SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_011970838.1 NCBI__GCF_000017145.1:WP_011970838.1 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)
52% identity, 64% coverage: 124:367/380 of query aligns to 7:252/271 of Q72J02

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Q72J02

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C192 (= C307) 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, 65% coverage: 120:367/380 of query aligns to 5:248/270 of D4GSF3

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D4GSF3

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C188 (= C307) 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.

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, 68% coverage: 114:370/380 of query aligns to 58:312/453 of Q9VLJ8

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Q9VLJ8

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T62 (≠ R118) 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)
41% identity, 65% coverage: 124:369/380 of query aligns to 65:320/482 of O59954

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O59954

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G82 (= G141) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
G100 (= G159) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
R130 (= R189) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
C185 (≠ G244) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
E215 (= E274) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
G264 (= G318) mutation to S: In cnxF142ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.

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, 66% coverage: 119:367/380 of query aligns to 3:247/249 of P12282

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P12282

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C

S

V

E

E

V

A

G

G

V

V

L

M

G

A

V

P

L

L

P

I

G

G

V

V

I

I

G

G

T

S

I

L

M

Q

A

A

T

M

E

E

A

A

I

I

K

K

I

M

L

L

L

A

G

G

I

Y

G

G

D

K

P

P

L

A

I

S

G

G

R

K

L

I

L

V

T

M

Y

Y

N

D

A

A

L

M

D

T

C
|
C

S

Q

F

F

H

R

D

E

L

M

E

K

V

L

P

M

A

R

N

N

P

P

H

G

C
|
C

E

E

Q

V

C
|
C

R14 (= R130) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
C44 (≠ S160) mutation to A: No effect.
R73 (= R189) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
C128 (≠ G244) mutation to A: No effect.; mutation to Y: No activity.
D130 (= D246) mutation to A: No activity.; mutation to E: Substantially reduced activity.
C142 (≠ S258) mutation to A: No effect.
C172 (= C290) mutation to A: No zinc bound and no enzyme activity.
C175 (= C293) mutation to A: No zinc bound and no enzyme activity.
C187 (= C307) mutation to A: No effect.
C231 (= C351) mutation to A: No effect.
C244 (= C364) mutation to A: No zinc bound and almost no enzyme activity.
C247 (= C367) mutation to A: No zinc bound and almost no enzyme activity.

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, 57% coverage: 120:335/380 of query aligns to 39:253/440 of P38820

query
sites
P38820

L

L

S

S

P

L

A

E

E

E

K

Y

E

Q

R

R

Y

Y

A

G

R

R

H

Q

L

M

S

I

I

V

P

E

E

E

V

T

G

G

A

G

-

V

E

A

G

G

Q

Q

A

V

L

K

L

L

L

K

S

N

K

T

K

K

V

V

A

L

L

V

V

V

G

G

A

A

G

G

L

L

G

G

S

C

P

P

L

A

A

L

F

P

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

T

Q

L

I

G

G

L

I

I

V

D

D

S

N

D

D

R

V

L

V

E

E

R

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

I

V

L

L

H

H

T

D

D

S

R

R

I

V

G

G

E

M

L

L

K

K

V

C

S

E

S

S

A

A

A

R

K

Q

S

Y

L

I

Q

T

A

K

F

L

N

N

P

P

D

H

V

I

A

N

L

V

N

V

L

T

H

Y

E

P

I

V

R

R

L

L

N

N

E

S

N

S

N

N

A

A

L

F

E

D

I

I

L

F

A

K

D

G

Y

Y

D

N

L

Y

V

I

I

L

D

D

G

C

S

T

D

D

N

S

L

P

A

L

T

T

R

R

Y

Y

V

L

V

V

S

S

D

D

A

V

S

A

T

V

L

N

L

L

S

G

I

I

P

T

M

V

I

V

Y

S

G

A

A

S

I

G

F

L

R

G

F

T

E

E

G

G

H

Q

V

L

S

T

A

I

F

L

W

-

P

-

N

N

G

F

P

N

S

N

G

I

G

G

P

P

C

C

Y

Y

R

R

C

C

L

F

F

Y

P

P

E

T

K

P

L

P

P

P

A

P

S

N

L

A

T

V

P

T

S

S

C
|
C

S

Q

E

E

V

G

G

G

V

V

L

I

G

G

V

P

L

C

P

I

G

G

V

L

I

V

G

G

T

T

I

M

M

M

A

A

T

V

E

E

A

T

I

L

K

K

I

L

L

I

L

L

G

G

I

I

C225 (= C307) 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.

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, 63% coverage: 113:353/380 of query aligns to 48:285/460 of O95396

