SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 14951 FitnessBrowser__Keio:14951 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)

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)
100% identity, 100% coverage: 1:249/249 of query aligns to 1:249/249 of P12282

query
sites
P12282

M

M

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P

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H

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D

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E

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E

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H

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D

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D

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C

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T

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D

N

N

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A

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R

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N

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L

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N

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G

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C

F

F

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R14 (= R14) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
C44 (= C44) mutation to A: No effect.
R73 (= R73) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
C128 (= C128) mutation to A: No effect.; mutation to Y: No activity.
D130 (= D130) mutation to A: No activity.; mutation to E: Substantially reduced activity.
C142 (= C142) mutation to A: No effect.
C172 (= C172) mutation to A: No zinc bound and no enzyme activity.
C175 (= C175) mutation to A: No zinc bound and no enzyme activity.
C187 (= C187) mutation to A: No effect.
C231 (= C231) mutation to A: No effect.
C244 (= C244) mutation to A: No zinc bound and almost no enzyme activity.
C247 (= C247) 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)
97% identity, 99% coverage: 2:248/249 of query aligns to 1:240/240 of 1jwbB

query
sites
1jwbB

A

A

E

E

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L

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F

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G

E

-

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-

A

-

L

-

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-

C

-

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-

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A

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M

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G

active site: R13 (= R14), D129 (= D130)
binding adenosine monophosphate: V36 (= V37), G37 (= G38), L38 (= L39), G39 (= G40), G40 (= G41), L60 (= L61), D61 (= D62), F62 (= F63), D63 (= D64), R72 (= R73), K85 (= K86), L108 (= L109), C127 (= C128), T128 (= T129), D129 (= D130), N130 (= N131), V133 (= V134)
binding zinc ion: C171 (= C172), C174 (= C175), C236 (= C244), C239 (= C247)

1jw9B Structure of the native moeb-moad protein complex (see paper)
97% identity, 99% coverage: 2:248/249 of query aligns to 1:240/240 of 1jw9B

query
sites
1jw9B

A

A

E

E

L

L

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S

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D

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Q

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E

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M

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L

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R

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Y

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D

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N

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I

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P

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H

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N

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E

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A

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A

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R

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L

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N

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A

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A

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C

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L

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R

L

L

F

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G

G

E

-

N

-

A

-

L

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T

-

C

-

V

-

E

E

A

A

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G

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M

M

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A

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L

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G

active site: R13 (= R14), D129 (= D130)
binding zinc ion: C171 (= C172), C174 (= C175), C236 (= C244), C239 (= C247)

1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
91% identity, 96% coverage: 2:240/249 of query aligns to 1:217/217 of 1jwaB

query
sites
1jwaB

A

A

E

E

L

L

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Y

Y

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A

A

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G

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N

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D

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D

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T

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G

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K

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A

A

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R

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D

A

A

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L

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T

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R

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I

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N

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P

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H

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I

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A

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I

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T

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P

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V

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N

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A

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L

L

L

D

D

A

A

E

E

L

L

A

A

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L

I

I

A

A

E

E

H

H

D

D

L

L

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L

L

D

D

C
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C

T
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T

D
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D

N
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N

V

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A

A

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V

R

R

N

N

Q

Q

L

L

N

N

A

A

G

G

C

C

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F

A

A

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K

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-

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-

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-

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F

-

G

-

E

-

N

-

A

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L

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-

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-

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E

A

A

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G

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M

M

A

A

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P

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L

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L

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A

A

M

M

E

E

A

A

I

I

K

K

M

M

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L

A

A

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K

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K

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M

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Y

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A

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C

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Q

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K

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M

R

R

active site: R13 (= R14), D129 (= D130)
binding adenosine-5'-triphosphate: V36 (= V37), G37 (= G38), G39 (= G40), G40 (= G41), L60 (= L61), D61 (= D62), F62 (= F63), D63 (= D64), N69 (= N70), R72 (= R73), Q73 (= Q74), K85 (= K86), L108 (= L109), C127 (= C128), T128 (= T129), D129 (= D130), N130 (= N131), V133 (= V134)

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)
44% identity, 99% coverage: 2:247/249 of query aligns to 62:309/453 of Q9VLJ8

query
sites
Q9VLJ8

A
x
T

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K

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K

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D

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D

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-

P

P

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C

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Y

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C

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-

P

F

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P

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C

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T

I

I

G

G

S

A

L

M

Q

Q

A

A

M

L

E

E

A

A

I

I

K

K

M

V

L

I

A

V

G

G

Y

M

G

G

K

D

P

V

A

L

S

A

G

G

K

R

I

L

V

L

M

I

Y

F

D

D

A

G

M

G

T

S

C

G

Q

V

F

F

R

R

E

N

M

I

K

R

L

I

M

R

-

S

R

K

N

R

P

P

G

N

C

C

E

H

V

M

C

C

T62 (≠ A2) modified: Phosphothreonine

P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
45% identity, 98% coverage: 4:248/249 of query aligns to 1:244/251 of P30138

