SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_164926908.1 NCBI__GCF_000006985.1:WP_164926908.1 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)

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)
46% identity, 100% coverage: 1:245/245 of query aligns to 1:253/271 of Q72J02

query
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Q72J02

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C192 (vs. gap) 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.

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)
43% identity, 100% coverage: 1:245/245 of query aligns to 3:249/270 of D4GSF3

query
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D4GSF3

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C188 (≠ A184) 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.

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)
41% identity, 99% coverage: 2:244/245 of query aligns to 63:309/453 of Q9VLJ8

query
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Q9VLJ8

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Sites not aligning to the query:

62 modified: Phosphothreonine

1zud3 Structure of this-thif protein complex (see paper)
42% identity, 99% coverage: 3:245/245 of query aligns to 1:239/240 of 1zud3

query
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1zud3

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active site: R11 (= R13), D127 (= D129)
binding calcium ion: L14 (≠ A16), D16 (≠ P18)
binding zinc ion: C169 (= C170), C235 (= C241), C238 (= C244)

P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
42% identity, 99% coverage: 3:245/245 of query aligns to 1:244/251 of P30138

query
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P30138

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R

G

C
|
C

A

P

L

V

C
|
C

G

G

C169 (= C170) binding Zn(2+)
C172 (= C173) binding Zn(2+)
W174 (≠ F175) mutation to A: No adenylation of ThiS.
C184 (≠ A184) mutation to S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth.
C240 (= C241) binding Zn(2+)
C243 (= C244) binding Zn(2+)

1zfnA Structural analysis of escherichia coli thif (see paper)
42% identity, 99% coverage: 3:245/245 of query aligns to 1:244/244 of 1zfnA

query
sites
1zfnA

L

M

S

N

D

D

E

R

Q

D

C

F

Q

M

R

R

Y

Y

A

S

R
|
R

H

Q

L

I

A

L

L

L

P

D

E

D

V

I

G

A

E

L

A

D

G

G

Q

Q

E

Q

K

K

L

L

H

D

S

S

K

Q

V

V

L

L

V

I

I
|
I

G
|
G

A

L

G
|
G

L

L

G

G

S

T

P

P

A

A

F

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

T

T

I

L

G

V

L

L

M

A

D
|
D

G

D

D

D

T

D

V

V

D

H

L

L

S

S

N

N

L

L

Q

Q

R
|
R

Q
|
Q

I

I

L

L

H

F

T

T

A

E

S

D

V

I

G

D

A

R

N

P

K
|
K

T

S

A

Q

S

V

A

S

Q

Q

E

Q

R

R

L

L

K

T

A

Q

L

L

D

N

P

P

S

D

I

I

R

Q

I

L

E

T

T

A

H

L

P

Q

F

Q

R

R

L

L

R

T

K

G

E

E

N

A

A

L

T

K

E

D

I

A

L

V

A

A

R

R

Y

A

D

D

F

V

V

V

I

L

D

D

A

C

T
|
T

D
|
D

N

N

F

M

A

A

S
x
T

R

R

F

Q

L

E

I

I

A

N

R

A

A

A

C

C

H

V

E

A

A

L

S

N

K

T

P

P

W

L

S

I

H

T

G

A

G

S

I

A

R

V

N

G

F

F

H

G

G

G

Q

Q

T

L

M

M

T

V

I

L

I

T

-

P

P

P

G

W

Q

E

T

Q

A

G

C
|
C

Y

Y

C

R

C
|
C

I

L

F

W

H

P

E

D

E

N

D

Q

E

E

-

P

S

E

K

R

E

N

A

C

I

R

P

T

Q

A

G

G

P

V

I

V

G

G

A

P

L

V

P

V

G

G

V

V

I

M

G

G

S

T

I

L

Q

Q

A

A

I

L

E

E

A

A

I

I

K

K

Y

L

L

L

L

S

N

G

I

I

G

E

T

T

L

P

L

A

T

G

D

E

A

-

L

L

M

R

T

L

F

F

D

D

A

G

L

K

T

S

M

S

S

Q

F

W

R

R

K

S

V

L

A

A

V

L

R

R

N

A

S

S

R

G

C
|
C

A

P

L

V

C
|
C

G

G

active site: R11 (= R13), D127 (= D129)
binding adenosine-5'-triphosphate: I34 (= I36), G35 (= G37), G37 (= G39), G38 (= G40), D59 (= D61), R70 (= R72), Q71 (= Q73), K83 (= K85), T126 (= T128), D127 (= D129), T131 (≠ S133)
binding zinc ion: C169 (= C170), C172 (= C173), C240 (= C241), C243 (= C244)