query
sites
O95396

P

P

V

L

E

P

K

P

H

K

R

A

Q

A

L

L

S

S

P

R

A

D

E

E

K

I

E

L

R

R

Y

Y

A

S

R

R

H

Q

L

L

S

V

I

L

P

P

E

E

V

L

G

G

A

V

E

H

G

G

Q

Q

A

L

L

R

L

L

L

G

S

T

K

A

K

C

V

V

A

L

L

I

V

V

G

G

A

C

G

G

L

L

G

G

S

C

P

P

L

L

A

A

F

Q

Y

Y

L

L

A

A

G

G

I

V

G

G

T

R

L

L

G

G

L

L

I

V

D

D

S

Y

D

D

R

V

L

V

E

E

R

M

S

S

N

N

L

L

Q

A

R

R

Q

Q

I

V

L

L

H

H

T

G

D

E

D

A

R

L

I

A

G

G

E

Q

L

A

K

K

V

A

S

F

S

S

A

A

K

A

S

S

L

L

Q

R

A

R

F

L

N

N

P

S

D

A

V

V

A

E

L

C

N

V

L

P

H

Y

E
x
T

I
x
Q

R
x
A

L
|
L

N
x
T

E
x
P

N
x
A

N
x
T

A
|
A

L
|
L

E
x
D

I
x
L

L
x
V

A
x
R

D
x
R

Y
|
Y

D
|
D

L
x
V

V
|
V

I
x
A

D
|
D

G
x
C

S
|
S

D
|
D

N
|
N

L
x
V

A
x
P

T
|
T

R
|
R

Y
|
Y

V
x
L

V
|
V

S
x
N

D
|
D

A
|
A

S
x
C

T
x
V

L
|
L

L
x
A

S
x
G

I
x
R

P
|
P

M
x
L

I
x
V

Y
x
S

G
x
A

A
x
S

I
x
A

F
x
L

R
|
R

F
|
F

E
|
E

G
|
G

H
x
Q

V
x
I

S
x
T

A
x
V

F
x
Y

W
x
H

P
x
Y

N
x
D

G

-

P

-

S

-

G
|
G

P
|
P

C
|
C

Y
|
Y

R
|
R

C
|
C

L
x
I

F
|
F

P
|
P

E
x
Q

K
x
P

L
x
P

P
|
P

A
|
A

S
x
E

L
x
T

T
x
V

P
x
T

S
x
N

C
|
C

S

A

E

D

V

G

G

G

V

V

L

L

G

G

V

V

L

V

P

T

G

G

V

V

I

L

G

G

T

C

I

L

M

Q

A

A

T

L

E

E

A

V

I

L

K

K

I

I

L

A

G

G

I

L

G

G

D

P

P

S

L

Y

I

S

G

G

R

S

L

L

T

L

Y

F

N

D

A

A

L

L

D

R

C

G

S

H

F

F

158:238 (vs. 223:306, 39% identical) Interaction with NFS1
C239 (= C307) 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)
38% identity, 66% coverage: 119:367/380 of query aligns to 2:239/240 of 1jwbB

query
sites
1jwbB

Q

E

L

L

S

S

P

D

A

Q

E

E

K

M

E

L

R

R

Y

Y

A

N

R
|
R

H

Q

L

I

S

I

I

L

P

R

E

G

V

F

G

D

A

F

E

D

G

G

Q

Q

A

E

L

A

L

L

L

K

S

D

K

S

K

R

V

V

A

L

L

I

V

V

G
|
G

A

L

G
|
G

L

L

G

G

S

C

P

A

L

A

A

S

F

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

I

V

G

G

T

N

L

L

G

T

L

L

I

L

D
|
D

S
x
F

D

D

R

T

L

V

E

S

R

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

I

T

L

L

H

H

T

S

D

D

D

A

R

T

I

V

G

G

E

Q

L

P

K
|
K

V

V

S

E

S

S

A

A

A

R

K

D

S

A

L

L

Q

T

A

R

F

I

N

N

P

P

D

H

V

I

A

A

L

I

N

T

L

P

H

V

E

N

I

A

R
x
L

L

L

N

D

E

D

N

A

N

E

A

L

L

A

E

A

I

L

L

I

A

A

D

E

Y

H

D

D

L

L

V

V

I

L

D

D

G
x
C

S
x
T

D
|
D

N
|
N

L

V

A

A

T
x
V

R

R

Y

N

V

Q

V

L

S

N

D

A

A

G

S

C

T

F

L

A

S

K

I

V

P

P

M

L

I

V

Y

S

G

G

A

A

I

A

F

I

R

R

F

M

E

E

G

G

H

Q

V

I

S

T

A

V

F

F

W

T

P

Y

N

Q

G

-

P

-

S

D

G

G

G

E

P

P

C
|
C

Y

Y

R

R

C

C

L

-

F

-

P

-

E

-

K

-

L

-

P

-

A

-

S

-

L

L

T

S

P

R

S

L

C

F

S

G

E

E

V

A

G

G

V

V

L

M

G

A

V

P

L

L

P

I

G

G

V

V

I

I

G

G

T

S

I

L

M

Q

A

A

T

M

E

E

A

A

I

I

K

K

I

M

L

L

L

A

G

G

I

Y

G

G

D

K

P

P

L

A

I

S

G

G

R

K

L

I

L

V

T

M

Y

Y

N

D

A

A

L

M

D

T

C

C

S

Q

F

F

H

R

D

E

L

M

E

K

V

L

P

M

A

R

N

N

P

P

H

G

C
|
C

E

E

Q

V

C
|
C

active site: R13 (= R130), D129 (= D246)
binding adenosine monophosphate: G37 (= G154), G39 (= G156), G40 (= G157), D61 (= D178), F62 (≠ S179), K85 (= K202), L108 (≠ R225), C127 (≠ G244), T128 (≠ S245), D129 (= D246), N130 (= N247), V133 (≠ T250)
binding zinc ion: C171 (= C290), C236 (= C364), C239 (= C367)

