SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing CA265_RS20190 FitnessBrowser__Pedo557:CA265_RS20190 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

Q9VLJ8 Adenylyltransferase and sulfurtransferase MOCS3; Molybdenum cofactor synthesis protein 3; Ubiquitin activating enzyme 4; EC 2.7.7.80; EC 2.8.1.11 from Drosophila melanogaster (Fruit fly) (see paper)
37% identity, 97% coverage: 2:334/345 of query aligns to 64:427/453 of Q9VLJ8

query
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Q9VLJ8

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Sites not aligning to the query:

62 modified: Phosphothreonine

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)
55% identity, 66% coverage: 4:229/345 of query aligns to 5:237/271 of Q72J02

query
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Q72J02

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C192 (= C184) modified: Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in TtuB); mutation to S: Not able to form a thioester complex with TtuB.

Sites not aligning to the query:

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

P38820 Adenylyltransferase and sulfurtransferase UBA4; Needs CLA4 to survive protein 3; Ubiquitin-like protein activator 4; EC 2.7.7.-; EC 2.8.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 4 papers)
39% identity, 94% coverage: 5:330/345 of query aligns to 42:410/440 of P38820

query
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P38820

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C225 (= C184) mutation C->A,S: Abolishes adenylyltransferase activity but not sulfurtransferase activity.
C397 (= C317) 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)
49% identity, 66% coverage: 2:227/345 of query aligns to 55:282/460 of O95396

query
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O95396

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158:238 (vs. 105:183, 46% identical) Interaction with NFS1
C239 (= C184) 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.

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)
45% identity, 66% coverage: 5:233/345 of query aligns to 64:295/482 of O59954

query
sites
O59954

E

E

L

Y

S

R

R

R

Y

Y

N

G

R

R

Q

Q

M

M

I

I

L

V

P

P

E

Q

L

F

G

G

L

L

A

Q

G
|
G

Q

Q

E

L

K

K

L

L

K

R

A

D

A

A

K

K

V

V

L

L

V

I

I

V

G

G

A

A

G

G

L

L

G
|
G

C

C

P

P

I

A

L

A

Q

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

E

T

I

I

G

G

I

L

I

V

D

D

D

G

D

D

V

T

V

V

E

E

L

A

S

S

N

N

L

L

H

H

R
|
R

Q

Q

I

V

L

L

Y

H

N

R

H

S

T

R

D

N

I

V

G

G

Q

K

P

L

K

K

A

V

K

D

V

S

A

A

A

I

E

E

K

Y

L

L

A

R

V

E

L

L

N

N

P

P

N

H

I

P

R

T

L

Y

K

I

V

A

Y

H

H

Q

E

A

R

H

F

L

T

T

A

P

A

R

S

E

A

A

A

P

K

D

I

I

C

F

R

K

D

D

Y

Y

D

D

L

L

I

I

I

L

D

D

C
|
C

S

T

D

D

N

N

F

P

S

A

T

T

R

R

Y

Y

L

L

V

I

N

S

D

D

T

T

C

A

V

V

A

L

L

L

G

G

K

K

I

P

L

L

L

V

F

S

G

A

S

S

I

A

L

L

Q

R

F

T

E
|
E

G

G

Q

Q

V

L

A

M

V

V

F

L

N

N

-

N

-

P

-

Q

-

P

-

G

-

D

Y

K

Q

T

G

G

S

G

A

P

N

C

Y

Y

R

R

D

C

L

V

Y

F

P

P

T

K

P

P

T

P

E

A

N

N

-

S

-

V

L

T

N

S

C

C

A

A

E

D

G

G

V

I

I

L

G

G

I

P

L

V

P

V

G
|
G

I

T

V

M

G

G

L

V

Y

L

M

Q

A

A

N

S

E

E

A

A

L

I

K

K

L

V

I

L

C

T

G

S

I

A

G

G

E

E

T

-

L

-

S

-

G

-

K

-

L

-

M

-

T

S

I

V

N

E

A

A

L

T

N

P

T

S

V

L

L

L

V

I

F

F

G82 (= G23) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
G100 (= G41) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
R130 (= R71) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
C185 (= C126) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
E215 (= E156) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
G264 (= G195) 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)
41% identity, 66% coverage: 2:227/345 of query aligns to 4:230/249 of P12282