query
sites
P30138

L

M

S

N

D

D

Q

R

E

D

M

F

L

M

R

R

Y

Y

N

S

R

R

Q

Q

I

I

I

L

L

L

R

D

G

D

F

I

D

A

F

L

D

D

G

G

Q

Q

E

Q

A

K

L

L

K

L

D

D

S

S

R

Q

V

V

L

L

I

I

V

I

G

G

L

L

G

G

L

L

G

G

C

T

A

P

A

A

S

A

Q

L

Y

Y

L

L

A

A

S

G

A

A

G

G

V

V

G

G

N

T

L

L

T

V

L

L

L

A

D

D

F

D

D

D

T

D

V

V

S

H

L

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

T

I

L

L

H

F

S

T

D

T

A

E

T

D

V

I

G

D

Q

R

P

P

K

K

V

S

E

Q

S

V

A

S

R

Q

D

Q

A

R

L

L

T

T

R

Q

I

L

N

N

P

P

H

D

I

I

A

Q

I

L

T

T

P

A

V

L

N

Q

A

Q

L

R

L

L

D

T

D

G

A

E

E

A

L

L

A

K

A

D

L

A

I

V

A

A

E

R

H

A

D

D

L

V

V

V

L

L

D

D

C

C

T

T

D

D

N

N

V

M

A

A

V

T

R

R

N

Q

Q

E

L

I

N

N

A

A

G

A

C

C

F

V

A

A

A

L

K

N

V

T

P

P

L

L

V

I

S

T

G

A

A

S

A

A

I

V

R

G

M

F

E

G

G

G

Q

Q

I

L

T

M

V

V

F

L

T

T

Y

P

Q

P

D

W

G

E

E

Q

P

G

C
|
C

Y

Y

R

R

C
|
C

L

L

S
x
W

R

P

L

D

F

N

G

Q

E

E

N

P

A

E

L

R

T

N

C
|
C

V

R

E

T

A

A

G

G

V

V

M

V

A

G

P

P

L

V

I

V

G

G

V

V

I

M

G

G

S

T

L

L

Q

Q

A

A

M

L

E

E

A

A

I

I

K

K

M

L

L

L

A

S

G

G

Y

I

G

E

K

T

P

P

A

A

S

-

G

G

K

E

I

L

V

R

M

L

Y

F

D

D

A

G

M

K

T

S

C

S

Q

Q

F

W

R

R

E

S

M

L

K

A

L

L

M

R

R

R

N

A

P

S

G

G

C
|
C

E

P

V

V

C
|
C

G

G

C169 (= C172) binding
C172 (= C175) binding
W174 (≠ S177) mutation to A: No adenylation of ThiS.
C184 (= C187) mutation to S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth.
C240 (= C244) binding
C243 (= C247) binding

1zfnA Structural analysis of escherichia coli thif (see paper)
45% identity, 98% coverage: 4:248/249 of query aligns to 1:244/244 of 1zfnA

query
sites
1zfnA

L

M

S

N

D

D

Q

R

E

D

M

F

L

M

R

R

Y

Y

N

S

R
|
R

Q

Q

I

I

I

L

L

L

R

D

G

D

F

I

D

A

F

L

D

D

G

G

Q

Q

E

Q

A

K

L

L

K

L

D

D

S

S

R

Q

V

V

L

L

I

I

V
x
I

G
|
G

L
|
L

G
|
G

L

L

G

G

C

T

A

P

A

A

S

A

Q

L

Y

Y

L

L

A

A

S

G

A

A

G

G

V

V

G

G

N

T

L

L

T

V

L

L

L
x
A

D
|
D

F

D

D
|
D

T

D

V

V

S

H

L

L

S

S

N
|
N

L

L

Q

Q

R
|
R

Q
|
Q

T

I

L

L

H

F

S

T

D

T

A

E

T

D

V

I

G

D

Q

R

P

P

K
|
K

V

S

E

Q

S

V

A

S

R

Q

D

Q

A

R

L

L

T

T

R

Q

I

L

N

N

P

P

H

D

I

I

A

Q

I

L

T

T

P

A

V

L

N

Q

A
x
Q

L
x
R

L
|
L

D

T

D

G

A

E

E

A

L

L

A

K

A

D

L

A

I

V

A

A

E

R

H

A

D

D

L

V

V

V

L

L

D

D

C
|
C

T
|
T

D
|
D

N

N

V

M

A

A

V
x
T

R

R

N

Q

Q

E

L

I

N

N

A

A

G

A

C

C

F

V

A

A

A

L

K

N

V

T

P

P

L

L

V

I

S

T

G

A

A

S

A

A

I

V

R

G

M

F

E

G

G

G

Q

Q

I

L

T

M

V

V

F

L

T

T

Y

P

Q

P

D

W

G

E

E

Q

P

G

C
|
C

Y

Y

R

R

C
|
C

L

L

S

W

R

P

L

D

F

N

G

Q

E

E

N

P

A

E

L

R

T

N

C

C

V

R

E

T

A

A

G

G

V

V

M

V

A

G

P

P

L

V

I

V

G

G

V

V

I

M

G

G

S

T

L

L

Q

Q

A

A

M

L

E

E

A

A

I

I

K

K

M

L

L

L

A

S

G

G

Y

I

G

E

K

T

P

P

A

A

S

-

G

G

K

E

I

L

V

R

M

L

Y

F

D

D

A

G

M

K

T

S

C

S

Q

Q

F

W

R

R

E

S

M

L

K

A

L

L

M

R

R

R

N

A

P

S

G

G

C
|
C

E

P

V

V

C
|
C

G

G

active site: R11 (= R14), D127 (= D130)
binding adenosine-5'-triphosphate: I34 (≠ V37), G35 (= G38), L36 (= L39), G37 (= G40), G38 (= G41), A58 (≠ L61), D59 (= D62), D61 (= D64), N67 (= N70), R70 (= R73), Q71 (= Q74), K83 (= K86), Q105 (≠ A108), R106 (≠ L109), L107 (= L110), C125 (= C128), T126 (= T129), D127 (= D130), T131 (≠ V134)
binding zinc ion: C169 (= C172), C172 (= C175), C240 (= C244), C243 (= C247)