1jw9B Structure of the native moeb-moad protein complex (see paper)
38% identity, 66% coverage: 119:367/380 of query aligns to 2:239/240 of 1jw9B

query
sites
1jw9B

Q

E

L

L

S

S

P

D

A

Q

E

E

K

M

E

L

R

R

Y

Y

A

N

R
|
R

H

Q

L

I

S

I

I

L

P

R

E

G

V

F

G

D

A

F

E

D

G

G

Q

Q

A

E

L

A

L

L

L

K

S

D

K

S

K

R

V

V

A

L

L

I

V

V

G

G

A

L

G

G

L

L

G

G

S

C

P

A

L

A

A

S

F

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

I

V

G

G

T

N

L

L

G

T

L

L

I

L

D

D

S

F

D

D

R

T

L

V

E

S

R

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

I

T

L

L

H

H

T

S

D

D

D

A

R

T

I

V

G

G

E

Q

L

P

K

K

V

V

S

E

S

S

A

A

A

R

K

D

S

A

L

L

Q

T

A

R

F

I

N

N

P

P

D

H

V

I

A

A

L

I

N

T

L

P

H

V

E

N

I

A

R

L

L

L

N

D

E

D

N

A

N

E

A

L

L

A

E

A

I

L

L

I

A

A

D

E

Y

H

D

D

L

L

V

V

I

L

D

D

G

C

S

T

D
|
D

N

N

L

V

A

A

T

V

R

R

Y

N

V

Q

V

L

S

N

D

A

A

G

S

C

T

F

L

A

S

K

I

V

P

P

M

L

I

V

Y

S

G

G

A

A

I

A

F

I

R

R

F

M

E

E

G

G

H

Q

V

I

S

T

A

V

F

F

W

T

P

Y

N

Q

G

-

P

-

S

D

G

G

G

E

P

P

C
|
C

Y

Y

R

R

C

C

L

-

F

-

P

-

E

-

K

-

L

-

P

-

A

-

S

-

L

L

T

S

P

R

S

L

C

F

S

G

E

E

V

A

G

G

V

V

L

M

G

A

V

P

L

L

P

I

G

G

V

V

I

I

G

G

T

S

I

L

M

Q

A

A

T

M

E

E

A

A

I

I

K

K

I

M

L

L

L

A

G

G

I

Y

G

G

D

K

P

P

L

A

I

S

G

G

R

K

L

I

L

V

T

M

Y

Y

N

D

A

A

L

M

D

T

C

C

S

Q

F

F

H

R

D

E

L

M

E

K

V

L

P

M

A

R

N

N

P

P

H

G

C
|
C

E

E

Q

V

C
|
C

active site: R13 (= R130), D129 (= D246)
binding zinc ion: C171 (= C290), C236 (= C364), C239 (= C367)

6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
39% identity, 57% coverage: 117:333/380 of query aligns to 3:214/423 of 6yubA

query
sites
6yubA

H

Q

R

K

Q

S

L

L

S

S

P

K

A

E

E

E

K

I

E

E

R

R

Y

Y

A

S

R

R

H

Q

L

M

S

I

I

V

P

P

E

G

V

M

G

G

A

K

E

E

G

G

Q

Q

A

L

L

R

L

L

L

M

S

N

K

A

K

K

V

V

A

L

L

I

V

I

G

G

A

A

G

G

L

L

G

G

S

C

P

P

L

A

A

A

F

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

T

T

L

I

G

G

L

I

I

V

D

D

S

G

D

D

R

S

L

V

E

E

R

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

I

V

L

A

H

H

T

A

D

T

D

K

R

R

I

V

G

G

E

M

L

L

K

K

V

V

S

D

S

S

A

L

A

I

K

T

S

H

L

L

Q

I

A

E

F

I

N

N

P

P

D

L

V

P

A

V

L

Y

N

V

L

P

H

Y

E

R

I

F

R

D

L

L

N

T

E

P

N

Q

N

N

A

A

L

A

E

Q

I

I

L

I

A

K

D

P

Y

W

D

D

L

V

V

I

I

L

D

D

G

C

S

T

D

D

N

N

L

P

A

A

T

T

R

R

Y

Y

V

L

V

I

S

S

D

D

A

V

S

C

T

V

L

L

S

G

I

K

P

P

M

L

I

V

Y

S

G

A

A

A

I

S

F

V

R

Q

F

K

E

S

G

G

H

Q

V

L

S

I

A

V

F

L

-

N

W

C

P

P

N

P

G

T

P

P

S

Q

G

G

-

V

-

N

-

K

-

A

G

A

P

P

C
|
C

Y

Y

R

R

C
|
C

L

C

F

F

P

-

E

-

K

-

L

-

P

-

A

-

S

-

L

-

T

-

P

-

S

-

C

-

S

K

E

K

V

P

G

G

V

I

L

M

G

G

V

P

L

V

P

V

G

G

V

M

I

M

G

G

T

V

I

A

M

Q

A

A

T

G

E

E

A

A

I

I

K

K

I

I

L

L

L

V

binding zinc ion: C183 (= C290), C186 (= C293)