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)
40% identity, 99% coverage: 3:244/245 of query aligns to 61:318/482 of O59954

query
sites
O59954

L

L

S

H

D

G

E

E

Q

E

C

Y

Q

R

R

R

Y

Y

A

G

R

R

H

Q

L

M

A

I

L

V

P

P

E

Q

V

F

G

G

E

L

A

Q

G
|
G

Q

Q

E

L

K

K

L

L

L

R

H

D

S

A

K

K

V

V

L

L

V

I

I

V

G

G

A

A

G

G

L

L

G
|
G

S

C

P

P

A

A

F

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

T

T

I

I

G

G

L

L

M

V

D

D

G

G

D

D

T

T

V

V

D

E

L

A

S

S

N

N

L

L

Q

H

R
|
R

Q

Q

I

V

L

L

H

H

T

R

T

S

A

R

S

N

V

V

G

G

A

K

N

L

K

K

T

V

A

D

S

S

A

A

Q

I

E

E

R

Y

L

L

K

R

A

E

L

L

D

N

P

P

S

H

I

P

R

T

I

Y

E

I

T

A

H

H

P

Q

F

A

R

H

L

L

R

T

K

P

E

R

N

E

A

A

T

P

E

D

I

I

L

F

A

K

R

D

Y

Y

D

D

F

L

V

I

I

L

D

D

A
x
C

T

T

D

D

N

N

F

P

A

A

S

T

R

R

F

Y

L

L

I

I

A

S

R

D

A

T

C

A

H

V

E

L

A

L

S

G

K

K

P

P

W

L

S

V

H

S

G

A

G

S

I

A

R

L

N

R

F

T

H
x
E

G

G

Q

Q

T

L

M

M

T

V

I

L

-

N

-

P

-

Q

I

P

P

P

G

G

Q

D

T

K

A

T

-

G

-

P

C

C

Y

Y

C

R

C

C

I

V

F

F

H

P

E

K

E

P

D

P

E

P

S

A

K

N

E

S

A

V

I

T

P

S

-

C

-

A

-

D

Q

G

G

G

P

I

I

L

G

G

A

P

L

V

P

V

G
|
G

V

T

I

M

G

G

S

V

I

L

Q

Q

A

A

I

S

E

E

A

A

I

I

K

K

Y

V

L

L

L

T

N

S

I

A

G

G

T

E

L

S

L

V

-

E

-

A

-

T

T

P

D

P

A

S

L

L

M

L

T

I

F

F

D

S

A

A

L

Y

T

S

M

S

-

P

S

Q

F

F

R

R

K

T

V

I

A

K

V

L

R

R

-

S

R

R

N

R

S

P

R

N

C

C

A

A

L

V

C

C

G82 (= G24) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
G100 (= G42) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
R130 (= R72) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
C185 (≠ A127) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
E215 (≠ H157) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
G264 (= G195) 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)
40% identity, 99% coverage: 3:245/245 of query aligns to 4:248/249 of P12282

query
sites
P12282

L

L

S

S

D

D

E

Q

Q

E

C

M

Q

L

R

R

Y

Y

A

N

R
|
R

H

Q

L

I

A

I

L

L

P

R

E

G

V

F

G

D

E

F

A

D

G

G

Q

Q

E

E

K

A

L

L

L

K

H

D

S

S

K

R

V

V

L

L

V

I

I

V

G

G

A

L

G

G

L

L

G

G

S
x
C

P

A

A

A

A

S

F

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

T

N

I

L

G

T

L

L

M

L

D

D

G

F

D

D

T

T

V

V

D

S

L

L

S

S

N

N

L

L

Q

Q

R
|
R

Q

Q

I

T

L

L

H

H

T

S

T

D

A

A

S

T

V

V

G

G

A

Q

N

P

K

K

T

V

A

E

S

S

A

A

Q

R

E

D

R

A

L

L

K

T

A

R

L

I

D

N

P

P

S

H

I

I

R

A

I

I

E

T

T

P

H

V

P

N

F

A

R

L

L

L

R

D

K

D

E

A

N

E

A

L

T

A

E

A

I

L

L

I

A

A

R

E

Y

H

D

D

F

L

V

V

I

L

D

D

A
x
C

T

T

D
|
D

N

N

F

V

A

A

S

V

R

R

F

N

L

Q

I

L

A

N

R

A

A

G

C
|
C

H

F

E

A

A

A

S

K

K

V

P

P

W

L

S

V

H

S

G

G

G

A

I

A

R

I

N

R

F

M

H

E

G

G

Q

Q

T

-

M

I

T

T

I

V

I

F

P

T

G

Y

Q

Q

T

D

A

G

-

E

-

P

C
|
C

Y

Y

C

R

C
|
C

I

L

F

S

H

R

E

L

E

F

D

G

E

E

S

N

K

A

-

L

E

T

A
x
C

I

V

P

E

Q

A

G

G

P

V

I

M

G

A

A

P

L

L

P

I

G

G

V

V

I

I

G

G

S

S

I

L

Q

Q

A

A

I

M

E

E

A

A

I

I

K

K

Y

M

L

L

L

A

N

G

I

Y

G

G

T

K

L

P

L

A

T

S

D

G

A

K

L

I

M

V

T

M

F

Y

D

D

A

A

L

M

T

T

M
x
C

S

Q

F

F

R

R

K

E

V

M

A

K

V

L

R

M

R

R

N

N

S

P

R

G

C
|
C

A

E

L

V

C
|
C

G

G

R14 (= R13) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
C44 (≠ S43) mutation to A: No effect.
R73 (= R72) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
C128 (≠ A127) mutation to A: No effect.; mutation to Y: No activity.
D130 (= D129) mutation to A: No activity.; mutation to E: Substantially reduced activity.
C142 (= C141) mutation to A: No effect.
C172 (= C170) mutation to A: No zinc bound and no enzyme activity.
C175 (= C173) mutation to A: No zinc bound and no enzyme activity.
C187 (≠ A184) mutation to A: No effect.
C231 (≠ M228) mutation to A: No effect.
C244 (= C241) mutation to A: No zinc bound and almost no enzyme activity.
C247 (= C244) mutation to A: No zinc bound and almost no enzyme activity.

