SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012759670.1 NCBI__GCF_000023185.1:WP_012759670.1 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)

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, 93% coverage: 14:267/274 of query aligns to 57:303/453 of Q9VLJ8

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T62 (≠ E19) modified: Phosphothreonine

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: 20:267/274 of query aligns to 60:312/482 of O59954

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O59954

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G82 (= G42) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
G100 (= G60) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
R130 (= R90) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
C185 (≠ G145) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
E215 (≠ D175) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
G264 (= G223) mutation to S: In cnxF142ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.

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)
48% identity, 89% coverage: 22:265/274 of query aligns to 4:245/271 of Q72J02

query
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Q72J02

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C192 (= C212) modified: Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in TtuB); mutation to S: Not able to form a thioester complex with TtuB.

Sites not aligning to the query:

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

P38820 Adenylyltransferase and sulfurtransferase UBA4; Needs CLA4 to survive protein 3; Ubiquitin-like protein activator 4; EC 2.7.7.-; EC 2.8.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 4 papers)
41% identity, 93% coverage: 20:273/274 of query aligns to 38:286/440 of P38820

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P38820

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C225 (= C212) 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.

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)
48% identity, 89% coverage: 21:264/274 of query aligns to 5:240/270 of D4GSF3

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D4GSF3

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E

T

A

T

G

G

I

V

I

L

G

G

A

V

L

L

T

P

G

G

V

T

I

V

G

G

T

C

M

I

M

Q

A

A

M

T

E

E

A

A

I

M

K

K

L

L

V

L

T

L

G

D

T

E

G

G

E

E

P

A

L

L

V

D

G

G

R

R

L

L

L

F

Y

Y

D

D

A

A

L

M

S

D

A

M

R

T

F

F

D

E

T

T

I

V

R

P

Y

Y

K

R

C188 (= C212) 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.

P12282 Molybdopterin-synthase adenylyltransferase; MoaD protein adenylase; Molybdopterin-converting factor subunit 1 adenylase; Sulfur carrier protein MoaD adenylyltransferase; EC 2.7.7.80 from Escherichia coli (strain K12) (see 2 papers)
40% identity, 91% coverage: 18:266/274 of query aligns to 1:241/249 of P12282

