SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_019895485.1 NCBI__GCF_000384235.1:WP_019895485.1 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)

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)
46% identity, 98% coverage: 1:247/253 of query aligns to 1:247/249 of P12282

query
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P12282

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R14 (= R14) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
C44 (≠ S44) 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 (≠ A128) 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 (= C173) mutation to A: No zinc bound and no enzyme activity.
C175 (= C176) mutation to A: No zinc bound and no enzyme activity.
C187 (= C188) mutation to A: No effect.
C231 (≠ M231) 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)
46% identity, 97% coverage: 3:247/253 of query aligns to 2:239/240 of 1jwbB

query
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1jwbB

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active site: R13 (= R14), D129 (= D130)
binding adenosine monophosphate: G37 (= G38), G39 (= G40), G40 (= G41), D61 (= D62), F62 (= F63), K85 (= K86), L108 (≠ R109), C127 (≠ A128), T128 (≠ S129), D129 (= D130), N130 (= N131), V133 (≠ T134)
binding zinc ion: C171 (= C173), C236 (= C244), C239 (= C247)

1jw9B Structure of the native moeb-moad protein complex (see paper)
46% identity, 97% coverage: 3:247/253 of query aligns to 2:239/240 of 1jw9B

query
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1jw9B

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active site: R13 (= R14), D129 (= D130)
binding zinc ion: C171 (= C173), C236 (= C244), C239 (= C247)

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)
42% identity, 97% coverage: 2:247/253 of query aligns to 62:309/453 of Q9VLJ8

query
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Q9VLJ8

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T62 (= T2) modified: Phosphothreonine

P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
45% identity, 99% coverage: 4:253/253 of query aligns to 1:249/251 of P30138

query
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P30138

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G

G

S

T

F

L

Q

Q

A

A

L

L

E

E

A

A

I

I

K

K

V

L

L

L

A

S

G

G

L

I

E

E

T

T

L

P

Q

A

G

G

R

E

L

L

L

R

L

L

L

F

D

D

G

G

L

K

S

S

M

S

Q

Q

C

W

Q

R

S

S

L

L

N

A

L

L

T

R

S

R

D

A

P

S

D

G

C
|
C

P

P

I

V

C
|
C

Q

G

P

G

G

S

K

N

S

A

D

D

C169 (= C173) binding Zn(2+)
C172 (= C176) binding Zn(2+)
W174 (≠ Y178) mutation to A: No adenylation of ThiS.
C184 (= C188) mutation to S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth.
C240 (= C244) binding Zn(2+)
C243 (= C247) binding Zn(2+)

1zfnA Structural analysis of escherichia coli thif (see paper)
46% identity, 96% coverage: 4:247/253 of query aligns to 1:243/244 of 1zfnA

query
sites
1zfnA

L

M

S

N

D

D

D

R

E

D

L

F

I

M

R

R

Y

Y

S

S

R
|
R

Q

Q

I

I

L

L

P

D

E

D

I

I

G

A

Y

L

A

D

G

G

Q

Q

A

Q

A

K

L

L

A

L

D

D

G

S

R

Q

I

V

L

L

I

I

M
x
I

G
|
G

L

L

G
|
G

L

L

G

G

S

T

P

P

V

A

A

A

L

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

Q

T

L

L

T

V

L

L

V

A

D
|
D

F

D

D

D

E

D

V

V

D

H

T

L

S

S

N

N

L

L

Q

Q

R
|
R

Q
|
Q

I

I

I

L

H

F

E

T

Q

T

H

E

N

D

V

I

N

D

Q

R

K

P

K
|
K

V

S

A

Q

S

V

A

S

R

Q

E

Q

R

R

I

L

A

T

R

Q

L

L

N

N

P

P

A

D

T

I

N

Q

V

L

I

T

T

A

H

L

E

Q

T

Q

R

R

L

L

D

T

E

G

E

E

Q

A

L

L

S

K

D

D

C

A

V

V

Q

A

A

R

A

A

D

D

V

V

V

L

D

D

A

C

S
x
T

D
|
D

N

N

F

M

A

A

T
|
T

R

R

F

Q

Q

E

L

I

N

N

R

A

L

A

C

C

H

V

R

A

H

L

L

N

T

T

P

P

L

L

V

I

S

T

G

A

A

S

A

A

I

V

R

G

W

F

E

G

G

G

Q

Q

L

L

T

M

T

V

F

L

D

-

F

-

R

-

Q

-

A

-

T

T

P

P

-

P

-

W

-

E

-

Q

-

G

C
|
C

Y

Y

Q

R

C
|
C

L

L

Y

W

P

P

D

D

T

N

S

Q

Q

E

A

P

D

E

A

R

N

N

C

C

A

R

Q

T

N

A

G

G

V

V

A

V

A

G

P

P

I

V

V

V

G

G

A

V

V

M

G

G

S

T

F

L

Q

Q

A

A

L

L

E

E

A

A

I

I

K

K

V

L

L

L

A

S

G

G

L

I

E

E

T

T

L

P

Q

A

G

G

R

E

L

L

L

R

L

L

L

F

D

D

G

G

L

K

S

S

M

S

Q

Q

C

W

Q

R

S

S

L

L

N

A

L

L

T

R

S

R

D

A

P

S

D

G

C
|
C

P

P

I

V

C
|
C

active site: R11 (= R14), D127 (= D130)
binding adenosine-5'-triphosphate: I34 (≠ M37), G35 (= G38), G37 (= G40), G38 (= G41), D59 (= D62), R70 (= R73), Q71 (= Q74), K83 (= K86), T126 (≠ S129), D127 (= D130), T131 (= T134)
binding zinc ion: C169 (= C173), C172 (= C176), C240 (= C244), C243 (= C247)

