SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012568196.1 NCBI__GCF_000016185.1:WP_012568196.1 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)
53% identity, 94% coverage: 7:266/276 of query aligns to 3:264/271 of Q72J02

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Q72J02

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C192 (= C194) 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.

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)
43% identity, 95% coverage: 5:266/276 of query aligns to 62:321/453 of Q9VLJ8

query
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Q9VLJ8

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T62 (≠ S5) modified: Phosphothreonine

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)
51% identity, 95% coverage: 1:263/276 of query aligns to 49:309/460 of O95396

query
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O95396

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158:238 (vs. 110:193, 56% identical) Interaction with NFS1
C239 (= C194) 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)
53% identity, 89% coverage: 11:255/276 of query aligns to 9:249/270 of D4GSF3

query
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D4GSF3

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C188 (= C194) 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.

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)
43% identity, 91% coverage: 6:257/276 of query aligns to 60:321/482 of O59954

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O59954

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Y

L

L

L

I

N

S

D

D

A

T

C

A

F

V

F

L

A

L

G

G

K

K

T

P

L

L

V

V

S

S

A

A

A

S

M

A

L

L

R

R

F

T

D
x
E

A

G

Q

Q

L

L

S

M

V

V

F

L

K

N

A

N

H

P

L

P

G

Q

E

P

P

P

-

G

-

D

-

K

-

T

-

G

H

G

P

P

C

C

Y

Y

R

R

C

C

I

V

F

F

R

P

E

K

P

P

P

A

G

N

T

S

I

V

P

T

S

S

C

C

S

A

E

D

G

G

V

I

L

L

G

G

A

P

L

V

P

V

G
|
G

A

T

M

M

G

G

S

V

L

L

Q

Q

A

A

I

S

E

E

V

A

L

I

K

K

E

V

L

L

L

T

G

S

I

A

G

G

E

E

S

S

L

V

S

E

G

A

-

T

-

P

R

S

L

L

L

I

V

F

A

S

A

A

L

Y

E

S

T

S

-

P

S

Q

F

F

R

R

T

T

V

I

R

K

V

L

R

R

-

S

R

R

D

R

P

P

G

N

C

C

P

A

L

V

C

C

G

S

G

A

D

E

G82 (= G28) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
G100 (= G46) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
R130 (= R76) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
C185 (≠ G131) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
E215 (≠ D161) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
G264 (= G205) mutation to S: In cnxF142ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.

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)
42% identity, 91% coverage: 6:257/276 of query aligns to 38:292/440 of P38820

query
sites
P38820

P

P

L

L

S

S

D

L

D

E

Q

E

I

Y

E

Q

R

R

Y

Y

A

G

R

R

H

Q

I

M

M

I

L

V

K

E

E

E

V

T

G

G

-

V

R

A

G

G

Q

Q

E

V

R

K

L

L

L

K

A

N

S

T

S

K

V

V

L

L

V

V

G

G

A

A

G

G

L

L

G

G

S

C

P

P

L

A

L

L

L

P

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

R

Q

I

I

G

G

V

I

I

V

D

D

H

N

D

D

S

V

V

V

D

E

L

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

V

V

I

L

H

H

D

D

G

S

A

S

S

R

V

V

G

G

R

M

P

L

K

K

V

C

E

E

S

S

A

A

A

R

A

Q

R

Y

I

I

A

T

A

K

L

L

T

N

P

P

D

H

V

I

R

N

V

V

E

V

A

T

H

Y

A

P

E

V

R

R

L

L

T

N

P

S

A

S

N

N

V

A

L

F

G

D

L

I

V

F

S

K

R

G

Y

Y

D

N

V

Y

V

I

A

L

D

D

G

C

S

T

D

D

N

S

F

P

A

L

T

T

R

R

F

Y

L

L

L

V

N

S

D

D

A

V

C

A

F

V

F

N

A

L

G

G

K

I

T

T

L

V

V

V

S

S

A

A

A

S

M

G

L

L

R

G

F

T

D

E

A

G

Q

Q

L

L

S

T

V

I

F

L

K

-

A

-

H

N

L

F

G

N

E

N

P

I

H

G

P

P

C

C

Y

Y

R

R

C

C

I

F

F

Y

R

P

E

T

P

P

G

N

T

A

I

V

P

T

S

S

C
|
C

S

Q

E

E

G

G

V

V

L

I

G

G

A

P

L

C

P

I

G

G

A

L

M

V

G

G

S

T

L

M

Q

M

A

A

I

V

E

E

V

T

L

L

K

K

E

L

L

I

L

L

G

G

I

I

-

Y

-

T

G

N

E

E

S

N

L

F

S

S

G

P

R

F

L

L

L

M

L

L

V

Y

A

S

A

G

L

F

-

P

E

Q

T

Q

S

S

F

L

R

R

T

T

V

F

R

K

V

M

R

R

-

G

R

R

D

Q

P

E

G

K

C

C

P

L

L

C

C

C

G

G

G

K

D

N

C225 (= C194) 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.

