SitesBLAST

R95 (= R95) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K119 (= K127) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
K168 (= K180) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KVYEE 168:172 (≠ KVREE 180:184) binding ATP
E171 (= E183) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E172 (= E184) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
E175 (= E187) binding ATP; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K189 (≠ A199) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KLEE 189:192 (≠ AIAE 199:202) binding ATP
E192 (= E202) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E193 (= E203) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
D196 (= D206) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K222 (= K232) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
KFERR 222:226 (= KFERR 232:236) binding ATP
R226 (= R236) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
W253 (= W263) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K257 (= K267) 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)
47% identity, 97% coverage: 3:270/276 of query aligns to 2:225/225 of 3crcA

query
sites
3crcA

Q

Q

L

I

P

D

D

R

L

L

H

T

L

I

M

M

A

Q

R

R

L

L

R

R

D

D

P

P

Q

E

H

N

G

G

C

C

P

P

W

W

D

D

L

K

Q

E

Q

Q

D

T

Y

F

A

A

S

T

I

I

V

A

P

P

H

Y

T

T

L

L

E

E

A

T

Y

Y

E

E

V

V

A

L

D

D

A

A

I

I

E

A

S

R

G

E

D

D

F

F

E

D

H

D

L

L

P

R

G

G

E

E

L

L

G

G

D

D

L

L

F

F

Q

Q

V

V

Y

F

Y

Y

S

A

Q

Q

L

M

A

A

R

Q

E

E

G

G

R

R

F

F

D

D

F

F

A

N

T

D

V

I

V

C

D

A

A

A

I

I

T

S

R

D

K

K

L

L

V

E

R

R

H

H

P

P

H

-

V

-

F

-

P

-

D

-

G

-

D

-

L

-

Y

-

G

-

S

-

P

-

E

-

L

-

P

-

R

-

L

-

D

-

E

-

A

-

I

-

K

-

R

-

W

-

E

-

I

-

K

-

A

-

E

-

R

-

A

-

E

-

K

-

A

-

P

-

E

-

Q

-

L

-

S

S

L

A

L

L

D

D

V

I

P

P

S

R

A

S

L

L

P

P

A

A

L

L

S

M

R

R

A

A

A

Q

K

K

L

I

Q

Q

K

K

R

R

A

C

A

A

Q

N

V

V

G

G

F

F

D

D

W

W

P

T

E

T

A

L

L

G

P

P

V

V

D

D

K

K

V

V

R

Y

E

E

L

I

D

D

E

E

V

V

L

M

E

Y

A

E

M

A

S

R

E

Q

N

A

-

V

D

D

P

Q

Q

A

A

K

I

L

A

E

E

E

L

M

G

G

D

D

L

L

F

F

V

A

V

T

V

V

N

N

L

L

A

A

R

R

H

H

L

L

K

G

V

T

D

K

P

A

E

E

N

I

A

A

L

L

R

Q

A

K

A

A

N

N

G

E

K

K

F
|
F

E

E

R

R

R
|
R

F

F

R

R

F

E

I

V

E

E

Q

R

A

I

L

V

R

-

D

-

A

A

G

A

R

R

P

G

I

L

E

E

N

M

C

T

D

D

L

L

E

E

E

T

L

M

D

E

A

E

L

V

W
|
W

G

Q

E

Q

A

V

K

A

K

R

A

Q

E

E

binding adenosine-5'-triphosphate: F190 (= F233), R193 (= R236), W218 (= W263)

3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
44% identity, 97% coverage: 3:270/276 of query aligns to 2:219/220 of 3crcB

