SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012051051.1 NCBI__GCF_000016765.1:WP_012051051.1 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)
47% identity, 100% coverage: 1:249/249 of query aligns to 1:253/271 of Q72J02

query
sites
Q72J02

M

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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.

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, 100% coverage: 1:249/249 of query aligns to 3:249/270 of D4GSF3

query
sites
D4GSF3

M

L

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S

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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.

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)
39% identity, 100% coverage: 2:249/249 of query aligns to 3:248/249 of P12282

query
sites
P12282

S

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R14 (= R13) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
C44 (≠ S43) mutation to A: No effect.
R73 (= R72) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
C128 (≠ G127) mutation to A: No effect.; mutation to Y: No activity.
D130 (= D129) mutation to A: No activity.; mutation to E: Substantially reduced activity.
C142 (≠ A141) mutation to A: No effect.
C172 (= C172) mutation to A: No zinc bound and no enzyme activity.
C175 (= C175) mutation to A: No zinc bound and no enzyme activity.
C187 (= C188) mutation to A: No effect.
C231 (≠ F232) mutation to A: No effect.
C244 (= C245) mutation to A: No zinc bound and almost no enzyme activity.
C247 (≠ A248) 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)
39% identity, 100% coverage: 2:249/249 of query aligns to 2:240/240 of 1jwbB

query
sites
1jwbB

S

E

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L

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Y

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C

Y

Y

R

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C

L

L

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active site: R13 (= R13), D129 (= D129)
binding adenosine monophosphate: G37 (= G37), G39 (= G39), G40 (= G40), D61 (= D61), F62 (≠ D62), K85 (= K85), L108 (≠ R108), C127 (≠ G127), T128 (≠ C128), D129 (= D129), N130 (= N130), V133 (≠ T133)
binding zinc ion: C171 (= C172), C236 (= C245), C239 (≠ A248)

1jw9B Structure of the native moeb-moad protein complex (see paper)
39% identity, 100% coverage: 2:249/249 of query aligns to 2:240/240 of 1jw9B

query
sites
1jw9B

S

E

L

L

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S

D

D

E

Q

Q

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L

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R

Y

Y

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K

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Q

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Y

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L

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A

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L

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S

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N

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K

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D

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D

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C
|
C

Y

Y

R

R

C

C

L

L

V

-

G

-

D

-

P

-

D

-

R

-

P

-

D

S

I

R

S

L

C

F

A

G

D

E

Q

A

G

G

V

V

L

M

G

A

A

P

L

L

T

I

G

G

V

V

M

I

G

G

S

S

L

L

G

Q

A

A

M

M

E

E

A

A

V

I

R

K

A

M

I

L

T

A

G

G

F

Y

G

G

D

K

D

P

P

A

A

S

G

G

R

K

L

I

L

V

L

M

V

Y

D

D

A

A

L

M

A

T

F

C

R

Q

F

F

R

R

T

E

I

M

A

K

V

L

P

M

K

R

D

N

P

P

G

G

C
|
C

R

E

C

V

A
x
C

G

G

active site: R13 (= R13), D129 (= D129)
binding zinc ion: C171 (= C172), C236 (= C245), C239 (≠ A248)

Q9VLJ8 Adenylyltransferase and sulfurtransferase MOCS3; Molybdenum cofactor synthesis protein 3; Ubiquitin activating enzyme 4; EC 2.7.7.80; EC 2.8.1.11 from Drosophila melanogaster (Fruit fly) (see paper)
41% identity, 98% coverage: 2:246/249 of query aligns to 63:307/453 of Q9VLJ8