query
sites
P12282

M

M

E

A

P

E

L

L

S

S

P

D

E

Q

E

E

I

M

A

L

R

R

Y

Y

H

N

R
|
R

H

Q

I

I

L

I

L

L

P

R

E

G

I

F

G

D

G

F

A

D

G

G

Q

Q

Q

E

K

A

L

L

K

K

A

D

A

S

R

R

V

V

L

L

V

I

I

V

G

G

A

L

G

G

L

L

G

G

A
x
C

P

A

V

A

L

S

Q

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

T

N

L

L

G

T

I

L

V

L

D

D

D

F

D

D

R

T

V

V

S

S

L

L

S

S

N

N

L

L

Q

Q

R
|
R

Q

Q

V

T

I

L

H

H

D

S

S

D

G

A

T

T

I

V

G

G

E

Q

L

P

K

K

T

V

E

E

S

S

A

A

A

R

F

D

A

A

I

L

A

T

R

R

L

I

N

N

P

P

H

H

V

I

R

A

L

I

I

T

R

P

F

V

E

N

E

A

R

L

F

L

S

D

P

D

E

A

A

E

G

L

R

A

Q

L

L

I

S

A

G

E

F

H

D

D

L

L

L

V

I

L

D

D

G
x
C

S

T

D
|
D

N

N

F

V

D

A

T

V

R

R

Y

N

A

Q

A

L

A

N

D

A

A

G

A
x
C

D

F

E

A

G

A

R

K

I

V

P

P

L

L

V

V

T

S

G

G

A

A

V

A

G

I

R

R

F

M

D

E

G

G

S

Q

L

I

T

T

V

V

L

F

K

-

P

-

Y

-

E

-

T

T

A

Y

E

Q

D

D

G

G

T

E

P

P

N
x
C

P

Y

R

R

Y
x
C

R

L

D

S

-

R

L

L

F

F

P

G

E

E

A

N

P

A

P

-

A

-

G

-

L

-

I

-

P

L

A

T

C
|
C

A

V

E

E

A

A

G

G

I

V

I

M

G

A

A

P

L

L

T

I

G

G

V

V

I

I

G

G

T

S

M

L

M

Q

A

A

M

M

E

E

A

A

I

I

K

K

L

M

V

L

T

A

G

G

T

Y

G

G

E

K

P

P

L

A

V

S

G

G

R

K

L

I

L

V

L

M

Y

Y

D

D

A

A

L

M

S

T

A
x
C

R

Q

F

F

D

R

T

E

I

M

R

K

Y

L

K

M

R

R

R

N

R14 (= R31) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
C44 (≠ A61) mutation to A: No effect.
R73 (= R90) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
C128 (≠ G145) mutation to A: No effect.; mutation to Y: No activity.
D130 (= D147) mutation to A: No activity.; mutation to E: Substantially reduced activity.
C142 (≠ A159) mutation to A: No effect.
C172 (≠ N193) mutation to A: No zinc bound and no enzyme activity.
C175 (≠ Y196) mutation to A: No zinc bound and no enzyme activity.
C187 (= C212) mutation to A: No effect.
C231 (≠ A256) mutation to A: No effect.

Sites not aligning to the query:

244 C→A: No zinc bound and almost no enzyme activity.
247 C→A: No zinc bound and almost no enzyme activity.

O95396 Adenylyltransferase and sulfurtransferase MOCS3; Molybdenum cofactor synthesis protein 3; Molybdopterin synthase sulfurylase; MPT synthase sulfurylase; EC 2.7.7.80; EC 2.8.1.11 from Homo sapiens (Human) (see 5 papers)
44% identity, 87% coverage: 21:258/274 of query aligns to 55:285/460 of O95396

