SitesBLAST

R95 (= R102) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K119 (= K127) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
K168 (= K176) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KVYEE 168:172 (≠ KITEE 176:180) binding ATP
E171 (= E179) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E172 (= E180) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
E175 (= E183) binding ATP; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K189 (≠ T196) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KLEE 189:192 (≠ TF-E 196:198) binding ATP
E192 (= E198) 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 (≠ KFTRR 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.

3crcA Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
48% identity, 96% coverage: 11:266/268 of query aligns to 3:225/225 of 3crcA

query
sites
3crcA

L

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D

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R

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A

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F

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Y

Y

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K

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L

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A

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R

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H

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P

H

-

V

-

F

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D

-

A

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K

-

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-

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-

E

-

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-

I

-

K

-

A

-

E

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-

R

-

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Q

-

A

-

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G

S

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L

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A

A

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R

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A

A

V

Q

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K

L

I

Q

Q

K

K

R

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C

A

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N

V

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F

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K

K

I

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E

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A

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R

D

E

E

L

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M

-

Y

E

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A

A

R

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N

A

L

V

T

V

A

D

E

Q

E

A

T

K

F

L

-

E

E

E

F

M

G

G

D

D

L

L

F

F

V

A

M

T

A

V

N

N

L

L

G

A

R

R

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H

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L

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G

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T

D

K

P

A

E

E

A

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A

A

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L

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A

K

A

A

N

N

A

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K

K

F
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F

T

E

R

R

R
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R

F

F

E

R

R

E

I

V

E

E

A

R

W

I

L

V

A

A

E

-

G

A

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R

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E

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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)
44% identity, 96% coverage: 11:266/268 of query aligns to 3:219/220 of 3crcB

query
sites
3crcB

L

I

P

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R

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L

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D

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F

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A

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A

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Q

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A

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A

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-

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-

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F

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K

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E

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-

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E

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D

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N

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A

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A

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E

binding adenosine-5'-triphosphate: F116 (= F165), W118 (= W167), K127 (= K176), E131 (= E180), E134 (= E183)
binding magnesium ion: E131 (= E180), E134 (= E183), E152 (= E199), D155 (= D202)

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)
44% identity, 96% coverage: 7:264/268 of query aligns to 4:251/255 of Q9X015

query
sites
Q9X015

A

A

G

G

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x
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R

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G

E41 (= E45) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
E42 (= E46) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
E45 (= E49) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
E61 (= E65) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
R97 (≠ A101) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
R98 (= R102) 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 (= E183) mutation to A: Has little effects on the NTPase activity.
E176 (= E186) mutation to A: Has little effects on the NTPase activity.
EE 185:186 (= EE 198:199) mutation to AA: Has little effects on the NTPase activity.

A0R3C4 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
41% identity, 56% coverage: 15:165/268 of query aligns to 91:238/324 of A0R3C4

query
sites
A0R3C4

L

V

A

A

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M

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-

A

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W

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E

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L

A222 (= A149) 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)
41% identity, 56% coverage: 15:165/268 of query aligns to 91:235/325 of P96379

query
sites
P96379

L

V

A

A

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M

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N

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A

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G

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D

-

A

A

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D

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Q

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W

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K

A

A

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E

E

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K

A

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Q

-

A

-

G

-

V

V

L

A

D

D

G

D

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V

A

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G

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A
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A

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A

A

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A

G

G

F

L

A219 (= A149) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.

7yh5B Mazg(mycobacterium tuberculosis) (see paper)
44% identity, 32% coverage: 15:99/268 of query aligns to 91:174/177 of 7yh5B

query
sites
7yh5B

L

V

A

A

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M

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Y

Y

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L

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E
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E

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E
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E

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A

L

D

D

A

A

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A

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E

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|
D

L

L

Q

Q

T

V

V

L

F

F

H

H

A

A

R

R

L

I

A

A

E

E

E

D

-

A

-

S

R

Q

G

S

L

P

F

F

D

T

F

I

E

D

A

D

V

V

A

A

K

D

G

T

I

L

A

M

D

R

K

K

M

L

binding magnesium ion: E119 (= E46), E122 (= E49), E138 (= E65), D141 (= D68)

2yxhA Crystal structure of mazg-related protein from thermotoga maritima
29% identity, 37% coverage: 11:109/268 of query aligns to 2:97/114 of 2yxhA

query
sites
2yxhA

L

V

P

E

R

R

L

L

A

E

I

I

M

I

E

E

R

R

L

-

R

-

D

-

P

S

E

L

R

R

G

K

C

C

P

P

W

W

D

L

V

E

E

K

Q

Q

T

S

F

I

A

E

S

T

I

L

A

L

P

E

Y

A

T

L

L

A

E

S

E
|
E

A

I

H

E

E
|
E

V

V

A

A

D

E

A

A

I

V

A

K

R

K

E

N

D

D

W

L

D

A

E

N

L

L

R

E

G

E

E
|
E

L

I

G

G

D
|
D

L

M

L

I

L

Y

Q
x
D

T

A

V

L

F

L

H

V

A

A

R

A

L

V

A

A

E

Q

E

R

R

D

G

Y

L

G

F

I

D

D

F

L

E

E

A

S

V

A

A

I

K

Q

G

K

I

V

A

V

D

E

K

K

M

I

I

S

A

H

R

R

H

K

P

P

H

W

V

L

F

F

G

W

D

E

binding magnesium ion: E34 (= E46), E34 (= E46), E37 (= E49), E53 (= E65), D56 (= D68), D60 (≠ Q72)

Query Sequence

>WP_011841098.1 NCBI__GCF_000015985.1:WP_011841098.1
MSDPFTAGPGLPRLLAIMERLRDPERGCPWDVEQTFASIAPYTLEEAHEVADAIAREDWD
ELRGELGDLLLQTVFHARLAEERGLFDFEAVAKGIADKMIARHPHVFGDASRDKSSDQQT
LDWERIKAAERAGRAQAGVLDGVALGLPALTRAVKLQKRAARVGFDWPSTGEVLDKITEE
ARELVEARDNLTAEETFEEFGDLLFVMANLGRHLKIDPEAALRAANAKFTRRFERIEAWL
AEEGRGPEDSTLAEMDALWDRAKAEERA

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