1zud3 Structure of this-thif protein complex (see paper)
45% identity, 98% coverage: 4:248/249 of query aligns to 1:239/240 of 1zud3

query
sites
1zud3

L

M

S

N

D

D

Q

R

E

D

M

F

L

M

R

R

Y

Y

N

S

R
|
R

Q

Q

I

I

I
x
L

L

L

R
x
D

G

D

F

I

D

A

F

L

D

D

G

G

Q

Q

E

Q

A

K

L

L

K

L

D

D

S

S

R

Q

V

V

L

L

I

I

V

I

G

G

L

L

G

G

L

L

G

G

C

T

A

P

A

A

S

A

Q

L

Y

Y

L

L

A

A

S

G

A

A

G

G

V

V

G

G

N

T

L

L

T

V

L

L

L

A

D

D

F

D

D

D

T

D

V

V

S

H

L

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

T

I

L

L

H

F

S

T

D

T

A

E

T

D

V

I

G

D

Q

R

P

P

K

K

V

S

E

Q

S

V

A

S

R

Q

D

Q

A

R

L

L

T

T

R

Q

I

L

N

N

P

P

H

D

I

I

A

Q

I

L

T

T

P

A

V

L

N

Q

A

Q

L

R

L

L

D

T

D

G

A

E

E

A

L

L

A

K

A

D

L

A

I

V

A

A

E

R

H

A

D

D

L

V

V

V

L

L

D

D

C

C

T

T

D
|
D

N

N

V

M

A

A

V

T

R

R

N

Q

Q

E

L

I

N

N

A

A

G

A

C

C

F

V

A

A

A

L

K

N

V

T

P

P

L

L

V

I

S

T

G

A

A

S

A

A

I

V

R

G

M

F

E

G

G

G

Q

Q

I

L

T

M

V

V

F

L

T

T

Y

P

Q

P

D

W

G

E

E

Q

P

G

C
|
C

Y

Y

R

R

C
|
C

L

-

S

-

R

-

L

L

F

W

G

P

E

D

N

N

A

Q

L

E

T

P

C

T

V

-

E

-

A

A

G

G

V

V

M

V

A

G

P

P

L

V

I

V

G

G

V

V

I

M

G

G

S

T

L

L

Q

Q

A

A

M

L

E

E

A

A

I

I

K

K

M

L

L

L

A

S

G

G

Y

I

G

E

K

T

P

P

A

A

S

-

G

G

K

E

I

L

V

R

M

L

Y

F

D

D

A

G

M

K

T

S

C

S

Q

Q

F

W

R

R

E

S

M

L

K

A

L

L

M

R

R

R

N

A

P

S

G

G

C
|
C

E

P

V

V

C
|
C

G

G

active site: R11 (= R14), D127 (= D130)
binding calcium ion: L14 (≠ I17), D16 (≠ R19)
binding zinc ion: C169 (= C172), C172 (= C175), C235 (= C244), C238 (= C247)

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)
42% identity, 98% coverage: 4:247/249 of query aligns to 61:318/482 of O59954

