 (= K169), R103 (= R190), H131 (= H218), Q134 (= Q221), T223 (= T316), P251 (= P355), G277 (= G386)
binding phosphoric acid mono(formamide)ester: S52 (= S138), T53 (= T139), R54 (= R140), T55 (= T141), R103 (= R190), Q134 (= Q221), M252 (≠ L356)

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)
35% identity, 91% coverage: 12:401/430 of query aligns to 1852:2213/2214 of P07259

query
sites
P07259

A

A

M

K

R

R

L

F

N
x
S

M

I

T

T

R

E

D

E

T

A

F

I

A

A

S

D

R

N

I

L

G

D

V

A

S

A

R

E

R

D

A

A

L

I

D

P

T

E

W

Q

L

P

L

L

P

E

D

Q

D

K

S

L

Q

M

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S

S

S

R

R

A

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M

P

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E

I

L

V

V

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A

R

-

F

-

V

-

S

-

E

-

I

-

V

-

H

-

G

-

E

-

P

P

G

G

E

A

K

-

Y

-

T

I

Q

Q

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N

V

L

D

-

S

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Q

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S

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L

I

A

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S

S

Q

N

M

N

L

P

F

F

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G

K

R

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H

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I

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A

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G

A

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A

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N

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N

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P

F

L

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F

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S

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A

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K

K

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N

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G

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N

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A

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-

L

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-

I

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N

G

G

A

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A

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G

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D

L

L

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K

Y

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G

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V

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L

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