1jwbB Structure of the covalent acyl-adenylate form of the moeb-moad protein complex (see paper)
40% identity, 99% coverage: 3:245/245 of query aligns to 3:240/240 of 1jwbB

query
sites
1jwbB

L

L

S

S

D

D

E

Q

Q

E

C

M

Q

L

R

R

Y

Y

A

N

R
|
R

H

Q

L

I

A

I

L

L

P

R

E

G

V

F

G

D

E

F

A

D

G

G

Q

Q

E

E

K

A

L

L

L

K

H

D

S

S

K

R

V

V

L

L

V

I

I

V

G
|
G

A

L

G
|
G

L

L

G

G

S

C

P

A

A

A

A

S

F

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

T

N

I

L

G

T

L

L

M

L

D
|
D

G
x
F

D

D

T

T

V

V

D

S

L

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

I

T

L

L

H

H

T

S

T

D

A

A

S

T

V

V

G

G

A

Q

N

P

K
|
K

T

V

A

E

S

S

A

A

Q

R

E

D

R

A

L

L

K

T

A

R

L

I

D

N

P

P

S

H

I

I

R

A

I

I

E

T

T

P

H

V

P

N

F

A

R
x
L

L

L

R

D

K

D

E

A

N

E

A

L

T

A

E

A

I

L

L

I

A

A

R

E

Y

H

D

D

F

L

V

V

I

L

D

D

A
x
C

T
|
T

D
|
D

N
|
N

F

V

A

A

S
x
V

R

R

F

N

L

Q

I

L

A

N

R

A

A

G

C

C

H

F

E

A

A

A

S

K

K

V

P

P

W

L

S

V

H

S

G

G

G

A

I

A

R

I

N

R

F

M

H

E

G

G

Q

Q

T

-

M

I

T

T

I

V

I

F

P

T

G

Y

Q

Q

T

D

A

G

-

E

-

P

C
|
C

Y

Y

C

R

C

C

I

L

F

S

H

R

E

L

E

F

D

G

E

E

S

A

K

-

E

-

A

-

I

-

P

-

Q

-

G

G

P

V

I

M

G

A

A

P

L

L

P

I

G

G

V

V

I

I

G

G

S

S

I

L

Q

Q

A

A

I

M

E

E

A

A

I

I

K

K

Y

M

L

L

L

A

N

G

I

Y

G

G

T

K

L

P

L

A

T

S

D

G

A

K

L

I

M

V

T

M

F

Y

D

D

A

A

L

M

T

T

M

C

S

Q

F

F

R

R

K

E

V

M

A

K

V

L

R

M

R

R

N

N

S

P

R

G

C
|
C

A

E

L

V

C
|
C

G

G

active site: R13 (= R13), D129 (= D129)
binding adenosine monophosphate: G37 (= G37), G39 (= G39), G40 (= G40), D61 (= D61), F62 (≠ G62), K85 (= K85), L108 (≠ R108), C127 (≠ A127), T128 (= T128), D129 (= D129), N130 (= N130), V133 (≠ S133)
binding zinc ion: C171 (= C170), C236 (= C241), C239 (= C244)

1jw9B Structure of the native moeb-moad protein complex (see paper)
40% identity, 99% coverage: 3:245/245 of query aligns to 3:240/240 of 1jw9B