query
sites
O95396

L

L

S

S

P

R

E

D

E

E

I

I

A

L

R

R

Y

Y

H

S

R

R

H

Q

I

L

L

V

L

L

P

P

E

E

I

L

G

G

G

V

A

H

G

G

Q

Q

Q

L

K

R

L

L

K

G

A

T

A

A

R

C

V

V

L

L

V

I

I

V

G

G

A

C

G

G

L

L

G

G

A

C

P

P

V

L

L

A

Q

Q

Y

Y

L

L

A

A

G

G

V

V

G

G

T

R

L

L

G

G

I

L

V

V

D

D

D

Y

D

D

R

V

V

V

S

E

L

M

S

S

N

N

L

L

Q

A

R

R

Q

Q

V

V

I

L

H

H

D

G

S

E

G

A

T

L

I

A

G

G

E

Q

L

A

K

K

T

A

E

F

S

S

A

A

F

A

A

S

I

L

A

R

R

R

L

L

N

N

P

S

H

A

V

V

R

E

L

C

I

V

R

P

F

Y

E
x
T

E
x
Q

R
x
A

F
x
L

S
x
T

P
|
P

E
x
A

A
x
T

G
x
A

R
x
L

R
x
D

Q
x
L

L
x
V

S
x
R

G
x
R

F
x
Y

D
|
D

L
x
V

I
x
A

D
|
D

G
x
C

S
|
S

D
|
D

N
|
N

F
x
V

D
x
P

T
|
T

R
|
R

Y
|
Y

A
x
L

A
x
V

A
x
N

D
|
D

A
|
A

A
x
C

D
x
V

E
x
L

G
x
A

R
x
G

I
x
R

P
|
P

L
|
L

V
|
V

T
x
S

G
x
A

A
x
S

V
x
A

G
x
L

R
|
R

F
|
F

D
x
E

G
|
G

S
x
Q

L
x
I

T
|
T

V
|
V

L
x
Y

K
x
H

P

-

Y

-

E

-

T

-

A

-

E
x
Y

D
|
D

G
|
G

T

-

P

-

N
x
G

P
|
P

R
x
C

Y
|
Y

R
|
R

D
x
C

L
x
I

F
|
F

P
|
P

E
x
Q

A
x
P

P
|
P

A
|
A

G
x
E

L
x
T

I
x
V

P
x
T

A
x
N

C
|
C

A

A

E

D

A

G

G

G

I

V

I

L

G

G

A

V

L

V

T

T

G

G

V

V

I

L

G

G

T

C

M

L

M

Q

A

A

M

L

E

E

A

V

I

L

K

K

L

I

V

A

T

A

G

G

T

L

G

G

E

P

P

S

L

Y

V

S

G

G

R

S

L

L

Y

F

D

D

A

A

L

L

S

R

A

G

R

H

F

F

158:238 (vs. 124:211, 33% identical) Interaction with NFS1
C239 (= C212) mutation to A: Impairs sulfurtransferase activity.

Sites not aligning to the query:

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

1jwbB Structure of the covalent acyl-adenylate form of the moeb-moad protein complex (see paper)
39% identity, 90% coverage: 21:266/274 of query aligns to 3:233/240 of 1jwbB

query
sites
1jwbB

L

L

S

S

P

D

E

Q

E

E

I

M

A

L

R

R

Y

Y

H

N

R
|
R

H

Q

I

I

L

I

L

L

P

R

E

G

I

F

G

D

G

F

A

D

G

G

Q

Q

Q

E

K

A

L

L

K

K

A

D

A

S

R

R

V

V

L

L

V

I

I

V

G
|
G

A

L

G
|
G

L

L

G

G

A

C

P

A

V

A

L

S

Q

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

T

N

L

L

G

T

I

L

V

L

D
|
D

D
x
F

D

D

R

T

V

V

S

S

L

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

V

T

I

L

H

H

D

S

S

D

G

A

T

T

I

V

G

G

E

Q

L

P

K
|
K

T

V

E

E

S

S

A

A

A

R

F

D

A

A

I

L

A

T

R

R

L

I

N

N

P

P

H

H

V

I

R

A

L

I

I

T

R

P

F

V

E

N

E

A

R
x
L

F

L

S

D

P

D

E

A

A

E

G

L

R

A

Q

L

L

I

S

A

G

E

F

H

D

D

L

L

L

V

I

L

D

D

G
x
C

S
x
T

D
|
D

N
|
N

F

V

D

A

T
x
V

R

R

Y

N

A

Q

A

L

A

N

D

A

A

G

A

C

D

F

E

A

G

A

R

K

I

V

P

P

L

L

V

V

T

S

G

G

A

A

V

A

G

I

R

R

F

M

D

E

G

G

S

Q

L

I

T

T

V

V

L

F

K

-

P

-

Y

-

E

-

T

T

A

Y

E

Q

D

D

G

G

T

E

P

P

N
x
C

P

Y

R

R

Y

C

R

L

D

S

-

R

L

L

F

F

P

-

E

-

A

-

P

-

A

-

G

-

L

-

I

-

P

-

A

-

C

-

A

G

E

E

A

A

G

G

I

V

I

M

G

A

A

P

L

L

T

I

G

G

V

V

I

I

G

G

T

S

M

L

M

Q

A

A

M

M

E

E

A

A

I

I

K

K

L

M

V

L

T

A

G

G

T

Y

G

G

E

K

P

P

L

A

V

S

G

G

R

K

L

I

L

V

L

M

Y

Y

D

D

A

A

L

M

S

T

A

C

R

Q

F

F

D

R

T

E

I

M

R

K

Y

L

K

M

R

R

R

N

active site: R13 (= R31), D129 (= D147)
binding adenosine monophosphate: G37 (= G55), G39 (= G57), G40 (= G58), D61 (= D79), F62 (≠ D80), K85 (= K103), L108 (≠ R126), C127 (≠ G145), T128 (≠ S146), D129 (= D147), N130 (= N148), V133 (≠ T151)
binding zinc ion: C171 (≠ N193)

