SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_013644802.1 NCBI__GCF_000191585.1:WP_013644802.1 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)

D4GSF3 SAMP-activating enzyme E1; Ubiquitin-like activating enzyme of archaea; Ubl-activating enzyme; EC 2.7.7.- from Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) (see paper)
40% identity, 74% coverage: 4:252/338 of query aligns to 12:257/270 of D4GSF3

query
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D4GSF3

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C188 (= C180) mutation to S: Loss of activity since this mutant is not able to complement a ubaA deletion in trans to restore sampylation and tRNA thiolation.

Q72J02 Sulfur carrier protein adenylyltransferase; E1-like protein TtuC; Sulfur carrier protein MoaD adenylyltransferase; Sulfur carrier protein ThiS adenylyltransferase; Sulfur carrier protein TtuB adenylyltransferase; tRNA two-thiouridine-synthesizing protein C; EC 2.7.7.80; EC 2.7.7.73; EC 2.7.7.- from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
38% identity, 72% coverage: 4:246/338 of query aligns to 10:255/271 of Q72J02

query
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Q72J02

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C192 (= C180) modified: Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in TtuB); mutation to S: Not able to form a thioester complex with TtuB.

Sites not aligning to the query:

268 C→S: Still able to form a thioester complex with TtuB.

P38820 Adenylyltransferase and sulfurtransferase UBA4; Needs CLA4 to survive protein 3; Ubiquitin-like protein activator 4; EC 2.7.7.-; EC 2.8.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 4 papers)
33% identity, 92% coverage: 3:312/338 of query aligns to 45:359/440 of P38820

query
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P38820

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C225 (= C180) mutation C->A,S: Abolishes adenylyltransferase activity but not sulfurtransferase activity.

Sites not aligning to the query:

397 mutation C->A,S: Abolishes sulfurtransferase activity but not adenylyltransferase activity.

P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
35% identity, 73% coverage: 4:251/338 of query aligns to 8:251/251 of P30138

query
sites
P30138

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C169 (= C163) binding Zn(2+)
C172 (= C166) binding Zn(2+)
W174 (≠ Y168) mutation to A: No adenylation of ThiS.
C184 (= C180) mutation to S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth.
C240 (= C240) binding Zn(2+)
C243 (= C243) binding Zn(2+)

1zfnA Structural analysis of escherichia coli thif (see paper)
36% identity, 71% coverage: 4:244/338 of query aligns to 8:244/244 of 1zfnA

query
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1zfnA

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A

G

S

A

A

I

V

G

G

T

F

S

G

G

G

M

Q

S

L

M

M

N

V

I

L

L

T

P

P

-

P

-

W

N

E

K

Q

A

G

C
|
C

I

Y

R

R

C
|
C

L

L

Y

W

P

P

G

D

V

N

P

Q

K

E

A

P

G

E

S

R

L

-

P

-

T

N

C

C

D

R

T

T

M

A

G

G

V

V

L

V

N

G

T

P

A

V

T

V

V

G

I

V

M

M

G

G

S

T

I

L

E

Q

T

A

T

L

E

E

A

A

L

I

K

K

I

L

L

L

L

S

G

G

Y

I

Y

-

D

-

E

E

S

T

T

P

D

A

S

G

N

E

L

L

I

R

V

L

Y

F

D

D

T

G

W

K

N

S

H

S

S

Q

F

W

D

R

T

S

I

L

S

A

V

L

R

R

K

R

N

A

E

S

K

G

C
|
C

E

P

C

V

C
|
C

G

G

active site: R11 (= R7), D127 (= D123)
binding adenosine-5'-triphosphate: I34 (≠ V30), G35 (= G31), G37 (= G33), G38 (≠ A34), D59 (= D55), R70 (= R66), Q71 (= Q67), K83 (= K79), T126 (= T122), D127 (= D123), T131 (= T127)
binding zinc ion: C169 (= C163), C172 (= C166), C240 (= C240), C243 (= C243)

Q9VLJ8 Adenylyltransferase and sulfurtransferase MOCS3; Molybdenum cofactor synthesis protein 3; Ubiquitin activating enzyme 4; EC 2.7.7.80; EC 2.8.1.11 from Drosophila melanogaster (Fruit fly) (see paper)
35% identity, 73% coverage: 3:249/338 of query aligns to 70:322/453 of Q9VLJ8

query
sites
Q9VLJ8

S

A

R

R

Y

Y

S

S

R

R

Q

Q

V

L

I

I

L

L

E

P

N

D

I

F

G

G

K

V

E

Q

G

G

Q

Q

E

L

K

K

L

L

L

K

K

N

S

S

V

V

A

L

I

I

V

V

G

G

C

L

G

G

A

G

L

L

G

G

T

C

V

P

A

A

N

Q

N

Y

L

L

A

A

R

A

A

A

G

G

V

C

G

G

K

H

I

L

T

G

I

L

I

V

D

D

R

Y

D

D

F

E

V

V

E

E

L

R

N

S

N

N

L

F

Q

H

R

R

Q

Q

M

I

L

L

F

H

D

S

E

E

K

D

D

R

V

C

G

G

A

M

P

S

K

K

A

A

V

E

A

S

A

A

A

R

Q

I

K

A

V

L

H

L

D

E

I

L

N

N

S

P

E

H

I

C

E

E

V

I

V

Q

P

C

V

H

I

S

K

R

D

M

L

L

N

Y

Y

P

T

H

N

N

A

A

E

M

E

H

L

I

E

R

N

G

V

Y

D

D

L

V

V

V

V

L

D

D

G

C

T

T

D

D

N

N

I

V

L

P

T

T

R

R

M

Y

L

L

V

L

N

S

D

D

I

A

C

C

V

V

K

M

N

L

K

S

I

K

P

P

W

L

I

V

Y

S

T

G

G

S

A

A

I

L

G

K

T

M

S

D

G

G

-

Q

M

L

S

T

M

V

N

Y

I

N

L

Y

P

A

N

N

K

G

A

P

C

C

I

Y

R

R

C

C

L

I

Y

F

P

P

G

V

V

P

P

P

K

P

A

P

G

E

S

A

L

V

P

T

T

N

C

C

D

G

T

D

M

G

G

G

V

V

L

L

N

G

T

A

A

V

T

T

V

G

I

T

M

I

G

G

S

A

I

M

E

Q

T

A

T

L

E

E

A

A

L

I

K

K

I

V

L

I

L

V

G

G

Y

M

Y

G

D

D

D

-

E

-

S

V

T

L

D

A

S

G

N

R

L

L

I

L

V

I

Y

F

D

D

T

G

W

G

N

S

H

G

S

V

F

F

D

R

T

N

I

I

S

R

V

I

R

R

-

S

K

K

N

R

E

P

K

N

C

C

E

H

C

M

C

C

G

S

N

A

Q

Q

-

P

-

L

-

I

-

T

-

E

-

L

-

I

N

N

Y

Y

E

E

Sites not aligning to the query:

62 modified: Phosphothreonine

1zud3 Structure of this-thif protein complex (see paper)
35% identity, 72% coverage: 4:245/338 of query aligns to 8:240/240 of 1zud3

query
sites
1zud3

R

R

Y

Y

S

S

R
|
R

Q

Q

V

I

I
x
L

L

L

E
x
D

N

D

I

I

G

A

K

L

E

D

G

G

Q

Q

E

Q

K

K

L

L

K

D

S

S

S

Q

V

V

A

L

I

I

V

I

G

G

C

L

G

G

A

G

L

L

G

G

T

T

V

P

A

A

N

L

N

Y

L

L

A

A

R

G

A

A

G

G

V

V

G

G

K

T

I

L

T

V

I

L

I

A

D

D

R

D

D

D

F

D

V

V

E

H

L

L

N

S

N

N

L

L

Q

Q

R

R

Q

Q

M

I

L

L

F

F

D

T

E

T

K

E

D

D

V

I

G

D

A

R

P

P

K

K

A

S

V

Q

A

V

A

S

A

Q

Q

Q

K

R

V

L

H

T

D

Q

I

L

N

N

S

P

E

D

I

I

E

Q

V

L

V

T

P

A

V

L

I

Q

K

Q

D

R

L

L

N

T

Y

G

T

E

N

A

A

L

E

K

E

D

L

A

L

V

E

A

N

R

V

A

D

D

L

V

V

V

V

L

D

D

G

C

T

T

D
|
D

N

N

I

M

L

A

T

T

R

R

M

Q

L

E

V

I

N

N

D

A

I

A

C

C

V

V

K

A

N

L

K

N

I

T

P

P

W

L

I

I

Y

T

T

A

G

S

A

A

I

V

G

G

T

F

S

G

G

G

M

Q

S

L

M

M

N

V

I

L

L

T

P

P

-

P

-

W

N

E

K

Q

A

G

C
|
C

I

Y

R

R

C

C

L

L

Y

W

P

P

G

D

V

N

P

Q

K

E

A

P

G

-

S

-

L

-

P

-

T

-

C

-

D

-

T

T

M

A

G

G

V

V

L

V

N

G

T

P

A

V

T

V

V

G

I

V

M

M

G

G

S

T

I

L

E

Q

T

A

T

L

E

E

A

A

L

I

K

K

I

L

L

L

L

S

G

G

Y

I

Y

-

D

-

E

E

S

T

T

P

D

A

S

G

N

E

L

L

I

R

V

L

Y

F

D

D

T

G

W

K

N

S

H

S

S

Q

F

W

D

R

T

S

I

L

S

A

V

L

R

R

K

R

N

A

E

S

K

G

C
|
C

E

P

C

V

C
|
C

G

G

N

G

active site: R11 (= R7), D127 (= D123)
binding calcium ion: L14 (≠ I10), D16 (≠ E12)
binding zinc ion: C169 (= C163), C235 (= C240), C238 (= C243)

O59954 Adenylyltransferase and sulfurtransferase uba4; Common component for nitrate reductase and xanthine dehydrogenase protein F; Ubiquitin-like protein activator 4; EC 2.7.7.80; EC 2.8.1.11 from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) (see paper)
34% identity, 71% coverage: 4:243/338 of query aligns to 68:318/482 of O59954

query
sites
O59954

R

R

Y

Y

S

G

R

R

Q

Q

V

M

I

I

L

V

E

P

N

Q

I

F

G

G

K

L

E

Q

G
|
G

Q

Q

E

L

K

K

L

L

L

R

K

D

S

A

S

K

V

V

A

L

I

I

V

V

G

G

C

A

G

G

A

G

L

L

G
|
G

T

C

V

P

A

A

N

L

N

Y

L

L

A

A

R

G

A

A

G

G

V

V

G

G

K

T

I

I

T

G

I

L

I

V

D

D

R

G

D

D

F

T

V

V

E

E

L

A

N

S

N

N

L

L

Q

H

R
|
R

Q

Q

M

V

L

L

F

H

D

R

E

S

K

R

D

N

V

V

G

G

A

K

P

L

K

K

A

V

V

D

A

S

A

A

A

I

Q

E

K

Y

V

L

H

R

D

E

I

L

N

N

S

P

E

H

I

P

E

T

V

Y

V

I

P

A

V

H

I

Q

K

A

D

H

L

L

N

T

Y

P

T

R

N

E

A

A

E

P

E

D

L

I

L

F

E

K

N

D

V

Y

D

D

L

L

V

I

V

L

D

D

G
x
C

T

T

D

D

N

N

I

P

L

A

T

T

R

R

M

Y

L

L

V

I

N

S

D

D

I

T

C

A

V

V

K

L

N

L

K

G

I

K

P

P

W

L

I

V

Y

S

T

A

G

S

A

A

I

L

G

R

T

T

S
x
E

G

G

-

Q

-

L

M

M

S

V

M

L

N

N

I

N

L

P

P

P

N

Q

K

P

-

P

-

G

-

D

-

K

-

T

-

G

A

P

C

C

I

Y

R

R

C

C

L

V

Y

F

P

P

G

K

V

P

P

P

K

P

A

A

G

N

S

S

L

V

P

T

T

S

C

C

D

A

T

D

M

G

G

G

V

I

L

L

N

G

T

P

A

V

T

V

V
x
G

I

T

M

M

G

G

S

V

I

L

E

Q

T

A

T

S

E

E

A

A

L

I

K

K

I

V

L

L

L

T

G

S

Y

A

Y

G

D

E

D

S

D

V

E

E

S

A

T

T

D

P

S

P

N

S

L

L

I

L

V

I

Y

F

D

S

T

A

W

Y

N

S

H

S

S

P

-

Q

F

F

D

R

T

T

I

I

S

K

V

L

R

R

-

S

K

R

N

R

E

P

K

N

C

C

E

A

C

V

C

C

G82 (= G18) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
G100 (= G36) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
R130 (= R66) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
C185 (≠ G121) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
E215 (≠ S151) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
G264 (≠ V191) mutation to S: In cnxF142ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.