query
sites
Q9VLJ8

S

K

L

L

T

T

D

N

E

D

Q

D

L

I

D

A

R

R

Y

Y

A

S

R

R

H

Q

I

L

I

I

L

L

K

P

E

D

I

F

G

G

G

V

A

Q

G

G

Q

Q

Q

L

A

K

L

L

L

K

K

N

A

S

T

S

V

V

A

L

V

I

I

V

G

G

A

L

G

G

I

L

G

G

S

C

P

P

A

A

I

A

Q

Q

Y

Y

L

L

A

A

G

G

I

C

G

G

L

H

L

L

R

G

V

L

I

V

D

D

D

Y

D

D

V

E

V

V

D

E

L

R

S

S

N

N

L

F

Q

H

R

R

Q

Q

T

I

L

L

F

H

G

S

T

E

A

D

D

R

I

C

G

G

C

M

P

S

K

K

A

A

E

E

V

S

A

A

A

R

A

I

R

A

V

L

A

L

A

E

M

L

N

N

P

P

D

H

V

C

L

E

V

I

E

Q

P

C

V

H

T

S

V

R

R

M

I

L

D

Y

A

P

D

H

T

N

A

A

D

M

D

H

L

I

E

R

G

G

A

Y

D

D

L

V

V

V

L

L

D

D

G

C

C

T

D

D

N

N

F

V

A

P

T

T

R

R

L

Y

A

L

V

L

S

S

D

D

A

A

A

C

T

V

R

M

L

L

G

S

I

K

P

P

L

L

V

V

S

S

A

G

A

S

V

A

G

L

Q

K

F

M

D

D

G

G

Q

Q

L

L

G

T

V

V

W

Y

R

N

G

-

W

-

E

Y

A

A

D

N

K

G

P

P

C

C

Y

Y

R

R

C

C

L

I

V

F

G

P

D

V

D

P

P

P

D

P

R

P

P

E

D

A

I

V

S

T

-

N

C

C

A

G

D

D

Q

G

G

G

V

V

L

L

G

G

A

A

L

V

T

T

G

G

V

T

M

I

G

G

S

A

L

M

G

Q

A

A

M

L

E

E

A

A

V

I

R

K

A

V

I

I

T

V

G

G

F

M

G

G

D

D

D

V

P

L

A

A

G

G

R

R

L

L

L

I

V

F

D

D

A

G

L

G

A

S

F

G

R

V

F

F

R

R

T

N

I

I

A

R

V

I

-

R

P

S

K

K

D

R

P

P

G

N

C

C

R

H

Sites not aligning to the query:

62 modified: Phosphothreonine

1zfnA Structural analysis of escherichia coli thif (see paper)
42% identity, 99% coverage: 3:249/249 of query aligns to 1:244/244 of 1zfnA

query
sites
1zfnA

L

M

T

N

D

D

E

R

Q

D

L

F

D

M

R

R

Y

Y

A

S

R
|
R

H

Q

I

I

I

L

L

L

K

D

E

D

I

I

G

A

G

L

A

D

G

G

Q

Q

A

K

L

L

K

D

A

S

T

Q

V

V

A

L

V

I

I
|
I

G
|
G

A

L

G
|
G

I

L

G

G

S

T

P

P

A

A

I

A

Q

L

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

L

T

L

L

R

V

V

L

I

A

D
|
D

D

D

V

D

V

V

D

H

L

L

S

S

N

N

L

L

Q

Q

R
|
R

Q
|
Q

T

I

L

L

F

F

G

T

T

T

A

E

D

D

I

I

G

D

C

R

P

P

K
|
K

A

S

E

Q

V

V

A

S

A

Q

R

R

V

L

A

T

A

Q

M

L

N

N

P

P

D

D

V

I

L

Q

V

L

E

T

P

A

V

L

T

Q

V

Q

R

R

I

L

D

T

A

G

D

E

T

A

A

L

D

K

D

D

L

A

L

V

E

A

G

R

A

A

D

D

L

V

V

V

L

L

D

D

G

C

C
x
T

D
|
D

N

N

F

M

A

A

T
|
T

R

R

L

Q

A

E

V

I

S

N

D

A

A

A

A

C

T

V

R

A

L

L

G

N

I

T

P

P

L

L

V

I

S

T

A

A

A

S

V

A

G

V

Q

G

F

F

D

G

G

G

Q

Q

L

L

G

M

V

V

W

L

R

T

-

P

G

P

W

W

E

E

A

-

D

-

K

Q

P

G

C
|
C

Y

Y

R

R

C
|
C

L

L

V

W

G

P

D

D

D

N

P

Q

D

E

R

-

P

P

D

E

I

R

S

N

C

C

A

R

D

T

Q

A

G

G

V

V

L

V

G

G

A

P

L

V

T

V

G

G

V

V

M

M

G

G

S

T

L

L

G

Q

A

A

M

L

E

E

A

A

V

I

R

K

A

L

I

L

T

S

G

G

F

I

G

-

D

E

D

T

P

P

A

A

G

G

R

E

L

L

L

R

L

L

V

F

D

D

A

G

L

K

A

S

F

S

R

Q

F

W

R

R

T

S

I

L

A

A

V

L

P

R

K

R

D

A

P

S

G

G

C
|
C

R

P

C

V

A
x
C

G

G

active site: R11 (= R13), D127 (= D129)
binding adenosine-5'-triphosphate: I34 (= I36), G35 (= G37), G37 (= G39), G38 (= G40), D59 (= D61), R70 (= R72), Q71 (= Q73), K83 (= K85), T126 (≠ C128), D127 (= D129), T131 (= T133)
binding zinc ion: C169 (= C172), C172 (= C175), C240 (= C245), C243 (≠ A248)

P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
42% identity, 99% coverage: 3:249/249 of query aligns to 1:244/251 of P30138