query
sites
P12282

L

L

V

S

K

D

E

Q

E

E

L

M

S

L

R

R

Y

Y

N

N

R
|
R

Q

Q

M

I

I

I

L

L

P

R

E

G

L

F

G

D

L

F

A

D

G

G

Q

Q

E

E

K

A

L

L

K

K

A

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

I

A

L

S

Q

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

E

N

I

L

G

T

I

L

D

D

D

F

D

D

V

T

V

V

E

S

L

L

S

S

N

N

L

L

H

Q

R
|
R

Q

Q

I

T

L

L

Y

H

N

S

H

D

T

A

D

T

I

V

G

G

Q

Q

P

P

K

K

A

V

K

E

V

S

A

A

A

R

E

D

K

A

L

L

A

T

V

R

L

I

N

N

P

P

N

H

I

I

R

A

L

I

K

T

V

P

Y

V

H

N

E

A

R

L

F

L

T

D

A

D

A

A

S

E

A

L

A

A

K

A

I

L

C

I

R

A

D

E

Y

H

D

D

L

L

I

V

I

L

D

D

C
|
C

S

T

D
|
D

N

N

F

V

S

A

T

V

R

R

Y

N

L

Q

V

L

N

N

D

A

T

G

C
|
C

V

F

A

A

L

A

G

K

K

V

I

P

L

L

L

V

F

S

G

G

S

A

I

A

L

I

Q

R

F

M

E

E

G

G

Q

Q

V

I

A

T

V

V

F

F

N

T

Y

Y

Q

Q

-

D

G

G

S

E

A

P

N
x
C

Y

Y

R

R

D
x
C

L

L

Y

S

P

R

T

L

P

F

P

G

T

E

E

N

N

A

L

L

N

T

C
|
C

A

V

E

E

G

A

G

G

V

V

I

M

G

A

I

P

L

L

P

I

G

G

I

V

V

I

G

G

L

S

Y

L

M

Q

A

A

N

M

E

E

A

A

L

I

K

K

L

M

I

L

C

A

G

G

I

Y

G

G

E

K

T

P

L

A

S

S

G

G

K

K

L

I

M

V

T

M

I

Y

N

D

A

A

L

M

N

T

R14 (= R12) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
C44 (= C42) mutation to A: No effect.
R73 (= R71) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
C128 (= C126) mutation to A: No effect.; mutation to Y: No activity.
D130 (= D128) mutation to A: No activity.; mutation to E: Substantially reduced activity.
C142 (= C140) mutation to A: No effect.
C172 (≠ N169) mutation to A: No zinc bound and no enzyme activity.
C175 (≠ D172) mutation to A: No zinc bound and no enzyme activity.
C187 (= C184) 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.

6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
44% identity, 60% coverage: 2:209/345 of query aligns to 7:212/289 of 6yubB

query
sites
6yubB

L

L

V

S

K

K

E

E

L

I

S

E

R

R

Y

Y

N

S

R

R

Q

Q

M

M

I

I

L

V

P

P

E

G

L

M

G

G

L

K

A

E

G

G

Q

Q

E

L

K

R

L

L

K

M

A

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

I

A

L

A

Q

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

E

T

I

I

G

G

I

I

I

V

D

D

D

G

D

D

V

S

V

V

E

E

L

T

S

S

N

N

L

L

H

H

R

R

Q

Q

I

V

L

A

Y

H

N

A

H

T

T

K

D

R

I

V

G

G

Q

M

P

L

K

K

A

V

K

D

V

S

A

L

A

I

E

T

K

H

L

L

A

I

V

E

L

I

N

N

P

P

N

L

I

P

R

V

L

Y

K

V

V

P

Y

Y

H

R

E

F

R

D

F

L

T

T

A

P

A

Q

S

N

A

A

K

Q

I

I

C

I

R

K

D

P

Y

W

D

D

L

V

I

I

I

L

D

D

C

C

S

T

D

D

N

N

F

P

S

A

T

T

R

R

Y

Y

L

L

V

I

N

S

D

D

T

V

C

C

V

V

A

L

L

L

G

G

K

K

I

P

L

L

L

V

F

S

G

A

S

A

I

S

L

V

Q

Q

F

K

E

S

G

G

Q

Q

V

L

A

I

V

V

F

L

N

N

Y

C

-

P

-

T

-

P

Q

Q

G

G

S

V

A

V

N

N

Y

K

R

K

D

A

L

-

Y

-

P

-

T

-

P

-

T

A

E

P

N
x
C

L

Y

N

R

C
|
C

A

C

E

F

G

K

G

G

V

I

I

M

G

G

I

P

L

V

P

V

G

G

I

M

V

M

G

G

L

V

Y

A

M

Q

A

A

N

G

E

E

A

A

L

I

K

K

L

I

I

L

binding zinc ion: C184 (≠ N181), C187 (= C184)

Sites not aligning to the query:

binding zinc ion: 265

6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
44% identity, 60% coverage: 2:209/345 of query aligns to 6:213/423 of 6yubA