query
sites
1jw9B

L

L

S

S

D

D

E

Q

Q

E

C

M

Q

L

R

R

Y

Y

A

N

R
|
R

H

Q

L

I

A

I

L

L

P

R

E

G

V

F

G

D

E

F

A

D

G

G

Q

Q

E

E

K

A

L

L

L

K

H

D

S

S

K

R

V

V

L

L

V

I

I

V

G

G

A

L

G

G

L

L

G

G

S

C

P

A

A

A

A

S

F

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

T

N

I

L

G

T

L

L

M

L

D

D

G

F

D

D

T

T

V

V

D

S

L

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

I

T

L

L

H

H

T

S

T

D

A

A

S

T

V

V

G

G

A

Q

N

P

K

K

T

V

A

E

S

S

A

A

Q

R

E

D

R

A

L

L

K

T

A

R

L

I

D

N

P

P

S

H

I

I

R

A

I

I

E

T

T

P

H

V

P

N

F

A

R

L

L

L

R

D

K

D

E

A

N

E

A

L

T

A

E

A

I

L

L

I

A

A

R

E

Y

H

D

D

F

L

V

V

I

L

D

D

A

C

T

T

D
|
D

N

N

F

V

A

A

S

V

R

R

F

N

L

Q

I

L

A

N

R

A

A

G

C

C

H

F

E

A

A

A

S

K

K

V

P

P

W

L

S

V

H

S

G

G

G

A

I

A

R

I

N

R

F

M

H

E

G

G

Q

Q

T

-

M

I

T

T

I

V

I

F

P

T

G

Y

Q

Q

T

D

A

G

-

E

-

P

C
|
C

Y

Y

C

R

C

C

I

L

F

S

H

R

E

L

E

F

D

G

E

E

S

A

K

-

E

-

A

-

I

-

P

-

Q

-

G

G

P

V

I

M

G

A

A

P

L

L

P

I

G

G

V

V

I

I

G

G

S

S

I

L

Q

Q

A

A

I

M

E

E

A

A

I

I

K

K

Y

M

L

L

L

A

N

G

I

Y

G

G

T

K

L

P

L

A

T

S

D

G

A

K

L

I

M

V

T

M

F

Y

D

D

A

A

L

M

T

T

M

C

S

Q

F

F

R

R

K

E

V

M

A

K

V

L

R

M

R

R

N

N

S

P

R

G

C
|
C

A

E

L

V

C
|
C

G

G

active site: R13 (= R13), D129 (= D129)
binding zinc ion: C171 (= C170), C236 (= C241), C239 (= C244)

6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
40% identity, 86% coverage: 2:211/245 of query aligns to 6:214/289 of 6yubB

query
sites
6yubB

S

S

L

L

S

S

D

K

E

E

Q

E

C

I

Q

E

R

R

Y

Y

A

S

R

R

H

Q

L

M

A

I

L

V

P

P

E

G

V

M

G

G

E

K

A

E

G

G

Q

Q

E

L

K

R

L

L

L

M

H

N

S

A

K

K

V

V

L

L

V

I

I

I

G

G

A

A

G

G

L

L

G

G

S

C

P

P

A

A

F

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

T

T

I

I

G

G

L

I

M

V

D

D

G

G

D

D

T

S

V

V

D

E

L

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

I

V

L

A

H

H

T

A

T

T

A

K

S

R

V

V

G

G

A

M

N

L

K

K

T

V

A

D

S

S

A

L

Q

I

E

T

R

H

L

L

K

I

A

E

L

I

D

N

P

P

S

L

I

P

R

V

I

Y

E

V

T

P

H

Y

P

R

F

F

R

D

L

L

R

T

K

P

E

Q

N

N

A

A

T

A

E

Q

I

I

L

I

A

K

R

P

Y

W

D

D

F

V

V

I

I

L

D

D

A

C

T

T

D

D

N

N

F

P

A

A

S

T

R

R

F

Y

L

L

I

I

A

S

R

D

A

V

C

C

H

V

E

L

A

L

S

G

K

K

P

P

W

L

S

V

H

S

G

A

I

S

R

V

N

Q

F

K

H

S

G

G

Q

Q

T

L

M

I

T

V

I

L

I

N

P

C

G

P

Q

P

T

T

-

P

-

Q

-

G

-

V

-

N

-

K

-

A

A

P

C
|
C

Y

Y

C

R

C
|
C

I

C

F

F

H

-

E

-

D

-

E

-

S

-

K

-

E

-

A

-

I

-

P

-

Q

K

G

G

P

I

I

M

G

G

A

P

L

V

P

V

G

G

V

M

I

M

G

G

S

V

I

A

Q

Q

A

A

I

G

E

E

A

A

I

I

K

K

Y

I

L

L

L

V

N

S

binding zinc ion: C184 (= C170), C187 (= C173)

Sites not aligning to the query:

binding zinc ion: 265

6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
40% identity, 86% coverage: 2:211/245 of query aligns to 5:215/423 of 6yubA

query
sites
6yubA

S

S

L

L

S

S

D

K

E

E

Q

E

C

I

Q

E

R

R

Y

Y

A

S

R

R

H

Q

L

M

A

I

L

V

P

P

E

G

V

M

G

G

E

K

A

E

G

G

Q

Q

E

L

K

R

L

L

L

M

H

N

S

A

K

K

V

V

L

L

V

I

I

I

G

G

A

A

G

G

L

L

G

G

S

C

P

P

A

A

F

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

T

T

I

I

G

G

L

I

M

V

D

D

G

G

D

D

T

S

V

V

D

E

L

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

I

V

L

A

H

H

T

A

T

T

A

K

S

R

V

V

G

G

A

M

N

L

K

K

T

V

A

D

S

S

A

L

Q

I

E

T

R

H

L

L

K

I

A

E

L

I

D

N

P

P

S

L

I

P

R

V

I

Y

E

V

T

P

H

Y

P

R

F

F

R

D

L

L

R

T

K

P

E

Q

N

N

A

A

T

A

E

Q

I

I

L

I

A

K

R

P

Y

W

D

D

F

V

V

I

I

L

D

D

A

C

T

T

D

D

N

N

F

P

A

A

S

T

R

R

F

Y

L

L

I

I

A

S

R

D

A

V

C

C

H

V

E

L

A

L

S

G

K

K

P

P

W

L

S

V

H

S

G

A

I

S

R

V

N

Q

F

K

H

S

G

G

Q

Q

T

L

M

I

T

V

I

L

I

N

P

C

G

P

Q

P

T

T

-

P

-

Q

-

G

-

V

-

N

-

K

-

A

A

P

C
|
C

Y

Y

C

R

C
|
C

I

C

F

F

H

K

E

K

E

P

D

-

E

-

S

-

K

-

E

-

A

-

I

-

P

-

Q

-

G

G

P

I

I

M

G

G

A

P

L

V

P

V

G

G

V

M

I

M

G

G

S

V

I

A

Q

Q

A

A

I

G

E

E

A

A

I

I

K

K

Y

I

L

L

L

V

N

S

binding zinc ion: C183 (= C170), C186 (= C173)