Sites not aligning to the query:

binding zinc ion: 236, 239

1jw9B Structure of the native moeb-moad protein complex (see paper)
39% identity, 90% coverage: 21:266/274 of query aligns to 3:233/240 of 1jw9B

query
sites
1jw9B

L

L

S

S

P

D

E

Q

E

E

I

M

A

L

R

R

Y

Y

H

N

R
|
R

H

Q

I

I

L

I

L

L

P

R

E

G

I

F

G

D

G

F

A

D

G

G

Q

Q

Q

E

K

A

L

L

K

K

A

D

A

S

R

R

V

V

L

L

V

I

I

V

G

G

A

L

G

G

L

L

G

G

A

C

P

A

V

A

L

S

Q

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

T

N

L

L

G

T

I

L

V

L

D

D

D

F

D

D

R

T

V

V

S

S

L

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

V

T

I

L

H

H

D

S

S

D

G

A

T

T

I

V

G

G

E

Q

L

P

K

K

T

V

E

E

S

S

A

A

A

R

F

D

A

A

I

L

A

T

R

R

L

I

N

N

P

P

H

H

V

I

R

A

L

I

I

T

R

P

F

V

E

N

E

A

R

L

F

L

S

D

P

D

E

A

A

E

G

L

R

A

Q

L

L

I

S

A

G

E

F

H

D

D

L

L

L

V

I

L

D

D

G

C

S

T

D
|
D

N

N

F

V

D

A

T

V

R

R

Y

N

A

Q

A

L

A

N

D

A

A

G

A

C

D

F

E

A

G

A

R

K

I

V

P

P

L

L

V

V

T

S

G

G

A

A

V

A

G

I

R

R

F

M

D

E

G

G

S

Q

L

I

T

T

V

V

L

F

K

-

P

-

Y

-

E

-

T

T

A

Y

E

Q

D

D

G

G

T

E

P

P

N
x
C

P

Y

R

R

Y

C

R

L

D

S

-

R

L

L

F

F

P

-

E

-

A

-

P

-

A

-

G

-

L

-

I

-

P

-

A

-

C

-

A

G

E

E

A

A

G

G

I

V

I

M

G

A

A

P

L

L

T

I

G

G

V

V

I

I

G

G

T

S

M

L

M

Q

A

A

M

M

E

E

A

A

I

I

K

K

L

M

V

L

T

A

G

G

T

Y

G

G

E

K

P

P

L

A

V

S

G

G

R

K

L

I

L

V

L

M

Y

Y

D

D

A

A

L

M

S

T

A

C

R

Q

F

F

D

R

T

E

I

M

R

K

Y

L

K

M

R

R

R

N

active site: R13 (= R31), D129 (= D147)
binding zinc ion: C171 (≠ N193)

Sites not aligning to the query:

binding zinc ion: 236, 239

1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
37% identity, 89% coverage: 21:265/274 of query aligns to 3:217/217 of 1jwaB

