SitesBLAST

R95 (= R98) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K119 (= K122) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
K168 (= K183) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KVYEE 168:172 (≠ KVEEE 183:187) binding ATP
E171 (= E186) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E172 (= E187) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
E175 (= E190) binding ATP; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K189 (= K202) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KLEE 189:192 (≠ KVAD 202:205) binding ATP
E192 (≠ D205) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E193 (= E206) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
D196 (= D209) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K222 (= K235) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
KFERR 222:226 (≠ KFRRR 235:239) binding ATP
R226 (= R239) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
W253 (= W266) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K257 (= K270) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.

3crcA Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
45% identity, 94% coverage: 7:267/277 of query aligns to 3:219/225 of 3crcA

query
sites
3crcA

I

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P

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-

A

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A

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-

M

-

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-

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Q

A

A

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N

-

D

-

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R

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A

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E

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M

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G

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F

A

A

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N

N

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K

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K

F
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F

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R
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R

F

F

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R

H

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E

E

Q

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A

A

A

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-

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W
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W

Q

Q

binding adenosine-5'-triphosphate: F190 (= F236), R193 (= R239), W218 (= W266)

Q9X015 Nucleoside triphosphate pyrophosphohydrolase/pyrophosphatase MazG; NTP-PPase; EC 3.6.1.1; EC 3.6.1.9 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
40% identity, 96% coverage: 7:271/277 of query aligns to 8:251/255 of Q9X015

query
sites
Q9X015

I

F

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E

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E

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K

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x
E

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x
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x
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G

E41 (= E41) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
E42 (= E42) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
E45 (= E45) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
E61 (= E61) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
R97 (= R97) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
R98 (= R98) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
K118 (= K122) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
E173 (≠ Q193) mutation to A: Has little effects on the NTPase activity.
E176 (≠ N196) mutation to A: Has little effects on the NTPase activity.
EE 185:186 (≠ DE 205:206) mutation to AA: Has little effects on the NTPase activity.

3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
42% identity, 94% coverage: 7:267/277 of query aligns to 3:213/220 of 3crcB

query
sites
3crcB

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K

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E
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E

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E

L

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M

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E

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D

L

L

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L

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F

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A

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V

N

N

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A

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L

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M

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E

L

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W

Q

Q

binding adenosine-5'-triphosphate: F116 (= F172), W118 (= W174), K127 (= K183), E131 (= E187), E134 (= E190)
binding magnesium ion: E131 (= E187), E134 (= E190), E152 (= E206), D155 (= D209)

P96379 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
35% identity, 60% coverage: 8:172/277 of query aligns to 85:235/325 of P96379

query
sites
P96379

Q

E

R

R

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L

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A

A

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D

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Q

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H

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D

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R

Y

Y

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E

A

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Y

Y

E

E

V

L

A

L

D

D

A

A

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S

M

V

D

D

D

Q

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L

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R

D

E

E

E

L

L

G

G

D

D

L

L

Q

Q

V

V

V

L

Y

F

H

H

A

A

Q

R

M

I

A

A

E

E

E

D

V

A

G

S

E

Q

-

S

-

P

F

F

S

T

F

I

G

D

D

D

V

V

V

A

E

D

A

T

V

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T

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K

K

M

L

I

G

R

N

R

R

H

A

P

P

H

G

V

V

F

L

A

A

R

-

S

G

D

E

A

S

D

I

T

S

P

L

E

E

A

D

V

Q

K

L

L

A

Q

Q

W

W

D

E

E

A

I

A

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K

Q

A

A

S

E

E

K

K

A

A

D

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R

-

H

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R

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M

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R

R

R

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G

S

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P

A

L

D

E

D

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G

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L

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G

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F

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P

P

A
|
A

L

L

V

A

E

L

A

A

L

Q

K

K

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Q

I

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Q

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R

A

A

A

Q

K

K

V

A

G

G

F

L

A219 (= A156) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.

A0R3C4 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
34% identity, 60% coverage: 8:172/277 of query aligns to 85:238/324 of A0R3C4