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)
43% identity, 91% coverage: 5:255/276 of query aligns to 2:248/249 of P12282

query
sites
P12282

S

A

P

E

L

L

S

S

D

D

D

Q

Q

E

I

M

E

L

R

R

Y

Y

A

N

R
|
R

H

Q

I

I

M

I

L

L

K

R

E

G

V

F

G

D

G

F

R

D

G

G

Q

Q

E

E

R

A

L

L

L

K

A

D

S

S

S

R

V

V

L

L

V

I

V

V

G

G

A

L

G

G

L

L

G

G

S
x
C

P

A

L

A

L

S

L

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

R

N

I

L

G

T

V

L

I

L

D

D

H

F

D

D

S

T

V

V

D

S

L

L

S

S

N

N

L

L

Q

Q

R
|
R

Q

Q

V

T

I

L

H

H

D

S

G

D

A

A

S

T

V

V

G

G

R

Q

P

P

K

K

V

V

E

E

S

S

A

A

A

R

A

D

R

A

I

L

A

T

A

R

L

I

T

N

P

P

D

H

V

I

R

A

V

I

E

T

A

P

H

V

A

N

E

A

R

L

L

L

T

D

P

D

A

A

N

E

V

L

L

A

G

A

L

L

V

I

S

A

R

E

Y

H

D

D

V

L

V

V

A

L

D

D

G
x
C

S

T

D
|
D

N

N

F

V

A

A

T

V

R

R

F

N

L

Q

L

L

N

N

D

A

A

G

C
|
C

F

F

F

A

A

A

G

K

K

V

T

P

L

L

V

V

S

S

A

G

A

A

M

A

L

I

R

R

F

M

D

E

A

G

Q

Q

L

I

S

T

V

V

F

F

K

T

A

Y

H

Q

L

D

G

G

E

E

P

-

H

-

P

P

C
|
C

Y

Y

R

R

C
|
C

I

L

F

S

R

R

E

L

P

F

P

G

P

E

P

N

G

A

T

L

I

-

P

-

S

T

C
|
C

S

V

E

E

G

A

G

G

V

V

L

M

G

A

A

P

L

L

P

I

G

G

A

V

M

I

G

G

S

S

L

L

Q

Q

A

A

I

M

E

E

V

A

L

I

K

K

E

M

L

L

L

A

G

G

I

Y

G

G

E

K

S

P

L

A

S

S

G

G

R

K

L

I

L

V

L

M

V

Y

A

D

A

A

L

M

E

T

T
x
C

S

Q

F

F

R

R

T

E

V

M

R

K

V

L

R

M

R

R

D

N

P

P

G

G

C
|
C

P

E

L

V

C
|
C

G

G

R14 (= R17) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
C44 (≠ S47) mutation to A: No effect.
R73 (= R76) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
C128 (≠ G131) mutation to A: No effect.; mutation to Y: No activity.
D130 (= D133) mutation to A: No activity.; mutation to E: Substantially reduced activity.
C142 (= C145) mutation to A: No effect.
C172 (= C177) mutation to A: No zinc bound and no enzyme activity.
C175 (= C180) mutation to A: No zinc bound and no enzyme activity.
C187 (= C194) mutation to A: No effect.
C231 (≠ T238) mutation to A: No effect.
C244 (= C251) mutation to A: No zinc bound and almost no enzyme activity.
C247 (= C254) 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)
42% identity, 91% coverage: 5:255/276 of query aligns to 1:240/240 of 1jwbB

query
sites
1jwbB

S

A

P

E

L

L

S

S

D

D

D

Q

Q

E

I

M

E

L

R

R

Y

Y

A

N

R
|
R

H

Q

I

I

M

I

L

L

K

R

E

G

V

F

G

D

G

F

R

D

G

G

Q

Q

E

E

R

A

L

L

L

K

A

D

S

S

S

R

V

V

L

L

V

I

V

V

G
|
G

A

L

G
|
G

L

L

G

G

S

C

P

A

L

A

L

S

L

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

R

N

I

L

G

T

V

L

I

L

D
|
D

H
x
F

D

D

S

T

V

V

D

S

L

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

V

T

I

L

H

H

D

S

G

D

A

A

S

T

V

V

G

G

R

Q

P

P

K
|
K

V

V

E

E

S

S

A

A

A

R

A

D

R

A

I

L

A

T

A

R

L

I

T

N

P

P

D

H

V

I

R

A

V

I

E

T

A

P

H

V

A

N

E

A

R
x
L

L

L

T

D

P

D

A

A

N

E

V

L

L

A

G

A

L

L

V

I

S

A

R

E

Y

H

D

D

V

L

V

V

A

L

D

D

G
x
C

S
x
T

D
|
D

N
|
N

F

V

A

A

T
x
V

R

R

F

N

L

Q

L

L

N

N

D

A

A

G

C

C

F

F

F

A

A

A

G

K

K

V

T

P

L

L

V

V

S

S

A

G

A

A

M

A

L

I

R

R

F

M

D

E

A

G

Q

Q

L

I

S

T

V

V

F

F

K

T

A

Y

H

Q

L

D

G

G

E

E

P

-

H

-

P

P

C
|
C

Y

Y

R

R

C

C

I

L

F

S

R

R

E

-

P

-

G

-

T

-

I

-

P

-

S

L

C

F

S

G

E

E

G

A

G

G

V

V

L

M

G

A

A

P

L

L

P

I

G

G

A

V

M

I

G

G

S

S

L

L

Q

Q

A

A

I

M

E

E

V

A

L

I

K

K

E

M

L

L

L

A

G

G

I

Y

G

G

E

K

S

P

L

A

S

S

G

G

R

K

L

I

L

V

L

M

V

Y

A

D

A

A

L

M

E

T

T

C

S

Q

F

F

R

R

T

E

V

M

R

K

V

L

R

M

R

R

D

N

P

P

G

G

C
|
C

P

E

L

V

C
|
C

G

G

active site: R13 (= R17), D129 (= D133)
binding adenosine monophosphate: G37 (= G41), G39 (= G43), G40 (= G44), D61 (= D65), F62 (≠ H66), K85 (= K89), L108 (≠ R112), C127 (≠ G131), T128 (≠ S132), D129 (= D133), N130 (= N134), V133 (≠ T137)
binding zinc ion: C171 (= C177), C236 (= C251), C239 (= C254)

