SitesBLAST

R95 (= R97) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K119 (= K121) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
K168 (= K174) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KVYEE 168:172 (≠ KVEEE 174:178) binding ATP
E171 (= E177) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E172 (= E178) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
E175 (= E181) binding ATP; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K189 (≠ H193) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KLEE 189:192 (≠ HVQE 193:196) binding ATP
E192 (= E196) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E193 (= E197) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
D196 (= D200) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K222 (= K226) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
KFERR 222:226 (≠ KFTRR 226:230) binding ATP
R226 (= R230) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
W253 (= W257) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K257 (= K261) 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, 93% coverage: 9:262/272 of query aligns to 6:223/225 of 3crcA

query
sites
3crcA

L

L

T

T

L

I

M

M

A

Q

R

R

L

L

R

R

D

D

P

P

E

E

T

N

G

G

C

C

A

P

W

W

D

D

V

K

K

E

Q

Q

D

T

F

F

V

A

S

T

L

I

I

A

P

P

Y

Y

T

T

I

L

E

E

A

T

Y

Y

E

E

V

V

A

L

D

D

A

A

I

I

E

A

R

R

N

E

D

D

F

F

D

D

L

L

R

R

G

G

E

E

L

L

G

G

D

D

L

L

L

F

Q

Q

V

V

F

F

H

Y

S

A

R

Q

I

M

A

A

E

Q

E

E

R

E

G

G

L

R

F

F

D

D

F

F

E

N

Q

D

V

I

A

C

A

A

G

A

I

I

S

S

E

D

K

K

L

L

V

E

S

R

R

R

H

H

P

P

H

-

V

-

F

-

A

-

G

-

V

-

N

-

F

-

E

-

T

-

D

-

E

-

Q

-

R

-

Q

-

A

-

W

-

D

-

A

-

K

-

A

-

Q

-

E

-

R

-

Q

-

K

-

N

-

T

-

G

-

N

-

K

-

P

-

E

-

S

S

V

A

L

L

S

D

G

D

V

I

A

P

K

R

S

S

L

L

P

P

A

A

L

L

V

M

A

R

C

A

E

Q

K

K

I

I

Q

Q

N

K

R

R

A

C

A

A

S

N

H

V

G

G

F

F

D

D

W

W

P

T

D

T

V

L

D

G

P

P

V

V

F

V

D

D

K

K

V

V

E

Y

E

E

L

I

Q

D

E

E

V

V

-

M

H

Y

E

E

A

A

W

R

Q

Q

S

A

-

V

G

V

D

D

Q

Q

A

A

H

K

V

L

Q

E

E

E

V

M

G

G

D

D

L

L

L

F

V

A

V

T

V

V

N

N

L

L

A

A

R

R

H

H

L

L

K

G

V

T

N

K

P

A

E

E

I

I

A

A

L

L

K

Q

E

K

A

A

T

N

K

E

K

K

F
|
F

T

E

R

R

R
|
R

F

F

N

R

Y

E

I

V

E

E

K

R

Q

I

I

V

E

A

A

A

S

R

G

G

R

L

Q

E

L

M

R

T

E

D

C

L

E

E

L

T

A

M

E

E

L

-

D

-

G

E

L

V

W
|
W

H

Q

E

Q

A

V

K

A

R

R

binding adenosine-5'-triphosphate: F190 (= F227), R193 (= R230), W218 (= W257)