query
sites
O59954

L

L

S

H

D

G

Q

E

E

E

M

Y

L

R

R

R

Y

Y

N

G

R

R

Q

Q

I

M

I

I

L

V

R

P

G

Q

F

F

D

G

F

L

D

Q

G
|
G

Q

Q

E

L

A

K

L

L

K

R

D

D

S

A

R

K

V

V

L

L

I

I

V

V

G

G

L

A

G

G

L

L

G
|
G

C

C

A

P

A

A

S

A

Q

L

Y

Y

L

L

A

A

S

G

A

A

G

G

V

V

G

G

N

T

L

I

T

G

L

L

L

V

D

D

F

G

D

D

T

T

V

V

S

E

L

A

S

S

N

N

L

L

Q

H

R
|
R

Q

Q

T

V

L

L

H

H

S

R

D

S

A

R

T

N

V

V

G

G

Q

K

P

L

K

K

V

V

E

D

S

S

A

A

R

I

D

E

A

Y

L

L

T

R

R

E

I

L

N

N

P

P

H

H

I

P

A

T

I

Y

T

I

P

A

V

H

N

Q

A

A

L

H

L

L

D

T

D

P

A

R

E

E

L

A

A

P

A

D

L

I

I

F

A

K

E

D

H

Y

D

D

L

L

V

I

L

L

D

D

C
|
C

T

T

D

D

N

N

V

P

A

A

V

T

R

R

N

Y

Q

L

L

I

N

S

A

D

G

T

C

A

F

V

A

L

K

G

V

K

P

P

L

L

V

V

S

S

G

A

A

S

A

A

I

L

R

R

M

T

E
|
E

G

G

Q

Q

I

L

T

M

V

V

F

L

T

N

Y

N

-

P

-

Q

-

P

-

G

-

D

Q

K

D

T

G

G

E

G

P

P

C

C

Y

Y

R

R

C

C

L

V

-

F

S

P

R

K

L

P

F

P

G

P

E

A

N

N

A

S

L

V

T

T

-

S

C

C

V

A

E

D

A

G

G

G

V

I

M

L

A

G

P

P

L

V

I

V

G
|
G

V

T

I

M

G

G

S

V

L

L

Q

Q

A

A

M

S

E

E

A

A

I

I

K

K

M

V

L

L

A

T

G

S

Y

A

G

G

K

E

P

S

A

V

S

E

G

A

-

T

-

P

K

S

I

L

V

L

M

I

Y

F

D

S

A

A

M

Y

T

S

C

S

-

P

Q

Q

F

F

R

R

E

T

M

I

K

K

L

L

M

R

-

S

R

R

N

R

P

P

G

N

C

C

E

A

V

V

C

C

G82 (= G25) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
G100 (= G43) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
R130 (= R73) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
C185 (= C128) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
E215 (= E158) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
G264 (= G198) mutation to S: In cnxF142ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.

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 4 papers)
46% identity, 93% coverage: 2:233/249 of query aligns to 53:285/460 of O95396

query
sites
O95396

A

A

E

A

L

L

S

S

D

R

Q

D

E

E

M

I

L

L

R

R

Y

Y

N

S

R

R

Q

Q

I

L

I

V

L

L

R

P

G

E

F

L

D

G

F

V

D

H

G

G

Q

Q

E

L

A

R

L

L

K

G

D

T

S

A

R

C

V

V

L

L

I

I

V

V

G

G

L

C

G

G

L

L

G

G

C

C

A

P

A

L

S

A

Q

Q

Y

Y

L

L

A

A

S

A

A

A

G

G

V

V

G

G

N

R

L

L

T

G

L

L

L

V

D

D

F

Y

D

D

T

V

V

V

S

E

L

M

S

S

N

N

L

L

Q

A

R

R

Q

Q

T

V

L

L

H

H

S

G

D

E

A

A

T

L

V

A

G

G

Q

Q

P

A

K

K

V

A

E

F

S

S

A

A

R

A

D

A

A

S

L

L

T

R

R

R

I

L

N

N

P

S

H

A

I

V

A

E

I

C

T

V

P

P

V

Y

N

T

A

Q

L

A

L

L

D

T

D

P

A

A

E

T

L

A

A

L

A

D

L

L

I

V

A

R

E

R

H

Y

D

D

L

V

V

V

L

A

D

D

C

C

T

S

D

D

N

N

V

V

A

P

V

T

R

R

N

Y

Q

L

L

V

N

N

A

D

G

A

C

C

F

V

A

L

A

A

K

G

V

R

P

P

L

L

V

V

S

S

G

A

A

S

A

A

I

L

R

R

M

F

E

E

G

G

Q

Q

I

I

T

T

V

V

F

Y

T

H

Y

Y

Q

-

D

D

G

G

E

G

P

P

C

C

Y

Y

R

R

C

C

L

I

-

F

-

P

S

Q

R

P

L

P

F

P

G

A

E

E

N

T

A

V

L

T

T

N

C
|
C

V

A

E

D

A

G

G

G

V

V

M

L

A

G

P

V

L

V

I

T

G

G

V

V

I

L

G

G

S

C

L

L

Q

Q

A

A

M

L

E

E

A

V

I

L

K

K

M

I

L

A

A

A

G

G

Y

L

G

G

K

P

P

S

A

Y

S

S

G

G

K

S

I

L

V

L

M

L

Y

F

D

D

A

A

M

L

T

R

C

G

Q

H

F

F

C239 (= C187) 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; 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.

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)
40% identity, 98% coverage: 4:248/249 of query aligns to 3:253/271 of Q72J02