1jw9B Structure of the native moeb-moad protein complex (see paper)
42% identity, 91% coverage: 5:255/276 of query aligns to 1:240/240 of 1jw9B

query
sites
1jw9B

S

A

P

E

L

L

S

S

D

D

D

Q

Q

E

I

M

E

L

R

R

Y

Y

A

N

R
|
R

H

Q

I

I

M

I

L

L

K

R

E

G

V

F

G

D

G

F

R

D

G

G

Q

Q

E

E

R

A

L

L

L

K

A

D

S

S

S

R

V

V

L

L

V

I

V

V

G

G

A

L

G

G

L

L

G

G

S

C

P

A

L

A

L

S

L

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

R

N

I

L

G

T

V

L

I

L

D

D

H

F

D

D

S

T

V

V

D

S

L

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

V

T

I

L

H

H

D

S

G

D

A

A

S

T

V

V

G

G

R

Q

P

P

K

K

V

V

E

E

S

S

A

A

A

R

A

D

R

A

I

L

A

T

A

R

L

I

T

N

P

P

D

H

V

I

R

A

V

I

E

T

A

P

H

V

A

N

E

A

R

L

L

L

T

D

P

D

A

A

N

E

V

L

L

A

G

A

L

L

V

I

S

A

R

E

Y

H

D

D

V

L

V

V

A

L

D

D

G

C

S

T

D
|
D

N

N

F

V

A

A

T

V

R

R

F

N

L

Q

L

L

N

N

D

A

A

G

C

C

F

F

F

A

A

A

G

K

K

V

T

P

L

L

V

V

S

S

A

G

A

A

M

A

L

I

R

R

F

M

D

E

A

G

Q

Q

L

I

S

T

V

V

F

F

K

T

A

Y

H

Q

L

D

G

G

E

E

P

-

H

-

P

P

C
|
C

Y

Y

R

R

C

C

I

L

F

S

R

R

E

-

P

-

G

-

T

-

I

-

P

-

S

L

C

F

S

G

E

E

G

A

G

G

V

V

L

M

G

A

A

P

L

L

P

I

G

G

A

V

M

I

G

G

S

S

L

L

Q

Q

A

A

I

M

E

E

V

A

L

I

K

K

E

M

L

L

L

A

G

G

I

Y

G

G

E

K

S

P

L

A

S

S

G

G

R

K

L

I

L

V

L

M

V

Y

A

D

A

A

L

M

E

T

T

C

S

Q

F

F

R

R

T

E

V

M

R

K

V

L

R

M

R

R

D

N

P

P

G

G

C
|
C

P

E

L

V

C
|
C

G

G

active site: R13 (= R17), D129 (= D133)
binding zinc ion: C171 (= C177), C236 (= C251), C239 (= C254)

P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
41% identity, 92% coverage: 7:259/276 of query aligns to 1:251/251 of P30138

query
sites
P30138

L

M

S

N

D

D

D

R

Q

D

I

F

E

M

R

R

Y

Y

A

S

R

R

H

Q

I

I

M

L

L

L

K

D

E

D

V

I

G

A

G

L

R

D

G

G

Q

Q

E

Q

R

K

L

L

A

D

S

S

S

Q

V

V

L

L

V

I

G

G

A

L

G

G

L

L

G

G

S

T

P

P

L

A

L

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

R

T

I

L

G

V

V

L

I

A

D

D

H

D

D

D

S

D

V

V

D

H

L

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

V

I

I

L

H

F

D

T

G

T

A

E

S

D

V

I

G

D

R

R

P

P

K

K

V

S

E

Q

S

V

A

S

A

Q

R

R

I

L

A

T

A

Q

L

L

T

N

P

P

D

D

V

I

R

Q

V

L

E

T

A

A

H

L

A

Q

E

Q

R

R

L

L

T

T

P

G

A

E

N

A

V

L

L

K

G

D

L

A

V

V

S

A

R

R

Y

A

D

D

V

V

A

L

D

D

G

C

S

T

D

D

N

N

F

M

A

A

T

T

R

R

F

Q

L

E

L

I

N

N

D

A

A

A

C

C

F

V

F

A

A

L

G

N

K

T

T

P

L

L

V

I

S

T

A

A

A

S

M

A

L

V

R

G

F

F

D

G

A

G

Q

Q

L

L

S

M

V

V

F

L

K

T

A

P

H

P

L

W

G

-

E

-

P

E

H

Q

P

G

C
|
C

Y

Y

R

R

C
|
C

I

L

F
x
W

R

P

E

D

P

N

P

Q

P

E

P

P

G

E

T

R

I

-

P

-

S

N

C
|
C

S

R

E

T

G

A

G

G

V

V

L

V

G

G

A

P

L

V

P

V

G

G

A

V

M

M

G

G

S

T

L

L

Q

Q

A

A

I

L

E

E

V

A

L

I

K

K

E

L

L

L

L

S

G

G

I

I

G

-

E

E

S

T

L

P

S

A

G

G

R

E

L

L

L

R

L

L

V

F

A

D

A

G

L

K

E

S

T

S

S

Q

F

W

R

R

T

S

V

L

R

A

V

L

R

R

D

A

P

S

G

G

C
|
C

P

P

L

V

C
|
C

G

G

-

S

-

N

-

A

D

D

P

P

V

V

C169 (= C177) binding Zn(2+)
C172 (= C180) binding Zn(2+)
W174 (≠ F182) mutation to A: No adenylation of ThiS.
C184 (= C194) mutation to S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth.
C240 (= C251) binding Zn(2+)
C243 (= C254) binding Zn(2+)