query
sites
P30138

L

M

T

N

D

D

E

R

Q

D

L

F

D

M

R

R

Y

Y

A

S

R

R

H

Q

I

I

I

L

L

L

K

D

E

D

I

I

G

A

G

L

A

D

G

G

Q

Q

A

K

L

L

K

D

A

S

T

Q

V

V

A

L

V

I

I

I

G

G

A

L

G

G

I

L

G

G

S

T

P

P

A

A

I

A

Q

L

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

L

T

L

L

R

V

V

L

I

A

D

D

V

D

V

V

D

H

L

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

T

I

L

L

F

F

G

T

T

T

A

E

D

D

I

I

G

D

C

R

P

P

K

K

A

S

E

Q

V

V

A

S

A

Q

R

R

V

L

A

T

A

Q

M

L

N

N

P

P

D

D

V

I

L

Q

V

L

E

T

P

A

V

L

T

Q

V

Q

R

R

I

L

D

T

A

G

D

E

T

A

A

L

D

K

D

D

L

A

L

V

E

A

G

R

A

A

D

D

L

V

V

V

L

L

D

D

G

C

C

T

D

D

N

N

F

M

A

A

T

T

R

R

L

Q

A

E

V

I

S

N

D

A

A

A

A

C

T

V

R

A

L

L

G

N

I

T

P

P

L

L

V

I

S

T

A

A

A

S

V

A

G

V

Q

G

F

F

D

G

G

G

Q

Q

L

L

G

M

V

V

W

L

R

T

-

P

G

P

W

W

E

E

A

-

D

-

K

Q

P

G

C
|
C

Y

Y

R

R

C
|
C

L

L

V
x
W

G

P

D

D

D

N

P

Q

D

E

R

-

P

P

D

E

I

R

S

N

C
|
C

A

R

D

T

Q

A

G

G

V

V

L

V

G

G

A

P

L

V

T

V

G

G

V

V

M

M

G

G

S

T

L

L

G

Q

A

A

M

L

E

E

A

A

V

I

R

K

A

L

I

L

T

S

G

G

F

I

G

-

D

E

D

T

P

P

A

A

G

G

R

E

L

L

L

R

L

L

V

F

D

D

A

G

L

K

A

S

F

S

R

Q

F

W

R

R

T

S

I

L

A

A

V

L

P

R

K

R

D

A

P

S

G

G

C
|
C

R

P

C

V

A
x
C

G

G

C169 (= C172) binding Zn(2+)
C172 (= C175) binding Zn(2+)
W174 (≠ V177) 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 (= C245) binding Zn(2+)
C243 (≠ A248) binding Zn(2+)

1zud3 Structure of this-thif protein complex (see paper)
42% identity, 99% coverage: 3:249/249 of query aligns to 1:239/240 of 1zud3

query
sites
1zud3

L

M

T

N

D

D

E

R

Q

D

L

F

D

M

R

R

Y

Y

A

S

R
|
R

H

Q

I

I

I
x
L

L

L

K
x
D

E

D

I

I

G

A

G

L

A

D

G

G

Q

Q

A

K

L

L

K

D

A

S

T

Q

V

V

A

L

V

I

I

I

G

G

A

L

G

G

I

L

G

G

S

T

P

P

A

A

I

A

Q

L

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

L

T

L

L

R

V

V

L

I

A

D

D

V

D

V

V

D

H

L

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

T

I

L

L

F

F

G

T

T

T

A

E

D

D

I

I

G

D

C

R

P

P

K

K

A

S

E

Q

V

V

A

S

A

Q

R

R

V

L

A

T

A

Q

M

L

N

N

P

P

D

D

V

I

L

Q

V

L

E

T

P

A

V

L

T

Q

V

Q

R

R

I

L

D

T

A

G

D

E

T

A

A

L

D

K

D

D

L

A

L

V

E

A

G

R

A

A

D

D

L

V

V

V

L

L

D

D

G

C

C

T

D
|
D

N

N

F

M

A

A

T

T

R

R

L

Q

A

E

V

I

S

N

D

A

A

A

A

C

T

V

R

A

L

L

G

N

I

T

P

P

L

L

V

I

S

T

A

A

A

S

V

A

G

V

Q

G

F

F

D

G

G

G

Q

Q

L

L

G

M

V

V

W

L

R

T

-

P

G

P

W

W

E

E

A

-

D

-

K

Q

P

G

C
|
C

Y

Y

R

R

C

C

L

L

V

W

G

-

D

-

P

-

D

-

R

-

P

P

D

D

I

N

S

Q

C

E

A

P

D

T

Q

A

G

G

V

V

L

V

G

G

A

P

L

V

T

V

G

G

V

V

M

M

G

G

S

T

L

L

G

Q

A

A

M

L

E

E

A

A

V

I

R

K

A

L

I

L

T

S

G

G

F

I

G

-

D

E

D

T

P

P

A

A

G

G

R

E

L

L

L

R

L

L

V

F

D

D

A

G

L

K

A

S

F

S

R

Q

F

W

R

R

T

S

I

L

A

A

V

L

P

R

K

R

D

A

P

S

G

G

C
|
C

R

P

C

V

A
x
C

G

G

active site: R11 (= R13), D127 (= D129)
binding calcium ion: L14 (≠ I16), D16 (≠ K18)
binding zinc ion: C169 (= C172), C235 (= C245), C238 (≠ A248)

P38820 Adenylyltransferase and sulfurtransferase UBA4; Needs CLA4 to survive protein 3; Ubiquitin-like protein activator 4; EC 2.7.7.-; EC 2.8.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 4 papers)
37% identity, 99% coverage: 3:249/249 of query aligns to 39:290/440 of P38820