query
sites
Q72J02

L

W

S

T

D

K

Q

E

E

E

M

L

L

D

R

R

Y

Y

N

H

R

R

Q

Q

I

M

I

I

L

L

R

P

G

Q

F

V

D

G

F

P

D

E

G

G

Q

Q

E

E

A

R

L

L

K

K

D

R

S

A

R

S

V

V

L

V

I

V

V

V

G

G

L

A

G

G

L

L

G

G

C

V

A

P

A

V

S

L

Q

Q

Y

Y

L

L

A

V

S

A

A

A

G

G

V

V

G

G

N

R

L

V

T

G

L

V

D

E

F

M

D

D

T

R

V

V

S

E

L

V

S

S

N

N

L

L

Q

H

R

R

Q

Q

T

V

L

L

H

Y

S

T

D

T

A

E

T

D

V

V

G

G

Q

E

P

P

K

K

V

A

E

L

S

V

A

A

R

Q

D

K

A

R

L

L

T

Q

R

A

I

L

N

N

P

P

H

L

I

V

A

R

I

V

T

E

P

A

V

Y

N

P

A

V

L

R

L

L

D

T

D

S

A

E

E

N

L

A

A

L

A

E

L

I

I

L

A

R

E

P

H

Y

D

D

L

L

V

V

L

V

D

D

C

A

T

S

D

D

N

N

V

F

A

P

V

T

R

R

N

Y

Q

L

L

V

N

N

A

D

G

A

C

A

F

V

A

L

K

G

V

K

P

P

L

L

V

V

S

F

G

G

A

A

A

I

I

Y

R

Q

M

F

E

D

G

G

Q

Q

I

V

T

A

V

V

F

F

T

H

Y

H

Q

P

-

T

-

L

D

H

G

G

E

E

-

M

-

G

P

P

C

C

Y

Y

R

R

C

C

L

L

S

F

R

P

L

K

F

P

G

P

E

P

N

P

A

G

L

A

-

V

-

P

T

S

C
|
C

V

A

E

E

A

A

G

G

V

V

M

F

A

G

P

V

L

L

I

P

G

A

V

V

I

V

G

G

S

S

L

L

Q

M

A

A

M

A

E

E

A

A

I

L

K

K

M

V

L

L

A

L

G

G

Y

I

G

G

K

K

P

P

A

L

S

A

G

G

K

H

I

L

V

L

M

L

Y

Y

D

D

A

A

M

L

T

E

C

A

Q

S

F

F

R

R

E

K

M

L

K

T

L

V

M

R

R

R

N

N

P

P

G

R

C

C

E

P

V

V

C

C

G

G

C192 (= C187) 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)
42% identity, 99% coverage: 4:249/249 of query aligns to 5:250/270 of D4GSF3

query
sites
D4GSF3

L

L

S

D

D

A

Q

T

E

Q

M

L

L

D

R

R

Y

Y

N

S

R

R

Q

H

I

I

L

M

R

D

G

E

F

V

D

G

F

P

D

E

G

G

Q

Q

E

G

A

R

L

L

K

L

D

S

S

S

R

R

V

V

L

V

I

V

V

V

G

G

L

A

G

G

L

L

G

G

C

A

A

P

A

A

S

I

Q

Q

Y

Y

L

L

A

A

S

A

A

V

G

G

V

V

G

G

N

E

L

L

T

V

L

V

D

D

F

D

D

D

T

V

V

V

S

E

L

R

S

S

N

N

L

L

Q

Q

R

R

Q

Q

T

V

L

V

H

H

S

C

D

D

A

D

T

D

V

V

G

G

Q

T

P

P

K

K

V

A

E

E

S

S

A

A

R

A

D

A

A

F

L

V

T

R

R

G

I

L

N

N

P

P

H

D

I

V

A

S

I

V

T

E

P

P

V

V

N

E

A

A

L

R

L

V

D

D

D

K

A

S

E

N

L

V

A

H

A

E

L

V

I

V

A

A

E

G

H

S

D

D

L

V

V

V

L

V

D

D

C

A

T

S

D

D

N

N

V

F

A

P

V

T

R

R

N

Y

Q

L

L

L

N

N

A

D

G

V

C

C

F

R

A

F

A

E

K

G

V

I

P

P

L

L

V

V

S

H

G

G

A

A

A

I

I

Y

R

K

M

F

E

E

G

G

Q

Q

I

A

T

T

V

T

F

L

T

V

Y

-

Q

P

D

D

G

G

E

-

P

P

C

C

Y

Y

R

R

C

C

L

L

S

F

R

P

L

E

F

A

G

P

E

E

N

P

A

G

L

T

T

V

-

P

-

D

C
|
C

V

A

E

T

A

T

G

G

V

V

M

L

A

G

P

V

L

L

I

P

G

G

V

T

I

V

G

G

S

C

L

I

Q

Q

A

A

M

T

E

E

A

A

I

M

K

K

M

L

L

L

A

L

G

D

Y

E

G

G

K

E

P

A

A

L

S

D

G

G

K

R

I

L

V

L

M

F

Y

Y

D

D

A

A

M

M

T

D

C

M

Q

T

F

F

R

E

E

T

M

V

K

P

L

Y

M

R

R

T

N

N

P

P

G

D

C

C

E

P

V

V

C

C

G

G

Q

E

C188 (= C187) 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.

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)
37% identity, 99% coverage: 4:249/249 of query aligns to 39:291/440 of P38820