query
sites
1jwaB

L

L

S

S

P

D

E

Q

E

E

I

M

A

L

R

R

Y

Y

H

N

R
|
R

H

Q

I

I

L

I

L

L

P

R

E

G

I

F

G

D

G

F

A

D

G

G

Q

Q

Q

E

K

A

L

L

K

K

A

D

A

S

R

R

V

V

L

L

V

I

I

V

G

G

A

L

G
|
G

L

L

G

G

A

C

P

A

V

A

L

S

Q

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

T

N

L

L

G

T

I

L

V

L

D
|
D

D
x
F

D

D

R

T

V

V

S

S

L

L

S

S

N

N

L

L

Q

Q

R
|
R

Q

Q

V

T

I

L

H

H

D

S

S

D

G

A

T

T

I

V

G

G

E

Q

L

P

K
|
K

T

V

E

E

S

S

A

A

A

R

F

D

A

A

I

L

A

T

R

R

L

I

N

N

P

P

H

H

V

I

R

A

L

I

I

T

R

P

F

V

E

N

E

A

R
x
L

F

L

S

D

P

D

E

A

A

E

G

L

R

A

Q

L

L

I

S

A

G

E

F

H

D

D

L

L

L

V

I

L

D

D

G

C

S

T

D
|
D

N
|
N

F

V

D

A

T
x
V

R

R

Y

N

A

Q

A

L

A

N

D

A

A

G

A

C

D

F

E

A

G

A

R

K

I

V

P

P

L

L

V

V

T

S

G

G

A

A

V

A

G

I

R

R

F

M

D

E

G

G

S

Q

L

I

T

T

V

V

L

F

K

T

P

-

Y

-

E

-

T

-

A

-

E

-

D

-

G

-

T

-

P

-

N

-

P

-

R

-

Y

-

R

-

D

-

L

-

F

-

P

-

E

-

A

-

P

-

A

-

G

-

L

-

I

-

P

-

A

-

C

-

A

Y

E

E

A

A

G

G

I

V

I

M

G

A

A

P

L

L

T

I

G

G

V

V

I

I

G

G

T

S

M

L

M

Q

A

A

M

M

E

E

A

A

I

I

K

K

L

M

V

L

T

A

G

G

T

Y

G

G

E

K

P

P

L

A

V

S

G

G

R

K

L

I

L

V

L

M

Y

Y

D

D

A

A

L

M

S

T

A

C

R

Q

F

F

D

R

T

E

I

M

R

K

Y

L

K

M

R

R

active site: R13 (= R31), D129 (= D147)
binding adenosine-5'-triphosphate: G39 (= G57), G40 (= G58), D61 (= D79), F62 (≠ D80), R72 (= R90), K85 (= K103), L108 (≠ R126), D129 (= D147), N130 (= N148), V133 (≠ T151)

6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
38% identity, 80% coverage: 21:238/274 of query aligns to 7:213/289 of 6yubB

query
sites
6yubB

L

L

S

S

P

K

E

E

I

I

A

E

R

R

Y

Y

H

S

R

R

H

Q

I

M

L

I

L

V

P

P

E

G

I

M

G

G

G

K

A

E

G

G

Q

Q

Q

L

K

R

L

L

K

M

A

N

A

A

R

K

V

V

L

L

V

I

I

I

G

G

A

A

G

G

L

L

G

G

A

C

P

P

V

A

L

A

Q

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

T

T

L

I

G

G

I

I

V

V

D

D

D

G

D

D

R

S

V

V

S

E

L

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

V

V

I

A

H

H

D

A

S

T

G

K

T

R

I

V

G

G

E

M

L

L

K

K

T

V

E

D

S

S

A

L

A

I

F

T

A

H

I

L

A

I

R

E

L

I

N

N

P

P

H

L

V

P

R

V

L

Y

I

V

R

P

F

Y

E

R

E

F

R

D

F

L

S

T

P

P

E

Q

A

N

G

A

R

A

R

Q

Q

I

L

I

S

K

G

P

F

W

D

D

L

V

L

I

I

L

D

D

G

C

S

T

D

D

N

N

F

P

D

A

T

T

R

R

Y

Y

A

L

A

I

A

S

D

D

A

V

A

C

D

V

E

L

G

L

R

G

I

K

P

P

L

L

V

V

T

S

G

A

A

A

V

S

G

V

R

Q

F

K

D

S

G

G

S

Q

L

L

T

I

V

V

L

L

K

N

P

C

Y

P

E

P

T

T

A

P

E

Q

-

G

-

V

D

N

G

K

T

K

P

A

N

A

P

P

R
x
C

Y

Y

R

R

D

-

L

-

F

-

P

-

E

-

A

-

P

-

A

-

G

-

L

-

I

-

P

-

A

-

C
|
C

A

C

E

F

A

K

G

G

I

I

I

M

G

G

A

P

L

V

T

V

G

G

V

M

I

M

G

G

T

V

M

A

M

Q

A

A

M

G

E

E

A

A

I

I

K

K

L

I

V

L

T

V

binding zinc ion: C184 (≠ R195), C187 (= C212)

