SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing CA265_RS12640 FitnessBrowser__Pedo557:CA265_RS12640 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)
49% identity, 61% coverage: 4:228/368 of query aligns to 9:234/271 of Q72J02

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Q72J02

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C192 (= C186) 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.

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)
32% identity, 98% coverage: 5:364/368 of query aligns to 68:474/482 of O59954

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O59954

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G82 (≠ A19) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
G100 (= G37) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
R130 (= R67) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
C185 (≠ G122) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
E215 (= E152) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
G264 (= G197) mutation to S: In cnxF142ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.

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)
34% identity, 93% coverage: 5:345/368 of query aligns to 71:427/453 of Q9VLJ8

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Sites not aligning to the query:

62 modified: Phosphothreonine

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)
34% identity, 97% coverage: 4:360/368 of query aligns to 45:428/440 of P38820

query
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P38820

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Q

Q

E

Q

Q

S

Y

L

T

R

I

T

-

F

-

K

-

M

-

R

-

G

-

R

-

Q

-

E

-

K

N

C

I

L

S

C

H

C

G

G

G

K

G

N

Y

R

T

T

L

I

P

T

K

K

T

E

V

A

D

I

E

E

F

K

L

G

N

E

M

I

D

N

Y

Y

Q

E

-

L

-

F

-

C

-

G

-

A

-

R

-

N

-

Y

D

N

T

V

S

C

E

E

G

-

P

P

Q

D

G

E

Y

R

I

I

E

S

I

V

D

D

A

A

G

F

E

Q

L

R

V

I

K

Y

L

K

Q

D

-

E

-

F

L

L

E

A

S

K

T

H

I

I

L

F

I

L

D

D

V

V

R

R

E

P

R

S

H

H

E

H

V

Y

P

E

I

I

L

S

D

H

K

F

Q

P

I

E

F

A

T

V

Q

N

V

I

P

P

M

I

S

K

E

N

F

L

G

R

A

D

F

M

M

N

S

G

-

D

-

L

K

K

E

K

F

L

Y

Q

Q

E

K

K

-

L

-

P

-

S

-

V

-

E

-

K

-

D

-

S

H

N

V

I

V

V

L

I

I

L

C
|
C

Q

R

H

Y

G

G

I

N

R

D

S

S

V

Q

A

L

A

A

A

T

E

R

A

L

M

L

Q

K

E

D

K

K

Y

F

G

G

D

-

A

F

K

S

K

N

I

V

Y

R

S

D

L

V

K

R

G

G

I

Y

V

F

K

K

C225 (= C186) mutation C->A,S: Abolishes adenylyltransferase activity but not sulfurtransferase activity.
C397 (= C328) mutation C->A,S: Abolishes sulfurtransferase activity but not adenylyltransferase activity.

6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
33% identity, 98% coverage: 4:364/368 of query aligns to 12:415/423 of 6yubA