Sites not aligning to the query:

binding zinc ion: 266, 269

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)
38% identity, 99% coverage: 3:245/245 of query aligns to 39:290/440 of P38820

query
sites
P38820

L

L

S

S

D

L

E

E

Q

E

C

Y

Q

Q

R

R

Y

Y

A

G

R

R

H

Q

L

M

A

I

L

V

P

E

E

E

V

T

G

G

-

G

E

V

A

A

G

G

Q

Q

E

V

K

K

L

L

L

K

H

N

S

T

K

K

V

V

L

L

V

V

I

V

G

G

A

A

G

G

L

L

G

G

S

C

P

P

A

A

A

L

F

P

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

T

Q

I

I

G

G

L

I

M

V

D

D

G

N

D

D

T

V

V

V

D

E

L

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

I

V

L

L

H

H

T

D

T

S

A

S

S

R

V

V

G

G

A

M

N

L

K

K

T

C

A

E

S

S

A

A

Q

R

E

Q

R

Y

L

I

K

T

A

K

L

L

D

N

P

P

S

H

I

I

R

N

I

V

E

V

T

T

H

Y

P

P

F

V

R

R

L

L

R

N

K

S

E

S

N

N

A

A

T

F

E

D

I

I

L

F

A

K

R

G

Y

Y

D

N

F

Y

V

I

I

L

D

D

A

C

T

T

D

D

N

S

F

P

A

L

S

T

R

R

F

Y

L

L

I

V

A

S

R

D

-

V

A

A

C

V

H

N

E

L

A

G

S

I

K

T

P

V

W

V

S

S

H

A

G

S

G

G

I

L

R

G

N

T

F

E

H

G

G

Q

Q

L

T

T

M

I

T

L

I

N

I

F

P

N

G

N

Q

I

T

G

A

P

C

C

Y

Y

C

R

C

C

I

-

F

F

H

Y

E

P

E

T

D

P

E

P

S

P

K

P

E

N

A

A

I

V

P

T

Q

S

-
x
C

-

Q

-

E

-

G

G

G

P

V

I

I

G

G

A

P

L

C

P

I

G

G

V

L

I

V

G

G

S

T

I

M

Q

M

A

A

I

V

E

E

A

T

I

L

K

K

Y

L

L

I

L

L

N

G

I

I

G

Y

T

T

-

N

-

E

L

N

L

F

T

S

D

P

A

F

L

L

M

M

T

L

F

Y

D

S

A

G

L

F

-

P

T

Q

M

Q

S

S

F

L

R

R

K

T

V

F

A

K

V

M

R

R

-

G

R

R

N

Q

S

E

R

K

C

C

A

L

L

C

C

C

G

G

C225 (vs. gap) 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.

1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
38% identity, 96% coverage: 3:237/245 of query aligns to 3:217/217 of 1jwaB

query
sites
1jwaB

L

L

S

S

D

D

E

Q

Q

E

C

M

Q

L

R

R

Y

Y

A

N

R
|
R

H

Q

L

I

A

I

L

L

P

R

E

G

V

F

G

D

E

F

A

D

G

G

Q

Q

E

E

K

A

L

L

L

K

H

D

S

S

K

R

V

V

L

L

V

I

I

V

G

G

A

L

G
|
G

L

L

G

G

S

C

P

A

A

A

A

S

F

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

T

N

I

L

G

T

L

L

M

L

D
|
D

G
x
F

D

D

T

T

V

V

D

S

L

L

S

S

N

N

L

L

Q

Q

R
|
R

Q

Q

I

T

L

L

H

H

T

S

T

D

A

A

S

T

V

V

G

G

A

Q

N

P

K
|
K

T

V

A

E

S

S

A

A

Q

R

E

D

R

A

L

L

K

T

A

R

L

I

D

N

P

P

S

H

I

I

R

A

I

I

E

T

T

P

H

V

P

N

F

A

R
x
L

L

L

R

D

K

D

E

A

N

E

A

L

T

A

E

A

I

L

L

I

A

A

R

E

Y

H

D

D

F

L

V

V

I

L

D

D

A

C

T

T

D
|
D

N
|
N

F

V

A

A

S
x
V

R

R

F

N

L

Q

I

L

A

N

R

A

A

G

C

C

H

F

E

A

A

A

S

K

K

V

P

P

W

L

S

V

H

S

G

G

G

A

I

A

R

I

N

R

F

M

H

E

G

G

Q

Q

T

I

M

-

T

-

I

-

P

-

G

-

Q

-

T

-

A

-

C

-

Y

-

C

-

C

T

I

V

F

F

H

T

E

Y

E

E

D

-

E

-

S

-

K

-

E

-

A

-

I

-

P

-

Q

A

G

G

P

V

I

M

G

A

A

P

L

L

P

I

G

G

V

V

I

I

G

G

S

S

I

L

Q

Q

A

A

I

M

E

E

A

A

I

I

K

K

Y

M

L

L

L

A

N

G

I

Y

G

G

T

K

L

P

L

A

T

S

D

G

A

K

L

I

M

V

T

M

F

Y

D

D

A

A

L

M

T

T

M

C

S

Q

F

F

R

R

K

E

V

M

A

K

V

L

R

M

R

R

active site: R13 (= R13), D129 (= D129)
binding adenosine-5'-triphosphate: G39 (= G39), G40 (= G40), D61 (= D61), F62 (≠ G62), R72 (= R72), K85 (= K85), L108 (≠ R108), D129 (= D129), N130 (= N130), V133 (≠ S133)