1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
43% identity, 93% coverage: 3:238/253 of query aligns to 2:215/217 of 1jwaB

query
sites
1jwaB

Q

E

L

L

S

S

D

D

D

Q

E

E

L

M

I

L

R

R

Y

Y

S

N

R
|
R

Q

Q

I

I

L

I

L

L

P

R

E

G

I

F

G

D

Y

F

A

D

G

G

Q

Q

A

E

A

A

L

L

A

K

D

D

G

S

R

R

I

V

L

L

I

I

M

V

G

G

L

L

G
|
G

L

L

G

G

S

C

P

A

V

A

A

S

L

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

Q

N

L

L

T

T

L

L

V

L

D
|
D

F
|
F

D

D

E

T

V

V

D

S

T

L

S

S

N

N

L

L

Q

Q

R
|
R

Q

Q

I

T

I

L

H

H

E

S

Q

D

H

A

N

T

V

V

N

G

Q

Q

K

P

K
|
K

V

V

A

E

S

S

A

A

R

R

E

D

R

A

I

L

A

T

R

R

L

I

N

N

P

P

A

H

T

I

N

A

V

I

I

T

T

P

H

V

E

N

T

A

R
x
L

L

L

D

D

E

D

E

A

Q

E

L

L

S

A

D

A

C

L

V

I

Q

A

A

E

A

H

D

D

V

L

V

V

V

L

D

D

A

C

S

T

D
|
D

N
|
N

F

V

A

A

T
x
V

R

R

F

N

Q

Q

L

L

N

N

R

A

L

G

C

C

H

F

R

A

H

A

L

K

T

V

P

P

L

L

V

V

S

S

G

G

A

A

I

I

R

R

W

M

E

E

G

G

Q

Q

L

I

T

T

T

V

F

F

D

T

F

Y

R

-

Q

-

A

-

T

-

P

-

C

-

Y

-

Q

-

C

-

L

-

Y

-

P

-

D

-

T

-

S

-

Q

-

A

-

D

-

A

-

N

-

C

-

A

-

Q

E

N

A

G

G

V

V

A

M

A

A

P

P

I

L

V

I

G

G

A

V

V

I

G

G

S

S

F

L

Q

Q

A

A

L

M

E

E

A

A

I

I

K

K

V

M

L

L

A

A

G

G

L

Y

-

G

E

K

T

P

L

A

Q

S

G

G

R

K

L

I

L

V

L

M

L

Y

D

D

G

A

L

M

S

T

M

C

Q

Q

C

F

Q

R

S

E

L

M

N

K

L

L

active site: R13 (= R14), D129 (= D130)
binding adenosine-5'-triphosphate: G39 (= G40), G40 (= G41), D61 (= D62), F62 (= F63), R72 (= R73), K85 (= K86), L108 (≠ R109), D129 (= D130), N130 (= N131), V133 (≠ T134)

1zud3 Structure of this-thif protein complex (see paper)
44% identity, 96% coverage: 4:247/253 of query aligns to 1:238/240 of 1zud3

query
sites
1zud3

L

M

S

N

D

D

D

R

E

D

L

F

I

M

R

R

Y

Y

S

S

R
|
R

Q

Q

I

I

L
|
L

L

L

P
x
D

E

D

I

I

G

A

Y

L

A

D

G

G

Q

Q

A

Q

A

K

L

L

A

L

D

D

G

S

R

Q

I

V

L

L

I

I

M

I

G

G

L

L

G

G

L

L

G

G

S

T

P

P

V

A

A

A

L

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

Q

T

L

L

T

V

L

L

V

A

D

D

F

D

D

D

E

D

V

V

D

H

T

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

I

I

I

L

H

F

E

T

Q

T

H

E

N

D

V

I

N

D

Q

R

K

P

K

K

V

S

A

Q

S

V

A

S

R

Q

E

Q

R

R

I

L

A

T

R

Q

L

L

N

N

P

P

A

D

T

I

N

Q

V

L

I

T

T

A

H

L

E

Q

T

Q

R

R

L

L

D

T

E

G

E

E

Q

A

L

L

S

K

D

D

C

A

V

V

Q

A

A

R

A

A

D

D

V

V

V

L

D

D

A

C

S

T

D
|
D

N

N

F

M

A

A

T

T

R

R

F

Q

Q

E

L

I

N

N

R

A

L

A

C

C

H

V

R

A

H

L

L

N

T

T

P

P

L

L

V

I

S

T

G

A

A

S

A

A

I

V

R

G

W

F

E

G

G

G

Q

Q

L

L

T

M

T

V

F

L

D

-

F

-

R

-

Q

-

A

-

T

T

P

P

-

P

-

W

-

E

-

Q

-

G

C
|
C

Y

Y

Q

R

C

C

L

L

Y

W

P

P

D

D

T

N

S

Q

Q

E

A

P

D

T

A

A

N

G

C

V

A

V

Q

G

N

P

G

V

V

V

A

G

A

-

P

-

I

-

V

-

G

-

A

V

V

M

G

G

S

T

F

L

Q

Q

A

A

L

L

E

E

A

A

I

I

K

K

V

L

L

L

A

S

G

G

L

I

E

E

T

T

L

P

Q

A

G

G

R

E

L

L

L

R

L

L

L

F

D

D

G

G

L

K

S

S

M

S

Q

Q

C

W

Q

R

S

S

L

L

N

A

L

L

T

R

S

R

D

A

P

S

D

G

C
|
C

P

P

I

V

C
|
C

active site: R11 (= R14), D127 (= D130)
binding calcium ion: L14 (= L17), D16 (≠ P19)
binding zinc ion: C169 (= C173), 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)
40% identity, 96% coverage: 4:247/253 of query aligns to 61:318/482 of O59954