1zfnA Structural analysis of escherichia coli thif (see paper)
40% identity, 90% coverage: 7:255/276 of query aligns to 1:244/244 of 1zfnA

query
sites
1zfnA

L

M

S

N

D

D

D

R

Q

D

I

F

E

M

R

R

Y

Y

A

S

R
|
R

H

Q

I

I

M

L

L

L

K

D

E

D

V

I

G

A

G

L

R

D

G

G

Q

Q

E

Q

R

K

L

L

A

D

S

S

S

Q

V

V

L

L

V

I

V
x
I

G
|
G

A

L

G
|
G

L

L

G

G

S

T

P

P

L

A

L

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

R

T

I

L

G

V

V

L

I

A

D
|
D

H

D

D

D

S

D

V

V

D

H

L

L

S

S

N

N

L

L

Q

Q

R
|
R

Q
|
Q

V

I

I

L

H

F

D

T

G

T

A

E

S

D

V

I

G

D

R

R

P

P

K
|
K

V

S

E

Q

S

V

A

S

A

Q

R

R

I

L

A

T

A

Q

L

L

T

N

P

P

D

D

V

I

R

Q

V

L

E

T

A

A

H

L

A

Q

E

Q

R

R

L

L

T

T

P

G

A

E

N

A

V

L

L

K

G

D

L

A

V

V

S

A

R

R

Y

A

D

D

V

V

A

L

D

D

G

C

S
x
T

D
|
D

N

N

F

M

A

A

T
|
T

R

R

F

Q

L

E

L

I

N

N

D

A

A

A

C

C

F

V

F

A

A

L

G

N

K

T

T

P

L

L

V

I

S

T

A

A

A

S

M

A

L

V

R

G

F

F

D

G

A

G

Q

Q

L

L

S

M

V

V

F

L

K

T

A

P

H

P

L

W

G

-

E

-

P

E

H

Q

P

G

C
|
C

Y

Y

R

R

C
|
C

I

L

F

W

R

P

E

D

P

N

P

Q

P

E

P

P

G

E

T

R

I

-

P

-

S

N

C

C

S

R

E

T

G

A

G

G

V

V

L

V

G

G

A

P

L

V

P

V

G

G

A

V

M

M

G

G

S

T

L

L

Q

Q

A

A

I

L

E

E

V

A

L

I

K

K

E

L

L

L

L

S

G

G

I

I

G

-

E

E

S

T

L

P

S

A

G

G

R

E

L

L

L

R

L

L

V

F

A

D

A

G

L

K

E

S

T

S

S

Q

F

W

R

R

T

S

V

L

R

A

V

L

R

R

D

A

P

S

G

G

C
|
C

P

P

L

V

C
|
C

G

G

active site: R11 (= R17), D127 (= D133)
binding adenosine-5'-triphosphate: I34 (≠ V40), G35 (= G41), G37 (= G43), G38 (= G44), D59 (= D65), R70 (= R76), Q71 (= Q77), K83 (= K89), T126 (≠ S132), D127 (= D133), T131 (= T137)
binding zinc ion: C169 (= C177), C172 (= C180), C240 (= C251), C243 (= C254)

1zud3 Structure of this-thif protein complex (see paper)
40% identity, 91% coverage: 7:256/276 of query aligns to 1:240/240 of 1zud3