Sites not aligning to the query:

binding zinc ion: 265

6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
38% identity, 80% coverage: 21:238/274 of query aligns to 6:214/423 of 6yubA

query
sites
6yubA

L

L

S

S

P

K

E

E

I

I

A

E

R

R

Y

Y

H

S

R

R

H

Q

I

M

L

I

L

V

P

P

E

G

I

M

G

G

G

K

A

E

G

G

Q

Q

Q

L

K

R

L

L

K

M

A

N

A

A

R

K

V

V

L

L

V

I

I

I

G

G

A

A

G

G

L

L

G

G

A

C

P

P

V

A

L

A

Q

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

T

T

L

I

G

G

I

I

V

V

D

D

D

G

D

D

R

S

V

V

S

E

L

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

V

V

I

A

H

H

D

A

S

T

G

K

T

R

I

V

G

G

E

M

L

L

K

K

T

V

E

D

S

S

A

L

A

I

F

T

A

H

I

L

A

I

R

E

L

I

N

N

P

P

H

L

V

P

R

V

L

Y

I

V

R

P

F

Y

E

R

E

F

R

D

F

L

S

T

P

P

E

Q

A

N

G

A

R

A

R

Q

Q

I

L

I

S

K

G

P

F

W

D

D

L

V

L

I

I

L

D

D

G

C

S

T

D

D

N

N

F

P

D

A

T

T

R

R

Y

Y

A

L

A

I

A

S

D

D

A

V

A

C

D

V

E

L

G

L

R

G

I

K

P

P

L

L

V

V

T

S

G

A

A

A

V

S

G

V

R

Q

F

K

D

S

G

G

S

Q

L

L

T

I

V

V

L

L

K

N

P

C

Y

P

E

P

T

T

A

P

E

Q

-

G

-

V

D

N

G

K

T

K

P

A

N

A

P

P

R
x
C

Y

Y

R

R

D
x
C

L

C

F

F

P

-

E

-

A

-

P

-

A

-

G

-

L

-

I

-

P

-

A

-

C

-

A

K

E

K

A

P

G

G

I

I

I

M

G

G

A

P

L

V

T

V

G

G

V

M

I

M

G

G

T

V

M

A

M

Q

A

A

M

G

E

E

A

A

I

I

K

K

L

I

V

L

T

V

binding zinc ion: C183 (≠ R195), C186 (≠ D198)

Sites not aligning to the query:

binding zinc ion: 266, 269

1zfnA Structural analysis of escherichia coli thif (see paper)
38% identity, 89% coverage: 21:265/274 of query aligns to 1:236/244 of 1zfnA