query
sites
6yubA

L

L

V

S

K

K

E

E

L

I

S

E

R

R

Y

Y

N

S

R

R

Q

Q

M

M

I

I

L

V

P

P

E

G

L

M

G

G

L

K

A

E

G

G

Q

Q

E

L

K

R

L

L

K

M

A

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

I

A

L

A

Q

Q

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

E

T

I

I

G

G

I

I

I

V

D

D

D

G

D

D

V

S

V

V

E

E

L

T

S

S

N

N

L

L

H

H

R

R

Q

Q

I

V

L

A

Y

H

N

A

H

T

T

K

D

R

I

V

G

G

Q

M

P

L

K

K

A

V

K

D

V

S

A

L

A

I

E

T

K

H

L

L

A

I

V

E

L

I

N

N

P

P

N

L

I

P

R

V

L

Y

K

V

V

P

Y

Y

H

R

E

F

R

D

F

L

T

T

A

P

A

Q

S

N

A

A

K

Q

I

I

C

I

R

K

D

P

Y

W

D

D

L

V

I

I

I

L

D

D

C

C

S

T

D

D

N

N

F

P

S

A

T

T

R

R

Y

Y

L

L

V

I

N

S

D

D

T

V

C

C

V

V

A

L

L

L

G

G

K

K

I

P

L

L

L

V

F

S

G

A

S

A

I

S

L

V

Q

Q

F

K

E

S

G

G

Q

Q

V

L

A

I

V

V

F

L

N

N

Y

C

-

P

-

T

-

P

Q

Q

G

G

S

V

A

V

N

N

Y

K

R

K

D

-

L

-

Y

-

P

-

T

A

P

A

P

P

T
x
C

E

Y

N

R

L
x
C

N

C

C

F

A

K

E

K

G

P

G

G

V

I

I

M

G

G

I

P

L

V

P

V

G

G

I

M

V

M

G

G

L

V

Y

A

M

Q

A

A

N

G

E

E

A

A

L

I

K

K

L

I

I

L

binding zinc ion: C183 (≠ T179), C186 (≠ L182)

Sites not aligning to the query:

binding zinc ion: 266, 269

1jwbB Structure of the covalent acyl-adenylate form of the moeb-moad protein complex (see paper)
40% identity, 66% coverage: 2:227/345 of query aligns to 3:222/240 of 1jwbB

query
sites
1jwbB

L

L

V

S

K

D

E

Q

E

E

L

M

S

L

R

R

Y

Y

N

N

R
|
R

Q

Q

M

I

I

I

L

L

P

R

E

G

L

F

G

D

L

F

A

D

G

G

Q

Q

E

E

K

A

L

L

K

K

A

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

I

A

L

S

Q

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

E

N

I

L

G

T

I

L

D
|
D

D
x
F

D

D

V

T

V

V

E

S

L

L

S

S

N

N

L

L

H

Q

R

R

Q

Q

I

T

L

L

Y

H

N

S

H

D

T

A

D

T

I

V

G

G

Q

Q

P

P

K
|
K

A

V

K

E

V

S

A

A

A

R

E

D

K

A

L

L

A

T

V

R

L

I

N

N

P

P

N

H

I

I

R

A

L

I

K

T

V

P

Y

V

H

N

E

A

R
x
L

F

L

T

D

A

D

A

A

S

E

A

L

A

A

K

A

I

L

C

I

R

A

D

E

Y

H

D

D

L

L

I

V

I

L

D

D

C
|
C

S
x
T

D
|
D

N
|
N

F

V

S

A

T
x
V

R

R

Y

N

L

Q

V

L

N

N

D

A

T

G

C

C

V

F

A

A

L

A

G

K

K

V

I

P

L

L

L

V

F

S

G

G

S

A

I

A

L

I

Q

R

F

M

E

E

G

G

Q

Q

V

I

A

T

V

V

F

F

N

T

Y

Y

Q

Q

-

D

G

G

S

E

A

P

N
x
C

Y

Y

R

R

D

C

L

L

Y

S

P

R

T

L

P

-

T

-

E

-

N

-

L

-

N

-

C

F

A

G

E

E

G

A

G

G

V

V

I

M

G

A

I

P

L

L

P

I

G

G

I

V

V

I

G

G

L

S

Y

L

M

Q

A

A

N

M

E

E

A

A

L

I

K

K

L

M

I

L

C

A

G

G

I

Y

G

G

E

K

T

P

L

A

S

S

G

G

K

K

L

I

M

V

T

M

I

Y

N

D

A

A

L

M

N

T

active site: R13 (= R12), D129 (= D128)
binding adenosine monophosphate: G37 (= G36), G39 (= G38), G40 (= G39), D61 (= D60), F62 (≠ D61), K85 (= K84), L108 (≠ R107), C127 (= C126), T128 (≠ S127), D129 (= D128), N130 (= N129), V133 (≠ T132)
binding zinc ion: C171 (≠ N169)

Sites not aligning to the query:

binding zinc ion: 236, 239

1jw9B Structure of the native moeb-moad protein complex (see paper)
40% identity, 66% coverage: 2:227/345 of query aligns to 3:222/240 of 1jw9B