Sites not aligning to the query:

binding zinc ion: 266, 269

6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
39% identity, 57% coverage: 117:333/380 of query aligns to 4:213/289 of 6yubB

query
sites
6yubB

H

Q

R

K

Q

S

L

L

S

S

P

K

A

E

E

E

K

I

E

E

R

R

Y

Y

A

S

R

R

H

Q

L

M

S

I

I

V

P

P

E

G

V

M

G

G

A

K

E

E

G

G

Q

Q

A

L

L

R

L

L

L

M

S

N

K

A

K

K

V

V

A

L

L

I

V

I

G

G

A

A

G

G

L

L

G

G

S

C

P

P

L

A

A

A

F

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

T

T

L

I

G

G

L

I

I

V

D

D

S

G

D

D

R

S

L

V

E

E

R

T

S

S

N

N

L

L

Q

H

R

R

Q

Q

I

V

L

A

H

H

T

A

D

T

D

K

R

R

I

V

G

G

E

M

L

L

K

K

V

V

S

D

S

S

A

L

A

I

K

T

S

H

L

L

Q

I

A

E

F

I

N

N

P

P

D

L

V

P

A

V

L

Y

N

V

L

P

H

Y

E

R

I

F

R

D

L

L

N

T

E

P

N

Q

N

N

A

A

L

A

E

Q

I

I

L

I

A

K

D

P

Y

W

D

D

L

V

V

I

I

L

D

D

G

C

S

T

D

D

N

N

L

P

A

A

T

T

R

R

Y

Y

V

L

V

I

S

S

D

D

A

V

S

C

T

V

L

L

S

G

I

K

P

P

M

L

I

V

Y

S

G

A

A

A

I

S

F

V

R

Q

F

K

E

S

G

G

H

Q

V

L

S

I

A

V

F

L

-

N

W

C

P

P

N

P

G

T

P

P

S

Q

G

G

-

V

-

N

-

K

-

A

G

A

P

P

C
|
C

Y

Y

R

R

C
|
C

L

C

F

F

P

K

E

-

K

-

L

-

P

-

A

-

S

-

L

-

T

-

P

-

S

-

C

-

S

-

E

-

V

-

G

G

V

I

L

M

G

G

V

P

L

V

P

V

G

G

V

M

I

M

G

G

T

V

I

A

M

Q

A

A

T

G

E

E

A

A

I

I

K

K

I

I

L

L

L

V

binding zinc ion: C184 (= C290), C187 (= C293)

Sites not aligning to the query:

binding zinc ion: 265

1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
35% identity, 63% coverage: 119:358/380 of query aligns to 2:215/217 of 1jwaB

query
sites
1jwaB

Q

E

L

L

S

S

P

D

A

Q

E

E

K

M

E

L

R

R

Y

Y

A

N

R
|
R

H

Q

L

I

S

I

I

L

P

R

E

G

V

F

G

D

A

F

E

D

G

G

Q

Q

A

E

L

A

L

L

L

K

S

D

K

S

K

R

V

V

A

L

L

I

V

V

G

G

A

L

G
|
G

L

L

G

G

S

C

P

A

L

A

A

S

F

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

I

V

G

G

T

N

L

L

G

T

L

L

I

L

D
|
D

S
x
F

D

D

R

T

L

V

E

S

R

L

S

S

N

N

L

L

Q

Q

R
|
R

Q

Q

I

T

L

L

H

H

T

S

D

D

D

A

R

T

I

V

G

G

E

Q

L

P

K
|
K

V

V

S

E

S

S

A

A

A

R

K

D

S

A

L

L

Q

T

A

R

F

I

N

N

P

P

D

H

V

I

A

A

L

I

N

T

L

P

H

V

E

N

I

A

R
x
L

L

L

N

D

E

D

N

A

N

E

A

L

L

A

E

A

I

L

L

I

A

A

D

E

Y

H

D

D

L

L

V

V

I

L

D

D

G

C

S

T

D
|
D

N
|
N

L

V

A

A

T
x
V

R

R

Y

N

V

Q

V

L

S

N

D

A

A

G

S

C

T

F

L

A

S

K

I

V

P

P

M

L

I

V

Y

S

G

G

A

A

I

A

F

I

R

R

F

M

E

E

G

G

H

Q

V

I

S

T

A

V

F

F

W

T

P

-

N

-

G

-

P

-

S

-

G

-

P

-

C

-

Y

-

R

-

C

-

L

-

F

-

P

-

E

-

K

-

L

-

P

-

A

-

S

-

L

-

T

-

P

-

S

-

C

-

S

Y

E

E

V

A

G

G

V

V

L

M

G

A

V

P

L

L

P

I

G

G

V

V

I

I

G

G

T

S

I

L

M

Q

A

A

T

M

E

E

A

A

I

I

K

K

I

M

L

L

L

A

G

G

I

Y

G

G

D

K

P

P

L

A

I

S

G

G

R

K

L

I

L

V

T

M

Y

Y

N

D

A

A

L

M

D

T

C

C

S

Q

F

F

H

R

D

E

L

M

E

K

V

L

active site: R13 (= R130), D129 (= D246)
binding adenosine-5'-triphosphate: G39 (= G156), G40 (= G157), D61 (= D178), F62 (≠ S179), R72 (= R189), K85 (= K202), L108 (≠ R225), D129 (= D246), N130 (= N247), V133 (≠ T250)