query
sites
1zud3

L

M

S

N

D

D

D

R

Q

D

I

F

E

M

R

R

Y

Y

A

S

R
|
R

H

Q

I

I

M
x
L

L

L

K
x
D

E

D

V

I

G

A

G

L

R

D

G

G

Q

Q

E

Q

R

K

L

L

A

D

S

S

S

Q

V

V

L

L

V

I

G

G

A

L

G

G

L

L

G

G

S

T

P

P

L

A

L

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

R

T

I

L

G

V

V

L

I

A

D

D

H

D

D

D

S

D

V

V

D

H

L

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

V

I

I

L

H

F

D

T

G

T

A

E

S

D

V

I

G

D

R

R

P

P

K

K

V

S

E

Q

S

V

A

S

A

Q

R

R

I

L

A

T

A

Q

L

L

T

N

P

P

D

D

V

I

R

Q

V

L

E

T

A

A

H

L

A

Q

E

Q

R

R

L

L

T

T

P

G

A

E

N

A

V

L

L

K

G

D

L

A

V

V

S

A

R

R

Y

A

D

D

V

V

A

L

D

D

G

C

S

T

D
|
D

N

N

F

M

A

A

T

T

R

R

F

Q

L

E

L

I

N

N

D

A

A

A

C

C

F

V

F

A

A

L

G

N

K

T

T

P

L

L

V

I

S

T

A

A

A

S

M

A

L

V

R

G

F

F

D

G

A

G

Q

Q

L

L

S

M

V

V

F

L

K

T

A

P

H

P

L

W

G

-

E

-

P

E

H

Q

P

G

C
|
C

Y

Y

R

R

C

C

I

L

F

W

R

P

E

D

P

N

P

Q

P

E

P

P

G

-

T

-

I

-

P

-

S

-

C

-

S

-

E

T

G

A

G

G

V

V

L

V

G

G

A

P

L

V

P

V

G

G

A

V

M

M

G

G

S

T

L

L

Q

Q

A

A

I

L

E

E

V

A

L

I

K

K

E

L

L

L

L

S

G

G

I

I

G

-

E

E

S

T

L

P

S

A

G

G

R

E

L

L

L

R

L

L

V

F

A

D

A

G

L

K

E

S

T

S

S

Q

F

W

R

R

T

S

V

L

R

A

V

L

R

R

D

A

P

S

G

G

C
|
C

P

P

L

V

C
|
C

G

G

active site: R11 (= R17), D127 (= D133)
binding calcium ion: L14 (≠ M20), D16 (≠ K22)
binding zinc ion: C169 (= C177), C235 (= C251), C238 (= C254)

1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
38% identity, 88% coverage: 5:247/276 of query aligns to 1:217/217 of 1jwaB

query
sites
1jwaB

S

A

P

E

L

L

S

S

D

D

D

Q

Q

E

I

M

E

L

R

R

Y

Y

A

N

R
|
R

H

Q

I

I

M

I

L

L

K

R

E

G

V

F

G

D

G

F

R

D

G

G

Q

Q

E

E

R

A

L

L

L

K

A

D

S

S

S

R

V

V

L

L

V

I

V

V

G

G

A

L

G
|
G

L

L

G

G

S

C

P

A

L

A

L

S

L

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

R

N

I

L

G

T

V

L

I

L

D
|
D

H
x
F

D

D

S

T

V

V

D

S

L

L

S

S

N

N

L

L

Q

Q

R
|
R

Q

Q

V

T

I

L

H

H

D

S

G

D

A

A

S

T

V

V

G

G

R

Q

P

P

K
|
K

V

V

E

E

S

S

A

A

A

R

A

D

R

A

I

L

A

T

A

R

L

I

T

N

P

P

D

H

V

I

R

A

V

I

E

T

A

P

H

V

A

N

E

A

R
x
L

L

L

T

D

P

D

A

A

N

E

V

L

L

A

G

A

L

L

V

I

S

A

R

E

Y

H

D

D

V

L

V

V

A

L

D

D

G

C

S

T

D
|
D

N
|
N

F

V

A

A

T
x
V

R

R

F

N

L

Q

L

L

N

N

D

A

A

G

C

C

F

F

F

A

A

A

G

K

K

V

T

P

L

L

V

V

S

S

A

G

A

A

M

A

L

I

R

R

F

M

D

E

A

G

Q

Q

L

I

S

T

V

V

F

F

K

T

A

-

H

-

L

-

G

-

E

-

P

-

H

-

P

-

C

-

Y

-

R

-

C

-

I

-

F

-

R

-

E

-

P

-

G

-

T

-

I

-

P

-

S

-

C

-

S

Y

E

E

G

A

G

G

V

V

L

M

G

A

A

P

L

L

P

I

G

G

A

V

M

I

G

G

S

S

L

L

Q

Q

A

A

I

M

E

E

V

A

L

I

K

K

E

M

L

L

L

A

G

G

I

Y

G

G

E

K

S

P

L

A

S

S

G

G

R

K

L

I

L

V

L

M

V

Y

A

D

A

A

L

M

E

T

T

C

S

Q

F

F

R

R

T

E

V

M

R

K

V

L

R

M

R

R

active site: R13 (= R17), D129 (= D133)
binding adenosine-5'-triphosphate: G39 (= G43), G40 (= G44), D61 (= D65), F62 (≠ H66), R72 (= R76), K85 (= K89), L108 (≠ R112), D129 (= D133), N130 (= N134), V133 (≠ T137)

6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
40% identity, 78% coverage: 7:220/276 of query aligns to 6:214/423 of 6yubA