P12282 Molybdopterin-synthase adenylyltransferase; MoaD protein adenylase; Molybdopterin-converting factor subunit 1 adenylase; Sulfur carrier protein MoaD adenylyltransferase; EC 2.7.7.80 from Escherichia coli (strain K12) (see 2 papers)
36% identity, 72% coverage: 4:245/338 of query aligns to 11:249/249 of P12282

query
sites
P12282

R

R

Y

Y

S

N

R
|
R

Q

Q

V

I

I

I

L

L

E

R

N

G

I

F

G

D

K

F

E

D

G

G

Q

Q

E

E

K

A

L

L

L

K

K

D

S

S

S

R

V

V

A

L

I

I

V

V

G

G

C

L

G

G

A

G

L

L

G

G

T
x
C

V

A

A

A

A

S

N

Q

N

Y

L

L

A

A

R

S

A

A

G

G

V

V

G

G

K

N

I

L

T

T

I

L

D

D

R

F

D

D

F

T

V

V

E

S

L

L

N

S

N

N

L

L

Q

Q

R
|
R

Q

Q

M

T

L

L

F

H

D

S

E

D

K

A

D

T

V

V

G

G

A

Q

P

P

K

K

A

V

V

E

A

S

A

A

A

R

Q

D

K

A

V

L

H

T

D

R

I

I

N

N

S

P

E

H

I

I

E

A

V

I

V

T

P

P

V

V

I

N

K

A

D

L

L

L

N

D

Y

D

T

A

N

E

A

L

E

A

L

L

L

I

E

A

N

E

V

H

D

D

L

L

V

V

V

L

D

D

G
x
C

T

T

D
|
D

N

N

I

V

L

A

T

V

R

R

M

N

L

Q

V

L

N

N

D

A

I

G

C
|
C

V

F

K

A

N

A

K

K

I

V

P

P

W

L

I

V

Y

S

T

G

G

A

A

A

I

I

G

R

T

M

S

E

G

G

M

Q

-

I

-

T

S

V

M

F

N

T

I

Y

L

Q

P

D

N

G

K

E

A

P

C
|
C

I

Y

R

R

C
|
C

L

L

Y

S

P

R

G

L

V

F

P

G

K

E

A

-

G

-

S

N

L

A

P

L

T

T

C
|
C

D

V

T

E

M

A

G

G

V

V

L

M

N

A

T

P

A

L

T

I

V

G

I

V

M

I

G

G

S

S

I

L

E

Q

T

A

T

M

E

E

A

A

L

I

K

K

I

M

L

L

L

A

G

G

Y

Y

Y

-

D

-

D

G

E

K

S

P

T

A

D

S

S

G

N

K

L

I

I

V

V

M

Y

Y

D

D

T

A

W

M

N

T

H
x
C

S

Q

F

F

D

R

T

E

I

M

S

K

V

L

R

M

K

R

N

N

E

P

K

G

C
|
C

E

E

C

V

C
|
C

G

G

N

Q

R14 (= R7) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
C44 (≠ T37) mutation to A: No effect.
R73 (= R66) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
C128 (≠ G121) mutation to A: No effect.; mutation to Y: No activity.
D130 (= D123) mutation to A: No activity.; mutation to E: Substantially reduced activity.
C142 (= C135) mutation to A: No effect.
C172 (= C163) mutation to A: No zinc bound and no enzyme activity.
C175 (= C166) mutation to A: No zinc bound and no enzyme activity.
C187 (= C180) mutation to A: No effect.
C231 (≠ H227) mutation to A: No effect.
C244 (= C240) mutation to A: No zinc bound and almost no enzyme activity.
C247 (= C243) mutation to A: No zinc bound and almost no enzyme activity.

O95396 Adenylyltransferase and sulfurtransferase MOCS3; Molybdenum cofactor synthesis protein 3; Molybdopterin synthase sulfurylase; MPT synthase sulfurylase; EC 2.7.7.80; EC 2.8.1.11 from Homo sapiens (Human) (see 5 papers)
37% identity, 72% coverage: 4:246/338 of query aligns to 62:303/460 of O95396

query
sites
O95396

R

R

Y

Y

S

S

R

R

Q

Q

V

L

I

V

L

L

E

P

N

E

I

L

G

G

K

V

E

H

G

G

Q

Q

E

L

K

R

L

L

L

G

K

T

S

A

S

C

V

V

A

L

I

I

V

V

G

G

C

C

G

G

A

G

L

L

G

G

T

C

V

P

A

L

A

A

N

Q

N

Y

L

L

A

A

R

A

A

A

G

G

V

V

G

G

K

R

I

L

T

G

I

L

I

V

D

D

R

Y

D

D

F

V

V

V

E

E

L

M

N

S

N

N

L

L

Q

A

R

R

Q

Q

M

V

L

L

F

H

D

G

E

E

K

A

D

L

V

A

G

G

A

Q

P

A

K

K

A

A

V

F

A

S

A

A

Q

A

K

S

V

L

H

R

D

R

I

L

N

N

S

S

E

A

I

V

E

E

V

C

V

V

P

P

V

Y

I
x
T

K
x
Q

D
x
A

L
|
L

N
x
T

Y
x
P

T
x
A

N
x
T

A
|
A

E
x
L

E
x
D

L
|
L

L
x
V

E
x
R

N
x
R

V
x
Y

D
|
D

L
x
V

V
|
V

V
x
A

D
|
D

G
x
C

T
x
S

D
|
D

N
|
N

I
x
V

L
x
P

T
|
T

R
|
R

M
x
Y

L
|
L

V
|
V

N
|
N

D
|
D

I
x
A

C
|
C

V
|
V

K
x
L

N
x
A

K
x
G

I
x
R

P
|
P

W
x
L

I
x
V

Y
x
S

T
x
A

G
x
S

A
|
A

I
x
L

G
x
R

T
x
F

S
x
E

G
|
G

-
x
Q

M
x
I

S
x
T

M
x
V

N
x
Y

I
x
H

L
x
Y

P
x
D

N
x
G

K
x
G

A
x
P

C
|
C

I
x
Y

R
|
R

C
|
C

L
x
I

Y
x
F

P
|
P

G
x
Q

V
x
P

P
|
P

K
x
P

A
|
A

G
x
E

S
x
T

L
x
V

P
x
T

T
x
N

C
|
C

D

A

T

D

M

G

G

G

V

V

L

L

N

G

T

V

A

V

T

T

V

G

I

V

M

L

G

G

S

C

I

L

E

Q

T

A

T

L

E

E

A

V

L

L

K

K

I

I

L

A

G

G

Y

L

Y

-

D

-

D

G

E

P

S

S

T

Y

D

S

S

G

N

S

L

L

I

L

V

L

Y

F

D

D

T

A

W

L

N

R

H

G

S

H

F

F

D

R

T

S

I

I

S

R

V

L

R

R

K

S

N

R

E

R

K

L

-

D

C

C

E

A

C

A

C

C

G

G

N

E

Q

R

158:238 (vs. 100:179, 31% identical) Interaction with NFS1
C239 (= C180) mutation to A: Impairs sulfurtransferase activity.