query
sites
3crcB

Q

Q

L

I

P

D

D

R

L

L

H

T

L

I

M

M

A

Q

R

R

L

L

R

-

D

-

P

-

Q

-

H

-

G

-

C

-

P

-

W

W

D

D

L

K

Q

E

Q

Q

D

T

Y

F

A

A

S

T

I

I

V

A

P

P

H

Y

T

T

L

L

E

E

A

T

Y

Y

E

E

V

V

A

L

D

D

A

A

I

I

E

A

S

R

G

E

D

D

F

F

E

D

H

D

L

L

P

R

G

G

E

E

L

L

G

G

D

D

L

L

F

F

Q

Q

V

V

Y

F

Y

Y

S

A

Q

Q

L

M

A

A

R

Q

E

E

G

G

R

R

F

F

D

D

F

F

A

N

T

D

V

I

V

C

D

A

A

A

I

I

T

S

R

D

K

K

L

L

V

-

R

-

H

-

P

-

H

-

V

-

F

-

P

-

D

-

G

-

D

-

L

-

Y

-

G

-

S

-

P

-

E

-

L

-

P

-

R

-

L

-

D

-

E

-

A

-

I

-

K

-

R

-

W

-

E

-

I

-

K

-

A

-

E

-

E

E

R

R

A

A

E

Q

K

H

A

S

A

A

A

-

P

-

E

-

Q

-

L

-

S

-

L

-

L

L

D

D

V

I

P

P

S

R

A

S

L

L

P

P

A

A

L

L

S

M

R

R

A

A

A

Q

K

K

L

I

Q

Q

K

K

R

R

A

C

A

A

Q

N

V

V

G

G

F
|
F

D

D

W
|
W

P

T

E

T

A

L

L

G

P

P

V

V

D

D

K
|
K

V

V

R

Y

E

E

E
|
E

L

I

D

D

E
|
E

V

V

L

M

E

Y

A

E

M

A

S

R

E

Q

N

A

-

V

D

D

P

Q

Q

A

A

K

I

L

A

E

E

E

E
|
E

L

M

G

G

D
|
D

L

L

F

F

V

A

V

T

V

V

N

N

L

L

A

A

R

R

H

H

L

L

K

G

V

T

D

K

P

A

E

E

N

I

A

A

L

L

R

Q

A

K

A

A

N

N

G

E

K

K

F

F

E

E

R

R

F

F

R

R

F

E

I

V

E

E

Q

R

A

I

L

V

R

A

D

A

A

R

G

G

R

L

P

E

I

M

E

T

N

G

C

V

D

D

L

L

E

E

E

T

L

M

D

E

A

E

L

V

W

W

G

Q

E

Q

A

V

K

A

K

R

A

Q

E

E

binding adenosine-5'-triphosphate: F116 (= F169), W118 (= W171), K127 (= K180), E131 (= E184), E134 (= E187)
binding magnesium ion: E131 (= E184), E134 (= E187), E152 (= E203), D155 (= D206)

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)
39% identity, 97% coverage: 6:272/276 of query aligns to 10:255/255 of Q9X015