query
sites
6yubA

L

L

S

S

D

K

D

E

Q

E

I

I

E

E

R

R

Y

Y

A

S

R

R

H

Q

I

M

M

I

L

V

K

P

E

G

V

M

G

G

G

K

R

E

G

G

Q

Q

E

L

R

R

L

L

L

M

A

N

S

A

S

K

V

V

L

L

V

I

G

G

A

A

G

G

L

L

G

G

S

C

P

P

L

A

L

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

R

T

I

I

G

G

V

I

I

V

D

D

H

G

D

D

S

S

V

V

D

E

L

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

V

V

I

A

H

H

D

A

G

T

A

K

S

R

V

V

G

G

R

M

P

L

K

K

V

V

E

D

S

S

A

L

A

I

A

T

R

H

I

L

A

I

A

E

L

I

T

N

P

P

D

L

V

P

R

V

V

Y

E

V

A

P

H

Y

A

R

E

F

R

D

L

L

T

T

P

P

A

Q

N

N

V

A

L

A

G

Q

L

I

V

I

S

K

R

P

Y

W

D

D

V

V

V

I

A

L

D

D

G

C

S

T

D

D

N

N

F

P

A

A

T

T

R

R

F

Y

L

L

L

I

N

S

D

D

A

V

C

C

F

V

F

L

A

L

G

G

K

K

T

P

L

L

V

V

S

S

A

A

M

S

L

V

R

Q

F

K

D

S

A

G

Q

Q

L

L

S

I

V

V

F

L

K

N

A

C

H

P

-

P

-

T

-

P

-

Q

-

G

-

V

L

N

G

K

E

K

P

A

H

A

P

P

C
|
C

Y

Y

R

R

C
|
C

I

C

F

F

R

K

E

K

P

P

P

-

G

-

T

-

I

-

P

-

S

-

C

-

S

-

E

-

G

-

G

G

V

I

L

M

G

G

A

P

L

V

P

V

G

G

A

M

M

M

G

G

S

V

L

A

Q

Q

A

A

I

G

E

E

V

A

L

I

K

K

E

I

L

L

L

V

binding zinc ion: C183 (= C177), C186 (= C180)

Sites not aligning to the query:

binding zinc ion: 266, 269

6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
40% identity, 78% coverage: 7:220/276 of query aligns to 7:213/289 of 6yubB

query
sites
6yubB

L

L

S

S

D

K

D

E

Q

E

I

I

E

E

R

R

Y

Y

A

S

R

R

H

Q

I

M

M

I

L

V

K

P

E

G

V

M

G

G

G

K

R

E

G

G

Q

Q

E

L

R

R

L

L

L

M

A

N

S

A

S

K

V

V

L

L

V

I

G

G

A

A

G

G

L

L

G

G

S

C

P

P

L

A

L

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

R

T

I

I

G

G

V

I

I

V

D

D

H

G

D

D

S

S

V

V

D

E

L

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

V

V

I

A

H

H

D

A

G

T

A

K

S

R

V

V

G

G

R

M

P

L

K

K

V

V

E

D

S

S

A

L

A

I

A

T

R

H

I

L

A

I

A

E

L

I

T

N

P

P

D

L

V

P

R

V

V

Y

E

V

A

P

H

Y

A

R

E

F

R

D

L

L

T

T

P

P

A

Q

N

N

V

A

L

A

G

Q

L

I

V

I

S

K

R

P

Y

W

D

D

V

V

V

I

A

L

D

D

G

C

S

T

D

D

N

N

F

P

A

A

T

T

R

R

F

Y

L

L

L

I

N

S

D

D

A

V

C

C

F

V

F

L

A

L

G

G

K

K

T

P

L

L

V

V

S

S

A

A

M

S

L

V

R

Q

F

K

D

S

A

G

Q

Q

L

L

S

I

V

V

F

L

K

N

A

C

H

P

-

P

-

T

-

P

-

Q

-

G

-

V

L

N

G

K

E

K

P

A

H

A

P

P

C
|
C

Y

Y

R

R

C
|
C

I

C

F

F

R

K

E

-

P

-

G

-

T

-

I

-

P

-

S

-

C

-

S

-

E

-

G

-

G

G

V

I

L

M

G

G

A

P

L

V

P

V

G

G

A

M

M

M

G

G

S

V

L

A

Q

Q

A

A

I

G

E

E

V

A

L

I

K

K

E

I

L

L

L

V

binding zinc ion: C184 (= C177), C187 (= C180)

Sites not aligning to the query:

binding zinc ion: 265

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: 34:195/276 of query aligns to 25:182/628 of O42939

query
sites
O42939

A

S

S

A

S

K

V

V

L

L

V

L

V

V

G

G

A

A

G

G

L

I

G

G

S

C

P

E

L

L

L

K

Y

N

L

L

A

L

A

M

A

S

G

G

V

V

G

K

R

E

I

V

G

H

V

I

I

I

D

D

H

L

D

D

S

T

V

I

D

D

L

L

S

S

N

N

L

L

Q

N

R

R

Q

Q

V

F

I

L

H

F

D

R

G

K

A

K

S

H

V

V

G

K

R

Q

P

P

K

K

V

A

E

I

S

V

A

A

A

K

R

T

I

A

A

S

L

F

T

N

P

P

D

N

V

V

R

K

V

L

E

E

A

A

-

Y

H

H

A

A

E

N

R

I

L

K

T

E

P

D

A

R

N

F

V

N

L

V

G

A

L

W

V

F

S

R

R

Q

Y

F

D

D

V

L

V

V

A

F

D

N

G

A

S

L

D

D

N

N

F

L

A

D

T

A

R

R

F

R

L

H

L

V

N

N

D

K

A

Q

C

C

F

L

A

A

G

S

K

V

T

P

L

L

V

I

S

E

A

S

A

G

M

T

L

T

R

G

F

F

D

L

A

G

Q

Q

L

V

S

Q

V

V

F

I

K

I

A

H

H

G

L

K

G

T

E

E

P

-

H

-

P

-

C

C

Y

Y

R

D

C

C

I

N

F

P

R

K

E

E

P

-

P

P

G

K

T

T

I

Y

P

P

S

V

C

C

S

T

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)
32% identity, 60% coverage: 30:195/276 of query aligns to 14:175/650 of Q7SXG4