query
sites
P38820

L

L

T

S

D

L

E

E

Q

E

L

Y

D

Q

R

R

Y

Y

A

G

R

R

H

Q

I

M

I

I

L

V

K

E

E

E

I

T

G

G

-

V

A

A

G

G

Q

Q

Q

V

A

K

L

L

L

K

K

N

A

T

T

K

V

V

A

L

V

V

I

V

G

G

A

A

G

G

I

L

G

G

S

C

P

P

A

A

I

L

Q

P

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

L

Q

L

I

R

G

V

I

I

V

D

D

D

N

D

D

V

V

D

E

L

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

T

V

L

L

F

H

G

D

T

S

A

S

D

R

I

V

G

G

C

M

P

L

K

K

A

C

E

E

V

S

A

A

A

R

A

Q

R

Y

V

I

A

T

A

K

M

L

N

N

P

P

D

H

V

I

L

N

V

V

E

V

P

T

V

Y

T

P

V

V

R

R

I

L

D

N

A

S

D

S

T

N

A

A

D

F

D

D

L

I

L

F

E

K

G

G

A

Y

D

N

L

Y

V

I

L

L

D

D

G

C

C

T

D

D

N

S

F

P

A

L

T

T

R

R

L

Y

A

L

V

V

S

S

D

D

A

V

A

A

T

V

R

N

L

L

G

G

I

I

P

T

L

V

V

V

S

S

A

A

A

S

V

G

G

L

Q

G

F

T

D

E

G

G

Q

Q

L

L

G

T

V

I

W

L

R

-

G

N

W

F

E

N

A

N

D

I

K

G

P

P

C

C

Y

Y

R

R

C

C

L

F

V

Y

G

P

D

T

D

P

P

P

D

P

R

-

P

P

D

N

-

A

-

V

I

T

S

S

C
|
C

A

Q

D

E

Q

G

G

G

V

V

L

I

G

G

A

P

L

C

T

I

G

G

V

L

M

V

G

G

S

T

L

M

G

M

A

A

M

V

E

E

A

T

V

L

R

K

A

L

I

I

T

L

G

G

F

I

G

Y

D

T

D

N

P

E

A

N

G

F

R

S

L

P

L

F

L

L

V

M

D

L

A

Y

L

S

A

G

F

F

R

P

F

Q

R

Q

T

S

I

L

A

R

V

T

P

F

K

K

D

M

P

R

G

G

-

R

-

Q

-

E

-

K

C

C

R

L

C

C

A

C

G

G

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.

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)
37% identity, 98% coverage: 3:245/249 of query aligns to 61:315/482 of O59954

query
sites
O59954

L

L

T

H

D

G

E

E

Q

E

L

Y

D

R

R

R

Y

Y

A

G

R

R

H

Q

I

M

I

I

L

V

K

P

E

Q

I

F

G

G

G

L

A

Q

G
|
G

Q

Q

Q

L

A

K

L

L

L

R

K

D

A

A

T

K

V

V

A

L

V

I

I

V

G

G

A

A

G

G

I

L

G
|
G

S

C

P

P

A

A

I

A

Q

L

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

L

T

L

I

R

G

V

L

I

V

D

D

D

G

D

D

V

T

V

V

D

E

L

A

S

S

N

N

L

L

Q

H

R
|
R

Q

Q

T

V

L

L

F

H

G

R

T

S

A

R

D

N

I

V

G

G

C

K

P

L

K

K

A

V

E

D

V

S

A

A

A

I

A

E

R

Y

V

L

A

R

A

E

M

L

N

N

P

P

D

H

V

P

L

T

V

Y

E

I

P

A

V

H

T

Q

V

A

R

H

I

L

D

T

A

P

D

R

T

E

A

A

D

P

D

D

L

I

L

F

E

K

G

D

A

Y

D

D

L

L

V

I

L

L

D

D

G
x
C

C

T

D

D

N

N

F

P

A

A

T

T

R

R

L

Y

A

L

V

I

S

S

D

D

A

T

A

A

T

V

R

L

L

L

G

G

I

K

P

P

L

L

V

V

S

S

A

A

A

S

V

A

G

L

Q

R

F

T

D
x
E

G

G

Q

Q

L

L

G

M

V

V

W

L

R

N

-

N

-

P

-

Q

-

P

G

G

W

D

E

K

A

T

D

G

K

G

P

P

C

C

Y

Y

R

R

C

C

L

V

V

F

G

P

D

K

D

P

P

P

D

P

R

A

P

N

D

S

I

V

-

T

S

S

C

C

A

A

D

D

Q

G

G

G

V

I

L

L

G

G

A

P

L

V

T

V

G
|
G

V

T

M

M

G

G

S

V

L

L

G

Q

A

A

M

S

E

E

A

A

V

I

R

K

A

V

I

L

T

T

G

S

F

A

G

G

D

E

D

S

-

V

-

E

-

A

-

T

P

P

A

P

G

S

R

L

L

L

L

I

L

F

V

S

D

A

A

Y

L

S

A

S

F

P

R

Q

F

F

R

R

T

T

I

I

A

K

V

L

-

R

P

S

K

R

D

R

P

P

G

N

C

C

G82 (= G24) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
G100 (= G42) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
R130 (= R72) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
C185 (≠ G127) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
E215 (≠ D157) 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)
44% identity, 94% coverage: 2:234/249 of query aligns to 54:285/460 of O95396