query
sites
Q9X015

D

E

L

L

L

V

H

S

L

I

M

M

A

E

R

K

L

L

R

R

D

S

P

P

Q

E

H

-

G

G

C

C

P

E

W

W

D

D

L

R

Q

K

Q

Q

D

T

Y

H

A

E

S

S

I

L

V

K

P

P

H

Y

T

L

L

I

E
|
E

A

C

Y

Y

E
|
E

V

L

A

I

D

E

A

A

I

I

E

D

S

E

G

K

D

N

F

D

E

D

H

M

L

M

P

K

G

E

E
|
E

L

L

G

G

D

D

L

V

L

L

F

L

Q

Q

V

V

Y

F

Y

H

S

A

Q

Q

L

I

A

A

R

R

E

E

E

R

G

G

R

A

F

F

D

T

F

I

A

E

T

D

V

V

V

I

D

R

A

T

I

L

T

N

R

E

K

K

L

L

V

I

R
|
R

H

H

P

P

H

H

V

V

F

F

P

G

D

D

G

S

D

P

L

G

Y

Y

G

S

S

Y

P

-

E

-

L

-

P

-

R

-

L

-

D

-

E

-

A

-

I

-

K

-

R

K

R

Q

W

W

E

E

E

D

I

I

K
|
K

A

A

E

Q

E

E

R

K

A

G

E

K

K

K

A

K

A

S

A

-

P

-

E

-

Q

-

L

-

S

S

L

R

L

I

D

G

D

E

V

I

P

N

S

P

A

L

L

V

P

P

A

A

L

L

S

S

R

M

A

A

A

R

K

R

L

I

Q

Q

K

E

R

N

A

A

A

S

Q

Q

V

V

G

G

F

F

D

D

W

W

P

K

E

D

A

P

L

E

P

G

V

V

V

Y

D

E

K

K

V

I

R

E

E

E

E

-

L

-

D

-

E

E

V

L

L

K

E
|
E

A

L

M

K

S
x
E

E

A

N

K

D

D

P

P

Q

R

A

E

I

L

A

E

E
|
E

L

F

G

G

D

D

L

L

F

F

V

S

V

I

V

V

N

N

L

L

A

S

R

R

H

F

L

L

K

N

V

V

D

D

P

P

E

E

N

S

A

A

L

L

R

R

A

K

A

A

N

T

G

R

K

K

F

F

E

V

R

E

R

R

F

F

R

K

F

K

I

M

E

E

Q

E

A

L

L

I

R

E

D

K

A

D

G

G

R

L

P

V

I

L

E

E

N

E

C

L

D

P

L

I

E

E

E

K

L

L

D

D

A

E

L

Y

W

W

G

E

E

K

A

A

K

K

K

G

A

G

E

D

R

E

S

T

E41 (= E38) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
E42 (= E39) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
E45 (= E42) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
E61 (= E58) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
R97 (= R94) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
R98 (= R95) 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 (= E190) mutation to A: Has little effects on the NTPase activity.
E176 (≠ S193) mutation to A: Has little effects on the NTPase activity.
EE 185:186 (= EE 202:203) 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)
38% identity, 61% coverage: 3:169/276 of query aligns to 86:238/324 of A0R3C4

query
sites
A0R3C4

Q

R

L

L

P

V

D

D

L

A

L

V

H

A

L

L

M

M

A

D

R

K

L

L

R

R

D

-

P

-

Q

-

H

T

G

S

C

G

P

P

W

W

D

E

L

S

Q

E

Q

Q

D

T

Y

H

A

D

S

S

I

L

V

R

P

R

H

Y

T

L

L

L

E

E

A

T

Y

Y

E

E

V

L

A

F

D

D

A

A

I

V

E

R

S

S

G

G

D

N

F

A

E

D

H

E

L

L

P

R

G

E

E

E

L

L

G

G

D

D

L

V

L

L

F

L

Q

Q

V

V

V

L

Y

F

Y

H

S

A

Q

R

L

I

A

A

R

E

E

D

E

A

G

P

R

H

F

H

D

P

F

F

A

S

T

I

-

D

V

V

V

A

D

D

A

A

I

L

T

V

R

R

K

K

L

L

V

G

R

N

R

R

H

V

P

P

H

A

V

V

F

L

P

-

D

-

G

-

D

-

L

-

Y

-

G

-

S

A

P

G

E

E

L

S

P

I

R

S

L

L

D

D

E

E

A

Q

A

L

I

A

K

Q

R

-

W

W

E

E

I

R

K

K

A

A

E

Q

E

E

R

K

A

K

E

V

K

K

A

A

A

R

A

A

P

-

E

-

Q

-

L

-

S

S

L

S

L

M

D

D

V

V

P

P

S

T

A

G

L

Q

P

P

A
|
A

L

L

S

A

R

L

A

A

A

Q

K

K

L

V

Q

L

K

A

R

R

A

V

A

S

Q

Q

V

A

G

G

F

L

A222 (= A153) 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)
30% identity, 89% coverage: 3:249/276 of query aligns to 86:282/325 of P96379