query
sites
1jw9B

L

L

V

S

K

D

E

Q

E

E

L

M

S

L

R

R

Y

Y

N

N

R
|
R

Q

Q

M

I

I

I

L

L

P

R

E

G

L

F

G

D

L

F

A

D

G

G

Q

Q

E

E

K

A

L

L

K

K

A

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

I

A

L

S

Q

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

E

N

I

L

G

T

I

L

D

D

D

F

D

D

V

T

V

V

E

S

L

L

S

S

N

N

L

L

H

Q

R

R

Q

Q

I

T

L

L

Y

H

N

S

H

D

T

A

D

T

I

V

G

G

Q

Q

P

P

K

K

A

V

K

E

V

S

A

A

A

R

E

D

K

A

L

L

A

T

V

R

L

I

N

N

P

P

N

H

I

I

R

A

L

I

K

T

V

P

Y

V

H

N

E

A

R

L

F

L

T

D

A

D

A

A

S

E

A

L

A

A

K

A

I

L

C

I

R

A

D

E

Y

H

D

D

L

L

I

V

I

L

D

D

C

C

S

T

D
|
D

N

N

F

V

S

A

T

V

R

R

Y

N

L

Q

V

L

N

N

D

A

T

G

C

C

V

F

A

A

L

A

G

K

K

V

I

P

L

L

L

V

F

S

G

G

S

A

I

A

L

I

Q

R

F

M

E

E

G

G

Q

Q

V

I

A

T

V

V

F

F

N

T

Y

Y

Q

Q

-

D

G

G

S

E

A

P

N
x
C

Y

Y

R

R

D

C

L

L

Y

S

P

R

T

L

P

-

T

-

E

-

N

-

L

-

N

-

C

F

A

G

E

E

G

A

G

G

V

V

I

M

G

A

I

P

L

L

P

I

G

G

I

V

V

I

G

G

L

S

Y

L

M

Q

A

A

N

M

E

E

A

A

L

I

K

K

L

M

I

L

C

A

G

G

I

Y

G

G

E

K

T

P

L

A

S

S

G

G

K

K

L

I

M

V

T

M

I

Y

N

D

A

A

L

M

N

T

active site: R13 (= R12), D129 (= D128)
binding zinc ion: C171 (≠ N169)

Sites not aligning to the query:

binding zinc ion: 236, 239

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)
44% identity, 65% coverage: 6:229/345 of query aligns to 9:233/270 of D4GSF3

query
sites
D4GSF3

E

Q

L

L

S

D

R

R

Y

Y

N

S

R

R

Q

H

M

I

I

I

L

M

P

D

E

E

L

V

G

G

L

P

A

E

G

G

Q

Q

E

G

K

R

L

L

K

L

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

I

A

L

I

Q

Q

Y

Y

L

L

A

A

A

V

G

G

V

V

G

G

E

E

I

L

G

V

I

V

D

D

V

V

E

E

L

R

S

S

N

N

L

L

H

Q

R

R

Q

Q

I

V

L

V

Y

H

N

C

H

D

T

D

D

D

I

V

G

G

Q

T

P

P

K

K

A

A

K

E

V

S

A

A

E

A

K

F

L

V

A

R

V

G

L

L

N

N

P

P

N

D

I

V

R

S

L

V

K

E

V

P

Y

V

H

E

E

A

R

R

F

V

T

D

A

K

A

S

S

N

A

V

A

H

K

E

I

V

C

V

R

A

D

G

Y

S

D

D

L

V

I

V

D

D

C

A

S

S

D

D

N

N

F

F

S

P

T

T

R

R

Y

Y

L

L

V

L

N

N

D

D

T

V

C

C

V

R

A

F

L

E

G

G

K

I

I

P

L

L

L

V

F

H

G

G

S

A

I

I

L

Y

Q

K

F

F

E

E

G

G

Q

Q

V

A

A

T

V

T

F

L

N

V

Y

P

Q

D

G

G

S

P

A

C

N

-

Y

Y

R

R

D

C

L

L

Y

F

P

P

T

E

P

A

P

P

T

E

E

P

N

G

L

T

-

V

-

P

N

D

C
|
C

A

A

E

T

G

T

G

G

V

V

I

L

G

G

I

V

L

L

P

P

G

G

I

T

V

V

G

G

L

C

Y

I

M

Q

A

A

N

T

E

E

A

A

L

M

K

K

L

L

I

L

C

L

G

D

I

E

G

G

E

E

T

A

L

L

S

D

G

G

K

R

L

L

M

L

T

F

I

Y

N

D

A

A

L

M

N

D

N

M

T

T

C188 (= C184) 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.

1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
38% identity, 66% coverage: 2:227/345 of query aligns to 3:207/217 of 1jwaB