query
sites
O95396

S

A

L

L

T

S

D

R

E

D

Q

E

L

I

D

L

R

R

Y

Y

A

S

R

R

H

Q

I

L

I

V

L

L

K

P

E

E

I

L

G

G

G

V

A

H

G

G

Q

Q

Q

L

A

R

L

L

L

G

K

T

A

A

T

C

V

V

A

L

V

I

I

V

G

G

A

C

G

G

I

L

G

G

S

C

P

P

A

L

I

A

Q

Q

Y

Y

L

L

A

A

G

G

I

V

G

G

L

R

L

L

R

G

V

L

I

V

D

D

D

Y

D

D

V

V

D

E

L

M

S

S

N

N

L

L

Q

A

R

R

Q

Q

T

V

L

L

F

H

G

G

T

E

A

A

D

L

I

A

G

G

C

Q

P

A

K

K

A

A

E

F

V

S

A

A

R

S

V

L

A

R

M

L

N

N

P

S

D

A

V

V

L

E

V

C

E

V

P

P

V

Y

T
|
T

V
x
Q

R
x
A

I
x
L

D
x
T

A
x
P

D
x
A

T
|
T

A
|
A

D
x
L

D
|
D

L
|
L

L
x
V

E
x
R

G
x
R

A
x
Y

D
|
D

L
x
V

V
|
V

L
x
A

D
|
D

G
x
C

C
x
S

D
|
D

N
|
N

F
x
V

A
x
P

T
|
T

R
|
R

L
x
Y

A
x
L

V
|
V

S
x
N

D
|
D

A
|
A

A
x
C

T
x
V

R
x
L

L
x
A

G
|
G

I
x
R

P
|
P

L
|
L

V
|
V

S
|
S

A
|
A

A
x
S

V
x
A

G
x
L

Q
x
R

F
|
F

D
x
E

G
|
G

Q
|
Q

L
x
I

G
x
T

V
|
V

W
x
Y

R
x
H

G

-

W

-

E
x
Y

A
x
D

D
x
G

K
x
G

P
|
P

C
|
C

Y
|
Y

R
|
R

C
|
C

L
x
I

V
x
F

G
x
P

D
x
Q

D
x
P

P
|
P

D
x
P

R
x
A

P
x
E

D
x
T

I
x
V

S
x
T

-
x
N

C
|
C

A

A

D

D

Q

G

G

G

V

V

L

L

G

G

A

V

L

V

T

T

G

G

V

V

M

L

G

G

S

C

L

L

G

Q

A

A

M

L

E

E

A

V

V

L

R

K

A

I

I

A

T

A

G

G

F

L

G

G

D

P

D

S

P

Y

A

S

G

G

R

S

L

L

V

F

D

D

A

A

L

L

A

R

F

G

R

H

F

F

158:238 (vs. 106:187, 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.

1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
37% identity, 96% coverage: 2:241/249 of query aligns to 2:217/217 of 1jwaB

query
sites
1jwaB

S

E

L

L

T

S

D

D

E

Q

Q

E

L

M

D

L

R

R

Y

Y

A

N

R
|
R

H

Q

I

I

L

L

K

R

E

G

I

F

G

D

G

F

A

D

G

G

Q

Q

Q

E

A

A

L

L

L

K

K

D

A

S

T

R

V

V

A

L

V

I

I

V

G

G

A

L

G
|
G

I

L

G

G

S

C

P

A

A

A

I

S

Q

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

I

V

G

G

L

N

L

L

R

T

V

L

I

L

D
|
D

D
x
F

D

D

V

T

V

V

D

S

L

L

S

S

N

N

L

L

Q

Q

R
|
R

Q

Q

T

T

L

L

F

H

G

S

T

D

A

A

D

T

I

V

G

G

C

Q

P

P

K
|
K

A

V

E

E

V

S

A

A

A

R

A

D

R

A

V

L

A

T

A

R

M

I

N

N

P

P

D

H

V

I

L

A

V

I

E

T

P

P

V

V

T

N

V

A

R
x
L

I

L

D

D

A

D

D

A

T

E

A

L

D

A

L

L

L

I

E

A

G

E

A

H

D

D

L

L

V

V

L

L

D

D

G

C

C

T

D
|
D

N
|
N

F

V

A

A

T
x
V

R

R

L

N

A

Q

V

L

S

N

D

A

A

G

A

C

T

F

R

A

L

A

G

K

I

V

P

P

L

L

V

V

S

S

A

G

A

A

V

A

G

I

Q

R

F

M

D

E

G

G

Q

Q

L

I

G

T

V

V

W

F

R

T

G

-

W

Y

E

E

A

A

D

-

K

-

P

-

C

-

Y

-

R

-

C

-

L

-

V

-

G

-

D

-

P

-

D

-

R

-

P

-

D

-

I

-

S

-

C

-

A

-

D

-

Q

-

G

G

V

V

L

M

G

A

A

P

L

L

T

I

G

G

V

V

M

I

G

G

S

S

L

L

G

Q

A

A

M

M

E

E

A

A

V

I

R

K

A

M

I

L

T

A

G

G

F

Y

G

G

D

K

D

P

P

A

A

S

G

G

R

K

L

I

L

V

L

M

V

Y

D

D

A

A

L

M

A

T

F

C

R

Q

F

F

R

R

T

E

I

M

A

K

V

L

P

M

K

R

active site: R13 (= R13), D129 (= D129)
binding adenosine-5'-triphosphate: G39 (= G39), G40 (= G40), D61 (= D61), F62 (≠ D62), R72 (= R72), K85 (= K85), L108 (≠ R108), D129 (= D129), N130 (= N130), V133 (≠ T133)