3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
44% identity, 93% coverage: 9:262/272 of query aligns to 6:217/220 of 3crcB

query
sites
3crcB

L

L

T

T

L

I

M

M

A

Q

R

R

L

L

R

-

D

-

P

-

E

-

T

-

G

-

C

-

A

-

W

W

D

D

V

K

K

E

Q

Q

D

T

F

F

V

A

S

T

L

I

I

A

P

P

Y

Y

T

T

I

L

E

E

A

T

Y

Y

E

E

V

V

A

L

D

D

A

A

I

I

E

A

R

R

N

E

D

D

F

F

D

D

L

L

R

R

G

G

E

E

L

L

G

G

D

D

L

L

L

F

Q

Q

V

V

F

F

H

Y

S

A

R

Q

I

M

A

A

E

Q

E

E

R

E

G

G

L

R

F

F

D

D

F

F

E

N

Q

D

V

I

A

C

A

A

G

A

I

I

S

S

E

D

K

K

L

L

V

-

S

-

R

-

H

-

P

-

H

-

V

-

F

-

A

-

G

-

V

-

N

-

F

-

E

-

T

-

D

-

E

-

Q

-

R

-

Q

-

A

-

W

-

D

-

A

-

K

-

A

-

Q

-

E

E

R

R

Q

A

Q

Q

K

-

N

-

T

-

G

-

N

-

K

-

P

-

E

H

S

S

V

A

L

L

S

D

G

D

V

I

A

P

K

R

S

S

L

L

P

P

A

A

L

L

V

M

A

R

C

A

E

Q

K

K

I

I

Q

Q

N

K

R

R

A

C

A

A

S

N

H

V

G

G

F
|
F

D

D

W
|
W

P

T

D

T

V

L

D

G

P

P

V

V

F

V

D

D

K
|
K

V

V

E

Y

E

E

E
|
E

L

I

Q

D

E
|
E

V

V

-

M

H

Y

E

E

A

A

W

R

Q

Q

S

A

G

V

-

V

D

D

Q

Q

A

A

H

K

V

L

Q

E

E

E

E
|
E

V

M

G

G

D
|
D

L

L

L

F

V

A

V

T

V

V

N

N

L

L

A

A

R

R

H

H

L

L

K

G

V

T

N

K

P

A

E

E

I

I

A

A

L

L

K

Q

E

K

A

A

T

N

K

E

K

K

F

F

T

E

R

R

F

F

N

R

Y

E

I

V

E

E

K

R

Q

I

I

V

E

A

A

A

S

R

G

G

R

L

Q

E

L

M

R

T

E

G

C

V

E

D

L

L

A

E

E

T

L

M

D

E

G

E

L

V

W

W

H

Q

E

Q

A

V

K

A

R

R

binding adenosine-5'-triphosphate: F116 (= F163), W118 (= W165), K127 (= K174), E131 (= E178), E134 (= E181)
binding magnesium ion: E131 (= E178), E134 (= E181), E152 (= E197), D155 (= D200)

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)
45% identity, 93% coverage: 8:261/272 of query aligns to 10:250/255 of Q9X015