query
sites
6yubA

E

E

R

R

Y

Y

N

S

R

R

Q

Q

I

M

I

I

L

V

K

P

G

G

F

M

G

G

E

K

E

E

A

G

Q

Q

Q

L

K

R

L

L

L

M

R

N

A

A

K

K

V

V

L

L

V

I

I

I

G

G

A

A

G

G

L

L

G

G

C

C

P

P

A

A

L

A

Q

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

H

T

I

I

G

G

I

I

V

V

D

D

D

G

D

D

T

S

I

V

S

E

L

T

S

S

N

N

L

L

H

H

R

R

Q

Q

I

V

L

A

F

H

T

A

T

T

A

K

D

R

I

V

G

G

K

M

L

L

K

K

V

V

E

D

V

S

A

L

A

I

K

T

R

H

L

L

Q

I

E

E

M

I

N

N

T

P

Q

L

I

P

G

V

I

Y

I

V

R

P

H

Y

P

R

I

F

R

D

L

L

Q

T

K

P

N

Q

N

N

I

A

L

A

D

Q

I

I

V

I

S

K

R

P

Y

W

D

D

Y

V

I

I

L

L

D

D

G

C

T

T

D

D

N

N

F

P

E

A

S

T

R

R

Y

Y

L

L

I

I

N

S

D

D

A

V

C

C

A

V

L

L

N

G

K

K

P

P

L

L

I

V

F

S

A

A

V

S

S

V

G

Q

F

K

E

S

G

G

Q

Q

L

L

A

I

I

V

F

L

N

N

A

C

P

P

D

P

H

T

L

P

T

Q

P

G

S

V

T

V

N

N

-

K

-

A

-

P

-
x
C

Y

Y

R

R

D
x
C

L

C

F

F

P

K

I

K

P

P

P

-

D

-

K

-

G

-

E

-

V

-

A

-

N

-

C

-

A

-

E

-

N

-

G

G

I

I

I

M

G

G

V

P

L

V

P

V

G

G

I

M

L

M

G

G

T

V

M

A

A

Q

A

A

A

G

E

E

T

A

I

I

K

K

L

I

I

L

A

V

-

S

-

Q

-

L

-

H

-

M

-

P

K

K

I

E

G

G

Q

E

A

E

L

V

T

S

-

P

N

E

K

K

I

N

L

L

S

V

Y

Q

N

P

L

T

L

L

T

L

Q

I

E

Y

Q

T

Y

Y

T

D

I

L

N

N

-

S

-

A

-

I

-

G

-

P

-

Y

-

S

-

F

-

R

-

A

I

L

S

K

H

M

G

G

-

R

-

K

-

D

-
x
C

-

F

-

A

-
x
C

G

G

Y

E

T

N

L

S

P

T

K

L

T

T

V

L

D

D

E

G

F

I

L

K

-

S

-

G

N

N

M

P

D

N

Y

Y

-

V

-

G

-

N

-

M

-

T

Q

Q

D

S

T

T

S

N

E

L

G

A

P

P

Q

E

G

D

Y

R

I

I

E

T

I

A

D

T

A

A

-

Y

G

N

E

E

L

K

V

R

K

R

L

N

Q

G

Q

E

L

L

E

G

S

E

T

H

I

I

L

L

I

L

D

D

V

T

R

R

E

E

R

K

H

E

E

H

V

F

P

S

I

F

L

G

D

S

K

I

Q

P

I

G

F

A

T

V

Q

N

V

V

P

P

M

F

S

S

E

K

F

F

G

L

A

V

-

K

-

A

-

S

-

I

-

K

-

R

-

P

-

A

-

E

-

L

F

P

M

M

S

Q

K

P

E

A

F

S

Y

D

Q

E

K

A

H

P

V

I

V

V

L

V

I

V

C

C

Q

R

H

R

G

G

I

Q

R

D

S

S

V

Q

A

E

A

V

E

E

A

K

M

L

Q

K

E

E

-

L

-

G

-

L

K

D

Y

N

G

G

D

G

A

K

K

R

K

K

I

I

Y

M

S

D

L

I

K

V

G

G

I

M

V

K

K

A

C

W

R

R

D

D

H

E

binding zinc ion: C183 (vs. gap), C186 (≠ D172), C266 (vs. gap), C269 (vs. gap)

6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
44% identity, 57% coverage: 4:211/368 of query aligns to 13:212/289 of 6yubB