6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
37% identity, 85% coverage: 2:213/249 of query aligns to 6:212/289 of 6yubB

query
sites
6yubB

S

S

L

L

T

S

D

K

E

E

Q

E

L

I

D

E

R

R

Y

Y

A

S

R

R

H

Q

I

M

I

I

L

V

K

P

E

G

I

M

G

G

G

K

A

E

G

G

Q

Q

Q

L

A

R

L

L

L

M

K

N

A

A

T

K

V

V

A

L

V

I

I

I

G

G

A

A

G

G

I

L

G

G

S

C

P

P

A

A

I

A

Q

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

L

T

L

I

R

G

V

I

I

V

D

D

D

G

D

D

V

S

V

V

D

E

L

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

T

V

L

A

F

H

G

A

T

T

A

K

D

R

I

V

G

G

C

M

P

L

K

K

A

V

E

D

V

S

A

L

A

I

A

T

R

H

V

L

A

I

A

E

M

I

N

N

P

P

D

L

V

P

L

V

V

Y

E

V

P

P

V

Y

T

R

V

F

R

D

I

L

D

T

A

P

D

Q

T

N

A

A

D

A

D

Q

L

I

E

K

G

P

A

W

D

D

L

V

V

I

L

L

D

D

G

C

C

T

D

D

N

N

F

P

A

A

T

T

R

R

L

Y

A

L

V

I

S

S

D

D

A

V

A

C

T

V

R

L

L

L

G

G

I

K

P

P

L

L

V

V

S

S

A

A

V

S

G

V

Q

Q

F

K

D

S

G

G

Q

Q

L

L

G

I

V

V

W

L

-

N

-

C

-

P

-

T

-

P

R

Q

G

G

W

V

E

V

A

N

D

K

K

K

-

A

P

P

C
|
C

Y

Y

R

R

C
|
C

L

C

V

F

G

-

D

-

P

-

D

-

R

-

P

-

D

-

I

-

S

-

C

-

A

-

D

-

Q

K

G

G

V

I

L

M

G

G

A

P

L

V

T

V

G

G

V

M

M

M

G

G

S

V

L

A

G

Q

A

A

M

G

E

E

A

A

V

I

R

K

A

I

I

L

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

Sites not aligning to the query:

binding zinc ion: 265

6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
37% identity, 85% coverage: 2:213/249 of query aligns to 5:213/423 of 6yubA

query
sites
6yubA

S

S

L

L

T

S

D

K

E

E

Q

E

L

I

D

E

R

R

Y

Y

A

S

R

R

H

Q

I

M

I

I

L

V

K

P

E

G

I

M

G

G

G

K

A

E

G

G

Q

Q

Q

L

A

R

L

L

L

M

K

N

A

A

T

K

V

V

A

L

V

I

I

I

G

G

A

A

G

G

I

L

G

G

S

C

P

P

A

A

I

A

Q

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

L

T

L

I

R

G

V

I

I

V

D

D

D

G

D

D

V

S

V

V

D

E

L

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

T

V

L

A

F

H

G

A

T

T

A

K

D

R

I

V

G

G

C

M

P

L

K

K

A

V

E

D

V

S

A

L

A

I

A

T

R

H

V

L

A

I

A

E

M

I

N

N

P

P

D

L

V

P

L

V

V

Y

E

V

P

P

V

Y

T

R

V

F

R

D

I

L

D

T

A

P

D

Q

T

N

A

A

D

A

D

Q

L

I

E

K

G

P

A

W

D

D

L

V

V

I

L

L

D

D

G

C

C

T

D

D

N

N

F

P

A

A

T

T

R

R

L

Y

A

L

V

I

S

S

D

D

A

V

A

C

T

V

R

L

L

L

G

G

I

K

P

P

L

L

V

V

S

S

A

A

V

S

G

V

Q

Q

F

K

D

S

G

G

Q

Q

L

L

G

I

V

V

W

L

-

N

-

C

-

P

-

T

-

P

R

Q

G

G

W

V

E

V

A

N

D

K

K

K

-

A

P

P

C
|
C

Y

Y

R

R

C
|
C

L

C

V

F

G

-

D

-

P

-

D

K

R

K

P

P

D

-

I

-

S

-

C

-

A

-

D

-

Q

-

G

G

V

I

L

M

G

G

A

P

L

V

T

V

G

G

V

M

M

M

G

G

S

V

L

A

G

Q

A

A

M

G

E

E

A

A

V

I

R

K

A

I

I

L

binding zinc ion: C183 (= C172), C186 (= C175)

Sites not aligning to the query:

binding zinc ion: 266, 269

O42939 Ubiquitin-activating enzyme E1-like; Pmt3-activating enzyme subunit 2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 61% coverage: 31:181/249 of query aligns to 26:175/628 of O42939