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)
38% identity, 100% coverage: 2:245/245 of query aligns to 54:301/460 of O95396

query
sites
O95396

S

A

L

L

S

S

D

R

E

D

Q

E

C

I

Q

L

R

R

Y

Y

A

S

R

R

H

Q

L

L

A

V

L

L

P

P

E

E

V

L

G

G

E

V

A

H

G

G

Q

Q

E

L

K

R

L

L

L

G

H

T

S

A

K

C

V

V

L

L

V

I

I

V

G

G

A

C

G

G

L

L

G

G

S

C

P

P

A

L

A

A

F

Q

Y

Y

L

L

A

A

G

G

V

V

G

G

T

R

I

L

G

G

L

L

M

V

D

D

G

Y

D

D

T

V

V

V

D

E

L

M

S

S

N

N

L

L

Q

A

R

R

Q

Q

I

V

L

L

H

H

T

G

T

E

A

A

S

L

V

A

G

G

A

Q

N

A

K

K

T

A

A

F

S

S

A

A

Q

A

E

A

R

S

L

L

K

R

A

R

L

L

D

N

P

S

S

A

I

V

R

E

I

C

E

V

T

P

H

Y

P
x
T

F
x
Q

R
x
A

L
|
L

R
x
T

K
x
P

E
x
A

N
x
T

A
|
A

T
x
L

E
x
D

I
x
L

L
x
V

A
x
R

R
|
R

Y
|
Y

D
|
D

F
x
V

V
|
V

I
x
A

D
|
D

A
x
C

T
x
S

D
|
D

N
|
N

F
x
V

A
x
P

S
x
T

R
|
R

F
x
Y

L
|
L

I
x
V

A
x
N

R
x
D

A
|
A

C
|
C

H
x
V

E
x
L

A
|
A

S
x
G

K
x
R

P
|
P

W
x
L

S
x
V

H
x
S

G
x
A

G
x
S

I
x
A

R
x
L

N
x
R

F
|
F

H
x
E

G
|
G

Q
|
Q

T
x
I

M
x
T

T
x
V

I
x
Y

I
x
H

P
x
Y

G
x
D

Q
x
G

T
x
G

A
x
P

C
|
C

Y
|
Y

C
x
R

C
|
C

I
|
I

F
|
F

H
x
P

E
x
Q

E
x
P

D
x
P

E
x
P

S
x
A

K
x
E

E
x
T

A
x
V

I
x
T

-
x
N

-
x
C

-

A

P

D

Q

G

G

G

P

V

I

L

G

G

A

V

L

V

P

T

G

G

V

V

I

L

G

G

S

C

I

L

Q

Q

A

A

I

L

E

E

A

V

I

L

K

K

Y

I

L

A

N

G

I

L

G

G

T

P

L

S

L

Y

T

S

D

G

A

S

L

L

M

L

T

L

F

F

D

D

A

A

L

L

T

R

M

G

S

H

F

F

R

R

K

S

V

I

A

R

V

L

R

R

R

S

N

R

S

R

R

L

-

D

C

C

A

A

L

A

C

C

G

G

158:238 (vs. 106:185, 28% identical) Interaction with NFS1
C239 (vs. gap) 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.

6h77B E1 enzyme for ubiquitin like protein activation in complex with ubl (see paper)
27% identity, 94% coverage: 11:241/245 of query aligns to 18:268/302 of 6h77B