query
sites
6yubB

E

E

R

R

Y

Y

N

S

R

R

Q

Q

I

M

I

I

L

V

K

P

G

G

F

M

G

G

E

K

E

E

A

G

Q

Q

Q

L

K

R

L

L

L

M

R

N

A

A

K

K

V

V

L

L

V

I

I

I

G

G

A

A

G

G

L

L

G

G

C

C

P

P

A

A

L

A

Q

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

H

T

I

I

G

G

I

I

V

V

D

D

D

G

D

D

T

S

I

V

S

E

L

T

S

S

N

N

L

L

H

H

R

R

Q

Q

I

V

L

A

F

H

T

A

T

T

A

K

D

R

I

V

G

G

K

M

L

L

K

K

V

V

E

D

V

S

A

L

A

I

K

T

R

H

L

L

Q

I

E

E

M

I

N

N

T

P

Q

L

I

P

G

V

I

Y

I

V

R

P

H

Y

P

R

I

F

R

D

L

L

Q

T

K

P

N

Q

N

N

I

A

L

A

D

Q

I

I

V

I

S

K

R

P

Y

W

D

D

Y

V

I

I

L

L

D

D

G

C

T

T

D

D

N

N

F

P

E

A

S

T

R

R

Y

Y

L

L

I

I

N

S

D

D

A

V

C

C

A

V

L

L

N

G

K

K

P

P

L

L

I

V

F

S

A

A

V

S

S

V

G

Q

F

K

E

S

G

G

Q

Q

L

L

A

I

I

V

F

L

N

N

A

C

P

P

D

P

H

T

L

P

T

Q

P

G

S

V

T

V

N

N

Y

K

R

K

D

-

L

-

F

-

P

-

I

-

P

-

D

-

K

A

G

A

E

P

V
x
C

A

Y

N

R

C
|
C

A

C

E

F

N

K

G

G

I

I

I

M

G

G

V

P

L

V

P

V

G

G

I

M

L

M

G

G

T

V

M

A

A

Q

A

A

A

G

E

E

T

A

I

I

K

K

L

I

I

L

binding zinc ion: C184 (≠ V183), C187 (= C186)

Sites not aligning to the query:

binding zinc ion: 265

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)
41% identity, 61% coverage: 5:228/368 of query aligns to 62:281/460 of O95396

query
sites
O95396

R

R

Y

Y

N

S

R

R

Q

Q

I

L

I

V

L

L

K

P

G

E

F

L

G

G

E

V

E

H

A

G

Q

Q

Q

L

K

R

L

L

L

G

R

T

A

A

K

C

V

V

L

L

V

I

I

V

G

G

A

C

G

G

L

L

G

G

C

C

P

P

A

L

L

A

Q

Q

Y

Y

L

L

A

A

G

G

I

V

G

G

H

R

I

L

G

G

I

L

V

V

D

D

D

Y

D

D

T

V

I

V

S

E

L

M

S

S

N

N

L

L

H

A

R

R

Q

Q

I

V

L

L

F

H

T

G

T

E

A

A

D

L

I

A

G

G

K

Q

L

A

K

K

V

A

E

F

V

S

A

A

K

A

R

S

L

L

Q

R

E

R

M

L

N

N

T

S

Q

A

I

V

G

E

I

C

I

V

R

P

H

Y

P
x
T

I
x
Q

R
x
A

L
|
L

Q
x
T

K
x
P

N
x
A

N
x
T

I
x
A

L
|
L

D
|
D

I
x
L

V
|
V

S
x
R

R
|
R

Y
|
Y

D
|
D

Y
x
V

I
x
V

L
x
A

D
|
D

G
x
C

T
x
S

D
|
D

N
|
N

F
x
V

E
x
P

S
x
T

R
|
R

Y
|
Y

L
|
L

I
x
V

N
|
N

D
|
D

A
|
A

C
|
C

A
x
V

L
|
L

L
x
A

N
x
G

K
x
R

P
|
P

L
|
L

I
x
V

F
x
S

A
|
A

A
x
S

V
x
A

S
x
L

G
x
R

F
|
F

E
|
E

G
|
G

Q
|
Q

L
x
I

A
x
T

I
x
V

F
x
Y

N

-

A

-

P

-

D

-

H
|
H

L
x
Y

T
x
D

P
x
G

S
x
G

T
x
P

N
x
C

Y
|
Y

R
|
R

D
x
C

L
x
I

F
|
F

P
|
P

I
x
Q

P
|
P

D
x
P

K
x
A

G
x
E

E
x
T

V
|
V

A
x
T

N
|
N

C
|
C

A

A

E

D

N

G

G

G

I

V

I

L

G

G

V

V

L

V

P

T

G

G

I

V

L

L

G

G

T

C

M

L

A

Q

A

A

A

L

E

E

T

V

I

L

K

K

L

I

I

A

A

A

K

G

I

L

G

G

Q

P

A

S

L

Y

T

S

N

G

K

S

I

L

L

L

S

L

Y

F

N

D

L

A

L

L

158:238 (vs. 101:185, 40% identical) Interaction with NFS1
C239 (= C186) mutation to A: Impairs sulfurtransferase activity.

Sites not aligning to the query:

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

D4GSF3 SAMP-activating enzyme E1; Ubiquitin-like activating enzyme of archaea; Ubl-activating enzyme; EC 2.7.7.- from Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) (see paper)
41% identity, 63% coverage: 4:235/368 of query aligns to 11:237/270 of D4GSF3

query
sites
D4GSF3

E

D

R

R

Y

Y

N

S

R

R

Q

H

I

I

L

M

K

D

G

E

F

V

G

G

E

P

E

E

A

G

Q

Q

Q

G

K

R

L

L

R

S

A

S

K

R

V

V

L

V

V

V

I

V

G

G

A

A

G

G

L

L

G

G

C

A

P

P

A

A

L

I

Q

Q

Y

Y

L

L

A

A

A

V

G

G

I

V

G

G

H

E

I

L

G

V

I

V

V

V

D

D

T

V

I

V

S

E

L

R

S

S

N

N

L

L

H

Q

R

R

Q

Q

I

V

L

V

F

H

T

C

T

D

A

D

D

D

I

V

G

G

K

T

L

P

K

K

V

A

E

E

V

S

A

A

K

A

R

F

L

V

Q

R

E

G

M

L

N

N

T

P

Q

D

I

V

G

S

I

V

I

E

R

P

H

V

P

E

I

A

R

R

L

V

Q

D

K

K

N

S

N

N

I

V

L

H

D

E

I

V

V

V

S

A

R

G

Y

S

D

D

Y

V

I

V

L

V

D

D

G

A

T

S

D

D

N

N

F

F

E

P

S

T

R

R

Y

Y

L

L

I

L

N

N

D

D

A

V

C

C

A

R

L

F

L

E

N

G

K

I

P

P

L

L

I

V

F

H

A

G

A

A

V

I

S

Y

G

K

F

F

E

E

G

G

Q

Q

L

A

A

T

I

T

F

L

N

-

A

V

P

P

D

D

H

-

L

-

T

-

P

-

S

G

T

P

N

C

Y

Y

R

R

D

C

L

L

F

F

P

P

I

E

P

A

P

P

D

E

K

P

G

G

E

T

V

V

A

P

N

D

C
|
C

A

A

E

T

N

T

G

G

I

V

I

L

G

G

V

V

L

L

P

P

G

G

I

T

L

V

G

G

T

C

M

I

A

Q

A

A

A

T

E

E

T

A

I

M

K

K

L

L

I

L

A

L

K

D

I

E

G

G

Q

E

A

A

L

L

T

D

N

G

K

R

I

L

L

L

S

F

Y

Y

N

D

L

A

L

M

T

D

Q

M

E

T

Q

F

Y

E

T

T

I

V

C188 (= C186) 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, 61% coverage: 5:229/368 of query aligns to 11:230/249 of P12282

query
sites
P12282

R

R

Y

Y

N

N

R
|
R

Q

Q

I

I

L

L

K

R

G

G

F

F

G

D

E

F

E

D

A

G

Q

Q

Q

E

K

A

L

L

L

K

R

D

A

S

K

R

V

V

L

L

V

I

I

V

G

G

A

L

G

G

L

L

G

G

C
|
C

P

A

A

A

L

S

Q

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

I

V

G

G

H

N

I

L

G

T

I

L

V

L

D

D

D

F

D

D

T

T

I

V

S

S

L

L

S

S

N

N

L

L

H

Q

R
|
R

Q

Q

I

T

L

L

F

H

T

S

T

D

A

A

D

T

I

V

G

G

K

Q

L

P

K

K

V

V

E

E

V

S

A

A

A

R

K

D

R

A

L

L

Q

T

E

R

M

I

N

N

T

P

Q

H

I

I

G

A

I

I

I

T

R

P

H

V

P

N

I

A

R

L

L

L

Q

D

K

D

N

A

N

E

I

L

L

A

D

A

I

L

V

I

S

A

R

E

Y

H

D

D

Y

L

I

V

L

L

D

D

G
x
C

T

T

D
|
D

N

N

F

V

E

A

S

V

R

R

Y

N

L

Q

I

L

N

N

D

A

A

G

C
|
C

A

F

L

A

N

K

K

V

P

P

L

L

I

V

F

S

A

G

A

A

V

A

S

I

G

R

F

M

E

E

G

G

Q

Q

L

I

A

T

I

V

F

F

N

T

A

Y

P

Q

D

D

H

G

L

E

T

P

P
x
C

S

Y

T

R

N
x
C

Y

L

R

S

D

R

L

L

F

F

P

-

I

-

P

-

D

-

K

-

G

G

E

E

V

N

A

A

-

L

N

T

C
|
C

A

V

E

E

N

A

G

G

I

V

I

M

G

A

V

P

L

L

P

I

G

G

I

V

L

I

G

G

T

S

M

L

A

Q

A

A

A

M

E

E

T

A

I

I

K

K

L

M

I

L

A

A

K

G

I

Y

G

G

Q

K

A

P

L

A

T

S

N

G

K

K

I

I

L

V

S

M

Y

Y

N

D

L

A

L

M

T

T

R14 (= R8) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
C44 (= C38) mutation to A: No effect.
R73 (= R67) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
C128 (≠ G122) mutation to A: No effect.; mutation to Y: No activity.
D130 (= D124) mutation to A: No activity.; mutation to E: Substantially reduced activity.
C142 (= C136) mutation to A: No effect.
C172 (≠ P166) mutation to A: No zinc bound and no enzyme activity.
C175 (≠ N169) mutation to A: No zinc bound and no enzyme activity.
C187 (= C186) mutation to A: No effect.