query
sites
1jwaB

L

L

V

S

K

D

E

Q

E

E

L

M

S

L

R

R

Y

Y

N

N

R
|
R

Q

Q

M

I

I

I

L

L

P

R

E

G

L

F

G

D

L

F

A

D

G

G

Q

Q

E

E

K

A

L

L

K

K

A

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

I

A

L

S

Q

Q

Y

Y

L

L

A

A

A

S

A

A

G

G

V

V

G

G

E

N

I

L

G

T

I

L

D
|
D

D
x
F

D

D

V

T

V

V

E

S

L

L

S

S

N

N

L

L

H

Q

R
|
R

Q

Q

I

T

L

L

Y

H

N

S

H

D

T

A

D

T

I

V

G

G

Q

Q

P

P

K
|
K

A

V

K

E

V

S

A

A

A

R

E

D

K

A

L

L

A

T

V

R

L

I

N

N

P

P

N

H

I

I

R

A

L

I

K

T

V

P

Y

V

H

N

E

A

R
x
L

F

L

T

D

A

D

A

A

S

E

A

L

A

A

K

A

I

L

C

I

R

A

D

E

Y

H

D

D

L

L

I

V

I

L

D

D

C

C

S

T

D
|
D

N
|
N

F

V

S

A

T
x
V

R

R

Y

N

L

Q

V

L

N

N

D

A

T

G

C

C

V

F

A

A

L

A

G

K

K

V

I

P

L

L

L

V

F

S

G

G

S

A

I

A

L

I

Q

R

F

M

E

E

G

G

Q

Q

V

I

A

T

V

V

F

F

N

T

Y

Y

Q

-

G

-

S

-

A

-

N

-

Y

-

R

-

D

-

L

-

Y

-

P

-

T

-

P

-

T

-

E

-

N

-

L

-

N

-

C

-

A

-

E

E

G

A

G

G

V

V

I

M

G

A

I

P

L

L

P

I

G

G

I

V

V

I

G

G

L

S

Y

L

M

Q

A

A

N

M

E

E

A

A

L

I

K

K

L

M

I

L

C

A

G

G

I

Y

G

G

E

K

T

P

L

A

S

S

G

G

K

K

L

I

M

V

T

M

I

Y

N

D

A

A

L

M

N

T

active site: R13 (= R12), D129 (= D128)
binding adenosine-5'-triphosphate: G39 (= G38), G40 (= G39), D61 (= D60), F62 (≠ D61), R72 (= R71), K85 (= K84), L108 (≠ R107), D129 (= D128), N130 (= N129), V133 (≠ T132)

P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
42% identity, 63% coverage: 5:220/345 of query aligns to 4:219/251 of P30138

query
sites
P30138

E

R

E

D

L

F

S

M

R

R

Y

Y

N

S

R

R

Q

Q

M

I

I

L

L

L

P

D

E

D

L

I

G

A

L

L

A

D

G

G

Q

Q

E

Q

K

K

L

L

K

L

A

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

I

A

L

A

Q

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

E

T

I

L

G

V

I

L

I

A

D

D

V

D

V

V

E

H

L

L

S

S

N

N

L

L

H

Q

R

R

Q

Q

I

I

L

L

Y

F

N

T

H

T

T

E

D

D

I

I

G

D

Q

R

P

P

K

K

A

S

K

Q

V

V

A

S

A

Q

E

Q

K

R

L

L

A

T

V

Q

L

L

N

N

P

P

N

D

I

I

R

Q

L

L

K

T

V

A

Y

L

H

Q

E

Q

R

R

F

L

T

T

A

G

A

E

S

A

A

L

A

K

K

D

I

A

C

V

R

A

D

R

Y

A

D

D

L

V

I

V

I

L

D

D

C

C

S

T

D

D

N

N

F

M

S

A

T

T

R

R

Y

Q

L

E

V

I

N

N

D

A

T

A

C

C

V

V

A

A

L

L

G

N

K

T

I

P

L

L

L

I

F

T

G

A

S

S

I

A

L

V

Q

G

F

F

E

G

G

G

Q

Q

V

L

A

M

V

V

F

L

N

T

-

P

-

W

Y

E

Q

Q

G

G

S
x
C

A

-

N

-

Y

Y

R

R

D
x
C

L

L

Y
x
W

P

P

T

D

P

N

P

Q

T

E

E

P

N

E

L

R

N

N

C
|
C

A

R

E

T

G

A

G

G

V

V

I

V

G

G

I

P

L

V

P

V

G

G

I

V

V

M

G

G

L

T

Y

L

M

Q

A

A

N

L

E

E

A

A

L

I

K

K

L

L

I

L

C

S

G

G

I

I

G

-

E

E

T

T

L

P

S

A

G

G

K

E

L

L

C169 (≠ S167) binding
C172 (≠ D172) binding
W174 (≠ Y174) mutation to A: No adenylation of ThiS.
C184 (= C184) 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

1zfnA Structural analysis of escherichia coli thif (see paper)
42% identity, 63% coverage: 5:220/345 of query aligns to 4:219/244 of 1zfnA

query
sites
1zfnA

E

R

E

D

L

F

S

M

R

R

Y

Y

N

S

R
|
R

Q

Q

M

I

I

L

L

L

P

D

E

D

L

I

G

A

L

L

A

D

G

G

Q

Q

E

Q

K

K

L

L

K

L

A

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

I

A

L

A

Q

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

E

T

I

L

G

V

I

L

I

A

D
|
D

D

D

V

D

V

V

E

H

L

L

S

S

N

N

L

L

H

Q

R
|
R

Q
|
Q

I

I

L

L

Y

F

N

T

H

T

T

E

D

D

I

I

G

D

Q

R

P

P

K
|
K

A

S

K

Q

V

V

A

S

A

Q

E

Q

K

R

L

L

A

T

V

Q

L

L

N

N

P

P

N

D

I

I

R

Q

L

L

K

T

V

A

Y

L

H

Q

E

Q

R

R

F

L

T

T

A

G

A

E

S

A

A

L

A

K

K

D

I

A

C

V

R

A

D

R

Y

A

D

D

L

V

I

V

I

L

D

D

C

C

S
x
T

D
|
D

N

N

F

M

S

A

T
|
T

R

R

Y

Q

L

E

V

I

N

N

D

A

T

A

C

C

V

V

A

A

L

L

G

N

K

T

I

P

L

L

L

I

F

T

G

A

S

S

I

A

L

V

Q

G

F

F

E

G

G

G

Q

Q

V

L

A

M

V

V

F

L

N

T

-

P

-

W

Y

E

Q

Q

G

G

S
x
C

A

-

N

-

Y

Y

R

R

D
x
C

L

L

Y

W

P

P

T

D

P

N

P

Q

T

E

E

P

N

E

L

R

N

N

C

C

A

R

E

T

G

A

G

G

V

V

I

V

G

G

I

P

L

V

P

V

G

G

I

V

V

M

G

G

L

T

Y

L

M

Q

A

A

N

L

E

E

A

A

L

I

K

K

L

L

I

L

C

S

G

G

I

I

G

-

E

E

T

T

L

P

S

A

G

G

K

E

L

L

active site: R11 (= R12), D127 (= D128)
binding adenosine-5'-triphosphate: I34 (= I35), G35 (= G36), G37 (= G38), G38 (= G39), D59 (= D60), R70 (= R71), Q71 (= Q72), K83 (= K84), T126 (≠ S127), D127 (= D128), T131 (= T132)
binding zinc ion: C169 (≠ S167), C172 (≠ D172)