query
sites
6h77B

Y

Y

A

S

R

R

H

L

L

M

A

A

L

L

P

K

E

R

V

M

G

G

-

I

E

V

A

S

G

D

Q

Y

E

E

K

K

L

I

L

R

H

T

S

F

K

A

V

V

L

A

V

I

I

V

G
|
G

A

V

G
|
G

L

V

G

G

S

S

P

V

A

T

A

A

F

E

Y

M

L

L

A

T

A

R

A

C

G

G

V

I

G

G

T

K

I

L

G

L

L

L

M

F

D
|
D

G
x
Y

D
|
D

T

K

V

V

D

E

L

L

S

A

N
|
N

L

M

Q

N

R
|
R

Q

-

I

L

L

F

H

F

T

Q

T

P

A

H

S

Q

V

A

G

G

A

L

N

S

K
|
K

T

V

A

Q

S

A

A

A

Q

E

E

H

R

T

L

L

K

R

A

N

L

I

D

N

P

P

S

D

I

V

R

L

I

F

E

E

T

V

H

H

P

N

F

Y

R
x
N

L
x
I

R

T

K

T

-

V

E

E

N

N

A

F

T

Q

E

H

I

F

L

M

A

D

R

R

-

I

-

S

-

N

-

G

-

L

-

E

-

G

-

K

-

P

Y

V

D

D

F

L

V

V

I

L

D

S

A

C

T

V

D
|
D

N
|
N

F

F

A

E

S

A

R

R

F

M

L

T

I

I

A

N

R

T

A

A

C

C

H

N

E

E

A

L

S

G

K

Q

P

T

W

W

S

M

H

E

G

S

G

G

I

V

R

S

N

E

-

N

-

A

F

V

H

S

G

G

Q

H

T

I

M

Q

T

L

I

I

P

P

G

G

Q

E

T

S

A

A

C
|
C

Y

F

C

A

C
|
C

I

A

-

P

-

L

-

V

-

A

-

N

F

I

H

D

E

E

E

K

D

T

E

L

S

K

K

R

E

E

A

G

I

V

P

C

Q

A

G

A

P

S

I

L

G

P

A

T

L

T

P

M

G

G

V

V

I

V

G

A

S

G

I

I

Q

L

A

V

I

Q

E

N

A

V

I

L

K

K

Y

F

L

L

N

N

I

F

G

G

T

T

L

V

L

-

T

-

D

S

A

F

L

Y

M

L

T

G

F

Y

D

N

A

A

L

M

T

Q

M

D

S

F

F

F

R

P

K

T

V

M

A

S

V

M

R

K

R

P

N

N

S

P

R

Q

C
|
C

binding adenosine-5'-triphosphate: G45 (= G37), G47 (= G39), G48 (= G40), D69 (= D61), Y70 (≠ G62), D71 (= D63), N77 (= N69), R80 (= R72), K92 (= K85), N115 (≠ R108), I116 (≠ L109), D148 (= D129), N149 (= N130)
binding zinc ion: C191 (= C170), C194 (= C173), C268 (= C241)

Sites not aligning to the query:

binding zinc ion: 273

Q9GZZ9 Ubiquitin-like modifier-activating enzyme 5; Ubiquitin-activating enzyme 5; ThiFP1; UFM1-activating enzyme; Ubiquitin-activating enzyme E1 domain-containing protein 1 from Homo sapiens (Human) (see 12 papers)
27% identity, 94% coverage: 11:241/245 of query aligns to 53:303/404 of Q9GZZ9