query
sites
P38820

L

L

S

S

D

L

Q

E

E

E

M

Y

L

Q

R

R

Y

Y

N

G

R

R

Q

Q

I

M

I

I

L

V

R

E

G

E

F

T

D

G

-

G

F

V

D

A

G

G

Q

Q

E

V

A

K

L

L

K

K

D

N

S

T

R

K

V

V

L

L

I

V

V

V

G

G

L

A

G

G

L

L

G

G

C

C

A

P

A

A

S

L

Q

P

Y

Y

L

L

A

A

S

G

A

A

G

G

V

V

G

G

N

Q

L

I

T

G

L

I

L

V

D

D

F

N

D

D

T

V

V

V

S

E

L

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

T

V

L

L

H

H

S

D

D

S

A

S

T

R

V

V

G

G

Q

M

P

L

K

K

V

C

E

E

S

S

A

A

R

R

D

Q

A

Y

L

I

T

T

R

K

I

L

N

N

P

P

H

H

I

I

A

N

I

V

T

V

P

T

V

Y

N

P

A

V

L

R

L

L

D

N

D

S

A

S

E

N

L

A

A

F

A

D

L

I

I

F

A

K

E

G

H

Y

D

N

L

Y

V

I

L

L

D

D

C

C

T

T

D

D

N

S

V

P

A

L

V

T

R

R

N

Y

Q

L

L

V

N

S

A

D

G

V

C

A

F

V

A

N

A

L

K

G

V

I

P

T

L

V

V

V

S

S

G

A

A

S

A

G

I

L

R

G

M

T

E

E

G

G

Q

Q

I

L

T

T

V

I

F

L

T

N

Y

F

Q

N

D

N

G

I

E

G

P

P

C

C

Y

Y

R

R

C

C

L

F

-

Y

S

P

R

T

L

P

F

P

G

P

E

P

N

N

A

A

L

V

T

T

-

S

C
|
C

V

Q

E

E

A

G

G

G

V

V

M

I

A

G

P

P

L

C

I

I

G

G

V

L

I

V

G

G

S

T

L

M

Q

M

A

A

M

V

E

E

A

T

I

L

K

K

M

L

L

I

A

L

G

G

Y

I

-

Y

-

T

G

N

K

E

P

N

A

F

S

S

G

P

K

F

I

L

V

M

M

L

Y

Y

D

S

A

G

M

F

T

P

C

Q

Q

Q

-

S

F

L

R

R

E

T

M

F

K

K

L

M

M

R

-

G

R

R

N

Q

P

E

G

K

C

C

E

L

V

C

C

C

G

G

Q

K

C225 (= C187) 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.

6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
36% identity, 99% coverage: 4:249/249 of query aligns to 6:271/423 of 6yubA

query
sites
6yubA

L

L

S

S

D

K

Q

E

E

E

M

I

L

E

R

R

Y

Y

N

S

R

R

Q

Q

I

M

I

I

L

V

R

P

G

G

F

M

D

G

F

K

D

E

G

G

Q

Q

E

L

A

R

L

L

K

M

D

N

S

A

R

K

V

V

L

L

I

I

V

I

G

G

L

A

G

G

L

L

G

G

C

C

A

P

A

A

S

A

Q

Q

Y

Y

L

L

A

A

S

G

A

A

G

G

V

V

G

G

N

T

L

I

T

G

L

I

L

V

D

D

F

G

D

D

T

S

V

V

S

E

L

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

T

V

L

A

H

H

S

A

D

T

A

K

T

R

V

V

G

G

Q

M

P

L

K

K

V

V

E

D

S

S

A

L

R

I

D

T

A

H

L

L

T

I

R

E

I

I

N

N

P

P

H

L

I

P

A

V

I

Y

T

V

P

P

V

Y

N

R

A

F

L

D

L

L

D

T

D

P

A

Q

E

N

L

A

A

A

A

Q

L

I

I

I

A

K

E

P

H

W

D

D

L

V

V

I

L

L

D

D

C

C

T

T

D

D

N

N

V

P

A

A

V

T

R

R

N

Y

Q

L

L

I

N

S

A

D

G

V

C

C

F

V

A

L

K

G

V

K

P

P

L

L

V

V

S

S

G

A

A

A

A

S

I

V

R

Q

M

K

E

S

G

G

Q

Q

I

L

T

I

V

V

F

L

T

N

-

C

-

P

-

T

-

P

-

Q

-

G

-

V

Y

N

Q

K

D

K

G

A

E

A

P

P

C
|
C

Y

Y

R

R

C
|
C

L

C

S

F

R

K

L

-

F

-

G

-

E

-

N

-

A

-

L

-

T

-

C

-

V

-

E

K

A

P

G

G

V

I

M

M

A

G

P

P

L

V

I

V

G

G

V

M

I

M

G

G

S

V

L

A

Q

Q

A

A

M

G

E

E

A

A

I

I

K

K

M

I

L

L

A

V

G

S

-

Q

-

L

Y

H

G

M

K

P

P

P

A

K

S

E

G

G

K

E

-

E

-

V

-

S

-

P

-

E

-

K

-

N

-

L

-

V

-

Q

-

P

-

T

-

L

I

I

V

Y

M

T

Y

Y

D

D

A

L

M

N

T

S

C

A

-

I

-

G

-

P

-

Y

Q

S

F

F

R

R

E

A

M

L

K

K

L

M

-

G

M

G

R

R

N

K

P

K

G

D

C
|
C

E

F

V

A

C
|
C

G

G

Q

E

binding zinc ion: C183 (= C172), C186 (= C175), C266 (= C244), C269 (= C247)

6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
36% identity, 99% coverage: 3:249/249 of query aligns to 6:270/289 of 6yubB