Sites not aligning to the query:

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

1zfnA Structural analysis of escherichia coli thif (see paper)
45% identity, 57% coverage: 5:214/368 of query aligns to 8:212/244 of 1zfnA

query
sites
1zfnA

R

R

Y

Y

N

S

R
|
R

Q

Q

I

I

I

L

L

L

K

D

G

D

F

I

G

A

E

L

E

D

A

G

Q

Q

K

K

L

L

R

D

A

S

K

Q

V

V

L

L

V

I

I
|
I

G
|
G

A

L

G
|
G

L

L

G

G

C

T

P

P

A

A

L

A

Q

L

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

H

T

I

L

G

V

I

L

V

A

D
|
D

D

D

T

D

I

V

S

H

L

L

S

S

N

N

L

L

H

Q

R
|
R

Q
|
Q

I

I

L

L

F

F

T

T

A

E

D

D

I

I

G

D

K

R

L

P

K
|
K

V

S

E

Q

V

V

A

S

A

Q

K

Q

R

R

L

L

Q

T

E

Q

M

L

N

N

T

P

Q

D

I

I

G

Q

I

L

I

T

R

A

H

L

P

Q

I

Q

R

R

L

L

Q

T

K

G

N

E

N

A

I

L

L

K

D

D

I

A

V

V

S

A

R

R

Y

A

D

D

Y

V

I

V

L

L

D

D

G

C

T
|
T

D
|
D

N

N

F

M

E

A

S
x
T

R

R

Y

Q

L

E

I

I

N

N

D

A

A

A

C

C

A

V

L

A

L

L

N

N

K

T

P

P

L

L

I

I

F

T

A

A

A

S

V

A

S

V

G

G

F

F

E

G

G

G

Q

Q

L

L

A

M

I

V

F

L

N

T

A

P

P

P

D

W

H

E

L

-

T

-

P

-

S

Q

T

G

N
x
C

Y

Y

R

R

D
x
C

L

L

F

W

P

-

I

-

P

P

P

D

D

N

K

Q

G

E

E

P

V

E

A

R

N

N

C

C

A

R

E

T

N

A

G

G

I

V

G

G

V

P

L

V

P

V

G

G

I

V

L

M

G

G

T

T

M

L

A

Q

A

A

A

L

E

E

T

A

I

I

K

K

L

L

I

L

A

S

K

G

I

I

active site: R11 (= R8), D127 (= D124)
binding adenosine-5'-triphosphate: I34 (= I31), G35 (= G32), G37 (= G34), G38 (= G35), D59 (= D56), R70 (= R67), Q71 (= Q68), K83 (= K80), T126 (= T123), D127 (= D124), T131 (≠ S128)
binding zinc ion: C169 (≠ N169), C172 (≠ D172)

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)
45% identity, 57% coverage: 5:214/368 of query aligns to 8:212/251 of P30138