query
sites
Q9GZZ9

Y

Y

A

S

R
|
R

H

L

L
x
M

A

A

L

L

P

K

E

R

V

M

G

G

-

I

E

V

A

S

G

D

Q

Y

E

E

K

K

L

I

L

R

H

T

S

F

K

A

V

V

L

A

V

I

I

V

G

G

A

V

G

G

G
|
G

L

V

G

G

S

S

P

V

A

T

A

A

F

E

Y

M

L

L

A

T

A

R

A

C

G

G

V

I

G

G

T

K

I

L

G

L

L

L

M

F

D
|
D

G

Y

D

D

T

K

V

V

D

E

L

L

S

A

N

N

L

M

Q

N

R

R

Q

-

I

L

L

F

H

F

T

Q

T

P

A

H

S

Q

V

A

G

G

A

L

N

S

K
|
K

T

V

A

Q

S

A

A

A

Q

E

E

H

R

T

L

L

K

R

A

N

L

I

D

N

P

P

S

D

I

V

R

L

I

F

E

E

T

V

H

H

P

N

F

Y

R
x
N

L

I

R

T

K

T

-

V

E

E

N

N

A

F

T

Q

E

H

I

F

L

M

A

D

R

R

-

I

-

S

-

N

-

G

-
x
G

-

L

-

E

-

G

-

K

-

P

Y

V

D

D

F

L

V

V

I

L

D

S

A

C

T

V

D

D

N
|
N

F

F

A

E

S

A

R
|
R

F

M

L

T

I

I

A

N

R

T

A

A

C

C

H

N

E

E

A

L

S

G

K

Q

P

T

W

W

S

M

H

E

G

S

G

G

I

V

R

S

N

E

-

N

-

A

F

V

H

S

G

G

Q
x
H

T
x
I

M
x
Q

T

L

I

I

P

P

G

G

Q

E

T

S

A

A

C
|
C

Y

F

C

A

C
|
C

I
x
A

-
x
P

-
x
L

-

V

-

A

-

N

F

I

H

D

E

E

E

K

D

T

E

L

S

K

K
x
R

E
|
E

A
x
G

I
x
V

P
x
C

Q
x
A

G
x
A

P
x
S

I
x
L

G
x
P

A
x
T

L
x
T

P
x
M

G
|
G

V
|
V

I
x
V

G
x
A

S
x
G

I
|
I

Q
x
L

A
x
V

I
x
Q

E
x
N

A
x
V

I
x
L

K
|
K

Y
x
F

L
|
L

N
|
N

I
x
F

G
|
G

T
|
T

L
x
V

L

-

T

-

D
x
S

A
x
F

L
x
Y

M
x
L

T
x
G

F
x
Y

D
x
N

A
|
A

L
x
M

T
x
Q

M
x
D

S
x
F

F
|
F

R
x
P

K
x
T

V
x
M

A
x
S

V
x
M

R
x
K

R
x
P

N
|
N

S
x
P

R
x
Q

C
|
C

R55 (= R13) to H: in DEE44; reduces UFM1 activating enzyme activity; dbSNP:rs774318611
M57 (≠ L15) to V: in DEE44; reduces UFM1 activating enzyme activity; reduces UFM1-DDRGK1 formation; dbSNP:rs532178791
G83 (= G40) binding ATP
D104 (= D61) binding ATP
K127 (= K85) binding ATP
N150 (≠ R108) binding ATP
G168 (vs. gap) to E: in DEE44; abolishes UFM1 activating enzyme activity; dbSNP:rs886039761
N184 (= N130) binding ATP
R188 (= R134) mutation to A: Abolished ability to activate UFM1.
HIQ 215:217 (≠ QTM 159:161) mutation to AQA: Abolished ability to activate UFM1.
C226 (= C170) binding Zn(2+)
C229 (= C173) binding Zn(2+)
APPL 230:233 (≠ I--- 174) mutation APPL->RPPA,FPPA: Abolished interaction with UFM1.
C250 (≠ P186) active site, Glycyl thioester intermediate; mutation to A: Abolished ability to activate UFM1.; mutation to S: Forms a stable intermediate complex.
V260 (= V196) to M: in DEE44; reduces UFM1 activating enzyme activity; dbSNP:rs886039759
K271 (= K207) mutation to D: Impaired ability to activate UFM1 via a trans-binding mechanism.
D290 (≠ M228) mutation to K: Impaired homodimerization and ability to activate UFM1 via a trans-binding mechanism.
C303 (= C241) binding Zn(2+)

Sites not aligning to the query:

246:404 natural variant: Missing (in SCAR24; delocalizes protein to the nucleus; activates degradation through the ubiquitin proteasome pathway; decreases protein stability; disrupts interaction with UFM1)
308 binding Zn(2+)
310 K → E: in SCAR24; does not affect cytoplasm localization; decreases protein stability; does not affect interaction with UFM1; dbSNP:rs886039762
334:346 UFM1-interacting sequence (UIS)
336 mutation H->A,D: Impaired ability to activate UFM1.
341 W→A: Abolished interaction with UFM1 and GABARAPL2.
342 G→A: Decreased interaction with UFM1 without affecting interaction with GABARAPL2.
343 I→A: Abolished interaction with UFM1 and decreased interaction with GABARAPL2.
343:345 IEL→AEA: Impaired ability to activate UFM1.
345 L→A: Abolished interaction with UFM1 and decreased interaction with GABARAPL2.
346 V→A: Abolished interaction with UFM1 and decreased interaction with GABARAPL2.
371 A → T: in DEE44; reduces UFM1 activating enzyme activity; reduces UFM1 activating enzyme activity; reduces UFM1-DDRGK1 formation; dbSNP:rs114925667
389 D → Y: in DEE44; no effect on UFM1 activating enzyme activity; dbSNP:rs886039760

O42939 Ubiquitin-activating enzyme E1-like; Pmt3-activating enzyme subunit 2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 58% coverage: 31:173/245 of query aligns to 26:169/628 of O42939

query
sites
O42939

S

A

K

K

V

V

L

L

V

L

I

V

G

G

A

A

G

G

L

I

G

G

S

C

P

E

A

L

F

K

Y

N

L

L

A

L

A

M

A

S

G

G

V

V

G

K

T

E

I

V

G

H

L

I

M

I

D

D

G

L

D

D

T

T

V

I

D

D

L

L

S

S

N

N

L

L

Q

N

R

R

Q

Q

I

F

L

L

H

F

T

R

T

K

A

K

S

H

V

V

G

K

A

Q

N

P

K

K

T

A

A

I

S

V

A

A

Q

A

E

K

R

T

L

A

K

S

A

S

L

F

D

N

P

P

S

N

I

V

R

K

I

L

E

E

T

A

H

Y

P

H

F

A

R

N

L

I

R

K

K

E

E

D

N

R

A

F

T

N

E

V

I

A

L

W

A

F

R

R

-

Q

Y

F

D

D

F

L

V

V

I

F

D

N

A

A

T

L

D

D

N

N

F

L

A

D

S

A

R

R

F

R

L

H

I

V

A

N

R

K

A

Q

C

C

H

L

E

L

A

A

S

S

K

V

P

P

W

L

S

I

H

E

G

S

G

G

I

T

R

T

N

G

F

F

H

L

G

G

Q

Q

T

V

M

Q

T

V

I

I

P

H

G

G

Q

K

T

T

A

E

C

C

Y

Y

C

D

C

C

Sites not aligning to the query:

559 modified: Phosphoserine
563 modified: Phosphoserine

Q7SXG4 SUMO-activating enzyme subunit 2; Ubiquitin-like 1-activating enzyme E1B; Ubiquitin-like modifier-activating enzyme 2; EC 2.3.2.- from Danio rerio (Zebrafish) (Brachydanio rerio) (see paper)
33% identity, 76% coverage: 26:211/245 of query aligns to 14:195/650 of Q7SXG4

query
sites
Q7SXG4

E

D

K

S

L

L

L

S

H

S

S

C

K

R

V

V

L

L

V

V

I

V

G

G

A

A

G

G