Sites not aligning to the query:

binding zinc ion: 240, 243

1zud3 Structure of this-thif protein complex (see paper)
42% identity, 63% coverage: 5:220/345 of query aligns to 4:214/240 of 1zud3

query
sites
1zud3

E

R

E

D

L

F

S

M

R

R

Y

Y

N

S

R
|
R

Q

Q

M

I

I
x
L

L

L

P
x
D

E

D

L

I

G

A

L

L

A

D

G

G

Q

Q

E

Q

K

K

L

L

K

L

A

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

I

A

L

A

Q

L

Y

Y

L

L

A

A

A

G

A

A

G

G

V

V

G

G

E

T

I

L

G

V

I

L

I

A

D

D

V

D

V

V

E

H

L

L

S

S

N

N

L

L

H

Q

R

R

Q

Q

I

I

L

L

Y

F

N

T

H

T

T

E

D

D

I

I

G

D

Q

R

P

P

K

K

A

S

K

Q

V

V

A

S

A

Q

E

Q

K

R

L

L

A

T

V

Q

L

L

N

N

P

P

N

D

I

I

R

Q

L

L

K

T

V

A

Y

L

H

Q

E

Q

R

R

F

L

T

T

A

G

A

E

S

A

A

L

A

K

K

D

I

A

C

V

R

A

D

R

Y

A

D

D

L

V

I

V

I

L

D

D

C

C

S

T

D
|
D

N

N

F

M

S

A

T

T

R

R

Y

Q

L

E

V

I

N

N

D

A

T

A

C

C

V

V

A

A

L

L

G

N

K

T

I

P

L

L

L

I

F

T

G

A

S

S

I

A

L

V

Q

G

F

F

E

G

G

G

Q

Q

V

L

A

M

V

V

F

L

N

T

-

P

-

W

Y

E

Q

Q

G

G

S
x
C

A

-

N

-

Y

Y

R

R

D

C

L

L

Y

W

P

P

-

D

-

N

T

Q

P

E

P

P

T

T

E

A

N

G

L

V

N

V

C

G

A

P

E

V

G

V

G

G

V

V

I

M

G

G

I

T

L

L

P

-

G

-

I

-

V

-

G

-

L

-

Y

-

M

Q

A

A

N

L

E

E

A

A

L

I

K

K

L

L

I

L

C

S

G

G

I

I

G

-

E

E

T

T

L

P

S

A

G

G

K

E

L

L

active site: R11 (= R12), D127 (= D128)
binding calcium ion: L14 (≠ I15), D16 (≠ P17)
binding zinc ion: C169 (≠ S167)

Sites not aligning to the query:

binding zinc ion: 235, 238

O42939 Ubiquitin-activating enzyme E1-like; Pmt3-activating enzyme subunit 2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
39% identity, 44% coverage: 27:178/345 of query aligns to 23:174/628 of O42939

query
sites
O42939

L

F

K

K

A

S

A

A

K

K

V

V

L

L

V

L

I

V

G

G

A

A

G

G

L

I

G

G

C

C

P

E

I

L

L

L

Q

K

Y

N

L

L

A

L

A

M

A

S

G

G

V

V

G

K

E

E

I

V

G

H

I

I

D

D

D

L

D

D

V

T

V

I

E

D

L

L

S

S

N

N

L

L

H

N

R

R

Q

Q

I

F

L

L

Y

F

N

R

H

K

T

K

D

H

I

V

G

K

Q

Q

P

P

K

K

A

A

K

I

V

V

A

A

E

K

K

T

L

A

A

S

V

S

L

F

N

N

P

P

N

N

I

V

R

K

L

L

K

E

V

A

Y

Y

H

H

-

A

-

N

-

I

-

K

-

E

E

D

R

R

F

F

T

N

A

V

A

A

S

-

A

-

K

-

I

W

C

F

R

R

D

Q

Y

F

D

D

L

L

I

V

I

F

D

N

C

A

S

L

D

D

N

N

F

L

S

D

T

A

R

R

Y

R

L

H

V

V

N

N

D

K

T

Q

C

C

V

L

A

L

L

A

G

S

K

V

I

P

L

L

L

I

F

E

G

S

S

G

I

T

L

T

Q

G

F

F

E

L

G

G

Q

Q

V

V

A

Q

V

V

F

I

N

-

Y

I

Q

H

G

G

S

K

A

T

N

E

Y

C

R

Y

D

D

L

C

Y

N

P

P

T

K

P

E

P

P

Sites not aligning to the query:

559 modified: Phosphoserine
563 modified: Phosphoserine

P20973 Ubiquitin-activating enzyme E1 1; EC 6.2.1.45 from Triticum aestivum (Wheat) (see paper)
34% identity, 42% coverage: 3:148/345 of query aligns to 438:590/1051 of P20973

query
sites
P20973

V

L

K

K

E

P

E

K

L

N

S

S

R

R

Y

Y

N

D

R

A

Q

Q

M

I

I

S

L

V

P

-

E

-

L

F

G

G

L

S

A

K

G

L

Q

Q

E

N

K

K

L

L

K

E

A

E

A

A

K

K

V

I

L

F

V

M

I

V

G

G

A

S

G

G

G

A

L

L

G

G

C

C

P

E

I

F

L

L

Q

K

Y

N

L

L

A

A

A

L

A

M

G

G

V

I

-

S

-

C

-

S

-

Q

-

N

G

G

E

N

I

L

G

T

I

L

I

T

D

D

V

V

V

I

E

E

L

K

S

S

N

N

L

L

H

S

R

R

Q

Q

I

F

L

L

Y

F

N

R

H

D

T

W

D

N

I

I

G

G

Q

Q

P

P

K

K

A

S

K

T

V

V

A

A

E

T

K

A

L

A

A

M

V

V

L

I

N

N

P

P

N

K

I

L

R

H

L

V

K

E

V

A

Y

L

H

Q

E

N

R

R

F

A

T

S

A

P

A

E

S

T

A

E

-

N

-

V

-

F

-

N

A

D

K

A

I

F

C

W

R

E

D

N

Y

L

D

D

L

A

I

V

D

N

C

A

S

L

D

D

N

N

F

V

S

T

T

A

R

R

Y

M

L

Y

V

I

N

D

D

S

T

R

C

C

V

V

A

Y

L

F

G

Q

K

K

I

P

L

L

Sites not aligning to the query:

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

Q7SXG4 SUMO-activating enzyme subunit 2; Ubiquitin-like 1-activating enzyme E1B; Ubiquitin-like modifier-activating enzyme 2; EC 2.3.2.- from Danio rerio (Zebrafish) (Brachydanio rerio) (see paper)
30% identity, 46% coverage: 25:184/345 of query aligns to 14:186/650 of Q7SXG4

query
sites
Q7SXG4

E

D

K

S

L

L

K

S

A

S

A

C

K

R

V

V

L

L

V

V

I

V

G

G

A

A

G

G

L

I

G

G

C

C

P

E

I

L

L

L

Q

K

Y

N

L

L

A

V

A

L

A

T

G

G

V

F

G

K

E

N

I

I

G

E

I

V

I

I

D

D

D

L

D

D

V

T

V

I

E

D

L

V

S

S

N

N

L

L

H

N

R

R

Q

Q

I

F

L

L

Y

F

N

Q

H

K

T

K

D

H

I

V

G

G

Q

K

P

S

K

K

A

A

K

Q

V

V

A

A

A

K

E

E

K

S

L

V

A

L

V

R

L

F

N

C

P

P

N

S

I

A

R

N

L

I

K

T

V

A

Y

Y

H

H

E

D

R

S

F

I

T

M

A

N

A

P

S

D

-

Y

A

N

A

V

K

E

I

F

C

F

R

R

D

N

Y

F

D

Q

L

L

I

V

I

M

D

N

C

A

S

L

D

D

N

N

F

R

S

A

T

A

R

R

Y

N

L

H

V

V

N

N

D

R

T

M

C

C

V

L

A

A

L

A

G

D

K

I

I

P

L

L

L

I

F

E

G

S

S

G

I

T

L

A

Q

G

F

Y

E

L

G

G

Q

Q

V

V

A

T

V

V

F

I

N

K

Y

-

Q

K

G

G

S

Q

A

T

N

E

Y

C

R

Y

D

E

L

C

Y

Q

P

P

T

K

P

P

-

T

-

Q

-

K

-

T

-

F

-

P

-

G

-

C

-

T

-

I

-

R

-

N

-

T

P

P

T

S

E

E

N

P

L

I

N

H

C

C

Sites not aligning to the query:

599 modified: Phosphoserine

6xogB Structure of sumo1-ml786519 adduct bound to sae (see paper)
30% identity, 46% coverage: 25:184/345 of query aligns to 6:175/500 of 6xogB