query
sites
O59954

L

L

S

H

D

G

D

E

E

E

L

Y

I

R

R

R

Y

Y

S

G

R

R

Q

Q

I

M

L

I

L

V

P

P

E

Q

I

F

G

G

Y

L

A

Q

G
|
G

Q

Q

A

L

A

K

L

L

A

R

D

D

G

A

R

K

I

V

L

L

I

I

M

V

G

G

L

A

G

G

L

L

G
|
G

S

C

P

P

V

A

A

A

L

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

Q

T

L

I

T

G

L

L

V

V

D

D

F

G

D

D

E

T

V

V

D

E

T

A

S

S

N

N

L

L

Q

H

R
|
R

Q

Q

I

V

I

L

H

H

E

R

Q

S

H

R

N

N

V

V

N

G

Q

K

K

L

K

K

V

V

A

D

S

S

A

A

R

I

E

E

R

Y

I

L

A

R

R

E

L

L

N

N

P

P

A

H

T

P

N

T

V

Y

I

I

T

A

H

H

E

Q

T

A

R

H

L

L

D

T

E

P

E

R

Q

E

L

A

S

P

D

D

C

I

V

F

Q

K

A

D

A

Y

D

D

V

L

V

I

V

L

D

D

A
x
C

S

T

D

D

N

N

F

P

A

A

T

T

R

R

F

Y

Q

L

L

I

N

S

R

D

L

T

C

A

H

V

R

L

H

L

L

G

T

K

P

P

L

L

V

V

S

S

G

A

A

S

A

A

I

L

R

R

W

T

E
|
E

G

G

Q

Q

L

L

T

M

T

V

F

L

D

N

F

N

R

P

Q

Q

A

P

T

P

-

G

-

D

-

K

-

T

-

G

P

P

C

C

Y

Y

Q

R

C

C

L

V

Y

F

P

P

D

K

T

P

S

P

Q

P

A

A

D

N

A

S

-

V

-

T

N

S

C

C

A

A

Q

D

N

G

G

G

V

I

A

L

A

G

P

P

I

V

V

V

G
|
G

A

T

V

M

G

G

S

V

F

L

Q

Q

A

A

L

S

E

E

A

A

I

I

K

K

V

V

L

L

A

T

-

S

-

A

-

G

-

E

G

S

L

V

E

E

T

A

L

T

Q

P

G

P

R

S

L

L

L

I

L

F

D

S

G

A

L

Y

S

S

M

S

-

P

Q

Q

C

F

Q

R

S

T

L

I

N

K

L

L

T

R

S

S

-

R

D

R

P

P

D

N

C

C

P

A

I

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 (≠ A128) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
E215 (= E158) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
G264 (= G199) 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 5 papers)
45% identity, 89% coverage: 4:229/253 of query aligns to 55:281/460 of O95396

query
sites
O95396

L

L

S

S

D

R

D

D

E

E

L

I

I

L

R

R

Y

Y

S

S

R

R

Q

Q

I

L

L

V

L

L

P

P

E

E

I

L

G

G

Y

V

A

H

G

G

Q

Q

A

L

A

R

L

L

A

G

D

T

G

A

R

C

I

V

L

L

I

I

M

V

G

G

L

C

G

G

L

L

G

G

S

C

P

P

V

L

A

A

L

Q

Y

Y

L

L

A

A

G

G

V

V

G

G

Q

R

L

L

T

G

L

L

V

V

D

D

F

Y

D

D

E

V

V

V

D

E

T

M

S

S

N

N

L

L

Q

A

R

R

Q

Q

I

V

I

L

H

H

E

G

Q

E

H

A

N

L

V

A

N

G

Q

Q

K

A

K

K

V

A

A

F

S

S

A

A

R

A

E

A

R

S

I

L

A

R

R

R

L

L

N

N

P

S

A

A

T

V

N

E

V

C

I

V

T

P

H

Y

E
x
T

T
x
Q

R
x
A

L
|
L

D
x
T

E
x
P

E
x
A

Q
x
T

L
x
A

S
x
L

D
|
D

C
x
L

V
|
V

Q
x
R

A
x
R

A
x
Y

D
|
D

V
|
V

V
x
A

D
|
D

A
x
C

S
|
S

D
|
D

N
|
N

F
x
V

A
x
P

T
|
T

R
|
R

F
x
Y

Q
x
L

L
x
V

N
|
N

R
x
D

L
x
A

C
|
C

H
x
V

R
x
L

H
x
A

L
x
G

T
x
R

P
|
P

L
|
L

V
|
V

S
|
S

G
x
A

A
x
S

A
|
A

I
x
L

R
|
R

W
x
F

E
|
E

G
|
G

Q
|
Q

L
x
I

T
|
T

T
x
V

F
x
Y

D
x
H

F
x
Y

R

-

Q
x
D

A
x
G

T
x
G

P
|
P

C
|
C

Y
|
Y

Q
x
R

C
|
C

L
x
I

Y
x
F

P
|
P

D
x
Q

T
x
P

S
x
P

Q
x
P

A
|
A

D
x
E

-
x
T

-
x
V

A
x
T

N
|
N

C
|
C

A

A

Q

D

N

G

G

G

V

V

A

L

A

G

P

V

I

V

V

T

G

G

A

V

V

L

G

G

S

C

F

L

Q

Q

A

A

L

L

E

E

A

V

I

L

K

K

V

I

L

A

A

A

G

G

L

L

-

G

E

P

T

S

L

Y

Q

S

G

G

R

S

L

L

L

F

D

D

G

A

L

L

158:238 (vs. 107:187, 37% identical) Interaction with NFS1
C239 (= C188) 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.

