SitesBLAST

R95 (= R96) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K119 (= K129) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
K168 (= K184) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KVYEE 168:172 (≠ KLHEE 184:188) binding
E171 (= E187) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E172 (= E188) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
E175 (= E191) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K189 (≠ A208) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KLEE 189:192 (≠ AVED 208:211) binding
E192 (≠ D211) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E193 (= E212) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
D196 (= D215) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K222 (= K241) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
KFERR 222:226 (≠ KFDAR 241:245) binding
R226 (= R245) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
W253 (= W272) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K257 (= K276) 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)
44% identity, 95% coverage: 5:275/285 of query aligns to 3:221/225 of 3crcA

query
sites
3crcA

I

I

E

D

D

R

L

L

K

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

P

P

W

W

D

D

T

K

R

E

Q

Q

S

T

Y

F

R

A

T

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

R

R

E

E

D

D

Y

F

P

D

H

D

L

L

K

R

D

G

E

E

L

L

G

G

D

D

L

L

F

F

Q

Q

V

V

I

V

F

F

Y

Y

T

A

Q

Q

L

M

G

A

R

Q

E

E

D

E

G

G

H

R

F

F

D

D

F

F

D

N

G

D

V

I

V

C

D

A

H

A

L

I

V

S

R

D

K

K

L

L

V

E

R

R

H

H

P

P

H

-

V

-

F

-

P

-

E

-

G

-

T

-

L

-

E

-

S

-

I

-

D

-

P

-

D

-

N

-

R

-

P

-

D

-

E

-

A

-

W

-

I

-

K

-

E

-

S

-

W

-

E

-

R

-

I

-

K

-

A

-

E

-

R

-

A

-

M

-

K

-

P

-

A

-

P

-

E

-

A

-

S

-

A

-

P

-

V

-

S

S

R

A

L

L

D

D

G

D

I

I

A

P

R

R

T

S

L

L

P

P

A

A

M

L

A

M

R

R

A

A

E

Q

K

K

L

I

Q

Q

K

K

R

R

A

C

A

A

R

N

H

V

G

G

F

F

D

D

W

W

P

T

N

T

V

L

G

G

P

P

V

V

F

V

D

D

K

K

L

V

H

Y

E

E

I

I

D

D

E

E

L

V

K

-

E

-

A

M

W

Y

E

E

A

A

A

R

Q

Q

T

-

G

A

A

V

G

V

D

D

P

Q

D

A

A

K

V

L

E

E

D

E

E

E

L

M

G

G

D

D

L

L

F

F

V

A

C

T

V

V

N

N

L

L

A

A

R

R

F

H

M

L

K

G

V

T

N

K

P

A

E

E

Q

I

A

A

L

L

N

Q

R

K

T

A

N

N

H

E

K

K

F
|
F

D

E

A

R

R
|
R

F

F

R

R

A

E

I

V

E

E

R

R

V

I

L

V

E

A

R

A

E

R

G

G

R

L

D

E

M

M

D

T

E

D

E

-

S

-

L

L

E

E

A

T

L

M

D

E

A

E

V

V

W
|
W

Q

Q

A

Q

V

V

binding adenosine-5'-triphosphate: F190 (= F242), R193 (= R245), W218 (= W272)

3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
41% identity, 95% coverage: 5:275/285 of query aligns to 3:215/220 of 3crcB