query
sites
P30138

R

R

Y

Y

N

S

R

R

Q

Q

I

I

I

L

L

L

K

D

G

D

F

I

G

A

E

L

E

D

A

G

Q

Q

K

K

L

L

R

D

A

S

K

Q

V

V

L

L

V

I

I

I

G

G

A

L

G

G

L

L

G

G

C

T

P

P

A

A

L

A

Q

L

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

H

T

I

L

G

V

I

L

V

A

D

D

T

D

I

V

S

H

L

L

S

S

N

N

L

L

H

Q

R

R

Q

Q

I

I

L

L

F

F

T

T

A

E

D

D

I

I

G

D

K

R

L

P

K

K

V

S

E

Q

V

V

A

S

A

Q

K

Q

R

R

L

L

Q

T

E

Q

M

L

N

N

T

P

Q

D

I

I

G

Q

I

L

I

T

R

A

H

L

P

Q

I

Q

R

R

L

L

Q

T

K

G

N

E

N

A

I

L

L

K

D

D

I

A

V

V

S

A

R

R

Y

A

D

D

Y

V

I

V

L

L

D

D

G

C

T

T

D

D

N

N

F

M

E

A

S

T

R

R

Y

Q

L

E

I

I

N

N

D

A

A

A

C

C

A

V

L

A

L

L

N

N

K

T

P

P

L

L

I

I

F

T

A

A

A

S

V

A

S

V

G

G

F

F

E

G

G

G

Q

Q

L

L

A

M

I

V

F

L

N

T

A

P

P

P

D

W

H

E

L

-

T

-

P

-

S

Q

T

G

N
x
C

Y

Y

R

R

D
x
C

L

L

F
x
W

P

-

I

-

P

P

P

D

D

N

K

Q

G

E

E

P

V

E

A

R

N

N

C
|
C

A

R

E

T

N

A

G

G

I

V

G

G

V

P

L

V

P

V

G

G

I

V

L

M

G

G

T

T

M

L

A

Q

A

A

A

L

E

E

T

A

I

I

K

K

L

L

I

L

A

S

K

G

I

I

C169 (≠ N169) binding
C172 (≠ D172) binding
W174 (≠ F174) mutation to A: No adenylation of ThiS.
C184 (= C186) 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
243 binding

1zud3 Structure of this-thif protein complex (see paper)
47% identity, 46% coverage: 5:175/368 of query aligns to 8:175/240 of 1zud3

query
sites
1zud3

R

R

Y

Y

N

S

R
|
R

Q

Q

I

I

I
x
L

L

L

K
x
D

G

D

F

I

G

A

E

L

E

D

A

G

Q

Q

K

K

L

L

R

D

A

S

K

Q

V

V

L

L

V

I

I

I

G

G

A

L

G

G

L

L

G

G

C

T

P

P

A

A

L

A

Q

L

Y

Y

L

L

A

A

A

G

A

A

G

G

I

V

G

G

H

T

I

L

G

V

I

L

V

A

D

D

T

D

I

V

S

H

L

L

S

S

N

N

L

L

H

Q

R

R

Q

Q

I

I

L

L

F

F

T

T

A

E

D

D

I

I

G

D

K

R

L

P

K

K

V

S

E

Q

V

V

A

S

A

Q

K

Q

R

R

L

L

Q

T

E

Q

M

L

N

N

T

P

Q

D

I

I

G

Q

I

L

I

T

R

A

H

L

P

Q

I

Q

R

R

L

L

Q

T

K

G

N

E

N

A

I

L

L

K

D

D

I

A

V

V

S

A

R

R

Y

A

D

D

Y

V

I

V

L

L

D

D

G

C

T

T

D
|
D

N

N

F

M

E

A

S

T

R

R

Y

Q

L

E

I

I

N

N

D

A

A

A

C

C

A

V

L

A

L

L

N

N

K

T

P

P

L

L

I

I

F

T

A

A

A

S

V

A

S

V

G

G

F

F

E

G

G

G

Q

Q

L

L

A

M

I

V

F

L

N

T

A

P

P

P

D

W

H

E

L

-

T

-

P

-

S

Q

T

G

N
x
C

Y

Y

R

R

D

C

L

L

F

W

P

P

active site: R11 (= R8), D127 (= D124)
binding calcium ion: L14 (≠ I11), D16 (≠ K13)
binding zinc ion: C169 (≠ N169)

Sites not aligning to the query:

binding zinc ion: 235, 238

1jwbB Structure of the covalent acyl-adenylate form of the moeb-moad protein complex (see paper)
37% identity, 61% coverage: 5:229/368 of query aligns to 10:222/240 of 1jwbB