query
sites
6yubB

E

S

L

L

S

S

D

K

Q

E

E

E

M

I

L

E

R

R

Y

Y

N

S

R

R

Q

Q

I

M

I

I

L

V

R

P

G

G

F

M

D

G

F

K

D

E

G

G

Q

Q

E

L

A

R

L

L

K

M

D

N

S

A

R

K

V

V

L

L

I

I

V

I

G

G

L

A

G

G

L

L

G

G

C

C

A

P

A

A

S

A

Q

Q

Y

Y

L

L

A

A

S

G

A

A

G

G

V

V

G

G

N

T

L

I

T

G

L

I

L

V

D

D

F

G

D

D

T

S

V

V

S

E

L

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

T

V

L

A

H

H

S

A

D

T

A

K

T

R

V

V

G

G

Q

M

P

L

K

K

V

V

E

D

S

S

A

L

R

I

D

T

A

H

L

L

T

I

R

E

I

I

N

N

P

P

H

L

I

P

A

V

I

Y

T

V

P

P

V

Y

N

R

A

F

L

D

L

L

D

T

D

P

A

Q

E

N

L

A

A

A

A

Q

L

I

I

I

A

K

E

P

H

W

D

D

L

V

V

I

L

L

D

D

C

C

T

T

D

D

N

N

V

P

A

A

V

T

R

R

N

Y

Q

L

L

I

N

S

A

D

G

V

C

C

F

V

A

L

K

G

V

K

P

P

L

L

V

V

S

S

G

A

A

A

A

S

I

V

R

Q

M

K

E

S

G

G

Q

Q

I

L

T

I

V

V

F

L

T

N

-

C

-

P

-

T

-

P

-

Q

-

G

-

V

Y

N

Q

K

D

K

G

A

E

A

P

P

C
|
C

Y

Y

R

R

C
|
C

L

C

S

F

R

K

L

-

F

-

G

-

E

-

N

-

A

-

L

-

T

-

C

-

V

-

E

-

A

-

G

G

V

I

M

M

A

G

P

P

L

V

I

V

G

G

V

M

I

M

G

G

S

V

L

A

Q

Q

A

A

M

G

E

E

A

A

I

I

K

K

M

I

L

L

A

V

G

S

-

Q

-

L

Y

H

G

M

K

P

P

P

A

K

S

E

G

G

K

E

-

E

-

V

-

S

-

P

-

E

-

K

-

N

-

L

-

V

-

Q

-

P

-

T

-

L

I

I

V

Y

M

T

Y

Y

D

D

A

L

M

N

T

S

C

A

-

I

-

G

-

P

-

Y

Q

S

F

F

R

R

E

A

M

L

K

K

L

M

-

G

M

G

R

R

N

K

P

K

G

D

C
|
C

E

F

V

A

C

C

G

G

Q

E

binding zinc ion: C184 (= C172), C187 (= C175), C265 (= C244)

3h9jA Crystal structure of e. Coli mccb + ampcpp + semet mcca (see paper)
27% identity, 90% coverage: 26:249/249 of query aligns to 110:339/339 of 3h9jA

query
sites
3h9jA

Q

Q

E

D

A

K

L

L

K

K

D

N

S

A

R

K

V

V

L

V

I

I

V

L

G
|
G

L
x
C

G
|
G

L

I

G

G

C

N

A

H

A

V

S

S

Q

V

Y

I

L

L

A

A

S

T

A

S

G

G

V

I

G

G

N

E

L

I

T

I

L

L

L

I

D
|
D

F

N

D
|
D

T

Q

V

I

S

E

L

N

S

T

N

N

L

L

Q

T

R
|
R

Q
|
Q

T

V

L

L

H

F

S

S

D

E

A

D

T

D

V

V

G

G

Q

K

P

N

K
|
K

V

T

E

E

S

V

A

I

R

K

D

R

A

E

L

L

T

L

R

K

I

R

N

N

P

S

H

E

I

I

A

S

I

V

T

S

P

E

V

I

N

A

A
x
L

L
x
N

L
x
I

D

N

D

D

A

Y

E

T

L

D

A

L

A

H

L

K

I

V

A

P

E

E

H

A

D

D

L

I

V

W

L

V

D

V

C
x
S

T
x
A

D
|
D

N
x
H

-

P

V

F

A

N

V
x
L

R

I

N

N

Q

W

L

V

N

N

A

K

G

Y

C

C

F

V

A

R

A

A

K

N

V

Q

P

P

L

Y

V

I

S

N

G

A

A

G

A
x
Y

I
x
V

R

-

M

-

E

-

G

N

Q

D

I
|
I

T

A

V

V

F

F

-

G

-

P

T

L

Y

Y

Q

V

D

P

G

G

E

K

P

T

-

G

C
|
C

Y

Y

R

E

C
|
C

L

Q

S

K

R

K

L

E

F

N

G

I

E

D

N

H

A

K

L

I

T

K

C

L

V

I

E

N

A

S

-

R

-

F

-

K

-

P

G

A

V

T

M

F

A

A

P

P

L

V

I

N

G

N

V

V

I

A

G

A

S

A

L

L

Q

C

A

A

M

A

E

D

A

V

I

I

K

K

M

F

L

I

A

G

G

K

Y

Y

G

S

K

E

P

P

A

L

S

S

-

L

G

N

K

K

I
x
R

V

I

M
x
G

Y

I

D

W

A

S

M

D

T

E

C

I

Q

K

F

I

R

H

E

S

M
x
Q

K

N

L

M

M

G

R

R

N

S

P

P

G

V

C
|
C

E

S

V

V

C
|
C

G

G

Q

N

active site: R157 (= R73)
binding diphosphomethylphosphonic acid adenosyl ester: G122 (= G38), C123 (≠ L39), G124 (= G40), G125 (= G41), D146 (= D62), D148 (= D64), R157 (= R73), Q158 (= Q74), K170 (= K86), L192 (≠ A108), N193 (≠ L109), I194 (≠ L110), S212 (≠ C128), A213 (≠ T129), D214 (= D130), H215 (≠ N131), L219 (≠ V134), Y239 (≠ A154)
binding zinc ion: C257 (= C172), C260 (= C175), C334 (= C244), C337 (= C247)
binding : V240 (≠ I155), I243 (= I161), R313 (≠ I223), G315 (≠ M225), Q326 (≠ M236)