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, 97% coverage: 8:253/253 of query aligns to 9:254/270 of D4GSF3

query
sites
D4GSF3

E

Q

L

L

I

D

R

R

Y

Y

S

S

R

R

Q

H

I

I

L

I

L

M

P

D

E

E

I

V

G

G

Y

P

A

E

G

G

Q

Q

A

G

A

R

L

L

A

L

D

S

G

S

R

R

I

V

L

V

I

V

M

V

G

G

L

A

G

G

L

L

G

G

S

A

P

P

V

A

A

I

L

Q

Y

Y

L

L

A

A

A

V

G

G

V

V

G

G

Q

E

L

L

T

V

L

V

V

V

D

D

F

D

D

D

E

V

V

V

D

E

T

R

S

S

N

N

L

L

Q

Q

R

R

Q

Q

I

V

H

H

E

C

Q

D

H

D

N

D

V

V

N

G

Q

T

K

P

K

K

V

A

A

E

S

S

A

A

R

A

E

A

R

F

I

V

A

R

R

G

L

L

N

N

P

P

A

D

T

V

N

S

V

V

I

E

T

P

H

V

E

E

T

A

R

R

L

V

D

D

E

K

E

S

Q

N

L

V

S

H

D

E

C

V

V

V

Q

A

A

G

A

S

D

D

V

V

D

D

A

A

S

S

D

D

N

N

F

F

A

P

T

T

R

R

F

Y

Q

L

L

L

N

N

R

D

L

V

C

C

H

R

R

F

H

E

L

G

T

I

P

P

L

L

V

V

S

H

G

G

A

A

A

I

I

Y

R

K

W

F

E

E

G

G

Q

Q

L

A

T

T

F

L

D

-

F

-

R

-

R

V

Q

P

A

D

T

G

P

P

C

C

Y

Y

Q

R

C

C

L

L

Y

F

P

P

D

E

T

A

S

P

Q

E

A

P

D

G

A

T

-

V

-

P

N

D

C
|
C

A

A

Q

T

N

T

G

G

V

V

A

L

A

G

P

V

I

L

V

P

G

G

A

T

V

V

G

G

S

C

F

I

Q

Q

A

A

L

T

E

E

A

A

I

M

K

K

V

L

L

L

A

L

G

D

L

E

-

G

E

E

T

A

L

L

Q

D

G

G

R

R

L

L

L

F

L

Y

D

D

G

A

L

M

S

D

M

M

Q

T

C

F

Q

E

S

T

L

V

N

P

L

Y

T

R

S

T

D

N

P

P

D

D

C

C

P

P

I

V

C

C

Q

G

P

E

G

G

K

G

S

V

D

D

C188 (= C188) 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)
38% identity, 91% coverage: 4:232/253 of query aligns to 39:272/440 of P38820

query
sites
P38820

L

L

S

S

D

L

D

E

E

E

L

Y

I

Q

R

R

Y

Y

S

G

R

R

Q

Q

I

M

L

I

L

V

P

E

E

E

I

T

G

G

-

G

Y

V

A

A

G

G

Q

Q

A

V

A

K

L

L

A

K

D

N

G

T

R

K

I

V

L

L

I

V

M

V

G

G

L

A

G

G

L

L

G

G

S

C

P

P

V

A

A

L

L

P

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

Q

Q

L

I

T

G

L

I

V

V

D

D

F

N

D

D

E

V

V

V

D

E

T

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

I

V

I

L

H

H

E

D

Q

S

H

S

N

R

V

V

N

G

Q

M

K

L

K

K

V

C

A

E

S

S

A

A

R

R

E

Q

R

Y

I

I

A

T

R

K

L

L

N

N

P

P

A

H

T

I

N

N

V

V

I

V

T

T

H

Y

E

P

T

V

R

R

L

L

D

N

E

S

Q

N

L

A

S

F

D

D

C

I

V

F

Q

K

A

G

A

Y

D

N

V

Y

V

I

V

L

D

D

A

C

S

T

D

D

N

S

F

P

A

L

T

T

R

R

F

Y

Q

L

L

V

N

S

R

D

L

V

C

A

H

V

R

N

H

L

L

G

T

I

P

T

L

V

V

V

S

S

G

A

A

S

A

G

I

L

R

G

W

T

E

E

G

G

Q

Q

L

L

T

T

T

I

F

L

D

N

F

F

R

-

R

N

Q

N

A

I

T

G

P

P

C

C

Y

Y

Q

R

C

C

L

F

Y

Y

P

P

D

T

T

P

S

P

Q

P

A

P

D

N

A

A

-

V

-

T

N

S

C
|
C

A

Q

Q

E

N

G

G

G

V

V

A

I

A

G

P

P

I

C

V

I

G

G

A

L

V

V

G

G

S

T

F

M

Q

M

A

A

L

V

E

E

A

T

I

L

K

K

V

L

L

I

A

L

G

G

L

I

-

Y

-

T

-

N

E

E

T

N

L

F

Q

S

G

P

R

F

L

L

L

M

L

L

L

Y

D

S

G

G

L

F

S

P

M

Q

Q

Q

C225 (= C188) 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.