Sites not aligning to the query:

316 modified: Disulfide link with 324; C→A: Does not affect sulfurtransferase activity.
324 modified: Disulfide link with 316; C→A: Does not affect sulfurtransferase activity.
365 C→A: Does not affect sulfurtransferase activity.
412 active site, Cysteine persulfide intermediate; for sulfurtransferase activity; modified: Cysteine persulfide; C→A: Abolishes sulfurtransferase activity.
413 K→R: Does not affect sulfurtransferase specificity and activity.
414 L→K: Does not affect sulfurtransferase specificity and activity.
415 G→A: Does not affect sulfurtransferase specificity and activity.
416 N→V: Does not affect sulfurtransferase specificity and activity.
417 D→R: Results in 470-fold increased activity.; D→T: Results in 90-fold increased activity.
458 P→G: Does not affect sulfurtransferase specificity and activity.
460 Y→A: Does not affect sulfurtransferase specificity and activity.

1jwbB Structure of the covalent acyl-adenylate form of the moeb-moad protein complex (see paper)
35% identity, 71% coverage: 4:244/338 of query aligns to 10:240/240 of 1jwbB

query
sites
1jwbB

R

R

Y

Y

S

N

R
|
R

Q

Q

V

I

I

I

L

L

E

R

N

G

I

F

G

D

K

F

E

D

G

G

Q

Q

E

E

K

A

L

L

L

K

K

D

S

S

S

R

V

V

A

L

I

I

V

V

G
|
G

C

L

G
|
G

A
x
G

L

L

G

G

T

C

V

A

A

A

A

S

N

Q

N

Y

L

L

A

A

R

S

A

A

G

G

V

V

G

G

K

N

I

L

T

T

I

L

D
|
D

R
x
F

D

D

F

T

V

V

E

S

L

L

N

S

N

N

L

L

Q

Q

R

R

Q

Q

M

T

L

L

F

H

D

S

E

D

K

A

D

T

V

V

G

G

A

Q

P

P

K
|
K

A

V

V

E

A

S

A

A

A

R

Q

D

K

A

V

L

H

T

D

R

I

I

N

N

S

P

E

H

I

I

E

A

V

I

V

T

P

P

V

V

I

N

K

A

D
x
L

L

L

N

D

Y

D

T

A

N

E

A

L

E

A

L

L

L

I

E

A

N

E

V

H

D

D

L

L

V

V

V

L

D

D

G
x
C

T
|
T

D
|
D

N
|
N

I

V

L

A

T
x
V

R

R

M

N

L

Q

V

L

N

N

D

A

I

G

C

C

V

F

K

A

N

A

K

K

I

V

P

P

W

L

I

V

Y

S

T

G

G

A

A

A

I

I

G

R

T

M

S

E

G

G

M

Q

-

I

-

T

S

V

M

F

N

T

I

Y

L

Q

P

D

N

G

K

E

A

P

C
|
C

I

Y

R

R

C

C

L

L

Y

S

P

R

G

L

V

F

P

G

K

E

A

A

G

-

S

-

L

-

P

-

T

-

C

-

D

-

T

-

M

-

G

G

V

V

L

M

N

A

T

P

A

L

T

I

V

G

I

V

M

I

G

G

S

S

I

L

E

Q

T

A

T

M

E

E

A

A

L

I

K

K

I

M

L

L

L

A

G

G

Y

Y

Y

-

D

-

D

G

E

K

S

P

T

A

D

S

S

G

N

K

L

I

I

V

V

M

Y

Y

D

D

T

A

W

M

N

T

H

C

S

Q

F

F

D

R

T

E

I

M

S

K

V

L

R

M

K

R

N

N

E

P

K

G

C
|
C

E

E

C

V

C
|
C

G

G

active site: R13 (= R7), D129 (= D123)
binding adenosine monophosphate: G37 (= G31), G39 (= G33), G40 (≠ A34), D61 (= D55), F62 (≠ R56), K85 (= K79), L108 (≠ D102), C127 (≠ G121), T128 (= T122), D129 (= D123), N130 (= N124), V133 (≠ T127)
binding zinc ion: C171 (= C163), C236 (= C240), C239 (= C243)

1jw9B Structure of the native moeb-moad protein complex (see paper)
35% identity, 71% coverage: 4:244/338 of query aligns to 10:240/240 of 1jw9B