query
sites
1jwbB

R

R

Y

Y

N

N

R
|
R

Q

Q

I

I

L

L

K

R

G

G

F

F

G

D

E

F

E

D

A

G

Q

Q

Q

E

K

A

L

L

L

K

R

D

A

S

K

R

V

V

L

L

V

I

I

V

G
|
G

A

L

G
|
G

L

L

G

G

C

C

P

A

A

A

L

S

Q

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

I

V

G

G

H

N

I

L

G

T

I

L

V

L

D
|
D

D
x
F

D

D

T

T

I

V

S

S

L

L

S

S

N

N

L

L

H

Q

R

R

Q

Q

I

T

L

L

F

H

T

S

T

D

A

A

D

T

I

V

G

G

K

Q

L

P

K
|
K

V

V

E

E

V

S

A

A

A

R

K

D

R

A

L

L

Q

T

E

R

M

I

N

N

T

P

Q

H

I

I

G

A

I

I

I

T

R

P

H

V

P

N

I

A

R
x
L

L

L

Q

D

K

D

N

A

N

E

I

L

L

A

D

A

I

L

V

I

S

A

R

E

Y

H

D

D

Y

L

I

V

L

L

D

D

G
x
C

T
|
T

D
|
D

N
|
N

F

V

E

A

S
x
V

R

R

Y

N

L

Q

I

L

N

N

D

A

A

G

C

C

A

F

L

A

N

K

K

V

P

P

L

L

I

V

F

S

A

G

A

A

V

A

S

I

G

R

F

M

E

E

G

G

Q

Q

L

I

A

T

I

V

F

F

N

T

A

Y

P

Q

D

D

H

G

L

E

T

P

P
x
C

S

Y

T

R

N

C

Y

L

R

S

D

R

L

L

F

F

P

-

I

-

P

-

D

-

K

-

G

-

E

-

V

-

A

-

N

-

C

-

A

G

E

E

N

A

G

G

I

V

I

M

G

A

V

P

L

L

P

I

G

G

I

V

L

I

G

G

T

S

M

L

A

Q

A

A

A

M

E

E

T

A

I

I

K

K

L

M

I

L

A

A

K

G

I

Y

G

G

Q

K

A

P

L

A

T

S

N

G

K

K

I

I

L

V

S

M

Y

Y

N

D

L

A

L

M

T

T

active site: R13 (= R8), D129 (= D124)
binding adenosine monophosphate: G37 (= G32), G39 (= G34), G40 (= G35), D61 (= D56), F62 (≠ D57), K85 (= K80), L108 (≠ R103), C127 (≠ G122), T128 (= T123), D129 (= D124), N130 (= N125), V133 (≠ S128)
binding zinc ion: C171 (≠ P166)

Sites not aligning to the query:

binding zinc ion: 236, 239

1jw9B Structure of the native moeb-moad protein complex (see paper)
37% identity, 61% coverage: 5:229/368 of query aligns to 10:222/240 of 1jw9B

query
sites
1jw9B

R

R

Y

Y

N

N

R
|
R

Q

Q

I

I

L

L

K

R

G

G

F

F

G

D

E

F

E

D

A

G

Q

Q

Q

E

K

A

L

L

L

K

R

D

A

S

K

R

V

V

L

L

V

I

I

V

G

G

A

L

G

G

L

L

G

G

C

C

P

A

A

A

L

S

Q

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

I

V

G

G

H

N

I

L

G

T

I

L

V

L

D

D

D

F

D

D

T

T

I

V

S

S

L

L

S

S

N

N

L

L

H

Q

R

R

Q

Q

I

T

L

L

F

H

T

S

T

D

A

A

D

T

I

V

G

G

K

Q

L

P

K

K

V

V

E

E

V

S

A

A

A

R

K

D

R

A

L

L

Q

T

E

R

M

I

N

N

T

P

Q

H

I

I

G

A

I

I

I

T

R

P

H

V

P

N

I

A

R

L

L

L

Q

D

K

D

N

A

N

E

I

L

L

A

D

A

I

L

V

I

S

A

R

E

Y

H

D

D

Y

L

I

V

L

L

D

D

G

C

T

T

D
|
D

N

N

F

V

E

A

S

V

R

R

Y

N

L

Q

I

L

N

N

D

A

A

G

C

C

A

F

L

A

N

K

K

V

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P

L

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A

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A

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A

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G

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E

E

G

G

Q

Q

L

I

A

T

I

V

F

F

N

T

A

Y

P

Q

D

D

H

G

L

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T

P

P
x
C

S

Y

T

R

N

C

Y

L

R

S

D

R

L

L

F

F

P

-

I

-

P

-

D

-

K

-

G

-

E

-

V

-

A

-

N

-

C

-

A

G

E

E

N

A

G

G

I

V

I

M

G

A

V

P

L

L

P

I

G

G

I

V

L

I

G

G

T

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M

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A

Q

A

A

A

M

E

E

T

A

I

I

K

K

L

M

I

L

A

A

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Y

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G

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K

A

P

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A

T

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N

G

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I

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S

M

Y

Y

N

D

L

A

L

M

T

T

active site: R13 (= R8), D129 (= D124)
binding zinc ion: C171 (≠ P166)