3h5nA Crystal structure of e. Coli mccb + atp (see paper)
28% identity, 90% coverage: 26:248/249 of query aligns to 110:338/338 of 3h5nA

query
sites
3h5nA

Q

Q

E

D

A

K

L

L

K

K

D

N

S

A

R

K

V

V

L

V

I

I

V

L

G
|
G

L
x
C

G
|
G

L

I

G

G

C

N

A

H

A

V

S

S

Q

V

Y

I

L

L

A

A

S

T

A

S

G

G

V

I

G

G

N

E

L

I

T

I

L

L

L

I

D
|
D

F

N

D

D

T

Q

V

I

S

E

L

N

S

T

N
|
N

L

L

Q

T

R
|
R

Q
|
Q

T

V

L

L

H

F

S

S

D

E

A

D

T

D

V

V

G

G

Q

K

P

N

K
|
K

V

T

E

E

S

V

A

I

R

K

D

R

A

E

L

L

T

L

R

K

I

R

N

N

P

S

H

E

I

I

A

S

I

V

T

S

P

E

V

I

N

A

A
x
L

L
x
N

L
x
I

D

N

D

D

A

Y

E

T

L

D

A

L

A

H

L

K

I

V

A

P

E

E

H

A

D

D

L

I

V

W

L

V

D

V

C

S

T
x
A

D
|
D

N
x
H

-

P

V

F

A

N

V
x
L

R

I

N

N

Q

W

L

V

N

N

A

K

G

Y

C

C

F

V

A

R

A

A

K

N

V

Q

P

P

L

Y

V

I

S

N

G

A

A

G

A
x
Y

I

V

R

-

M

-

E

-

G

N

Q

D

I

I

T

A

V

V

F

F

-

G

-

P

T

L

Y

Y

Q

V

D

P

G

G

E

K

P

T

-

G

C
|
C

Y

Y

R

E

C
|
C

L

Q

S

K

R

K

L

E

F

N

G

I

E

D

N

H

A

K

L

I

T

K

C

L

V

I

E

N

A

S

-

R

-

F

-

K

-

P

G

A

V

T

M

F

A

A

P

P

L

V

I

N

G

N

V

V

I

A

G

A

S

A

L

L

Q

C

A

A

M

A

E

D

A

V

I

I

K

K

M

F

L

I

A

G

G

K

Y

Y

G

S

K

E

P

P

A

L

S

S

-

L

G

N

K

K

I

R

V

I

M

G

Y

I

D

W

A

S

M

D

T

E

C

I

Q

K

F

I

R

H

E

S

M

Q

K

N

L

M

M

G

R

R

N

S

P

P

G

V

C
|
C

E

S

V

V

C
|
C

G

G

active site: R157 (= R73)
binding adenosine-5'-triphosphate: G122 (= G38), C123 (≠ L39), G124 (= G40), G125 (= G41), D146 (= D62), N154 (= N70), R157 (= R73), Q158 (= Q74), K170 (= K86), L192 (≠ A108), N193 (≠ L109), I194 (≠ L110), A213 (≠ T129), D214 (= D130), H215 (≠ N131), L219 (≠ V134), Y239 (≠ A154)
binding zinc ion: C257 (= C172), C260 (= C175), C334 (= C244), C337 (= C247)

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, 61% coverage: 27:178/249 of query aligns to 14:165/650 of Q7SXG4

query
sites
Q7SXG4

E

D

A

S

L

L

K

S

D

S

S

C

R

R

V

V

L

L

I

V

V

V

G

G

L

A

G

G

L

I

G

G

C

C

A

E

A

L

S

L

Q

K

Y

N

L

L

A

V

S

L

A

T

G

G

V

F

G

K

N

N

L

I

T

E

L

V

L

I

D

D

F

L

D

D

T

T

V

I

S

D

L

V

S

S

N

N

L

L

Q

N

R

R

Q

Q

T

F

L

L

H

F

S

Q

D

K

A

K

T

H

V

V

G

G

Q

K

P

S

K

K

V

A

E

Q

S

V

A

A

R

K

D

E

A

S

L

V

T

L

R

R

I

F

N

C

P

P

H

S

I

A

A

N

I

I

T

T

P

A

V

Y

-

H

N

D

A

S

L

I

L

M

D

N

D

P

A

D

E

Y

L

N

A

V

A

E

L

F

I

F

A

R

E

N

H

F

D

Q

L

L

V

V

L

M

D

N

C

A

T

L

D

D

N

N

V

R

A

A

V

A

R

R

N

N

Q

H

L

V

N

N

A

R

G

M

C

C

F

L

A

A

K

D

V

I

P

P

L

L

V

I

S

E

G

S

A

G

A

T

I

A

R

G

M

Y

E

L

G

G

Q

Q

I

V

T

T

V

V

F

I

T

K

Y

K

Q

G

D

Q

G

T

E

E

P

-

C

C

Y

Y

R

E

C

C

L

Q

S

P

R

K

Sites not aligning to the query:

599 modified: Phosphoserine

O42939 Ubiquitin-activating enzyme E1-like; Pmt3-activating enzyme subunit 2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 59% coverage: 29:175/249 of query aligns to 23:169/628 of O42939

query
sites
O42939

L

F

K

K

D

S

S

A

R

K

V

V

L

L

I

L

V

V

G

G

L

A

G

G

L

I

G

G

C

C

A

E

A

L

S

L

Q

K

Y

N

L

L

A

L

S

M

A

S

G

G

V

V

G

K

N

E

L

V

T

H

L

I

D

D

F

L

D

D

T

T

V

I

S

D

L

L

S

S

N

N

L

L

Q

N

R

R

Q

Q