query
sites
O42939

A

A

T

K

V

V

A

L

V

L

I

V

G

G

A

A

G

G

I

I

G

G

S

C

P

E

A

L

I

L

Q

K

Y

N

L

L

A

L

A

M

A

S

G

G

I

V

G

K

L

E

L

V

R

H

V

I

I

I

D

D

D

L

D

D

V

T

V

I

D

D

L

L

S

S

N

N

L

L

Q

N

R

R

Q

Q

T

F

L

L

F

F

G

R

T

K

A

K

D

H

I

V

G

K

C

Q

P

P

K

K

A

A

E

I

V

V

A

A

A

K

R

T

V

A

A

S

M

F

N

N

P

P

D

N

V

V

L

K

V

L

E

E

P

A

V

Y

T

H

V

A

R

N

I

I

D

K

A

E

D

D

T

R

A

F

D

N

-

V

D

A

L

W

L

F

E

R

G

Q

A

F

D

D

L

L

V

V

L

F

D

N

G

A

C

L

D

D

N

N

F

L

A

D

T

A

R

R

L

R

A

H

V

V

S

N

D

K

A

Q

A

C

T

L

R

L

L

A

G

S

I

V

P

P

L

L

V

I

S

E

A

S

A

G

V

T

G

T

Q

G

F

F

D

L

G

G

Q

Q

L

V

G

Q

V

V

W

I

R

I

G

H

W

G

E

K

A

T

D

E

K

-

P

-

C

C

Y

Y

R

D

C

C

L

N

V

P

G

K

D

E

D

P

P

P

Sites not aligning to the query:

559 modified: Phosphoserine
563 modified: Phosphoserine

8seaA Cryo-em structure of a double loaded human uba7-ube2l6-isg15 thioester mimetic complex (form 1) (see paper)
35% identity, 58% coverage: 20:163/249 of query aligns to 402:548/992 of 8seaA

query
sites
8seaA

I

F

G

G

G

A

A

G

G

F

Q

Q

Q

E

A

K

L

L

L

R

K

R

A

Q

T

H

V

Y

A

L

V

L

I

V

G

G

A

A

G
|
G

G
x
A

I

I

G

G

S

C

P

E

A

L

I

L

Q

K

Y

V

L

F

A

A

A

L

A

V

G

G

I

L

G

G

L

A

-

G

-

N

-

S

-

G

L

L

R

T

V

V

I

V

D
|
D

D
x
M

D

D

V

H

V

I

D

E

L

R

S

S

N

N

L

L

Q

S

R

R

Q

Q

T

F

L

L

F

F

G

R

T

S

A

Q

D

D

I

V

G

G

C

R

P

P

K
|
K

A

A

E

E

V

V

A

A

R

A

V

A

A

R

A

G

M

L

N

N

P

P

D

D

V

L

L

Q

V

V

E

I

P

P

V

L

T

T

V

Y

R

P

I
x
L

D

D

A

P

D

T

T

T

A

E

-

H

-

I

-

Y

-

G

D

D

D

N

L

F

E

S

G

R

A

V

D

D

L

G

V

V

L

A

D

A

G

A

C
x
L

D
|
D

N

S

F

F

A

Q

T

A

R

R

L

R

A

Y

V

V

S

A

D

A

A

R

A

C

T

T

R

H

L

Y

G

L

I

K

P

P

L

L

V

L

S

E

A

A

A

-

V

-

G

-

Q

-

F

-

D

-

G

G

Q

T

L

S

G

G

V

T

W

W

binding adenosine monophosphate: G421 (= G39), A422 (≠ G40), D448 (= D61), M449 (≠ D62), K472 (= K85), L496 (≠ I109), L519 (≠ C128), D520 (= D129)

8oifA Structure of the ube1l activating enzyme bound to isg15 and ube2l6 (see paper)
35% identity, 58% coverage: 20:163/249 of query aligns to 348:494/704 of 8oifA

query
sites
8oifA

I

F

G

G

G

A

A

G

G

F

Q

Q

Q

E

A

K

L

L

L

R

K

R

A

Q

T

H

V

Y

A

L

V

L

I
x
V

G
|
G

A

A

G
|
G

G

A

I

I

G

G

S

C

P

E

A

L

I

L

Q

K

Y

V

L

F

A

A

A

L

A

V

G

G

I

L

G

G

L

A

-

G

-

N

-

S

-

G

L

L

R

T

V

V

I

V

D

D

D
x
M

D

D

V

H

V

I

D

E

L

R

S

S

N

N

L

L

Q

S

R

R

Q

Q

T

F

L

L

F

F

G

R

T

S

A

Q

D

D

I

V

G

G

C

R

P

P

K

K

A

A

E

E

V

V

A

A

R

A

V

A

A

R

A

G

M

L

N

N

P

P

D

D

V

L

L

Q

V

V

E

I

P

P

V

L

T

T

V

Y

R

P

I
x
L

D

D

A

P

D

T

T

T

A

E

-

H

-

I

-

Y

-

G

D

D

D

N

L

F

E

S

G

R

A

V

D

D

L

G

V

V

L

A

D

A

G

A

C
x
L

D
|
D

N

S

F

F

A

Q

T

A

R

R

L

R

A

Y

V

V

S

A

D

A

A

R

A

C

T

T

R

H

L

Y

G

L

I

K

P

P

L

L

V

L

S

E

A

A

A

-

V

-

G

-

Q

-

F

-

D

-

G

G

Q

T

L

S

G

G

V

T

W

W

binding adenosine monophosphate: V364 (≠ I36), G365 (= G37), G367 (= G39), M395 (≠ D62), L442 (≠ I109), L465 (≠ C128), D466 (= D129)