query
sites
Q9X015

E

E

L

L

L

V

T

S

L

I

M

M

A

E

R

K

L

L

R

R

D

S

P

P

E

E

T

-

G

G

C

C

A

E

W

W

D

D

V

R

K

K

Q

Q

D

T

F

H

V

E

S

S

L

L

I

K

P

P

Y

Y

T

L

I

I

E
|
E

A

C

Y

Y

E
|
E

V

L

A

I

D

E

A

A

I

I

E

D

R

E

N

K

D

N

F

D

D

D

D

M

L

M

R

K

G

E

E
|
E

L

L

G

G

D

D

L

V

L

L

Q

Q

V

V

F

F

H

H

S

A

R

Q

I

I

A

A

E

R

E

E

R

R

G

G

L

A

F

F

D

T

F

I

E

E

Q

D

V

V

A

I

A

R

G

T

I

L

S

N

E

E

K

K

L

L

V

I

S
x
R

R
|
R

H

H

P

P

H

H

V

V

F

F

A

G

G

-

V

-

N

-

F

-

E

D

T

S

D

P

E

G

Q

Y

R

S

Q

Y

Q

K

A

Q

W

W

D

E

D

D

A

I

K
|
K

A

A

Q

Q

E

E

R

K

Q

-

K

-

N

-

T

-

G

G

N

K

K

K

P

K

E

S

S

S

V

R

L

I

S

G

G

E

V

I

A

N

K

P

S

L

L

V

P

P

A

A

L

L

V

S

A

M

C

A

E

R

K

R

I

I

Q

Q

N

E

R

N

A

A

A

S

S

Q

H

V

G

G

F

F

D

D

W

W

P

K

D

D

V

P

D

E

P

G

V

V

F

Y

D

E

K

K

V

I

E

E

L

L

Q

K

E
|
E

V

L

H

K

E

-

A

-

W

-

Q
x
E

S

A

G

K

D

D

Q

P

A

R

H

E

V

L

Q

E

E
|
E

V

F

G

G

D

D

L

L

L

F

V

S

V

I

V

V

N

N

L

L

A

S

R

R

H

F

L

L

K

N

V

V

N

D

P

P

E

E

I

S

A

A

L

L

K

R

E

K

A

A

T

T

K

R

K

K

F

F

T

V

R

E

R

R

F

F

N

K

Y

K

I

M

E

E

K

E

Q

L

I

I

E

E

A

K

S

D

G

G

R

L

Q

V

L

L

R

E

E

E

C

L

E

P

L

I

A

E

E

K

L

L

D

D

G

E

L

Y

W

W

H

E

E

K

A

A

K

K

E41 (= E40) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
E42 (= E41) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
E45 (= E44) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
E61 (= E60) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
R97 (≠ S96) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
R98 (= R97) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
K118 (= K121) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
E173 (= E181) mutation to A: Has little effects on the NTPase activity.
E176 (≠ Q187) mutation to A: Has little effects on the NTPase activity.
EE 185:186 (= EE 196:197) 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)
39% identity, 57% coverage: 10:163/272 of query aligns to 91:238/324 of A0R3C4

query
sites
A0R3C4

L

V

T

A

L

L

M

M

A

D

R

K

L

L

R

R

D

-

P

-

E

-

T

T

G

S

C

G

A

P

W

W

D

E

V

S

K

E

Q

Q

D

T

F

H

V

D

S

S

L

L

I

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

N

G

D

N

F

A

D

D

D

E

L

L

R

R

G

E

E

E

L

L

G

G

D

D

L

V

L

L

Q

Q

V

V

V

L

F

F

H

H

S

A

R

R

I

I

A

A

E

E

E

D

R

A

G

P

-

H

L

P

F

F

D

S

F

I

E

D

Q

D

V

V

A

A

A

D

G

A

I

L

S

V

E

R

K

K

L

L

V

G

S

N

R

R

H

V

P

P

H

A

V

V

F

L

A

A

G

G

V

E

N

S

F

I

E

S

T

L

D

D

E

E

Q

Q

R

L

Q

A

Q

Q

A

-

W

W

D

E

A

R

K

K

A

A

Q

Q

E

E

R

K

Q

K

Q

V

K

K

N

A

T

R

G

A

N

S

K

S

P

M

E

D

S

D

V

V

L

P

S

T

G

G

V

-

A

-

K

-

S

-

L

Q

P

P

A
|
A

L

L

V

A

A

L

C

A

E

Q

K

K

I

V

Q

L

N

A

R

R

A

V

A

S

S

Q

H

A

G

G

F

L

A222 (= A147) 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)
39% identity, 57% coverage: 10:163/272 of query aligns to 91:235/325 of P96379