query
sites
Q7SXG4

E

D

R

S

L

L

L

S

A

S

S

C

S

R

V

V

L

L

V

V

G

G

A

A

G

G

L

I

G

G

S

C

P

E

L

L

L

K

Y

N

L

L

A

V

A

L

A

T

G

G

V

F

G

K

R

N

I

I

G

E

V

V

I

I

D

D

H

L

D

D

S

T

V

I

D

D

L

V

S

S

N

N

L

L

Q

N

R

R

Q

Q

V

F

I

L

H

F

D

Q

G

K

A

K

S

H

V

V

G

G

R

K

P

S

K

K

V

A

E

Q

S

V

A

A

A

K

A

E

R

S

I

V

A

L

A

R

L

F

T

C

P

P

D

S

V

A

R

N

V

I

E

T

A

A

-

Y

H

H

A

D

E

S

R

I

L

M

T

N

P

P

A

D

N

Y

V

N

L

V

G

E

L

F

V

F

S

R

R

N

Y

F

D

Q

V

L

V

V

A

M

D

N

G

A

S

L

D

D

N

N

F

R

A

A

T

A

R

R

F

N

L

H

L

V

N

N

D

R

A

M

C

C

F

L

F

A

A

A

G

D

K

I

T

P

L

L

V

I

S

E

A

S

A

G

M

T

L

A

R

G

F

Y

D

L

A

G

Q

Q

L

V

S

T

V

V

F

I

K

K

A

K

H

G

L

Q

G

T

E

E

P

-

H

-

P

-

C

C

Y

Y

R

E

C

C

I

-

F

-

R

Q

E

P

P

K

P

P

P

T

P

Q

G

K

T

T

I

F

P

P

S

G

C

C

S

T

Sites not aligning to the query:

599 modified: Phosphoserine

3kydB Human sumo e1~sumo1-amp tetrahedral intermediate mimic (see paper)
32% identity, 62% coverage: 26:195/276 of query aligns to 1:171/477 of 3kydB

query
sites
3kydB

G

S

R

R

G

G

Q

L

E

P

R

R

L

E

L

L

A

A

S

E

S

A

V

V

-

A

-

G

-

R

-

V

L

L

V

V

G

G

A

A

G

G

L
x
I

G

G

S

C

P

E

L

L

L

K

Y

N

L

L

A

V

A

L

A

T

G

G

V

F

G

S

R

H

I

I

G

D

V

L

I

I

D
|
D

H
x
L

D

D

S

T

V

I

D

D

L

V

S

S

N

N

L

L

Q

N

R

R

Q

Q

V

F

I

L

H

F

D

Q

G

K

A

K

S

H

V

V

G

G

R

R

P

S

K
|
K

V

A

E

Q

S

V

A

A

A

K

A

E

R

S

I

V

A

L

A

Q

L

F

T

Y

P

P

D

K

V

A

R

N

V

I

E

V

A

A

-

Y

H

H

A

D

E
x
S

R
x
I

L

M

T

N

P

P

A

D

N

Y

V

N

L

V

G

E

L

F

V

F

S

R

R

Q

Y

F

D

I

V

L

V

V

A

M

D

N

G

A

S
x
L

D
|
D

N
|
N

F

R

A

A

T

A

R

R

F

N

L

H

L

V

N

N

D

R

A

M

C

C

F

L

F

A

A

A

G

D

K

V

T

P

L

L

V

I

S

E

A

S

A

G

M

T

L

A

R

G

F

Y

D

L

A

G

Q

Q

L

V

S

T

V

T

F

I

K

K

A

K

H

G

L

V

G

T

E

E

P

-

H

-

P

-

C
|
C

Y

Y

R

E

C
|
C

I

-

F

-

R

H

E

P

P

K

P

P

P

T

P

Q

G

R

T

T

I

F

P

P

S

G

C
|
C

S
x
T

active site: D114 (= D133), C170 (= C194), T171 (≠ S195)
binding 5'-{[(3-aminopropyl)sulfonyl]amino}-5'-deoxyadenosine: I25 (≠ L45), D45 (= D65), L46 (≠ H66), K69 (= K89), S92 (≠ E111), I93 (≠ R112), L113 (≠ S132), D114 (= D133), N115 (= N134), C170 (= C194)
binding zinc ion: C155 (= C177), C158 (= C180)

Sites not aligning to the query:

active site: 173
binding 5'-{[(3-aminopropyl)sulfonyl]amino}-5'-deoxyadenosine: 173
binding zinc ion: 370, 373

3kycB Human sumo e1 complex with a sumo1-amp mimic (see paper)
32% identity, 61% coverage: 27:195/276 of query aligns to 1:170/548 of 3kycB