query
sites
1zfnA

L

M

S

N

P

D

E

R

E

D

I

F

A

M

R

R

Y

Y

H

S

R
|
R

H

Q

I

I

L

L

P

D

E

D

I

I

G

A

G

L

A

D

G

G

Q

Q

K

K

L

L

K

L

A

D

A

S

R

Q

V

V

L

L

V

I

I
|
I

G
|
G

A

L

G
|
G

L

L

G

G

A

T

P

P

V

A

L

A

Q

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

T

T

L

L

G

V

I

L

V

A

D
|
D

D

D

R

D

V

V

S

H

L

L

S

S

N

N

L

L

Q

Q

R
|
R

Q
|
Q

V

I

I

L

H

F

D

T

S

T

G

E

T

D

I

I

G

D

E

R

L

P

K
|
K

T

S

E

Q

S

V

A

S

A

Q

F

Q

A

R

I

L

A

T

R

Q

L

L

N

N

P

P

H

D

V

I

R

Q

L

L

I

T

R

A

F

L

E

Q

R

R

F

L

S

T

P

G

E

E

A

A

G

L

R

K

R

D

Q

A

L

V

S

A

G

R

F

A

D

D

L

V

I

L

D

D

G

C

S
x
T

D
|
D

N

N

F

M

D

A

T
|
T

R

R

Y

Q

A

E

A

I

A

N

D

A

A

A

A

C

D

V

E

A

G

L

R

N

I

T

P

P

L

L

V

I

T

T

G

A

A

S

V

A

G

V

R

G

F

F

D

G

G

G

S

Q

L

L

T

M

V

V

L

L

K

T

P

P

Y

-

E

-

T

P

A

W

E

E

D

Q

G

G

T
x
C

P

-

N

-

P

-

R

-

Y

Y

R

R

D
x
C

L

L

F

W

P

P

E

D

A

N

P

Q

P

E

A

P

G

E

L

-

I

-

P

R

A

N

C

C

A

R

E

T

A

A

G

G

I

V

G

G

A

P

L

V

T

V

G

G

V

V

I

M

G

G

T

T

M

L

M

Q

A

A

M

L

E

E

A

A

I

I

K

K

L

L

V

L

T

S

G

G

T

I

G

E

E

T

P

P

L

-

V

A

G

G

R

E

L

L

L

R

L

L

Y

F

D

D

A

G

L

K

S

S

A

S

R

Q

F

W

D

R

T

S

I

L

R

A

Y

L

K

R

R

R

active site: R11 (= R31), D127 (= D147)
binding adenosine-5'-triphosphate: I34 (= I54), G35 (= G55), G37 (= G57), G38 (= G58), D59 (= D79), R70 (= R90), Q71 (= Q91), K83 (= K103), T126 (≠ S146), D127 (= D147), T131 (= T151)
binding zinc ion: C169 (≠ T191), C172 (≠ D198)

Sites not aligning to the query:

binding zinc ion: 240, 243

P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
38% identity, 89% coverage: 21:265/274 of query aligns to 1:236/251 of P30138

query
sites
P30138

L

M

S

N

P

D

E

R

E

D

I

F

A

M

R

R

Y

Y

H

S

R

R

H

Q

I

I

L

L

P

D

E

D

I

I

G

A

G

L

A

D

G

G

Q

Q

K

K

L

L

K

L

A

D

A

S

R

Q

V

V

L

L

V

I

I

I

G

G

A

L

G

G

L

L

G

G

A

T

P

P

V

A

L

A

Q

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

T

T

L

L

G

V

I

L

V

A

D

D

R

D

V

V

S

H

L

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

V

I

I

L

H

F

D

T

S

T

G

E

T

D

I

I

G

D

E

R

L

P

K

K

T

S

E

Q

S

V

A

S

A

Q

F

Q

A

R

I

L

A

T

R

Q

L

L

N

N

P

P

H

D

V

I

R

Q

L

L

I

T

R

A

F

L

E

Q

R

R

F

L

S

T

P

G

E

E

A

A

G

L

R

K

R

D

Q

A

L

V

S

A

G

R

F

A

D

D

L

V

I

L

D

D

G

C

S

T

D

D

N

N

F

M

D

A

T

T

R

R

Y

Q

A

E

A

I

A

N

D

A

A

A

A

C

D

V

E

A

G

L

R

N

I

T

P

P

L

L

V

I

T

T

G

A

A

S

V

A

G

V

R

G

F

F

D

G

G

G

S

Q

L

L

T

M

V

V

L

L

K

T

P

P

Y

-

E

-

T

P

A

W

E

E

D

Q

G

G

T
x
C

P

-

N

-

P

-

R

-

Y

Y

R

R

D
x
C

L

L

F
x
W

P

P

-

D

-

N

E

Q

A

E

P

P

P

E

A

R

G

N

L

-

I

-

P

-

A

-

C
|
C

A

R

E

T

A

A

G

G

I

V

G

G

A

P

L

V

T

V

G

G

V

V

I

M

G

G

T

T

M

L

M

Q

A

A

M

L

E

E

A

A

I

I

K

K

L

L

V

L

T

S

G

G

T

I

G

E

E

T

P

P

L

-

V

A

G

G

R

E

L

L

L

R

L

L

Y

F

D

D

A

G

L

K

S

S

A

S

R

Q

F

W

D

R

T

S

I

L

R

A

Y

L

K

R

R

R

C169 (≠ T191) binding Zn(2+)
C172 (≠ D198) binding Zn(2+)
W174 (≠ F200) mutation to A: No adenylation of ThiS.
C184 (= C212) mutation to S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth.