query
sites
1jw9B

R

R

Y

Y

S

N

R
|
R

Q

Q

V

I

I

I

L

L

E

R

N

G

I

F

G

D

K

F

E

D

G

G

Q

Q

E

E

K

A

L

L

L

K

K

D

S

S

S

R

V

V

A

L

I

I

V

V

G

G

C

L

G

G

A

G

L

L

G

G

T

C

V

A

A

A

A

S

N

Q

N

Y

L

L

A

A

R

S

A

A

G

G

V

V

G

G

K

N

I

L

T

T

I

L

D

D

R

F

D

D

F

T

V

V

E

S

L

L

N

S

N

N

L

L

Q

Q

R

R

Q

Q

M

T

L

L

F

H

D

S

E

D

K

A

D

T

V

V

G

G

A

Q

P

P

K

K

A

V

V

E

A

S

A

A

A

R

Q

D

K

A

V

L

H

T

D

R

I

I

N

N

S

P

E

H

I

I

E

A

V

I

V

T

P

P

V

V

I

N

K

A

D

L

L

L

N

D

Y

D

T

A

N

E

A

L

E

A

L

L

L

I

E

A

N

E

V

H

D

D

L

L

V

V

V

L

D

D

G

C

T

T

D
|
D

N

N

I

V

L

A

T

V

R

R

M

N

L

Q

V

L

N

N

D

A

I

G

C

C

V

F

K

A

N

A

K

K

I

V

P

P

W

L

I

V

Y

S

T

G

G

A

A

A

I

I

G

R

T

M

S

E

G

G

M

Q

-

I

-

T

S

V

M

F

N

T

I

Y

L

Q

P

D

N

G

K

E

A

P

C
|
C

I

Y

R

R

C

C

L

L

Y

S

P

R

G

L

V

F

P

G

K

E

A

A

G

-

S

-

L

-

P

-

T

-

C

-

D

-

T

-

M

-

G

G

V

V

L

M

N

A

T

P

A

L

T

I

V

G

I

V

M

I

G

G

S

S

I

L

E

Q

T

A

T

M

E

E

A

A

L

I

K

K

I

M

L

L

L

A

G

G

Y

Y

Y

-

D

-

D

G

E

K

S

P

T

A

D

S

S

G

N

K

L

I

I

V

V

M

Y

Y

D

D

T

A

W

M

N

T

H

C

S

Q

F

F

D

R

T

E

I

M

S

K

V

L

R

M

K

R

N

N

E

P

K

G

C
|
C

E

E

C

V

C
|
C

G

G

active site: R13 (= R7), D129 (= D123)
binding zinc ion: C171 (= C163), C236 (= C240), C239 (= C243)

1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
33% identity, 69% coverage: 4:236/338 of query aligns to 10:217/217 of 1jwaB

query
sites
1jwaB

R

R

Y

Y

S

N

R
|
R

Q

Q

V

I

I

I

L

L

E

R

N

G

I

F

G

D

K

F

E

D

G

G

Q

Q

E

E

K

A

L

L

L

K

K

D

S

S

S

R

V

V

A

L

I

I

V

V

G

G

C

L

G
|
G

A
x
G

L

L

G

G

T

C

V

A

A

A

A

S

N

Q

N

Y

L

L

A

A

R

S

A

A

G

G

V

V

G

G

K

N

I

L

T

T

I

L

D
|
D

R
x
F

D

D

F

T

V

V

E

S

L

L

N

S

N

N

L

L

Q

Q

R
|
R

Q

Q

M

T

L

L

F

H

D

S

E

D

K

A

D

T

V

V

G

G

A

Q

P

P

K
|
K

A

V

V

E

A

S

A

A

A

R

Q

D

K

A

V

L

H

T

D

R

I

I

N

N

S

P

E

H

I

I

E

A

V

I

V

T

P

P

V

V

I

N

K

A

D
x
L

L

L

N

D

Y

D

T

A

N

E

A

L

E

A

L

L

L

I

E

A

N

E

V

H

D

D

L

L

V

V

V

L

D

D

G

C

T

T

D
|
D

N
|
N

I

V

L

A

T
x
V

R

R

M

N

L

Q

V

L

N

N

D

A

I

G

C

C

V

F

K

A

N

A

K

K

I

V

P

P

W

L

I

V

Y

S

T

G

G

A

A

A

I

I

G

R

T

M

S

E

G

G

M

-

S

Q

M

I

N

T

I

V

L

F

P

T

N

Y

K

E

A

A

C

-

I

-

R

-

C

-

L

-

Y

-

P

-

G

-

V

-

P

-

K

-

A

-

G

-

S

-

L

-

P

-

T

-

C

-

D

-

T

-

M

-

G

G

V

V

L

M

N

A

T

P

A

L

T

I

V

G

I

V

M

I

G

G

S

S

I

L

E

Q

T

A

T

M

E

E

A

A

L

I

K

K

I

M

L

L

L

A

G

G

Y

Y

Y

-

D

-

D

G

E

K

S

P

T

A

D

S

S

G

N

K

L

I

I

V

V

M

Y

Y

D

D

T

A

W

M

N

T

H

C

S

Q

F

F

D

R

T

E

I

M

S

K

V

L

R

M

K

R

active site: R13 (= R7), D129 (= D123)
binding adenosine-5'-triphosphate: G39 (= G33), G40 (≠ A34), D61 (= D55), F62 (≠ R56), R72 (= R66), K85 (= K79), L108 (≠ D102), D129 (= D123), N130 (= N124), V133 (≠ T127)

6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
33% identity, 74% coverage: 4:252/338 of query aligns to 14:277/289 of 6yubB

query
sites
6yubB

R

R

Y

Y

S

S

R

R

Q

Q

V

M

I

I

L

V

E

P

N

G

I

M

G

G

K

K

E

E

G

G

Q

Q

E

L

K

R

L

L

L

M

K

N

S

A

S

K

V

V

A

L

I

I

V

I

G

G

C

A

G

G

A

G

L

L

G

G

T

C

V

P

A

A

N

Q

N

Y

L

L

A

A

R

G

A

A

G

G

V

V

G

G

K

T

I

I

T

G

I

I

I

V

D

D

R

G

D

D

F

S

V

V

E

E

L

T

N

S

N

N

L

L

Q

H

R

R

Q

Q

M

V

L

A

F

H

D

A

E

T

K

K

D

R

V

V

G

G

A

M

P

L

K

K

A

V

V

D

A

S

A

L

A

I

Q

T

K

H

V

L

H

I

D

E

I

I

N

N

S

P

E

L

I

P

E

V

V

Y

V

V

P

P

V

Y

I

R

K

F

D

D

L

L

N

T

Y

P

T

Q

N

N

A

A

E

A

E

Q

L

I

E

K

N

P

V

W

D

D

L

V

V

I

V

L

D

D

G

C

T

T

D

D

N

N

I

P

L

A

T

T

R

R

M

Y

L

L

V

I

N

S

D

D

I

V

C

C

V

V

K

L

N

L

K

G

I

K

P

P

W

L

I

V

Y

S

T

A

G

A

A

S

I

V

G

Q

T

K

S

S

G

G

-

Q

-

L

M

I

S

V

M

L

N

N

I

C

L

P

P

P

N

T

K

P

A

Q

C

-

I

-

R

-

C

-

L

-

Y

-

P

-

G

G

V

V

-

V

-

N

P

K

K

K

A

A

G

A

S

P

L
x
C

P

Y

T

R

C
|
C

D

C

T

F

M

K

G

G

V

I

L

M

N

G

T

P

A

V

T

V

V

G

I

M

M

M

G

G

S

V

I

A

E

Q

T

A

T

G

E

E

A

A

L

I

K

K

I

I

L

L

L

V

G

S

Y

Q

Y

L

D

H

-

M

-

P

-

K

-

E

-

G

D

E

E

V

S

S

T

P

D

E

S

K

N

N

L

L

I

V

-

Q

-

P

-

T

-

L

-

I

-

Y

V

T

Y

Y

D

D

-

L

-

N

-

S

-

A

T

I

W

G

N

P

H

Y

S

S

F

F

D

R

T

A

I

L

S

K

V

M

R

G

K

G

N

R

E

K

K

K

-

D

C
|
C

E

F

C

A

C

C

G

G

N

E

Q

N

N

S

Y

T

E

L

Y

T

I

L

D

D

binding zinc ion: C184 (≠ L177), C187 (= C180), C265 (= C240)