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)
39% identity, 97% coverage: 3:247/253 of query aligns to 2:252/271 of Q72J02

query
sites
Q72J02

Q

R

L

W

S

T

D

K

D

E

E

E

L

L

I

D

R

R

Y

Y

S

H

R

R

Q

Q

I

M

L

I

L

L

P

P

E

Q

I

V

G

G

Y

P

A

E

G

G

Q

Q

A

E

A

R

L

L

A

K

D

R

G

A

R

S

I

V

L

V

I

V

M

V

G

G

L

A

G

G

L

L

G

G

S

V

P

P

V

V

A

L

L

Q

Y

Y

L

L

A

V

A

A

G

G

V

V

G

G

Q

R

L

V

T

G

L

V

V

V

D

E

F

M

D

D

E

R

V

V

D

E

T

V

S

S

N

N

L

L

Q

H

R

R

Q

Q

I

V

I

L

H

Y

E

T

Q

T

H

E

N

D

V

V

N

G

Q

E

K

P

K

K

V

A

A

L

S

V

A

A

R

Q

E

K

R

R

I

L

A

Q

R

A

L

L

N

N

P

P

A

L

T

V

N

R

V

V

I

E

T

A

H

Y

E

P

T

V

R

R

L

L

D

T

E

S

E

E

Q

N

L

A

S

L

D

E

C

I

V

L

Q

R

A

P

A

Y

D

D

V

L

V

V

D

D

A

A

S

S

D

D

N

N

F

F

A

P

T

T

R

R

F

Y

Q

L

L

V

N

N

R

D

L

A

C

A

H

V

R

L

H

L

L

G

T

K

P

P

L

L

V

V

S

F

G

G

A

A

A

I

I

Y

R

Q

W

F

E

D

G

G

Q

Q

L

V

T

A

T

V

F

F

D

H

-

H

-

P

-

T

F

L

R

H

R

G

Q

E

A

M

T

G

P

P

C

C

Y

Y

Q

R

C

C

L

L

Y

F

P

P

D

K

T

P

S

P

Q

P

A

P

D

G

A

A

-

V

-

P

N

S

C
|
C

A

A

Q

E

N

A

G

G

V

V

A

F

A

G

P

V

I

L

V

P

G

A

A

V

V

V

G

G

S

S

F

L

Q

M

A

A

L

A

E

E

A

A

I

L

K

K

V

V

L

L

A

L

G

G

L

I

-

G

E

K

T

P

L

L

Q

A

G

G

R

H

L

L

L

Y

D

D

G

A

L

L

S

E

M

A

Q

S

C

F

Q

R

S

K

L

L

N

T

L

V

T

R

S

R

D

N

P

P

D

R

C

C

P

P

I

V

C

C

C192 (= C188) 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.

6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
37% identity, 83% coverage: 4:213/253 of query aligns to 7:212/289 of 6yubB

query
sites
6yubB

L

L

S

S

D

K

D

E

E

E

L

I

I

E

R

R

Y

Y

S

S

R

R

Q

Q

I

M

L

I

L

V

P

P

E

G

I

M

G

G

Y

K

A

E

G

G

Q

Q

A

L

A

R

L

L

A

M

D

N

G

A

R

K

I

V

L

L

I

I

M

I

G

G

L

A

G

G

L

L

G

G

S

C

P

P

V

A

A

A

L

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

Q

T

L

I

T

G

L

I

V

V

D

D

F

G

D

D

E

S

V

V

D

E

T

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

I

V

I

A

H

H

E

A

Q

T

H

K

N

R

V

V

N

G

Q

M

K

L

K

K

V

V

A

D

S

S

A

L

R

I

E

T

R

H

I

L

A

I

R

E

L

I

N

N

P

P

A

L

T

P

N

V

V

Y

I

V

T

P

H

Y

E

R

T

F

R

D

L

L

D

T

E

P

E

Q

Q

N

L

A

S

A

D

Q

C

I

V

I

Q

K

A

P

A

W

D

D

V

V

V

I

V

L

D

D

A

C

S

T

D

D

N

N

F

P

A

A

T

T

R

R

F

Y

Q

L

L

I

N

S

R

D

L

V

C

C

H

V

R

L

H

L

L

G

T

K

P

P

L

L

V

V

S

S

G

A

A

A

A

S

I

V

R

Q

W

K

E

S

G

G

Q

Q

L

L

T

I

T

V

F

L

D

N

-

C

-

P

-

T

-

P

-

Q

-

G

-

V

F

V

R

N

R

K

Q

K

A

A

T

A

P

P

C
|
C

Y

Y

Q

R

C
|
C

L

C

Y

F

P

-

D

-

T

-

S

-

Q

-

A

-

D

-

A

-

N

-

C

-

A

-

Q

-

N

K

G

G

V

I

A

M

A

G

P

P

I

V

V

V

G

G

A

M

V

M

G

G

S

V

F

A

Q

Q

A

A

L

G

E

E

A

A

I

I

K

K

V

I

L

L

binding zinc ion: C184 (= C173), C187 (= C176)