P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
37% identity, 63% coverage: 127:367/380 of query aligns to 8:243/251 of P30138

query
sites
P30138

R

R

Y

Y

A

S

R

R

H

Q

L

I

S

L

I

L

P

D

E

D

V

I

G

A

A

L

E

D

G

G

Q

Q

A

Q

L

K

L

L

S

D

K

S

K

Q

V

V

A

L

L

I

V

I

G

G

A

L

G

G

L

L

G

G

S

T

P

P

L

A

A

A

F

L

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

T

T

L

L

G

V

L

L

I

A

D

D

S

D

D

D

R

D

L

V

E

H

R

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

I

I

L

L

H

F

T

T

D

T

D

E

R

D

I

I

G

D

E

R

L

P

K

K

V

S

S

Q

S

V

A

S

A

Q

K

Q

S

R

L

L

Q

T

A

Q

F

L

N

N

P

P

D

D

V

I

A

Q

L

L

N

T

L

A

H

L

E

Q

I

Q

R

R

L

L

N

T

E

G

N

E

N

A

A

L

L

K

E

D

I

A

L

V

A

A

D

R

Y

A

D

D

L

V

V

V

I

L

D

D

G

C

S

T

D

D

N

N

L

M

A

A

T

T

R

R

Y

Q

V

E

V

I

S

N

D

A

A

A

S

C

T

V

L

A

L

L

S

N

I

T

P

P

M

L

I

I

Y

T

G

A

A

S

I

A

F

V

R

G

F

F

E

G

G

G

H

Q

V

L

S

M

A

V

F

L

W

T

P

P

N

P

G

W

P

E

S

Q

G

G

G

-

P

-

C
|
C

Y

Y

R

R

C
|
C

L

L

F
x
W

P

P

E

D

K

N

L

Q

P

E

A

P

S

E

L

-

T

-

P

R

S

N

C
|
C

S

R

E

T

V

A

G

G

V

V

L

V

G

G

V

P

L

V

P

V

G

G

V

V

I

M

G

G

T

T

I

L

M

Q

A

A

T

L

E

E

A

A

I

I

K

K

I

L

L

L

L

S

G

G

I

I

G

E

D

T

P

P

L

-

I

A

G

G

R

E

L

L

L

R

T

L

Y

F

N

D

A

G

L

K

D

S

C

S

S

Q

F

W

H

R

D

S

L

L

E

A

V

L

P

R

A

R

N

A

P

S

H

G

C
|
C

E

P

Q

V

C
|
C

C169 (= C290) binding Zn(2+)
C172 (= C293) binding Zn(2+)
W174 (≠ F295) mutation to A: No adenylation of ThiS.
C184 (= C307) mutation to S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth.
C240 (= C364) binding Zn(2+)
C243 (= C367) binding Zn(2+)

1zfnA Structural analysis of escherichia coli thif (see paper)
37% identity, 63% coverage: 127:367/380 of query aligns to 8:243/244 of 1zfnA

query
sites
1zfnA

R

R

Y

Y

A

S

R
|
R

H

Q

L

I

S

L

I

L

P

D

E

D

V

I

G

A

A

L

E

D

G

G

Q

Q

A

Q

L

K

L

L

S

D

K

S

K

Q

V

V

A

L

L

I

V
x
I

G
|
G

A

L

G
|
G

L

L

G

G

S

T

P

P

L

A

A

A

F

L

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

T

T

L

L

G

V

L

L

I

A

D
|
D

S

D

D

D

R

D

L

V

E

H

R

L

S

S

N

N

L

L

Q

Q

R
|
R

Q
|
Q

I

I

L

L

H

F

T

T

D

T

D

E

R

D

I

I

G

D

E

R

L

P

K
|
K

V

S

S

Q

S

V

A

S

A

Q

K

Q

S

R

L

L

Q

T

A

Q

F

L

N

N

P

P

D

D

V

I

A

Q

L

L

N

T

L

A

H

L

E

Q

I

Q

R

R

L

L

N

T

E

G

N

E

N

A

A

L

L

K

E

D

I

A

L

V

A

A

D

R

Y

A

D

D

L

V

V

V

I

L

D

D

G

C

S
x
T

D
|
D

N

N

L

M

A

A

T
|
T

R

R

Y

Q

V

E

V

I

S

N

D

A

A

A

S

C

T

V

L

A

L

L

S

N

I

T

P

P

M

L

I

I

Y

T

G

A

A

S

I

A

F

V

R

G

F

F

E

G

G

G

H

Q

V

L

S

M

A

V

F

L

W

T

P

P

N

P

G

W

P

E

S

Q

G

G

G

-

P

-

C
|
C

Y

Y

R

R

C
|
C

L

L

F

W

P

P

E

D

K

N

L

Q

P

E

A

P

S

E

L

-

T

-

P

R

S

N

C

C

S

R

E

T

V

A

G

G

V

V

L

V

G

G

V

P

L

V

P

V

G

G

V

V

I

M

G

G

T

T

I

L

M

Q

A

A

T

L

E

E

A

A

I

I

K

K

I

L

L

L

L

S

G

G

I

I

G

E

D

T

P

P

L

-

I

A

G

G

R

E

L

L

L

R

T

L

Y

F

N

D

A

G

L

K

D

S

C

S

S

Q

F

W

H

R

D

S

L

L

E

A

V

L

P

R

A

R

N

A

P

S

H

G

C
|
C

E

P

Q

V

C
|
C

active site: R11 (= R130), D127 (= D246)
binding adenosine-5'-triphosphate: I34 (≠ V153), G35 (= G154), G37 (= G156), G38 (= G157), D59 (= D178), R70 (= R189), Q71 (= Q190), K83 (= K202), T126 (≠ S245), D127 (= D246), T131 (= T250)
binding zinc ion: C169 (= C290), C172 (= C293), C240 (= C364), C243 (= C367)