6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
31% identity, 74% coverage: 4:252/338 of query aligns to 13:278/423 of 6yubA

query
sites
6yubA

R

R

Y

Y

S

S

R

R

Q

Q

V

M

I

I

L

V

E

P

N

G

I

M

G

G

K

K

E

E

G

G

Q

Q

E

L

K

R

L

L

L

M

K

N

S

A

S

K

V

V

A

L

I

I

V

I

G

G

C

A

G

G

A

G

L

L

G

G

T

C

V

P

A

A

N

Q

N

Y

L

L

A

A

R

G

A

A

G

G

V

V

G

G

K

T

I

I

T

G

I

I

I

V

D

D

R

G

D

D

F

S

V

V

E

E

L

T

N

S

N

N

L

L

Q

H

R

R

Q

Q

M

V

L

A

F

H

D

A

E

T

K

K

D

R

V

V

G

G

A

M

P

L

K

K

A

V

V

D

A

S

A

L

A

I

Q

T

K

H

V

L

H

I

D

E

I

I

N

N

S

P

E

L

I

P

E

V

V

Y

V

V

P

P

V

Y

I

R

K

F

D

D

L

L

N

T

Y

P

T

Q

N

N

A

A

E

A

E

Q

L

I

E

K

N

P

V

W

D

D

L

V

V

I

V

L

D

D

G

C

T

T

D

D

N

N

I

P

L

A

T

T

R

R

M

Y

L

L

V

I

N

S

D

D

I

V

C

C

V

V

K

L

N

L

K

G

I

K

P

P

W

L

I

V

Y

S

T

A

G

A

A

S

I

V

G

Q

T

K

S

S

G

G

-

Q

-

L

M

I

S

V

M

L

N

N

I

C

L

P

P

P

N

T

K

P

-

Q

-

G

-

V

-

N

-

K

-

A

A

P

C
|
C

I

Y

R

R

C
|
C

L

C

Y

F

P

-

G

-

V

-

P

-

K

-

A

-

G

-

S

-

L

-

P

-

T

-

C

-

D

K

T

K

M

P

G

G

V

I

L

M

N

G

T

P

A

V

T

V

V

G

I

M

M

M

G

G

S

V

I

A

E

Q

T

A

T

G

E

E

A

A

L

I

K

K

I

I

L

L

L

V

G

S

Y

Q

Y

L

D

H

-

M

-

P

-

K

-

E

-

G

D

E

E

V

S

S

T

P

D

E

S

K

N

N

L

L

I

V

-

Q

-

P

-

T

-

L

-

I

-

Y

V

T

Y

Y

D

D

-

L

-

N

-

S

-

A

T

I

W

G

N

P

H

Y

S

S

F

F

D

R

T

A

I

L

S

K

V

M

R

G

K

G

N

R

E

K

K

K

-

D

C
|
C

E

F

C

A

C
|
C

G

G

N

E

Q

N

N

S

Y

T

E

L

Y

T

I

L

D

D

binding zinc ion: C183 (= C163), C186 (= C166), C266 (= C240), C269 (= C243)

P20973 Ubiquitin-activating enzyme E1 1; EC 6.2.1.45 from Triticum aestivum (Wheat) (see paper)
32% identity, 47% coverage: 3:160/338 of query aligns to 443:607/1051 of P20973

query
sites
P20973

S

S

R

R

Y

Y

S

D

R

A

Q

Q

V

I

I

S

L

V

E

-

N

-

I

F

G

G

K

S

E

K

G

L

Q

Q

E

N

K

K

L

L

L

E

K

E

S

A

S

K

V

I

A

F

I

M

V

V

G

G

C

S

G

G

A

A

L

L

G

G

T

C

V

E

A

F

A

L

N

K

N

N

L

L

A

A

R

L

A

M

G

G

V

I

-

S

-

C

-

S

-

Q

-

N

G

G

K

N

I

L

T

T

I

L

I

T

D

D

R

D

D

D

F

V

V

I

E

E

L

K

N

S

N

N

L

L

Q

S

R

R

Q

Q

M

F

L

L

F

F

D

R

E

D

K

W

D

N

V

I

G

G

A

Q

P

P

K

K

A

S

V

T

A

V

A

A

Q

T

K

A

V

A

H

M

D

V

I

I

N

N

S

P

E

K

I

L

E

H

V

-

V

V

P

E

V

A

I

L

K

Q

D

N

L

R

N

A

Y

S

T

P

N

E

A

T

E

E

E

N

L

V

L

F

-

N

-

D

-

A

-

F

-

W

E

E

N

N

V

L

D

D

L

A

V

V

D

N

G

A

T

L

D

D

N

N

I

V

L

T

T

A

R

R

M

M

L

Y

V

I

N

D

D

S

I

R

C

C

V

V

K

Y

N

F

K

Q

I

K

P

P

W

L

I

L

Y

E

T

S

G

G

A

T

I

L

G

G

T

A

S

K

G

C

M

N

S

T

M

Q

N

M

I

V

L

I

P

P

N

H

Sites not aligning to the query:

626 active site, Glycyl thioester intermediate; C→A: Abolishes enzyme activity.