Sites not aligning to the query:

binding zinc ion: 265

6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
37% identity, 83% coverage: 4:213/253 of query aligns to 6:213/423 of 6yubA

query
sites
6yubA

L

L

S

S

D

K

D

E

E

E

L

I

I

E

R

R

Y

Y

S

S

R

R

Q

Q

I

M

L

I

L

V

P

P

E

G

I

M

G

G

Y

K

A

E

G

G

Q

Q

A

L

A

R

L

L

A

M

D

N

G

A

R

K

I

V

L

L

I

I

M

I

G

G

L

A

G

G

L

L

G

G

S

C

P

P

V

A

A

A

L

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

Q

T

L

I

T

G

L

I

V

V

D

D

F

G

D

D

E

S

V

V

D

E

T

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

I

V

I

A

H

H

E

A

Q

T

H

K

N

R

V

V

N

G

Q

M

K

L

K

K

V

V

A

D

S

S

A

L

R

I

E

T

R

H

I

L

A

I

R

E

L

I

N

N

P

P

A

L

T

P

N

V

V

Y

I

V

T

P

H

Y

E

R

T

F

R

D

L

L

D

T

E

P

E

Q

Q

N

L

A

S

A

D

Q

C

I

V

I

Q

K

A

P

A

W

D

D

V

V

V

I

V

L

D

D

A

C

S

T

D

D

N

N

F

P

A

A

T

T

R

R

F

Y

Q

L

L

I

N

S

R

D

L

V

C

C

H

V

R

L

H

L

L

G

T

K

P

P

L

L

V

V

S

S

G

A

A

A

A

S

I

V

R

Q

W

K

E

S

G

G

Q

Q

L

L

T

I

T

V

F

L

D

N

-

C

-

P

-

T

-

P

-

Q

-

G

-

V

F

V

R

N

R

K

Q

K

A

A

T

A

P

P

C
|
C

Y

Y

Q

R

C
|
C

L

C

Y

F

P

-

D

-

T

-

S

-

Q

-

A

-

D

-

A

-

N

-

C

-

A

K

Q

K

N

P

G

G

V

I

A

M

A

G

P

P

I

V

V

V

G

G

A

M

V

M

G

G

S

V

F

A

Q

Q

A

A

L

G

E

E

A

A

I

I

K

K

V

I

L

L

binding zinc ion: C183 (= C173), C186 (= C176)

Sites not aligning to the query:

binding zinc ion: 266, 269

6xoiB Structure of sumo1-ml00752641 adduct bound to sae (see paper)
31% identity, 60% coverage: 28:179/253 of query aligns to 7:157/403 of 6xoiB

query
sites
6xoiB

A

A

L

V

A

A

D

G

G

G

R

R

I

V

L

L

I

V

M

V

G

G

L

A

G

G

G
|
G

L

I

G

G

S

C

P

E

V

L

A

L

L

K

Y

N

L

L

A

V

A

L

A

T

G

G

V

F

G

S

Q

H

L

I

T

D

L

L

V

I

D
|
D

F
x
L

D

D

E

T

V

I

D

D

T

V

S

S

N

N

L

L

Q

N

R

R

Q

Q

I

F

I

L

H

F

E

Q

Q

K

H

K

N

H

V

V

N

G

Q

R

K

S

K
|
K

V

A

A

Q

S

V

A

A

R

K

E

E

R

S

I

V

A

L

R

Q

L

F

N

Y

P

P

A

K

T

A

N

N

V

I

I

V

T

A

-

Y

H

H

E

D

T
x
S

R
x
I

L

M

D

N

E

P

E

D

Q

Y

L

N

S

V

D

E

C

F

V

F

Q

R

A

Q

A

F

D

I

V

L

V

V

V

M

D

N

A
|
A

S
x
L

D
|
D

N
|
N

F

R

A

A

T

A

R

R

F

N

Q

H

L

V

N

N

R

R

L

M

C

C

H

L

R

A

H

A

L

D

T

V

P

P

L

L

V

I

S

E

G

S

A

G

A

T

I

A

R

G

W

Y

E

L

G

G

Q

Q

L

V

T

T

F

-

D

-

F

I

R

K

Q

G

A

V

T

T

P

E

C
|
C

Y

Y

Q

E

C
|
C

L

H

Y

F

P

P

active site: D110 (= D130)
binding [(1R,2R,3S,4R)-4-{[5-(1-benzyl-1H-pyrazole-3-carbonyl)pyrimidin-4-yl]amino}-2,3-dihydroxycyclopentyl]methyl sulfamate: G20 (= G41), D41 (= D62), L42 (≠ F63), K65 (= K86), S88 (≠ T108), I89 (≠ R109), A108 (= A128), L109 (≠ S129), D110 (= D130), N111 (= N131)
binding zinc ion: C151 (= C173), C154 (= C176)

Sites not aligning to the query:

active site: 159, 160, 162
binding zinc ion: 353, 356

3kydB Human sumo e1~sumo1-amp tetrahedral intermediate mimic (see paper)
30% identity, 67% coverage: 28:197/253 of query aligns to 11:180/477 of 3kydB