1zud3 Structure of this-thif protein complex (see paper)
36% identity, 63% coverage: 127:367/380 of query aligns to 8:238/240 of 1zud3

query
sites
1zud3

R

R

Y

Y

A

S

R
|
R

H

Q

L

I

S
x
L

I

L

P
x
D

E

D

V

I

G

A

A

L

E

D

G

G

Q

Q

A

Q

L

K

L

L

S

D

K

S

K

Q

V

V

A

L

L

I

V

I

G

G

A

L

G

G

L

L

G

G

S

T

P

P

L

A

A

A

F

L

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

T

T

L

L

G

V

L

L

I

A

D

D

S

D

D

D

R

D

L

V

E

H

R

L

S

S

N

N

L

L

Q

Q

R

R

Q

Q

I

I

L

L

H

F

T

T

D

T

D

E

R

D

I

I

G

D

E

R

L

P

K

K

V

S

S

Q

S

V

A

S

A

Q

K

Q

S

R

L

L

Q

T

A

Q

F

L

N

N

P

P

D

D

V

I

A

Q

L

L

N

T

L

A

H

L

E

Q

I

Q

R

R

L

L

N

T

E

G

N

E

N

A

A

L

L

K

E

D

I

A

L

V

A

A

D

R

Y

A

D

D

L

V

V

V

I

L

D

D

G

C

S

T

D
|
D

N

N

L

M

A

A

T

T

R

R

Y

Q

V

E

V

I

S

N

D

A

A

A

S

C

T

V

L

A

L

L

S

N

I

T

P

P

M

L

I

I

Y

T

G

A

A

S

I

A

F

V

R

G

F

F

E

G

G

G

H

Q

V

L

S

M

A

V

F

L

W

T

P

P

N

P

G

W

P

E

S

Q

G

G

G

-

P

-

C
|
C

Y

Y

R

R

C

C

L

L

F

W

P

P

E

D

K

N

L

Q

P

E

A

P

S

T

L

A

T

G

P

V

S

V

C

G

S

P

E

V

V

V

G

-

V

-

L

-

G

-

V

-

L

-

P

-

G

G

V

V

I

M

G

G

T

T

I

L

M

Q

A

A

T

L

E

E

A

A

I

I

K

K

I

L

L

L

L

S

G

G

I

I

G

E

D

T

P

P

L

-

I

A

G

G

R

E

L

L

L

R

T

L

Y

F

N

D

A

G

L

K

D

S

C

S

S

Q

F

W

H

R

D

S

L

L

E

A

V

L

P

R

A

R

N

A

P

S

H

G

C
|
C

E

P

Q

V

C
|
C

active site: R11 (= R130), D127 (= D246)
binding calcium ion: L14 (≠ S133), D16 (≠ P135)
binding zinc ion: C169 (= C290), C235 (= C364), C238 (= C367)

O42939 Ubiquitin-activating enzyme E1-like; Pmt3-activating enzyme subunit 2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
35% identity, 43% coverage: 147:308/380 of query aligns to 25:182/628 of O42939

query
sites
O42939

S

S

K

A

K

K

V

V

A

L

L

L

V

V

G

G

A

A

G

G

L

I

G

G

S

C

P

E

L

L

A

L

F

K

Y

N

L

L

A

L

A

M

A

S

G

G

I

V

G

K

T

E

L

V

G

H

L

I

I

I

D

D

S

L

D

D

R

T

L

I

E

D

R

L

S

S

N

N

L

L

Q

N

R

R

Q

Q

I

F

L

L

H

F

T

R

D

K

R

H

I

V

G

K

E

Q

L

P

K

K

V

A

S

I

S

V

A

A

K

K

S

T

L

A

Q

S

A

S

F

F

N

N

P

P

D

N

V

V

A

K

L

L

-

E

-

A

-

Y

-

H

-

A

N

N

L

I

H

K

E

E

I

D

R

R

L

F

N

N

E

-

N

-

A

-

L

V

E

A

I

W

L

F

A

R

D

Q

Y

F

D

D

L

L

V

V

I

F

D

N

G

A

S

L

D

D

N

N

L

L

A

D

T

A

R

R

Y

R

V

H

V

V

S

N

D

K

A

Q

S

C

T

L

L

L

L

A

S

S

I

V

P

P

M

L

I

I

Y

E

G

S

A

G

I

T

F

T

R

G

F

F

E

L

G

G

H

Q

V

V

S

Q

A

V

F

I

W

I

P

-

N

H

G

G

P

K

S

T

G

E

G

-

P

-

C

C

Y

Y

R

D

C

C

L

-

F

-

P

N

E

P

K

K

L

E

P

P

A

P

S

K

L

T

T

Y

P

P

S

V

C

C

S

T

Sites not aligning to the query:

559 modified: Phosphoserine
563 modified: Phosphoserine

3h5nA Crystal structure of e. Coli mccb + atp (see paper)
24% identity, 65% coverage: 121:367/380 of query aligns to 85:337/338 of 3h5nA

query
sites
3h5nA

S

N

P

S

A

T

E

E

K

N

E

N

R

R

Y

Y

A

S

R

R

H

N

-

F

L

L

S

H

I

Y

P

Q

E

S

V

Y

G

G

A

A

E

N

G

P

-

V

-

L

-

V

Q

Q

A

D

L

K

L

L

L

K

S

N

K

A

K

K

V

V

A

V

L

I

V

L

G

G

A

C

G
|
G

G

G

L

I

G

G

S

N

P

H

L

V

A

S

F

V

Y

I

L

L

A

A

A

T

A

S

G

G

I

I

G

G

T

E

L

I

G

I

L

L

I

I

D
|
D

S

N

D

D

R

Q

L

I

E

E

R

N

S

T

N
|
N

L

L

Q

T

R
|
R

Q
|
Q

I

V

L

L

H

F

T

S

D

E

D

D

R

D

I

V

G

G

E

K

L

N

K
|
K

V

T

S

E

S

V

A

I

A

K

K

R

S

E

L

L

Q

L

A

K

F

R

N

N

P

S

D

E

V

I

A

S

L

V

N

S

L

E

H

I

E

A

I

L

R
x
N

L
x
I

N

N

E

D

N

Y

N

T

A

D

L

L

E

H

I

K

L

V

A

P

D

E

Y

A

D

D

L

I

V

W

I

V

D

V

G

S

S
x
A

D
|
D

-
x
H

-

P

-

F

-

N

-

L

-

I

N

N

L

W

A

V

T

N

R

K

Y

Y

V

C

V

V

S

R

D

A

A

N

S

Q

T

-

L

-

S

-

I

-

P

P

M

Y

I

I

Y

N

G

A

A

G

I

-

F

-

R

-

F

Y

E

V

G

N

H

D

V

I

S

A

A

V

F

F

W

G

P

P

-

L

N

Y

G

V

P

P

S

G

G

K

G

T

P

G

C
|
C

Y

Y

R

E

C
|
C

L

Q

F

K

P

K

E

E

K

N

L

I

-

D

-

H

P

K

A

I

S

K

L

L

T

I

P

N

S

S

C

R

S

F

E

K

V

P

G

A

V

T

L

F

G

A

V

P

L

V

P

N

G

N

V

V

I

A

G

A

T

A

I

L

M

C

A

A

T

A

E

D

A

V

I

I

K

K

I

F

L

I

L

G

G

K

I

Y

G

S

D

E

P

P

L

L

-

S

I

L

G

N

R

K

L

R

L

I

T

G

Y

I

N

W

A

S

L

D

D

E

C

I

S

K

F

I

H

H

D

S

L

Q

E

N

V

M

P

G

A

R

N

S

P

P

H

V

C
|
C

E

S

Q

V

C
|
C

active site: R157 (= R189)
binding adenosine-5'-triphosphate: G124 (= G156), D146 (= D178), N154 (= N186), R157 (= R189), Q158 (= Q190), K170 (= K202), N193 (≠ R225), I194 (≠ L226), A213 (≠ S245), D214 (= D246), H215 (vs. gap)
binding zinc ion: C257 (= C290), C260 (= C293), C334 (= C364), C337 (= C367)

3h9jA Crystal structure of e. Coli mccb + ampcpp + semet mcca (see paper)
24% identity, 65% coverage: 121:367/380 of query aligns to 85:337/339 of 3h9jA

query
sites
3h9jA

S

N

P

S

A

T

E

E

K

N

E

N

R

R

Y

Y

A

S

R

R

H

N

-

F

L

L

S

H

I

Y

P

Q

E

S

V

Y

G

G

A

A

E

N

G

P

-

V

-

L

-

V

Q

Q

A

D

L

K

L

L

L

K

S

N

K

A

K

K

V

V

A

V

L

I

V

L

G

G

A

C

G
|
G

L

I

G

G

S

N

P

H

L

V

A

S

F

V

Y

I

L

L

A

A

A

T

A

S

G

G

I

I

G

G

T

E

L

I

G

I

L

L

I

I

D
|
D

S

N

D
|
D

R

Q

L

I

E

E

R

N

S

T

N

N

L

L

Q

T

R
|
R

Q

Q

I

V

L

L

H

F

T

S

D

E

D

D

R

D

I

V

G

G

E

K

L

N

K
|
K

V

T

S

E

S

V

A

I

A

K

K

R

S

E

L

L

Q

L

A

K

F

R

N

N

P

S

D

E

V

I

A

S

L

V

N

S

L

E

H

I

E

A

I

L

R
x
N

L
x
I

N

N

E

D

N

Y

N

T

A

D

L

L

E

H

I

K

L

V

A

P

D

E

Y

A

D

D

L

I

V

W

I

V

D

V

G

S

S
x
A

D
|
D

-
x
H

-

P

-

F

-

N

-

L

-

I

N

N

L

W

A

V

T

N

R

K

Y

Y

V

C

V

V

S

R

D

A

A

N

S

Q

T

-

L

-

S

-

I

-

P

P

M

Y

I

I

Y

N

G

A

A

G

I

-

F

-

R

-

F

Y

E

V

G

N

H

D

V

I

S

A

A

V

F

F

W

G

P

P

-

L

N

Y

G

V

P

P

S

G

G

K

G

T

P

G

C
|
C

Y

Y

R

E

C

C

L

Q

F

K

P

K

E

E

K

N

L

I

-

D

-

H

P

K

A

I

S

K

L

L

T

I

P

N

S

S

C

R

S

F

E

K

V

P

G

A

V

T

L

F

G

A

V

P

L

V

P

N

G

N

V

V

I

A

G

A

T

A

I

L

M

C

A

A

T

A

E

D

A

V

I

I

K

K

I

F

L

I

L

G

G

K

I

Y

G

S

D

E

P

P

L

L

-

S

I

L

G

N

R

K

L
x
R

L

I

T
x
G

Y

I

N

W

A

S

L

D

D

E

C

I

S

K

F

I

H

H

D

S

L

Q

E

N

V

M

P

G

A

R

N

S

P

P

H

V

C
|
C

E

S

Q

V

C
|
C

active site: R157 (= R189)
binding diphosphomethylphosphonic acid adenosyl ester: G124 (= G156), G125 (= G157), D146 (= D178), D148 (= D180), R157 (= R189), K170 (= K202), N193 (≠ R225), I194 (≠ L226), A213 (≠ S245), D214 (= D246), H215 (vs. gap)
binding zinc ion: C257 (= C290), C334 (= C364), C337 (= C367)
binding : R313 (≠ L343), G315 (≠ T345)