P22314 Ubiquitin-like modifier-activating enzyme 1; Protein A1S9; Ubiquitin-activating enzyme E1; EC 6.2.1.45 from Homo sapiens (Human) (see 2 papers)
34% identity, 47% coverage: 2:159/338 of query aligns to 448:612/1058 of P22314

query
sites
P22314

Q

Q

S

N

R

R

Y

Y

S

D

R

G

Q

Q

V

V

I

A

L

V

E

-

N

-

I

F

G

G

K

S

E

D

G

L

Q

Q

E

E

K

K

L

L

L

G

K

K

S

Q

S

K

V

Y

A

F

I

L

V

V

G

G

C

A

G

G

A

A

L

I

G

G

T

C

V

E

A

L

N

K

N

N

L

F

A

A

R

M

A

I

G

G

V

L

G

G

-

C

-

G

-

E

-

G

K

E

I

I

T

I

I

V

I

T

D

D

R

M

D

D

F

T

V

I

E

E

L

K

N

S

N

N

L

L

Q

N

R

R

Q

Q

M

F

L

L

F

F

D

R

E

P

K

W

D

D

V

V

G

T

A

K

P

L

K

K

A

S

V

D

A

T

A

A

Q

A

K

A

V

V

H

R

D

Q

I

M

N

N

S

P

E

H

I

I

E

R

V

V

V

T

P

S

-

H

-

Q

-

N

-

R

V

V

I

G

K

P

D

D

L

T

N

E

Y

R

T

I

N

Y

A

D

E

D

L

F

E

Q

N

N

V

L

D

D

L

G

V

V

V

A

D

N

G

A

T

L

D

D

N

N

I

V

L

D

T

A

R

R

M

M

L

Y

V

M

N

D

D

R

I

R

C

C

V

V

K

Y

N

Y

K

R

I

K

P

P

W

L

I

L

Y

E

T

S

G

G

A

T

I

L

G

G

T

T

S

K

G

G

M

N

S

V

M

Q

N

V

I

V

L

I

P

P

Sites not aligning to the query:

1:66 mutation Missing: Localizes to the cytoplasm.
4 modified: Phosphoserine; S→A: Reduces phosphorylation.
8:11 KKRR→AAAA: Loss of nuclear localization and a 90-95% decrease in the phosphorylation.
41 M → L: in VEXAS; somatic mutation; the underlying nucleotide substitution affects normal alternative translation initiation and leads to aberrant initiation from M-67 to produce a shorter protein with strongly reduced enzymatic activity; M → T: in VEXAS; somatic mutation; the underlying nucleotide substitution affects normal alternative translation initiation and leads to aberrant initiation from M-67 to produce a shorter protein with strongly reduced enzymatic activity; M → V: in VEXAS; somatic mutation; does not affect ubiquitin activating enzyme activity; does not affect subcellular localization; the underlying nucleotide substitution affects normal alternative translation initiation and leads to aberrant initiation from M-67 to produce a shorter protein with strongly reduced enzymatic activity; M→A: Localizes to the nucleus; when associated with A-67.
67 M→A: Localizes to the nucleus; when associated with A-41. Localizes to the cytoplasm; when associated with 1-M--G-40 del.

6dc6C Crystal structure of human ubiquitin activating enzyme e1 (uba1) in complex with ubiquitin (see paper)
34% identity, 47% coverage: 2:159/338 of query aligns to 400:564/996 of 6dc6C

query
sites
6dc6C

Q

Q

S

N

R

R

Y

Y

S

D

R

G

Q

Q

V

V

I

A

L

V

E

-

N

-

I

F

G

G

K

S

E

D

G

L

Q

Q

E

E

K

K

L

L

L

G

K

K

S

Q

S

K

V

Y

A

F

I

L

V

V

G

G

C

A

G

G

A

A

L

I

G

G

T

C

V

E

A

L

N

K

N

N

L

F

A

A

R

M

A

I

G

G

V

L

G

G

-

C

-

G

-

E

-

G

K

E

I

I

T

I

I

V

I

T

D

D

R

M

D
|
D

F

T

V

I

E
|
E

L

K

N

S

N
|
N

L

L

Q

N

R
|
R

Q

Q

M

F

L

L

F

F

D

R

E

P

K

W

D

D

V

V

G

T

A

K

P

L

K
|
K

A

S

V

D

A

T

A

A

Q

A

K

A

V

V

H

R

D

Q

I

M

N

N

S

P

E

H

I

I

E

R

V

V

V

T

P

S

-

H

-

Q

-

N

-

R

V

V

I

G

K

P

D

D

L

T

N

E

Y

R

T

I

N

Y

A

D

E

D

L

F

E

Q

N

N

V

L

D

D

L

G

V

V

V

A

D

N

G

A

T

L

D
|
D

N

N

I

V

L

D

T

A

R

R

M

M

L

Y

V

M

N

D

D

R

I

R

C

C

V

V

K

Y

N

Y

K

R

I

K

P

P

W

L

I

L

Y

E

T

S

G

G

A

T

I

L

G

G

T

T

S

K

G

G

M

N

S

V

M

Q

N

V

I

V

L

I

P

P

active site: R467 (= R66), D528 (= D123)
binding magnesium ion: D458 (= D57), E461 (= E60)
binding pyrophosphate 2-: N464 (= N63), K480 (= K79)

Sites not aligning to the query:

active site: 9, 584, 585, 587
binding pyrophosphate 2-: 9

Q8TBC4 NEDD8-activating enzyme E1 catalytic subunit; NEDD8-activating enzyme E1C; Ubiquitin-activating enzyme E1C; Ubiquitin-like modifier-activating enzyme 3; Ubiquitin-activating enzyme 3; EC 6.2.1.64 from Homo sapiens (Human) (see 7 papers)
33% identity, 46% coverage: 27:180/338 of query aligns to 72:237/463 of Q8TBC4