query
sites
P96379

Q

R

L

L

P

V

D

D

L

A

L

V

H

A

L

M

M

M

A

D

R

K

L

L

R

R

D

T

P

-

Q

-

H

-

G

A

C

G

P

P

W

W

D

E

L

S

Q

E

Q

Q

D

T

Y

H

A

D

S

S

I

L

V

R

P

R

H

Y

T

L

L

L

E

E

A

T

Y

Y

E

E

V

L

A

L

D

D

A

A

I

V

E

R

S

S

G

G

D

S

F

V

E

D

H

Q

L

L

P

R

G

E

E

E

L

L

G

G

D

D

L

L

F

L

Q

Q

V

V

V

L

Y

F

Y

H

S

A

Q

R

L

I

A

A

R

E

E

D

E

A

G

S

R

Q

-

S

-

P

F

F

D

T

F

I

A

D

T

D

V

V

V

A

D

D

A

T

I

L

T

M

R

R

K

K

L

L

V

G

R

N

R

R

H

A

P

P

H

G

V

V

F

L

P

A

D

G

G

E

D

S

L

I

Y

S

G

L

S

E

P

D

E

Q

L

L

P

A

R

-

L

-

D

-

E

-

A

-

I

-

K

-

R

-

R

Q

W

W

E

E

E

A

I

A

K

K

A

A

E

S

E

E

R

K

A

A

E

R

K

K

A

S

A

V

A

A

P

-

E

-

Q

-

L

-

S

-

L

-

D

D

V

V

P

H

S

T

A

G

L

Q

P

P

A
|
A

L

L

S

A

R

L

A

A

A

Q

K

K

L

V

Q

I

K

Q

R

R

A

A

A

Q

Q

K

V

A

G

G

F

L

D

-

W

-

P

P

E

A

A

H

L

L

P

-

V

-

D

-

K

-

V

-

R

-

E

-

L

-

D

-

E

-

V

-

L

-

E

-

A

-

M

-

S

-

E

-

N

-

D

-

P

-

Q

-

A

-

I

I

A

P

E

D

E

E

L

-

G

-

D

-

L

-

F

-

V

-

V

I

V

T

N

S

L

V

A

S

R

V

H

S

L

A

K

D

V

V

D

D

P

A

E

E

N

N

A

T

L

L

R

R

A

T

A

A

N

V

G

L

K

D

F

F

E

I

R

D

R

R

F

L

R

R

F

C

I

A

E

E

Q

R

A

A

L

I

R

A

D

V

A

A

G

R

R

R

A219 (= A153) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.

7yh5B Mazg(mycobacterium tuberculosis) (see paper)
37% identity, 34% coverage: 3:95/276 of query aligns to 86:177/177 of 7yh5B

query
sites
7yh5B

Q

R

L

L

P

V

D

D

L

A

L

V

H

A

L

M

M

M

A

D

R

K

L

L

R

R

D

T

P

-

Q

-

H

-

G

A

C

G

P

P

W

W

D

E

L

S

Q

E

Q

Q

D

T

Y

H

A

D

S

S

I

L

V

R

P

R

H

Y

T

L

L

L

E

E

E
|
E

A

T

Y

Y

E
|
E

V

L

A

L

D

D

A

A

I

V

E

R

S

S

G

G

D

S

F

V

E

D

H

Q

L

L

P

R

G

E

E
|
E

L

L

G

G

D
|
D

L

L

F

L

Q

Q

V

V

V

L

Y

F

Y

H

S

A

Q

R

L

I

A

A

R

E

E

D

E

A

G

S

R

Q

F

S

D

P

F

F

A

T

T

I

-

D

V

V

V

A

D

D

A

T

I

L

T

M

R

R

K

K

L

L

V

G

R

N

R

R

binding magnesium ion: E119 (= E39), E122 (= E42), E138 (= E58), D141 (= D61)

2yxhA Crystal structure of mazg-related protein from thermotoga maritima
25% identity, 29% coverage: 21:100/276 of query aligns to 16:95/114 of 2yxhA

query
sites
2yxhA

C

C

P

P

W

W

D

L

L

E

Q

K

Q

Q

D

S

Y

I

A

E

S

T

I

L

V

L

P

E

H

A

T

L

L

A

E

S

E
|
E

A

I

Y

E

E
|
E

V

V

A

A

D

E

A

A

I

V

E

K

S

K

G

N

D

D

F

L

E

A

H

N

L

L

P

E

G

E

E
|
E

L

I

G

G

D
|
D

L

M

L

I

F

Y

Q
x
D

V

A

V

L

Y

L

Y

V

S

A

Q

A

L

V

A

A

R

Q

E

R

E

D

G

Y

R

G

F

I

D

D

F

L

A

E

T

S

V

A

V

I

D

Q

A

K

I

V

T

V

R

E

K

K

L

I

V

S

R

H

R

R

H

K

P

P

H

W

V

L

F

F

binding magnesium ion: E34 (= E39), E34 (= E39), E37 (= E42), E53 (= E58), D56 (= D61), D60 (≠ Q65)

Query Sequence

>WP_013983285.1 NCBI__GCF_000013785.1:WP_013983285.1
MYQLPDLLHLMARLRDPQHGCPWDLQQDYASIVPHTLEEAYEVADAIESGDFEHLPGELG
DLLFQVVYYSQLAREEGRFDFATVVDAITRKLVRRHPHVFPDGDLYGSPELPRLDEAAIK
RRWEEIKAEERAEKAAAPEQLSLLDDVPSALPALSRAAKLQKRAAQVGFDWPEALPVVDK
VREELDEVLEAMSENDPQAIAEELGDLLFVVVNLARHLKVDPENALRAANGKFERRFRFI
EQALRDAGRPIENCDLEELDALWGEAKKAERSPSCG

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