3kydB Human sumo e1~sumo1-amp tetrahedral intermediate mimic (see paper)
29% identity, 84% coverage: 33:242/249 of query aligns to 17:238/477 of 3kydB

query
sites
3kydB

V

V

A

L

V

V

I

V

G

G

A

A

G

G

I
|
I

G

G

S

C

P

E

A

L

I

L

Q

K

Y

N

L

L

A

V

A

L

A

T

G

G

I

F

G

S

L

H

L

I

R

D

V

L

I

I

D
|
D

D
x
L

D

D

V

T

V

I

D

D

L

V

S

S

N

N

L

L

Q

N

R

R

Q

Q

T

F

L

L

F

F

G

Q

T

K

A

K

D

H

I

V

G

G

C

R

P

S

K
|
K

A

A

E

Q

V

V

A

A

A

K

A

E

R

S

V

V

A

L

A

Q

M

F

N

Y

P

P

D

K

V

A

-

N

L

I

V

V

E

A

P

Y

V

H

T

D

V
x
S

R
x
I

I

M

D

N

A

P

D

D

T

Y

A

N

D

V

D

E

L

F

E

R

G

Q

A

F

D

I

L

L

V

V

L

M

D

N

G

A

C
x
L

D
|
D

N
|
N

F

R

A

A

T

A

R

R

L

N

A

H

V

V

S

N

D

R

A

M

A

C

T

L

R

A

L

A

G

D

I

V

P

P

L

L

V

I

S

E

A

S

A

G

V

T

G

A

Q

G

F

Y

D

L

G

G

Q

Q

L

V

-

T

-

I

-

K

G

G

V

V

W

T

R

E

G
x
C

W

Y

E

E

A
x
C

D

H

-

P

K

K

P

P

C

T

Y

Q

R

R

-

T

-

F

-

P

-

G

C
|
C

L
x
T

V

I

G
x
R

D

N

D

T

P

P

D

S

R

E

P

P

D

-

I

I

S

H

C

C

-

I

-

V

-

W

A

A

D

K

Q

Y

G

L

V

F

L

N

G

Q

A

L

L

F

T

T

G

K

V

E

M

W

G

A

S

K

L

S

G

T

A

G

M

Y

E

D

A

P

V

V

R

K

A

L

I

F

T

T

G

K

F

L

G

F

D

K

D

D

P

D

A

I

G

R

R

Y

L

L

L

T

V

M

D

D

A

K

L

L

A

-

F

W

R

R

F

K

R

R

T

K

I

P

A

P

V

V

P

P

K

L

D

D

active site: D114 (= D129), C170 (= C175), T171 (≠ L176), R173 (≠ G178)
binding 5'-{[(3-aminopropyl)sulfonyl]amino}-5'-deoxyadenosine: I25 (= I41), D45 (= D61), L46 (≠ D62), K69 (= K85), S92 (≠ V107), I93 (≠ R108), L113 (≠ C128), D114 (= D129), N115 (= N130), C170 (= C175), R173 (≠ G178)
binding zinc ion: C155 (≠ G165), C158 (≠ A168)

Sites not aligning to the query:

binding zinc ion: 370, 373

P20973 Ubiquitin-activating enzyme E1 1; EC 6.2.1.45 from Triticum aestivum (Wheat) (see paper)
33% identity, 53% coverage: 21:152/249 of query aligns to 453:593/1051 of P20973

query
sites
P20973

G

G

G

S

A

K

G

L

Q

Q

Q

N

A

K

L

L

L

E

K

E

A

A

T

K

V

I

A

F

V

M

I

V

G

G

A

S

G

G

G

A

I

L

G

G

S

C

P

E

A

F

I

L

Q

K

Y

N

L

L

A

A

A

L

A

M

G

G

I

I

-

S

-

C

-

S

-

Q

-

N

G

G

L

N

L

L

R

T

V

L

I

T

D

D

V

V

V

I

D

E

L

K

S

S

N

N

L

L

Q

S

R

R

Q

Q

T

F

L

L

F

F

G

R

T

D

A

W

D

N

I

I

G

G

C

Q

P

P

K

K

A

S

E

T

V

V

A

A

A

T

R

A

V

A

A

M

A

V

M

I

N

N

P

P

D

K

V

L

L

H

V

V

E

E

P

A

V

L

T

Q

V

N

R

R

I

A

D

S

A

P

D

E

T

T

A

E

-

N

-

V

-

F

-

N

D

D

D

A

L

F

L

W

E

E

G

N

A

L

D

D

L

A

V

V

L

V

D

N

G

A

C

L

D

D

N

N

F

V

A

T

T

A

R

R

L

M

A

Y

V

I

S

D

D

S

A

R

A

C

T

V

R

Y

L

F

G

Q

I

K

P

P

L

L

V

L

S

E

A

S

A

G

Sites not aligning to the query:

626 active site, Glycyl thioester intermediate; C→A: Abolishes enzyme activity.

Query Sequence

>WP_012051051.1 NCBI__GCF_000016765.1:WP_012051051.1
MSLTDEQLDRYARHIILKEIGGAGQQALLKATVAVIGAGGIGSPAIQYLAAAGIGLLRVI
DDDVVDLSNLQRQTLFGTADIGCPKAEVAAARVAAMNPDVLVEPVTVRIDADTADDLLEG
ADLVLDGCDNFATRLAVSDAATRLGIPLVSAAVGQFDGQLGVWRGWEADKPCYRCLVGDD
PDRPDISCADQGVLGALTGVMGSLGAMEAVRAITGFGDDPAGRLLLVDALAFRFRTIAVP
KDPGCRCAG

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