Sites not aligning to the query:

binding zinc ion: 236, 239

1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
36% identity, 61% coverage: 5:229/368 of query aligns to 10:207/217 of 1jwaB

query
sites
1jwaB

R

R

Y

Y

N

N

R
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R

Q

Q

I

I

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L

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R

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G

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F

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G

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Q

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Y

L

L

A

A

A

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A

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G

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G

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N

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D
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x
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R

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L

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N

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A

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x
V

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N

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Q

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F

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T

A

-

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Y

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-

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-

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-

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E

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N

A

G

G

I

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G

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G

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G

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K

L

M

I

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A

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S

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G

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K

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M

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Y

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D

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L

M

T

T

active site: R13 (= R8), D129 (= D124)
binding adenosine-5'-triphosphate: G39 (= G34), G40 (= G35), D61 (= D56), F62 (≠ D57), R72 (= R67), K85 (= K80), L108 (≠ R103), D129 (= D124), N130 (= N125), V133 (≠ S128)

O42939 Ubiquitin-activating enzyme E1-like; Pmt3-activating enzyme subunit 2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 38% coverage: 18:157/368 of query aligns to 18:158/628 of O42939

query
sites
O42939

E

E

A

A

Q

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N

L

F

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A

A

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K

V

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A

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D

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N

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N

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Q

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N

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V

Sites not aligning to the query:

559 modified: Phosphoserine
563 modified: Phosphoserine

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)
38% identity, 35% coverage: 27:154/368 of query aligns to 48:187/454 of O65041

query
sites
O65041

K

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V

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I

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G

A

A

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G

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N

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N

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A

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E

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Y

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-

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F

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K

G

G

Q

H

Sites not aligning to the query:

215 C→A: Loss of binding to RUB1.

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)
32% identity, 42% coverage: 5:157/368 of query aligns to 450:609/1058 of P22314

query
sites
P22314

R

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C

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S

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N

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G

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A

Q

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V

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.

6dc6C Crystal structure of human ubiquitin activating enzyme e1 (uba1) in complex with ubiquitin (see paper)
32% identity, 42% coverage: 5:157/368 of query aligns to 402:561/996 of 6dc6C

query
sites
6dc6C

R

R

Y

Y

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D

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E

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S

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N

L

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R

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Q

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M

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-

I

-

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-

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R

N

Y

L

D

D

Y

G

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V

L

A

D

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G

A

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D
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D

N

N

F

V

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A

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Y

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M

N

D

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C

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active site: R467 (= R67), D528 (= D124)
binding magnesium ion: D458 (= D58), E461 (≠ S61)
binding pyrophosphate 2-: N464 (= N64), K480 (= K80)

Sites not aligning to the query:

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

5um6A Crystal structure of s. Pombe uba1 in a closed conformation (see paper)
32% identity, 44% coverage: 5:167/368 of query aligns to 373:542/962 of 5um6A

query
sites
5um6A

R

R

Y

Y

N

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-

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S

active site: R438 (= R67), D501 (= D124)

Sites not aligning to the query:

active site: 557, 558, 560
binding N-(2-{[(4-chlorophenyl)methyl]disulfanyl}ethyl)decan-1-amine: 99, 271

Query Sequence

>CA265_RS12640 FitnessBrowser__Pedo557:CA265_RS12640
MSAERYNRQIILKGFGEEAQQKLLRAKVLVIGAGGLGCPALQYLAAAGIGHIGIVDDDTI
SLSNLHRQILFTTADIGKLKVEVAAKRLQEMNTQIGIIRHPIRLQKNNILDIVSRYDYIL
DGTDNFESRYLINDACALLNKPLIFAAVSGFEGQLAIFNAPDHLTPSTNYRDLFPIPPDK
GEVANCAENGIIGVLPGILGTMAAAETIKLIAKIGQALTNKILSYNLLTQEQYTINISHG
GGYTLPKTVDEFLNMDYQDTSEGPQGYIEIDAGELVKLQQLESTILIDVRERHEVPILDK
QIFTQVPMSEFGAFMSKEFYQKHVVLICQHGIRSVAAAEAMQEKYGDAKKIYSLKGGIVK
CRDHFLRP

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