SitesBLAST

R95 (= R103) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K119 (= K127) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
K168 (≠ E172) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KVYEE 168:172 (≠ EVQRQ 172:176) binding ATP
E171 (≠ R175) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E172 (≠ Q176) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
E175 (≠ S179) binding ATP; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K189 (≠ A195) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KLEE 189:192 (≠ ASEK 195:198) binding ATP
E192 (≠ K198) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E193 (= E199) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
D196 (= D202) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K222 (= K228) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
KFERR 222:226 (≠ KFLRR 228:232) binding ATP
R226 (= R232) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
W253 (= W259) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K257 (= K263) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.

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)
38% identity, 94% coverage: 15:263/266 of query aligns to 10:250/255 of Q9X015

query
sites
Q9X015

E

E

L

L

R

V

D

S

V

I

L

M

N

E

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K

L

L

L

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E

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G

C

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W

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Q

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E

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Y

E
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E

L

L

I

I

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E

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A

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I

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D

A

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N

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E

M

L

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G

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D

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F

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N

A

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A

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F

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M

I

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D

A

V

L

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R

H

T

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L

A

N

A

E

K

K

M

L

I

I

R
|
R

H

H

P

P

H

H

V

V

F

F

G

G

K

-

R

-

F

-

D

D

T

S

Q

P

E

G

Q

Y

L

S

W

Y

D

K

N

Q

W

W

E

E

K

D

T

I

K
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K

K

A

Q

Q

E

E

K

K

E

G

S

K

E

K

G

K

S

S

K

S

G

R

V

I

F

G

D

E

S

I

L

N

P

P

K

L

G

-

L

V

P

P

P

A

L

L

L

S

R

M

S

A

Y

R

R

R

I

I

N

Q

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E

K

N

A

A

A

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G

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W

W

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S

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-

R

-

Q

-

Y

Y

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T

E

E

E

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L

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K

Q
x
E

A

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L

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E
|
E

A

A

G

K

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D

T

P

D

R

A

E

S

L

E

E

K
x
E

E
|
E

F

F

G

G

D

D

L

L

F

F

T

S

L

I

V

V

E

N

L

L

G

S

R

R

R

F

K

L

G

N

I

V

K

D

A

P

N

E

A

S

A

A

L

L

D

R

F

K

A

A

N

T

Q

R

K

K

F

F

L

V

R

E

R

R

F

F

A

K

Q

K

M

M

E

E

K

E

M

L

A

I

E

E

E

K

R

D

G

G

Q

L

S

V

L

L

D

E

M

L

D

P

L

I

D

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A

K

M

L

N

D

Q

E

L

Y

W

W

D

E

E

K

A

A

K

K

E41 (= E46) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
E42 (= E47) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
E45 (= E50) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
E61 (= E66) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
R97 (= R102) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
R98 (= R103) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
K118 (= K127) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
E173 (≠ Q186) mutation to A: Has little effects on the NTPase activity.
E176 (= E189) mutation to A: Has little effects on the NTPase activity.
EE 185:186 (≠ KE 198:199) mutation to AA: Has little effects on the NTPase activity.

3crcA Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
32% identity, 94% coverage: 16:266/266 of query aligns to 6:225/225 of 3crcA

query
sites
3crcA

L

L

R

L

D

T

V

I

L

M

N

Q

S

R

L

L

L

R

G

D

P

P

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E

-

N

G

G

C

C

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P

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W

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K

K

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Q

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A

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A

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A

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G

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A

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A

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A

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K

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P

H

-

V

-

F

-

G

-

K

-

R

-

F

-

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-

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-

Q

-

E

-

Q

-

L

-

W

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N

-

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E

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-

T

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-

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K

-

E

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-

E

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A

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L

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Y

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A

C

A

A

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N

N

V

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-

L

-

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-

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Q

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I

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M

T

Y

E

E

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A

Q

R

Q

Q

A

A

L

V

E

-

A

-

G

V

D

D

T

Q

D

A

A

K

S

L

E

E

K

E

E

E

F

M

G

G

D

D

L

L

F

F

T

A

L

T

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V

E

N

L

L

G

A

R

R

R

H

K

L

G

G

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T

K

K

A

A

N

E

A

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A

A

L

L

D

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F

K

A

A

N

N

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K

F
|
F

L

E

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R
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R