query
sites
A0R3C4

Q

E

R

R

L

L

I

V

A

D

I

A

M

V

A

A

A

L

L

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R

D

E

K

P

L

K

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T

G

S

C

G

P

P

W

W

D

E

I

S

V

E

Q

Q

T

T

F

H

E

D

T

S

I

L

K

R

P

R

Y

Y

T

L

I

L

E

E

A

T

Y

Y

E

E

V

L

A

F

D

D

A

A

I

V

E

R

R

S

H

G

D

N

M

A

D

D

D

E

L

L

C

R

D

E

E

E

L

L

G

G

D

D

L

V

L

L

Q

Q

V

V

V

L

Y

F

H

H

A

A

Q

R

M

I

A

A

E

E

E

D

V

A

G

P

-

H

E

P

F

F

S

S

F

I

G

D

D

D

V

V

V

A

E

D

A

A

V

L

T

V

R

R

K

K

M

L

I

G

R

N

R

R

H

V

P

P

H

A

V

V

F

L

A

A

R

G

S

E

D

S

A

I

D

S

T

L

P

D

E

E

A

Q

V

L

K

A

L

-

Q

Q

W

W

D

E

E

E

I

R

K

K

Q

A

A

Q

E

E

K

K

A

K

D

V

R

K

H

A

R

R

R

-

M

-

R

-

G

-

L

-

P

-

L

-

E

-

H

-

S

A

G

S

H

S

L

M

G

D

S

D

V

V

Q

P

R

T

S

G

F

Q

P

P

A
|
A

L

L

V

A

E

L

A

A

L

Q

K

K

L

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Q

L

E

A

R

R

A

V

A

S

K

Q

V

A

G

G

F

L

A222 (= A156) mutation to E: Pyrophosphohydrolase activity is reduced 30-fold.

7yh5B Mazg(mycobacterium tuberculosis) (see paper)
39% identity, 33% coverage: 8:98/277 of query aligns to 85:177/177 of 7yh5B

query
sites
7yh5B

Q

E

R

R

L

L

I

V

A

D

I

A

M

V

A

A

A

M

L

M

R

D

E

K

P

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K

R

T

T

G

A

C

G

P

P

W

W

D

E

I

S

V

E

Q

Q

T

T

F

H

E

D

T

S

I

L

K

R

P

R

Y

Y

T

L

I

L

E

E

E
|
E

A

T

Y

Y

E
|
E

V

L

A

L

D

D

A

A

I

V

E

R

R

S

H

G

D

S

M

V

D

D

D

Q

L

L

C

R

D

E

E
|
E

L

L

G

G

D
|
D

L

L

Q

Q

V

V

V

L

Y

F

H

H

A

A

Q

R

M

I

A

A

E

E

E

D

V

A

G

S

E

Q

-

S

-

P

F

F

S

T

F

I

G

D

D

D

V

V

V

A

E

D

A

T

V

L

T

M

R

R

K

K

M

L

I

G

R

N

R

R

binding magnesium ion: E119 (= E42), E122 (= E45), E138 (= E61), D141 (= D64)

2yxhA Crystal structure of mazg-related protein from thermotoga maritima
30% identity, 42% coverage: 7:123/277 of query aligns to 2:114/114 of 2yxhA

query
sites
2yxhA

I

V

Q

E

R

R

L

L

I

L

A

E

I

I

M

I

A

E

-

R

A

S

L

L

R

R

E

K

P

-

K

-

T

-

G

-

C

C

P

P

W

W

D

L

I

E

V

K

Q

Q

T

S

F

I

E

E

T

T

I

L

K

L

P

E

Y

A

T

L

I

A

E

S

E
|
E

A

I

Y

E

E
|
E

V

V

A

A

D

E

A

A

I

V

E

K

R

K

H

N

D

D

M

L

D

A

D

N

L

L

C

E

D

E

E
|
E

L

I

G

G

D
|
D

L

M

L

-

Q

-

V

-

V

I

Y

Y

H
x
D

A

A

Q

L

M

L

A

V

E

A

V

V

G

A

E

Q

F

R

S

D

F

Y

G

G

-

I

-

D

-

L

-

E

D

S

V

A

V

I

E

Q

A

K

V

V

T

V

R

E

K

K

M

I

I

S

R

H

R

R

H

K

P

P

H

W

V

L

F

F

A

W

R

E

S

E

D

K

A

I

D

S

T

L

P

E

E

E

A

A

V

E

K

K

L

I

Q

-

W

W

D

K

E

E

I

R

K

K

Q

K

binding magnesium ion: E34 (= E42), E34 (= E42), E37 (= E45), E53 (= E61), D56 (= D64), D60 (≠ H72)

Query Sequence

>WP_012707860.1 NCBI__GCF_000018545.1:WP_012707860.1
MEPSRDIQRLIAIMAALREPKTGCPWDIVQTFETIKPYTIEEAYEVADAIERHDMDDLCD
ELGDLLLQVVYHAQMAEEVGEFSFGDVVEAVTRKMIRRHPHVFARSDADTPEAVKLQWDE
IKQAEKADRHRRRMRRGLPLEEHSGHLGSVQRSFPALVEALKLQERAAKVGFDWSEPAPI
LDKVEEEIGELRQALNDGDRRKVADELGDLIFALVNIGRHVGTDPEMALRGTNTKFRRRF
SHIEQELHAGGETLDAASLERMEELWQAAKAIERQLT

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