query
sites
6xogB

E

E

K

A

L

V

K

A

A

G

K

R

V

V

L

L

V

V

I

V

G

G

A

A

G

G

L

I

G

G

C

C

P

E

I

L

L

L

Q

K

Y

N

L

L

A

V

A

L

A

T

G

G

V

F

G

S

E

H

I

I

G

D

I

L

I

I

D
|
D

D
x
L

D

D

V

T

V

I

E

D

L

V

S

S

N

N

L

L

H

N

R

R

Q

Q

I

F

L

L

Y

F

N

Q

H

K

T

K

D

H

I

V

G

G

Q

R

P

S

K
|
K

A

A

K

Q

V

V

A

A

A

K

E

E

K

S

L

V

A

L

V

Q

L

F

N

Y

P

P

N

K

I

A

R

N

L

I

K

V

V

A

Y

Y

H

H

E

D

R
x
S

F
x
I

T
x
M

A

N

A

P

S

D

-

Y

A

N

A

V

K

E

I

F

C

F

R

R

D

Q

Y

F

D

I

L

L

I

V

I

M

D

N

C
x
A

S

L

D
|
D

N
|
N

F

R

S

A

T

A

R

R

Y

N

L

H

V

V

N

N

D

R

T

M

C

C

V

L

A

A

L

A

G

D

K

V

I

P

L

L

L

I

F

E

G

S

S

G

I

T

L

A

Q

G

F

Y

E

L

G

G

Q

Q

V

V

A

T

V

T

F

I

N

K

Y

-

Q

K

G

G

S

V

A

T

N

E

Y
x
C

R

Y

D

E

L
x
C

Y

H

P

P

T

K

P

P

-

T

-

F

-

P

-

G

-
x
C

-
x
T

-

I

-
x
R

-

N

-

T

P

P

T

S

E

E

N

P

L

I

N

H

C

C

active site: D110 (= D128), C163 (vs. gap), T164 (vs. gap), R166 (vs. gap)
binding {(1R,2R,3S,4R)-4-[(5-{4-[(1S)-1-(6-bromopyridin-2-yl)-1-hydroxyethyl]thiophene-2-carbonyl}pyrimidin-4-yl)amino]-2,3-dihydroxycyclopentyl}methyl sulfamate: D41 (= D60), L42 (≠ D61), K65 (= K84), S88 (≠ R107), I89 (≠ F108), M90 (≠ T109), A108 (≠ C126), D110 (= D128), N111 (= N129)
binding zinc ion: C151 (≠ Y170), C154 (≠ L173)

Sites not aligning to the query:

binding zinc ion: 398, 401

6xoiB Structure of sumo1-ml00752641 adduct bound to sae (see paper)
30% identity, 46% coverage: 25:184/345 of query aligns to 6:171/403 of 6xoiB

query
sites
6xoiB

E

E

K

A

L

V

K

A

A

G

K

R

V

V

L

L

V

V

I

V

G

G

A

A

G

G

G
|
G

L

I

G

G

C

C

P

E

I

L

L

L

Q

K

Y

N

L

L

A

V

A

L

A

T

G

G

V

F

G

S

E

H

I

I

G

D

I

L

I

I

D
|
D

D
x
L

D

D

V

T

V

I

E

D

L

V

S

S

N

N

L

L

H

N

R

R

Q

Q

I

F

L

L

Y

F

N

Q

H

K

T

K

D

H

I

V

G

G

Q

R

P

S

K
|
K

A

A

K

Q

V

V

A

A

A

K

E

E

K

S

L

V

A

L

V

Q

L

F

N

Y

P

P

N

K

I

A

R

N

L

I

K

V

V

A

Y

Y

H

H

E

D

R
x
S

F
x
I

T

M

A

N

A

P

S

D

A

Y

-

N

A

V

K

E

I

F

C

F

R

R

D

Q

Y

F

D

I

L

L

I

V

I

M

D

N

C
x
A

S
x
L

D
|
D

N
|
N

F

R

S

A

T

A

R

R

Y

N

L

H

V

V

N

N

D

R

T

M

C

C

V

L

A

A

L

A

G

D

K

V

I

P

L

L

L

I

F

E

G

S

S

G

I

T

L

A

Q

G

F

Y

E

L

G

G

Q

Q

V

V

A

T

V

T

F

I

N

K

Y

K

Q

G

G

V

S

T

A

E

N
x
C

Y

Y

R

E

D
x
C

L

H

Y

F

P

P

-

G

-
x
C

-
x
T

-

I

-
x
R

T

N

P

T

P

P

T

S

E

E

N

P

L

I

N

H

C

C

active site: D110 (= D128), C159 (vs. gap), T160 (vs. gap), R162 (vs. gap)
binding [(1R,2R,3S,4R)-4-{[5-(1-benzyl-1H-pyrazole-3-carbonyl)pyrimidin-4-yl]amino}-2,3-dihydroxycyclopentyl]methyl sulfamate: G20 (= G39), D41 (= D60), L42 (≠ D61), K65 (= K84), S88 (≠ R107), I89 (≠ F108), A108 (≠ C126), L109 (≠ S127), D110 (= D128), N111 (= N129)
binding zinc ion: C151 (≠ N169), C154 (≠ D172)

Sites not aligning to the query:

binding zinc ion: 353, 356

Query Sequence

>CA265_RS20190 FitnessBrowser__Pedo557:CA265_RS20190
MLVKEELSRYNRQMILPELGLAGQEKLKAAKVLVIGAGGLGCPILQYLAAAGVGEIGIID
DDVVELSNLHRQILYNHTDIGQPKAKVAAEKLAVLNPNIRLKVYHERFTAASAAKICRDY
DLIIDCSDNFSTRYLVNDTCVALGKILLFGSILQFEGQVAVFNYQGSANYRDLYPTPPTE
NLNCAEGGVIGILPGIVGLYMANEALKLICGIGETLSGKLMTINALNNTVLVFKIAAEKS
ADPAKPAATKNDKAIPEINKTTLNNWLETQADDVFLIDVRESYEHEEDNIGGINLPLYEL
TESLAAIPKNKNVVFYCQTGQRSKMAVQLLTGLYQGEVYSLKNGQ

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