F

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A

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Q

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M

V

E

E

K

R

M

I

A

V

E

A

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R

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-

S

-

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L

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L

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W
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W

D

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Q

A

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K

A

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S

Q

E

E

binding adenosine-5'-triphosphate: F190 (= F229), R193 (= R232), W218 (= W259)

3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
29% identity, 89% coverage: 31:266/266 of query aligns to 14:219/220 of 3crcB

query
sites
3crcB

W

W

D

D

K

K

D

E

Q

Q

T

T

P

F

A

A

S

T

L

I

C

A

D

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Y

Y

L

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A

L

E

E

T

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F

Y

E

E

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I

L

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A

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M

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A

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A

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-

H

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A

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A

F

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L

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A

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Y

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A

C

A

A

R

N

N

V

G

G

F
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F

T

D

W
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W

D

T

S

T

-

L

-

G

-

P

-

V

D

V

E

D

E
x
K

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V

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R

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Q
x
E

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x
E

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E

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W

A

Q

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Q

Q

A

A

L

V

E

-

A

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V

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T

Q

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A

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L

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E

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E
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E

F

M

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G

D
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D

L

L

F

F

T

A

L

T

V

V

E

N

L

L

G

A

R

R

R

H

K

L

G

G

I

T

K

K

A

A

N

E

A

I

A

A

L

L

D

Q

F

K

A

A

N

N

Q

E

K

K

F

F

L

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R

R

F

F

A

R

Q

E

M

V

E

E

K

R

M

I

A

V

E

A

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R

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G

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L

S

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L

M

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T

D

G

M

V

D

D

L

L

D

E

A

T

M

M

N

E

Q

E

L

V

W

W

D

Q

E

Q

A

V

K

A

Q

R

S

Q

E

E

binding adenosine-5'-triphosphate: F116 (= F165), W118 (= W167), K127 (≠ E172), E131 (≠ Q176), E134 (≠ S179)
binding magnesium ion: E131 (≠ Q176), E134 (≠ S179), E152 (= E199), D155 (= D202)

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, 51% coverage: 30:165/266 of query aligns to 102:238/324 of A0R3C4

query
sites
A0R3C4

P

P

W

W

D

E

K

S

D

E

Q

Q

T

T

P

H

A

D

S

S

L

L

C

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D

R

Y

Y

L

L

A

L

E

E

T

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F

Y

E

E

L

L

I

F

E

D

G

A

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A

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G

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N

T

A

R

D

E

E

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M

R

E

E

M

L

G

G

D

D

V

V

L

L

F

L

I

Q

L

V

L

L

F

F

M

H

N

A

T

R

L

I

H

A

E

E

Q

D

S

A

G

P

-

H

D

P

F

F

S

S

M

I

S

D

D

D

A

V

L

A

R

D

H

A

S

L

A

V

A

R

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K

M

L

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G

R

N

R

R

H

V

P

P

H

A

V

V

F

L

G

A

K

G

K

E

R

S

F

I

D

S

T

L

Q

D

E

E

Q

Q

L

L

W

A

D

-

N

Q

W

W

E

E

K

E

T

R

K

K

K

A

Q

Q

E

E

K

K

E

K

S

V

E

K

G

A

S

R

K

A

G

S

V

S

F

M

D

D

S

D

L

V

P

P

K

T

G

G

L

Q

P

P

P
x
A

L

L

L

A

R

L

S

A

Y

Q

R

K

I

V

N

L

S

A

K

R

A

V

A

S

R

Q

N

A

G

G

F

L

A222 (≠ P149) mutation to E: Pyrophosphohydrolase activity is reduced 30-fold.