query
sites
3kycB

R

R

G

G

Q

L

E

P

R

R

L

E

L

L

A

A

S

E

S

A

V

V

-

A

-

G

-

R

-

V

L

L

V

V

G

G

A

A

G
|
G

L

I

G

G

S

C

P

E

L

L

L

K

Y

N

L

L

A

V

A

L

A

T

G

G

V

F

G

S

R

H

I

I

G

D

V

L

I

I

D
|
D

H
x
L

D

D

S

T

V

I

D

D

L

V

S

S

N

N

L

L

Q

N

R

R

Q

Q

V

F

I

L

H

F

D

Q

G

K

A

K

S

H

V

V

G

G

R

R

P

S

K
|
K

V

A

E

Q

S

V

A

A

A

K

A

E

R

S

I

V

A

L

A

Q

L

F

T

Y

P

P

D

K

V

A

R

N

V

I

E

V

A

A

-

Y

H

H

A

D

E
x
S

R
x
I

L

M

T

N

P

P

A

D

N

Y

V

N

L

V

G

E

L

F

V

F

S

R

R

Q

Y

F

D

I

V

L

V

V

A

M

D

N

G

A

S
x
L

D
|
D

N
|
N

F

R

A

A

T

A

R

R

F

N

L

H

L

V

N

N

D

R

A

M

C

C

F

L

F

A

A

A

G

D

K

V

T

P

L

L

V

I

S

E

A

S

A

G

M

T

L

A

R

G

F

Y

D

L

A

G

Q

Q

L

V

S

T

V

T

F

I

K

K

A

K

H

G

L

V

G

T

E

E

P

-

H

-

P

-

C
|
C

Y

Y

R

E

C
|
C

I

-

F

-

R

H

E

P

P

K

P

P

P

T

P

Q

G

R

T

T

I

F

P

P

S

G

C
|
C

S
x
T

active site: D113 (= D133), C169 (= C194), T170 (≠ S195)
binding 5'-deoxy-5'-(sulfamoylamino)adenosine: G22 (= G43), G23 (= G44), D44 (= D65), L45 (≠ H66), K68 (= K89), S91 (≠ E111), I92 (≠ R112), L112 (≠ S132), D113 (= D133), N114 (= N134)
binding zinc ion: C154 (= C177), C157 (= C180)

Sites not aligning to the query:

active site: 172
binding zinc ion: 407, 410

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)
32% identity, 62% coverage: 26:195/276 of query aligns to 4:174/640 of Q9UBT2

query
sites
Q9UBT2

G

S

R

R

G

G

Q

L

E

P

R

R

L

E

L

L

A

A

S

E

S

A

V

V

-

A

-

G

-

R

-

V

L

L

V

V

G
|
G

A
|
A

G
|
G

L
x
I

G
|
G

S

C

P

E

L

L

L

K

Y

N

L

L

A

V

A

L

A

T

G

G

V

F

G

S

R

H

I

I

G

D

V

L

I

I

D
|
D

H

L

D

D

S

T

V

I

D

D

L

V

S

S

N
|
N

L
|
L

Q
x
N

R
|
R

Q

Q

V

F

I

L

H

F

D

Q

G

K

A

K

S

H

V

V

G

G

R

R

P

S

K
|
K

V

A

E

Q

S

V

A

A

A

K

A

E

R

S

I

V

A

L

A

Q

L

F

T

Y

P

P

D

K

V

A

R

N

V

I

E

V

A

A

-

Y

H

H

A

D

E
x
S

R
x
I

L

M

T

N

P

P

A

D

N

Y

V

N

L

V

G

E

L

F

V

F

S

R

R

Q

Y

F

D

I

V

L

V

V

A

M

D

N

G

A

S

L

D
|
D

N
|
N

F
x
R

A
|
A

T
x
A

R
|
R

F

N

L

H

L

V

N

N

D

R

A

M

C

C

F

L

F

A

A

A

G

D

K

V

T

P

L

L

V

I

S

E

A

S

A

G

M

T

L

A

R

G

F

Y

D

L

A

G

Q

Q

L

V

S

T

V

T

F

I

K

K

A

K

H

G

L

V

G

T

E

E

P

-

H

-

P

-

C

C

Y

Y

R

E

C

C

I

-

F

-

R

H

E

P

P

K

P

P

P

T

P

Q

G

R

T

T

I

F

P

P

S

G

C
|
C

S
x
T

G24 (= G41) to V: in ACCES; loss of function; does not rescue the abnormal phenotype in a zebrafish disease model; dbSNP:rs2075211884
GAGGIG 24:29 (≠ GAGGLG 41:46) binding ATP
D48 (= D65) binding ATP
N56 (= N73) mutation to A: Abolishes ATP-dependent activation of SUMO proteins.
NLNR 56:59 (≠ NLQR 73:76) binding ATP
L57 (= L74) mutation to A: Strongly reduces ATP-dependent activation of SUMO proteins.
R59 (= R76) mutation to A: Strongly reduces ATP-dependent activation of SUMO proteins.
K72 (= K89) binding ATP; mutation to A: Abolishes ATP-dependent activation of SUMO proteins.
SI 95:96 (≠ ER 111:112) binding ATP
D117 (= D133) mutation to A: Abolishes ATP-dependent activation of SUMO proteins.
DNRAAR 117:122 (≠ DNFATR 133:138) binding ATP
R122 (= R138) to G: in ACCES; loss of function; does not rescue the abnormal phenotype in a zebrafish disease model; dbSNP:rs1599889628
C173 (= C194) active site, Glycyl thioester intermediate; mutation to A: Loss of enzyme activity.
T174 (≠ S195) 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_012568196.1 NCBI__GCF_000016185.1:WP_012568196.1
MTPASPLSDDQIERYARHIMLKEVGGRGQERLLASSVLVVGAGGLGSPLLLYLAAAGVGR
IGVIDHDSVDLSNLQRQVIHDGASVGRPKVESAAARIAALTPDVRVEAHAERLTPANVLG
LVSRYDVVADGSDNFATRFLLNDACFFAGKTLVSAAMLRFDAQLSVFKAHLGEPHPCYRC
IFREPPPPGTIPSCSEGGVLGALPGAMGSLQAIEVLKELLGIGESLSGRLLLVAALETSF
RTVRVRRDPGCPLCGGDPVYRDLSHHLPPQGQAAHG

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