query
sites
3crcB

I

I

E

D

D

R

L

L

K

L

T

T

L

I

M

M

A

Q

R

R

L

L

R

-

D

-

P

-

E

-

T

-

G

-

C

-

P

-

W

W

D

D

T

K

R

E

Q

Q

S

T

Y

F

R

A

T

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

R

R

E

E

D

D

Y

F

P

D

H

D

L

L

K

R

D

G

E

E

L

L

G

G

D

D

L

L

F

F

Q

Q

V

V

I

V

F

F

Y

Y

T

A

Q

Q

L

M

G

A

R

Q

E

E

D

E

G

G

H

R

F

F

D

D

F

F

D

N

G

D

V

I

V

C

D

A

H

A

L

I

V

S

R

D

K

K

L

L

V

-

R

-

H

-

P

-

H

-

V

-

F

-

P

-

E

-

G

-

T

-

L

-

E

-

S

-

I

-

D

-

P

-

D

-

N

-

R

-

P

-

D

-

E

-

A

-

W

-

I

-

K

-

E

-

S

-

W

-

E

-

R

-

I

-

K

-

A

-

E

-

E

E

R

R

A

A

M

Q

K

H

P

S

A

A

P

-

E

-

A

-

S

-

A

-

P

-

V

-

S

-

R

-

L

L

D

D

G

D

I

I

A

P

R

R

T

S

L

L

P

P

A

A

M

L

A

M

R

R

A

A

E

Q

K

K

L

I

Q

Q

K

K

R

R

A

C

A

A

R

N

H

V

G

G

F
|
F

D

D

W
|
W

P

T

N

T

V

L

G

G

P

P

V

V

F

V

D

D

K
|
K

L

V

H

Y

E

E

E
|
E

I

I

D

D

E
|
E

L

V

K

-

E

-

A

M

W

Y

E

E

A

A

A

R

Q

Q

T

-

G

A

A

V

G

V

D

D

P

Q

D

A

A

K

V

L

E

E

D

E

E
|
E

L

M

G

G

D
|
D

L

L

F

F

V

A

C

T

V

V

N

N

L

L

A

A

R

R

F

H

M

L

K

G

V

T

N

K

P

A

E

E

Q

I

A

A

L

L

N

Q

R

K

T

A

N

N

H

E

K

K

F

F

D

E

A

R

R

R

F

F

R

R

A

E

I

V

E

E

R

R

V

I

L

V

E

A

R

A

E

R

G

G

R

L

D

E

M

M

D

T

E

G

E

V

S

D

L

L

E

E

A

T

L

M

D

E

A

E

V

V

W

W

Q

Q

A

Q

V

V

binding adenosine-5'-triphosphate: F116 (= F173), W118 (= W175), K127 (= K184), E131 (= E188), E134 (= E191)
binding magnesium ion: E131 (= E188), E134 (= E191), E152 (= E212), D155 (= D215)

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)
37% identity, 96% coverage: 5:277/285 of query aligns to 8:251/255 of Q9X015

query
sites
Q9X015

I

F

E

E

D

E

L

L

K

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

P

E

W

W

D

D

T

R

R

K

Q

Q

S

T

Y

H

R

E

T

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

R

E

E

K

D

N

Y

D

P

D

H

M

L

M

K

K

D

E

E
|
E

L

L

G

G

D

D

L

V

L

L

F

L

Q

Q

V

V

I

V

F

F

Y

H

T

A

Q

Q

L

I

G

A

R

R

E

E

D

R

G

G

H

A

F

F

D

T

F

I

D

E

G

D

V

V

V

I

D

R

H

T

L

L

V

N

R

E

K

K

L

L

V

I

R
|
R

H

H

P

P

H

H

V

V

F

F

P

G

E

D

G

S

T

P

L

-

E

-

S

-

I

-

D

-

P

-

D

-

N

-

R

-

P

-

D

-

E

-

A

G

W

Y

I

S

K

Y

E

K

S

Q

W

W

E

E

R

D

I

I

K
|
K

A

A

E

Q

E

E

R

K

A

G

M

K

K

K

P

K

A

S

P

-

E

-

A

-

S

-

A

-

P

-

V

-

S

S

R

R

L

I

D

G

G

E

I

I

A

N

R

P

T

L

L

V

P

P

A

A

M

L

A

S

R

M

A

A

E

R

K

R

L

I

Q

Q

K

E

R

N

A

A

A

S

R

Q

H

V

G

G

F

F

D

D

W

W

P

K

N

D

V

P

G

E

P

G

V

V

F

Y

D

E

K

K

L

I

H

E

E

E

I

-

D

-

E

-

L

-

K

-

E

-

A

-

W

-

E

L

A

K

A
x
E

Q

L

T

K

G
x
E

A

A

G

K

D

D

P

P

D

R

A

E

V

L

E

E

D
x
E

E
|
E

L

F

G

G

D

D

L

L

F

F

V

S

C

I

V

V

N

N

L

L

A

S

R

R

F

F

M

L

K

N

V

V

N

D

P

P

E

E

Q

S

A

A

L

L

N

R

R

K

T

A

N

T

H

R

K

K

F

F

D

V

A

E

R

R

F

F

R

K

A

K

I

M

E

E

R

E

V

L

L

I

E

E

R

K

E

D

G

G

R

L

D

V

M

L

D

E

E

E

E

L

S

P

L

I

E

E

A

K

L

L

D

D

A

E

V

Y

W

W

Q

E

A

K

V

A

K

K

G

G

E41 (= E39) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
E42 (= E40) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
E45 (= E43) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
E61 (= E59) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
R97 (= R95) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
R98 (= R96) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
K118 (= K129) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
E173 (≠ A199) mutation to A: Has little effects on the NTPase activity.
E176 (≠ G202) mutation to A: Has little effects on the NTPase activity.
EE 185:186 (≠ DE 211:212) 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)
34% identity, 59% coverage: 7:173/285 of query aligns to 89:238/324 of A0R3C4