query
sites
3kydB

A

A

L

V

A

A

D

G

G

G

R

R

I

V

L

L

I

V

M

V

G

G

L

A

G

G

L
x
I

G

G

S

C

P

E

V

L

A

L

L

K

Y

N

L

L

A

V

A

L

A

T

G

G

V

F

G

S

Q

H

L

I

T

D

L

L

V

I

D
|
D

F
x
L

D

D

E

T

V

I

D

D

T

V

S

S

N

N

L

L

Q

N

R

R

Q

Q

I

F

I

L

H

F

E

Q

Q

K

H

K

N

H

V

V

N

G

Q

R

K

S

K
|
K

V

A

A

Q

S

V

A

A

R

K

E

E

R

S

I

V

A

L

R

Q

L

F

N

Y

P

P

A

K

T

A

N

N

V

I

I

V

T

A

-

Y

H

H

E

D

T
x
S

R
x
I

L

M

D

N

E

P

E

D

Q

Y

L

N

S

V

D

E

C

F

V

F

Q

R

A

Q

A

F

D

I

V

L

V

V

V

M

D

N

A

A

S
x
L

D
|
D

N
|
N

F

R

A

A

T

A

R

R

F

N

Q

H

L

V

N

N

R

R

L

M

C

C

H

L

R

A

H

A

L

D

T

V

P

P

L

L

V

I

S

E

G

S

A

G

A

T

I

A

R

G

W

Y

E

L

G

G

Q

Q

L

V

T

T

F

-

D

-

F

I

R

K

Q

G

A

V

T

T

P

E

C
|
C

Y

Y

Q

E

C
|
C

L

H

Y

P

P

K

D

P

T

T

S

Q

Q

R

A

T

D

F

A

P

N

G

C
|
C

A
x
T

-

I

Q
x
R

N

N

G

T

V

P

A

S

A

E

P

P

I

I

active site: D114 (= D130), C170 (= C188), T171 (≠ A189), R173 (≠ Q190)
binding 5'-{[(3-aminopropyl)sulfonyl]amino}-5'-deoxyadenosine: I25 (≠ L42), D45 (= D62), L46 (≠ F63), K69 (= K86), S92 (≠ T108), I93 (≠ R109), L113 (≠ S129), D114 (= D130), N115 (= N131), C170 (= C188), R173 (≠ Q190)
binding zinc ion: C155 (= C173), C158 (= C176)

Sites not aligning to the query:

binding zinc ion: 370, 373

3kycB Human sumo e1 complex with a sumo1-amp mimic (see paper)
30% identity, 67% coverage: 28:197/253 of query aligns to 10:179/548 of 3kycB

query
sites
3kycB

A

A

L

V

A

A

D

G

G

G

R

R

I

V

L

L

I

V

M

V

G

G

L

A

G
|
G

L

I

G

G

S

C

P

E

V

L

A

L

L

K

Y

N

L

L

A

V

A

L

A

T

G

G

V

F

G

S

Q

H

L

I

T

D

L

L

V

I

D
|
D

F
x
L

D

D

E

T

V

I

D

D

T

V

S

S

N

N

L

L

Q

N

R

R

Q

Q

I

F

I

L

H

F

E

Q

Q

K

H

K

N

H

V

V

N

G

Q

R

K

S

K
|
K

V

A

A

Q

S

V

A

A

R

K

E

E

R

S

I

V

A

L

R

Q

L

F

N

Y

P

P

A

K

T

A

N

N

V

I

I

V

T

A

-

Y

H

H

E

D

T
x
S

R
x
I

L

M

D

N

E

P

E

D

Q

Y

L

N

S

V

D

E

C

F

V

F

Q

R

A

Q

A

F

D

I

V

L

V

V

V

M

D

N

A

A

S
x
L

D
|
D

N
|
N

F

R

A

A

T

A

R

R

F

N

Q

H

L

V

N

N

R

R

L

M

C

C

H

L

R

A

H

A

L

D

T

V

P

P

L

L

V

I

S

E

G

S

A

G

A

T

I

A

R

G

W

Y

E

L

G

G

Q

Q

L

V

T

T

F

-

D

-

F

I

R

K

Q

G

A

V

T

T

P

E

C
|
C

Y

Y

Q

E

C
|
C

L

H

Y

P

P

K

D

P

T

T

S

Q

Q

R

A

T

D

F

A

P

N

G

C
|
C

A
x
T

-

I

Q
x
R

N

N

G

T

V

P

A

S

A

E

P

P

I

I

active site: D113 (= D130), C169 (= C188), T170 (≠ A189), R172 (≠ Q190)
binding 5'-deoxy-5'-(sulfamoylamino)adenosine: G22 (= G40), G23 (= G41), D44 (= D62), L45 (≠ F63), K68 (= K86), S91 (≠ T108), I92 (≠ R109), L112 (≠ S129), D113 (= D130), N114 (= N131)
binding zinc ion: C154 (= C173), C157 (= C176)

Sites not aligning to the query:

binding zinc ion: 407, 410

1y8qB Sumo e1 activating enzyme sae1-sae2-mg-atp complex (see paper)
31% identity, 62% coverage: 28:183/253 of query aligns to 9:162/510 of 1y8qB

query
sites
1y8qB

A

A

L

V

A

A

D

G

G

G

R

R

I

V

L

L

I

V

M

V

G

G

L

A

G

G

L

I

G

G

S

C

P

E

V

L

A

L

L

K

Y

N

L

L

A

V

A

L

A

T

G

G

V

F

G

S

Q

H

L

I

T

D

L

L

V

I

D
|
D

F
x
L

D

D

E

T

V

I

D

D

T

V

S

S

N

N

L

L

Q

N

R

R

Q

Q

I

F

I

L

H

F

E

Q

Q

K

H

K

N

H

V

V

N

G

Q

R

K

S

K
|
K

V

A

A

Q

S

V

A

A

R

K

E

E

R

S

I

V

A

L

R

Q

L

F

N

Y

P

P

A

K

T

A

N

N

V

I

I

V

T

A

-

Y

H

H

E

D

T
x
S

R
x
I

L

M

D

N

E

P

E

D

Q

Y

L

N

S

V

D

E

C

F

V

F

Q

R

A

Q

A

F

D

I

V

L

V

V

V

M

D

N

A

A

S
x
L

D
|
D

N
|
N

F

R

A

A

T

A

R

R

F

N

Q

H

L

V

N

N

R

R

L

M

C

C

H

L

R

A

H

A

L

D

T

V

P

P

L

L

V

I

S

E

G

S

A

G

A

T

I

A

R

G

W

Y

E

L

G

G

Q

Q

L

V

T

T

F

-

D

-

F

I

R

K

Q

G

A

V

T

T

P

E

C
|
C

Y

Y

Q

E

C
|
C

L

-

Y

H

P

P

D

K

T

P

S

T

Q

Q

active site: D112 (= D130)
binding adenosine-5'-triphosphate: D43 (= D62), L44 (≠ F63), K67 (= K86), S90 (≠ T108), I91 (≠ R109), L111 (≠ S129), D112 (= D130), N113 (= N131)
binding zinc ion: C153 (= C173), C156 (= C176)