query
sites
P96379

L

V

T

A

L

M

M

M

A

D

R

K

L

L

R

R

D

-

P

-

E

-

T

T

G

A

C

G

A

P

W

W

D

E

V

S

K

E

Q

Q

D

T

F

H

V

D

S

S

L

L

I

R

P

R

Y

Y

T

L

I

L

E

E

A

T

Y

Y

E

E

V

L

A

L

D

D

A

A

I

V

E

R

R

S

N

G

D

S

F

V

D

D

D

Q

L

L

R

R

G

E

E

E

L

L

G

G

D

D

L

L

Q

Q

V

V

V

L

F

F

H

H

S

A

R

R

I

I

A

A

E

E

E

D

-

A

-

S

R

Q

G

S

L

P

F

F

D

T

F

I

E

D

Q

D

V

V

A

A

A

D

G

T

I

L

S

M

E

R

K

K

L

L

V

G

S

N

R

R

H

A

P

P

H

G

V

V

F

L

A

A

G

G

V

E

N

S

F

I

E

S

T

L

D

E

E

D

Q

Q

R

L

Q

A

Q

Q

A

-

W

W

D

E

D

A

A

A

K

K

A

A

Q

S

E

E

R

K

Q

A

Q

R

K

K

N

-

T

-

G

-

N

-

K

-

P

-

E

-

S

S

V

V

L

A

S

D

G

D

V

V

A

H

K

T

S

G

L

Q

P

P

A
|
A

L

L

V

A

A

L

C

A

E

Q

K

K

I

V

Q

I

N

Q

R

R

A

A

A

Q

S

K

H

A

G

G

F

L

A219 (= A147) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.

7yh5B Mazg(mycobacterium tuberculosis) (see paper)
43% identity, 32% coverage: 10:97/272 of query aligns to 91:177/177 of 7yh5B

query
sites
7yh5B

L

V

T

A

L

M

M

M

A

D

R

K

L

L

R

R

D

-

P

-

E

-

T

T

G

A

C

G

A

P

W

W

D

E

V

S

K

E

Q

Q

D

T

F

H

V

D

S

S

L

L

I

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

N

G

D

S

F

V

D

D

D

Q

L

L

R

R

G

E

E
|
E

L

L

G

G

D
|
D

L

L

Q

Q

V

V

V

L

F

F

H

H

S

A

R

R

I

I

A

A

E

E

E

D

-

A

-

S

R

Q

G

S

L

P

F

F

D

T

F

I

E

D

Q

D

V

V

A

A

A

D

G

T

I

L

S

M

E

R

K

K

L

L

V

G

S

N

R

R

binding magnesium ion: E119 (= E41), E122 (= E44), E138 (= E60), D141 (= D63)

2yxhA Crystal structure of mazg-related protein from thermotoga maritima
30% identity, 29% coverage: 23:102/272 of query aligns to 16:95/114 of 2yxhA

query
sites
2yxhA

C

C

A

P

W

W

D

L

V

E

K

K

Q

Q

D

S

F

I

V

E

S

T

L

L

I

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

N

N

D

D

F

L

D

A

D

N

L

L

R

E

G

E

E
|
E

L

I

G

G

D
|
D

L

M

L

I

L

Y

Q
x
D

V

A

V

L

F

L

H

V

S

A

R

A

I

V

A

A

E

Q

E

R

R

D

G

Y

L

G

F

I

D

D

F

L

E

E

Q

S

V

A

A

I

A

Q

G

K

I

V

S

V

E

E

K

K

L

I

V

S

S

H

R

R

H

K

P

P

H

W

V

L

F

F

binding magnesium ion: E34 (= E41), E34 (= E41), E37 (= E44), E53 (= E60), D56 (= D63), D60 (≠ Q67)

Query Sequence

>WP_013818507.1 NCBI__GCF_000214665.1:WP_013818507.1
MSLDKTRELLTLMARLRDPETGCAWDVKQDFVSLIPYTIEEAYEVADAIERNDFDDLRGE
LGDLLLQVVFHSRIAEERGLFDFEQVAAGISEKLVSRHPHVFAGVNFETDEQRQQAWDDA
KAQERQQKNTGNKPESVLSGVAKSLPALVACEKIQNRAASHGFDWPDVDPVFDKVEEELQ
EVHEAWQSGDQAHVQEEVGDLLLVVVNLARHLKVNPEIALKEATKKFTRRFNYIEKQIEA
SGRQLRECELAELDGLWHEAKRVQKNPRSGTQ

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