P96379 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
32% identity, 51% coverage: 30:165/266 of query aligns to 102:235/325 of P96379

query
sites
P96379

P

P

W

W

D

E

K

S

D

E

Q

Q

T

T

P

H

A

D

S

S

L

L

C

R

D

R

Y

Y

L

L

A

L

E

E

T

T

F

Y

E

E

L

L

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L

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D

G

A

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A

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G

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R

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E

M

L

G

G

D

D

V

L

L

L

F

L

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Q

L

V

L

L

F

F

M

H

N

A

T

R

L

I

H

A

E

E

Q

D

S

A

-

S

-

Q

G

S

D

P

F

F

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M

I

S

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D

D

A

V

L

A

R

D

H

T

S

L

A

M

A

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K

M

L

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G

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N

R

R

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A

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P

H

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V

F

L

G

A

K

G

K

E

R

S

F

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S

T

L

Q

E

E

D

Q

Q

L

L

W

-

D

A

N

Q

W

W

E

E

K

A

T

A

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K

K

A

Q

S

E

E

K

K

E

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S

-

E

-

G

A

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K

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G

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V

F

A

D

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S

D

L

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G

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P

P
x
A

L

L

L

A

R

L

S

A

Y

Q

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N

I

S

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K

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A

A

A

Q

R

K

N

A

G

G

F

L

A219 (≠ P149) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.

7yh5B Mazg(mycobacterium tuberculosis) (see paper)
38% identity, 24% coverage: 30:92/266 of query aligns to 102:166/177 of 7yh5B

query
sites
7yh5B

P

P

W

W

D

E

K

S

D

E

Q

Q

T

T

P

H

A

D

S

S

L

L

C

R

D

R

Y

Y

L

L

A

L

E

E

E
|
E

T

T

F

Y

E
|
E

L

L

I

L

E

D

G

A

I

V

R

R

A

S

G

G

D

S

T

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R

D

E

Q

T

L

M

R

E

E

E
|
E

M

L

G

G

D
|
D

V

L

L

L

F

L

I

Q

L

V

L

L

F

F

M

H

N

A

T

R

L

I

H

A

E

E

Q

D

S

A

-

S

-

Q

G

S

D

P

F

F

S

T

M

I

S

D

D

D

A

V

binding magnesium ion: E119 (= E47), E122 (= E50), E138 (= E66), D141 (= D69)

2yxhA Crystal structure of mazg-related protein from thermotoga maritima
24% identity, 35% coverage: 29:120/266 of query aligns to 16:109/114 of 2yxhA

query
sites
2yxhA

C

C

P

P

W

W

D

L

K

E

D

K

Q

Q

T

S

P

I

A

E

S

T

L

L

C

L

D

E

Y

A

L

L

A

A

E

S

E
|
E

T

I

F

E

E
|
E

L

V

I

A

E

E

G

A

I

V

R

K

A

K

G

N

D

D

T

L

R

A

E

N

T

L

M

E

E

E

E
|
E

M

I

G

G

D
|
D

V

M

L

I

F

Y

I
x
D

L

A

L

L

F

L

M

V

N

A

T

A

L

V

H

A

E

Q

Q

R

S

D

G

Y

D

G

F

I

S

D

M

L

S

E

D

S

A

A

L

I

R

Q

H

K

S

V

A

V

A

E

K

K

M

I

I

S

R

H

R

R

H

K

P

P

H

W

V

L

F

F

G

W

K

E

R

K

F

I

D

S

T

L

Q

E

-

E

-

A

E

E

Q

K

L

I

W

W

binding magnesium ion: E34 (= E47), E34 (= E47), E37 (= E50), E53 (= E66), D56 (= D69), D60 (≠ I73)

Query Sequence

>WP_018123527.1 NCBI__GCF_000375485.1:WP_018123527.1
MSERTFDDGAEALAELRDVLNSLLGPEGCPWDKDQTPASLCDYLAEETFELIEGIRAGDT
RETMEEMGDVLFILLFMNTLHEQSGDFSMSDALRHSAAKMIRRHPHVFGKKRFDTQEQLW
DNWEKTKKQEKESEGSKGVFDSLPKGLPPLLRSYRINSKAARNGFTWDSDEEVQRQYESE
WTEWQQALEAGDTDASEKEFGDLLFTLVELGRRKGIKANAALDFANQKFLRRFAQMEKMA
EERGQSLDDMDLDAMNQLWDEAKQSE

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