Sites not aligning to the query:

Q9UBT2 SUMO-activating enzyme subunit 2; Anthracycline-associated resistance ARX; Ubiquitin-like 1-activating enzyme E1B; Ubiquitin-like modifier-activating enzyme 2; EC 2.3.2.- from Homo sapiens (Human) (see 8 papers)
30% identity, 67% coverage: 28:197/253 of query aligns to 14:183/640 of Q9UBT2

query
sites
Q9UBT2

A

A

L

V

A

A

D

G

G

G

R

R

I

V

L

L

I

V

M

V

G
|
G

L
x
A

G
|
G

L
x
I

G
|
G

S

C

P

E

V

L

A

L

L

K

Y

N

L

L

A

V

A

L

A

T

G

G

V

F

G

S

Q

H

L

I

T

D

L

L

V

I

D
|
D

F

L

D

D

E

T

V

I

D

D

T

V

S

S

N
|
N

L
|
L

Q
x
N

R
|
R

Q

Q

I

F

I

L

H

F

E

Q

Q

K

H

K

N

H

V

V

N

G

Q

R

K

S

K
|
K

V

A

A

Q

S

V

A

A

R

K

E

E

R

S

I

V

A

L

R

Q

L

F

N

Y

P

P

A

K

T

A

N

N

V

I

I

V

T

A

-

Y

H

H

E

D

T
x
S

R
x
I

L

M

D

N

E

P

E

D

Q

Y

L

N

S

V

D

E

C

F

V

F

Q

R

A

Q

A

F

D

I

V

L

V

V

V

M

D

N

A

A

S

L

D
|
D

N
|
N

F
x
R

A
|
A

T
x
A

R
|
R

F

N

Q

H

L

V

N

N

R

R

L

M

C

C

H

L

R

A

H

A

L

D

T

V

P

P

L

L

V

I

S

E

G

S

A

G

A

T

I

A

R

G

W

Y

E

L

G

G

Q

Q

L

V

T

T

F

-

D

-

F

I

R

K

Q

G

A

V

T

T

P

E

C

C

Y

Y

Q

E

C

C

L

H

Y

P

P

K

D

P

T

T

S

Q

Q

R

A

T

D

F

A

P

N

G

C
|
C

A
x
T

-

I

Q

R

N

N

G

T

V

P

A

S

A

E

P

P

I

I

G24 (= G38) to V: in ACCES; loss of function; does not rescue the abnormal phenotype in a zebrafish disease model; dbSNP:rs2075211884
GAGGIG 24:29 (≠ GLGGLG 38:43) binding ATP
D48 (= D62) binding ATP
N56 (= N70) mutation to A: Abolishes ATP-dependent activation of SUMO proteins.
NLNR 56:59 (≠ NLQR 70:73) binding ATP
L57 (= L71) mutation to A: Strongly reduces ATP-dependent activation of SUMO proteins.
R59 (= R73) mutation to A: Strongly reduces ATP-dependent activation of SUMO proteins.
K72 (= K86) binding ATP; mutation to A: Abolishes ATP-dependent activation of SUMO proteins.
SI 95:96 (≠ TR 108:109) binding ATP
D117 (= D130) mutation to A: Abolishes ATP-dependent activation of SUMO proteins.
DNRAAR 117:122 (≠ DNFATR 130:135) binding ATP
R122 (= R135) to G: in ACCES; loss of function; does not rescue the abnormal phenotype in a zebrafish disease model; dbSNP:rs1599889628
C173 (= C188) active site, Glycyl thioester intermediate; mutation to A: Loss of enzyme activity.
T174 (≠ A189) mutation to A: Slightly reduced enzyme activity.

Sites not aligning to the query:

184 H→Q: No effect on enzyme activity.
235 I→A: Strongly reduced interaction with UBE2I; when associated with A-238.
238 I→A: Strongly reduced interaction with UBE2I; when associated with A-235.
307 L → R: in dbSNP:rs1043062
483 E → K: in ACCES; loss of function; does not rescue the abnormal phenotype in a zebrafish disease model; dbSNP:rs2075619600
484 mutation Missing: Strongly reduced interaction with UBE2I.
485 G→GGGG: Strongly reduced interaction with UBE2I.

Query Sequence

>WP_019895485.1 NCBI__GCF_000384235.1:WP_019895485.1
MTQLSDDELIRYSRQILLPEIGYAGQAALADGRILIMGLGGLGSPVALYLAAAGVGQLTL
VDFDEVDTSNLQRQIIHEQHNVNQKKVASARERIARLNPATNVITHETRLDEEQLSDCVQ
AADVVVDASDNFATRFQLNRLCHRHLTPLVSGAAIRWEGQLTTFDFRRQATPCYQCLYPD
TSQADANCAQNGVAAPIVGAVGSFQALEAIKVLAGLETLQGRLLLLDGLSMQCQSLNLTS
DPDCPICQPGKSD

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