O65041 NEDD8-activating enzyme E1 catalytic subunit; RUB-activating enzyme; Ubiquitin-activating enzyme E1-like protein; EC 6.2.1.64 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 42% coverage: 149:308/380 of query aligns to 48:216/454 of O65041

query
sites
O65041

K

R

V

I

A

L

L

V

V

I

G

G

A

A

G

G

L

L

G

G

S

C

P

E

L

L

A

L

F

K

Y

D

L

L

A

A

A

L

A

S

G

G

I

F

G

R

T

N

L

L

G

E

L

V

I

I

D

D

S

M

D

D

R

R

L

I

E

E

R

V

S

T

N

N

L

L

Q

N

R

R

Q

Q

I

F

L

L

H

F

T

R

D

I

D

E

R

D

I

V

G

G

E

K

L

P

K

K

V

A

S

E

S

V

A

A

K

K

S

R

L

V

Q

M

A

E

F

R

N

V

P

S

D

G

V

V

A

E

L

I

N

V

L

P

H

H

E

F

I

S

R

R

L

I

N

-

E

E

N

D

N

K

A

E

L

I

E

E

I

F

L

Y

A

N

D

D

Y

F

D

N

L

I

V

I

I

A

D

L

G

G

S

L

D

D

N

S

L

I

-

E

A

A

T

R

R

K

Y

Y

V

I

V

N

S

G

D

V

A

A

S

C

T

G

L

F

L

L

S

E

I

Y

-

N

-

E

-

D

-

T

-

P

-

K

-

R

-

E

-

T

-

I

-

K

P

P

M

M

I

V

Y

D

G

G

A

G

I

T

F

E

R

G

F

F

E

K

G

G

H

H

V

A

S

R

A

V

F

I

W

L

P

-

N

-

G

-

P

P

S

G

G

V

G

T

P

P

C

C

Y

F

R

E

C

C

-

T

-

I

-

Y

L

L

F

F

P

P

E

-

K

-

L

-

P

P

A

Q

S

V

L

K

T

F

P

P

S

L

C
|
C

S

T

C215 (= C307) mutation to A: Loss of binding to RUB1.

6mxvB The crystal structure of a rhodanese-like family protein from francisella tularensis subsp. Tularensis schu s4
32% identity, 31% coverage: 8:124/380 of query aligns to 18:133/251 of 6mxvB

query
sites
6mxvB

S

S

R

R

L

I

R

Q

E

E

S

-

L

C

S

S

R

V

I

D

S

D

V

I

E

Q

E

K

A

M

R

N

R

E

K

T

Q

Q

K

T

A

L

G

D

V

G

K

L

L

L

I

I

D

D

I

T

R

R

D

E

A

E

E

S

E

E

T

V

A

A

K

N

G

G

S

Y

P

I

V

P

G

N

A

A

V

I

R

H

I

L

S

S

R

K

S

G

F

I

L

I

E

E

L

S

Q

A

I

I

E

E

N

S

V

A

A

V

P

P

D

N

A

K

D

N

T

Q

E

K

L

M

M

Y

V

F

L

Y

C

C

A

G

S

G

D

G

T

F

R

R

A

S

L

A

F

L

A

V

A

A

D

D

D

K

L

L

N

R

R

E

L

M

G

G

Y

Y

S

K

S

N

V

V

H

I

W

S

V

V

D

D

G

G

F

W

Q

R

A

A

W

W

E

N

A

A

A

K

G

G

L

Y

P

P

V

T

E

V

K

S

H

P

R

N

Q

Q

L

F

S

R

P

P

A

N

E

E

Sites not aligning to the query:

binding magnesium ion: 179, 251

Query Sequence

>WP_011970838.1 NCBI__GCF_000017145.1:WP_011970838.1
MLRQERLSRLRESLSRISVEEARRKQKAGVKLIDIRDAEETAKGSPVGAVRISRSFLELQ
IENVAPDADTELMVLCASDTRALFAADDLNRLGYSSVHWVDGGFQAWEAAGLPVEKHRQL
SPAEKERYARHLSIPEVGAEGQALLLSKKVALVGAGGLGSPLAFYLAAAGIGTLGLIDSD
RLERSNLQRQILHTDDRIGELKVSSAAKSLQAFNPDVALNLHEIRLNENNALEILADYDL
VIDGSDNLATRYVVSDASTLLSIPMIYGAIFRFEGHVSAFWPNGPSGGPCYRCLFPEKLP
ASLTPSCSEVGVLGVLPGVIGTIMATEAIKILLGIGDPLIGRLLTYNALDCSFHDLEVPA
NPHCEQCQSNRDLPRMRAGL

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