Sites not aligning to the query:

240 binding Zn(2+)
243 binding Zn(2+)

1zud3 Structure of this-thif protein complex (see paper)
38% identity, 89% coverage: 21:265/274 of query aligns to 1:231/240 of 1zud3

query
sites
1zud3

L

M

S

N

P

D

E

R

E

D

I

F

A

M

R

R

Y

Y

H

S

R
|
R

H

Q

I

I

L
|
L

L

L

P
x
D

E

D

I

I

G

A

G

L

A

D

G

G

Q

Q

K

K

L

L

K

L

A

D

A

S

R

Q

V

V

L

L

V

I

I

I

G

G

A

L

G

G

L

L

G

G

A

T

P

P

V

A

L

A

Q

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

T

T

L

L

G

V

I

L

V

A

D

D

R

D

V

V

S

H

L

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

V

I

I

L

H

F

D

T

S

T

G

E

T

D

I

I

G

D

E

R

L

P

K

K

T

S

E

Q

S

V

A

S

A

Q

F

Q

A

R

I

L

A

T

R

Q

L

L

N

N

P

P

H

D

V

I

R

Q

L

L

I

T

R

A

F

L

E

Q

R

R

F

L

S

T

P

G

E

E

A

A

G

L

R

K

R

D

Q

A

L

V

S

A

G

R

F

A

D

D

L

V

I

L

D

D

G

C

S

T

D
|
D

N

N

F

M

D

A

T

T

R

R

Y

Q

A

E

A

I

A

N

D

A

A

A

A

C

D

V

E

A

G

L

R

N

I

T

P

P

L

L

V

I

T

T

G

A

A

S

V

A

G

V

R

G

F

F

D

G

G

G

S

Q

L

L

T

M

V

V

L

L

K

T

P

P

Y

-

E

-

T

P

A

W

E

E

D

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G

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x
C

P

-

N

-

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-

R

-

Y

Y

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M

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M

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A

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active site: R11 (= R31), D127 (= D147)
binding calcium ion: L14 (= L34), D16 (≠ P36)
binding zinc ion: C169 (≠ T191)

Sites not aligning to the query:

binding zinc ion: 235, 238

O42939 Ubiquitin-activating enzyme E1-like; Pmt3-activating enzyme subunit 2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 62% coverage: 44:213/274 of query aligns to 21:182/628 of O42939

query
sites
O42939

Q

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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)
27% identity, 57% coverage: 46:201/274 of query aligns to 16:172/650 of Q7SXG4

query
sites
Q7SXG4

L

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Sites not aligning to the query:

599 modified: Phosphoserine

P22314 Ubiquitin-like modifier-activating enzyme 1; Protein A1S9; Ubiquitin-activating enzyme E1; EC 6.2.1.45 from Homo sapiens (Human) (see 2 papers)
27% identity, 62% coverage: 43:212/274 of query aligns to 463:632/1058 of P22314

query
sites
P22314

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Sites not aligning to the query:

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

8ideA Structure of an ancient tsad-tsac-sua5-tcda modular enzyme (tsan) (see paper)
32% identity, 54% coverage: 21:168/274 of query aligns to 678:822/929 of 8ideA

query
sites
8ideA

L

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N

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Sites not aligning to the query:

binding manganese (ii) ion: 109, 113, 304

6dc6C Crystal structure of human ubiquitin activating enzyme e1 (uba1) in complex with ubiquitin (see paper)
29% identity, 53% coverage: 43:186/274 of query aligns to 415:567/996 of 6dc6C

query
sites
6dc6C

Q

Q

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D

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active site: R467 (= R90), D528 (= D147)
binding magnesium ion: D458 (= D81), E461 (≠ S84)
binding pyrophosphate 2-: N464 (= N87), K480 (= K103)

Sites not aligning to the query:

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

Query Sequence

>WP_012759670.1 NCBI__GCF_000023185.1:WP_012759670.1
MTEAAFPGVGRHDNIGAMEPLSPEEIARYHRHILLPEIGGAGQQKLKAARVLVIGAGGLG
APVLQYLAAAGVGTLGIVDDDRVSLSNLQRQVIHDSGTIGELKTESAAFAIARLNPHVRL
IRFEERFSPEAGRRQLSGFDLLIDGSDNFDTRYAAADAADEGRIPLVTGAVGRFDGSLTV
LKPYETAEDGTPNPRYRDLFPEAPPAGLIPACAEAGIIGALTGVIGTMMAMEAIKLVTGT
GEPLVGRLLLYDALSARFDTIRYKRRRTTQRQAG

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