query
sites
Q8TBC4

V

V

A

L

I

V

V

I

G

G

C

A

G

G

A

G

L

L

G

G

T

C

V

E

A

L

N

K

N

N

L

L

A

A

R

L

A

S

G

G

V

F

G

R

K

Q

I

I

T

H

I

V

I

I

D
|
D

R
x
M

D
|
D

F
x
T

V
x
I

E
x
D

L
x
V

N
x
S

N
|
N

L
|
L

Q
x
N

R
|
R

Q
|
Q

M
x
F

L
|
L

F
|
F

D
x
R

E
x
P

K
|
K

D
|
D

V
x
I

G
|
G

A
x
R

P
|
P

K
|
K

A

A

V

E

A

V

A

A

Q

E

K

F

V

L

H

N

D

D

I

R

N

V

S

P

E

N

I

C

E

N

V

V

P

P

V

H

-

F

-

N

-

K

I
|
I

K
x
Q

D
|
D

L
x
F

N
|
N

Y
x
D

T
|
T

N

-

A

-

E

-

L
x
F

L
x
Y

E
x
R

N
x
Q

V
x
F

D
x
H

L
x
I

V
x
I

V
|
V

D
x
C

G
|
G

T
x
L

D
|
D

N
x
S

I
|
I

L
x
I

T
x
A

R

R

M

R

L

W

V

I

N

N

D

G

I

M

C

L

V

I

-

S

-

L

-

N

-

Y

-

E

-

D

-

G

-

V

-

L

-

D

-
x
P

K

S

N

S

K
x
I

I

V

P
|
P

W

L

I

I

Y

D

T

G

G

G

A

T

I

E

G

G

T

F

S

K

G

G

M

N

S

A

M
x
R

N

V

I

I

L
|
L

P

P

N

G

-
x
M

K

T

A

A

C

C

I

I

R

E

C

C

L

T

Y

L

P

E

G
x
L

V
x
Y

P

P

K

P

A

Q

G

V

S

N

L

F

P

P

T

M

C
|
C

100:124 (vs. 55:79, 52% identical) binding ATP
I148 (= I100) mutation to A: No effect on NEDD8 adenylation.
148:171 (vs. 100:127, 29% identical) binding ATP
HI 160:161 (≠ DL 116:117) mutation to AA: Reduces affinity for UBE2M.
D167 (= D123) mutation to A: Abolishes NEDD8 adenylation.
P192 (vs. gap) mutation to A: Reduces affinity for UBE2M; when associated with A-195 and A-197.
I195 (≠ K139) mutation to A: Reduces affinity for UBE2M; when associated with A-192 and A-197.
P197 (= P141) mutation to A: Reduces affinity for UBE2M; when associated with A-192 and A-195.
R211 (≠ M155) mutation to Q: Abolishes specificity for NEDD8.
L214 (= L158) mutation to A: Reduces affinity for UBE2M; when associated with A-217.
M217 (vs. gap) mutation to A: Reduces affinity for UBE2M; when associated with A-214.
LY 227:228 (≠ GV 170:171) mutation to DD: Strongly reduces NEDD8 adenylation.
C237 (= C180) mutation to S: Abolishes thioester intermediate formation.

Sites not aligning to the query:

9 K → R: in dbSNP:rs17852113
65 F→G: Reduces affinity for UBE2M.
238 T→A: No effect on NEDD8 adenylation; impairs thioester intermediate formation.
242:248 Interaction with NAE1
292:295 Interaction with NAE1
310 I→A: No effect on NEDD8 adenylation or thioester intermediate formation; impairs NEDD8 transfer to UBE2M.
331 I→A: Reduces affinity for UBE2M.
352:357 YTYTFE→ATATA: Abolishes NEDD8 adenylation.
368 S→P: Impairs NEDD8 transfer to UBE2M.
369 Q→P: No effect on NEDD8 transfer to UBE2M.
370 L→P: Impairs NEDD8 transfer to UBE2M.
412 T→A: Impairs NEDD8 transfer to UBE2M.
415 L→A: Impairs NEDD8 transfer to UBE2M.
418 V→A: Impairs NEDD8 transfer to UBE2M.
421 I→A: Impairs NEDD8 transfer to UBE2M.
424 R→A: No effect on NEDD8 transfer to UBE2M.

3gznB Structure of nedd8-activating enzyme in complex with nedd8 and mln4924 (see paper)
33% identity, 46% coverage: 27:180/338 of query aligns to 40:205/429 of 3gznB

query
sites
3gznB

V

V

A

L

I

V

V

I

G

G

C

A

G
|
G

A
x
G

L

L

G

G

T

C

V

E

A

L

N

K

N

N

L

L

A

A

R

L

A

S

G

G

V

F

G

R

K

Q

I

I

T

H

I

V

I

I

D
|
D

R
x
M

D
|
D

F

T

V

I

E

D

L

V

N

S

N

N

L

L

Q

N

R

R

Q

Q

M

F

L

L

F

F

D

R

E

P

K

K

D

D

V

I

G

G

A

R

P

P

K

K

A

A

V

E

A

V

A

A

Q

E

K

F

V

L

H

N

D

D

I

R

N

V

S

P

E

N

I

C

E

N

V

V

P

P

V

H

-

F

-

N

-
x
K

I
|
I

K
x
Q

D

D

L

F

N

N

Y

D

T

T

N

-

A

-

E

-

L

F

L

Y

E

R

N

Q

V

F

D

H

L

I

V

I

V

V

D

C

G

G

T
x
L

D
|
D

N

S

I

I

L

I

T
x
A

R

R

M

R

L
x
W

V

I

N

N

D

G

I

M

C

L

V

I

-

S

-

L

-

N

-

Y

-

E

-

D

-

G

-

V

-

L

-

D

-

P

K

S

N

S

K

I

I

V

P

P

W

L

I

I

Y

D

T

G

G

G

A

T

I

E

G

G

T

F

S

K

G

G

M

N

S

A

M

R

N

V

I

I

L

L

P

P

N

G

-

M

K

T

A

A

C

C

I

I

R

E

C
|
C

L

T

Y

L

P

E

G

L

V

Y

P

P

K

P

A

Q

G

V

S

N

L

F

P

P

T

M

C
|
C

active site: D135 (= D123), C205 (= C180)
binding [(1S,2S,4R)-4-{4-[(1S)-2,3-dihydro-1H-inden-1-ylamino]-7H-pyrrolo[2,3-d]pyrimidin-7-yl}-2-hydroxycyclopentyl]methyl sulfamate: G46 (= G33), G47 (≠ A34), D68 (= D55), M69 (≠ R56), D70 (= D57), K115 (vs. gap), I116 (= I100), Q117 (≠ K101), L134 (≠ T122), D135 (= D123), A139 (≠ T127), W142 (≠ L130)
binding zinc ion: C191 (= C166)

Sites not aligning to the query:

active site: 10, 206, 208
binding zinc ion: 332, 335

Query Sequence

>WP_013644802.1 NCBI__GCF_000191585.1:WP_013644802.1
MQSRYSRQVILENIGKEGQEKLLKSSVAIVGCGALGTVAANNLARAGVGKITIIDRDFVE
LNNLQRQMLFDEKDVGAPKAVAAAQKVHDINSEIEVVPVIKDLNYTNAEELLENVDLVVD
GTDNILTRMLVNDICVKNKIPWIYTGAIGTSGMSMNILPNKACIRCLYPGVPKAGSLPTC
DTMGVLNTATVIMGSIETTEALKILLGYYDDDESTDSNLIVYDTWNHSFDTISVRKNEKC
ECCGNQNYEYIDSDEQEIITSLCGRNSIQITPADPKELSLKKIAENLEKLGKVKCSDFIM
IFSTEETEISLFRDGRAIIKGTNDEKVARSIYARYIGT

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