query
sites
A0R3C4

D

D

L

A

K

V

T

A

L

L

M

M

A

D

R

K

L

L

R

R

D

-

P

-

E

-

T

T

G

S

C

G

P

P

W

W

D

E

T

S

R

E

Q

Q

S

T

Y

H

R

D

T

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

R

S

E

G

D

N

Y

A

P

D

H

E

L

L

K

R

D

E

E

E

L

L

G

G

D

D

L

V

L

L

F

L

Q

Q

V

V

I

L

F

F

Y

H

T

A

Q

R

L

I

G

A

R

E

E

D

D

A

G

P

H

H

-

H

-

P

F

F

D

S

F

I

D

D

G

D

V

V

V

A

D

D

H

A

L

L

V

V

R

R

K

K

L

L

V

G

R

N

R

R

H

V

P

P

H

A

V

V

F

L

P

-

E

-

G

-

T

-

L

A

E

G

S

E

S

S

I

I

D

S

P

L

D

D

N

E

R

Q

P

-

D

-

E

-

A

-

W

-

I

-

K

L

E

A

S

Q

W

W

E

E

R

E

I

R

K

K

A

A

E

Q

E

E

R

K

A

K

M

V

K

K

P

-

A

-

P

-

E

-

A

-

S

-

A

A

P

R

V

A

S

S

R

S

L

M

D

D

G

D

I

V

A

P

R

T

T

G

L

Q

P

P

A
|
A

M

L

A

A

R

L

A

A

E

Q

K

K

L

V

Q

L

K

A

R

R

A

V

A

S

R

Q

H

A

G

G

F

L

A222 (= A157) 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)
33% identity, 59% coverage: 7:173/285 of query aligns to 89:235/325 of P96379

query
sites
P96379

D

D

L

A

K

V

T

A

L

M

M

M

A

D

R

K

L

L

R

R

D

-

P

-

E

-

T

T

G

A

C

G

P

P

W

W

D

E

T

S

R

E

Q

Q

S

T

Y

H

R

D

T

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

R

S

E

G

D

S

Y

V

P

D

H

Q

L

L

K

R

D

E

E

E

L

L

G

G

D

D

L

L

F

L

Q

Q

V

V

I

L

F

F

Y

H

T

A

Q

R

L

I

G

A

R

E

E

D

D

A

G

S

H

Q

-

S

-

P

F

F

D

T

F

I

D

D

G

D

V

V

V

A

D

D

H

T

L

L

V

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

E

-

G

-

T

-

L

-

E

G

S

E

S

S

I

I

D

S

P

L

D

E

N

D

R

Q

P

L

D

A

E

Q

A

-

W

-

I

-

K

-

E

-

S

-

W

W

E

E

R

A

I

A

K

K

A

A

E

S

E

E

R

K

A

A

M

R

K

K

P

-

A

-

P

-

E

-

A

-

S

-

A

-

P

-

V

-

S

S

R

V

L

A

D

D

G

D

I

V

A

H

R

T

T

G

L

Q

P

P

A
|
A

M

L

A

A

R

L

A

A

E

Q

K

K

L

V

Q

I

K

Q

R

R

A

A

A

Q

R

K

H

A

G

G

F

L

A219 (= A157) 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, 32% coverage: 7:96/285 of query aligns to 89:177/177 of 7yh5B

query
sites
7yh5B

D

D

L

A

K

V

T

A

L

M

M

M

A

D

R

K

L

L

R

R

D

-

P

-

E

-

T

T

G

A

C

G

P

P

W

W

D

E

T

S

R

E

Q

Q

S

T

Y

H

R

D

T

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

R

S

E

G

D

S

Y

V

P

D

H

Q

L

L

K

R

D

E

E
|
E

L

L

G

G

D
|
D

L

L

F

L

Q

Q

V

V

I

L

F

F

Y

H

T

A

Q

R

L

I

G

A

R

E

E

D

D

A

G

S

H

Q

-

S

-

P

F

F

D

T

F

I

D

D

G

D

V

V

V

A

D

D

H

T

L

L

V

M

R

R

K

K

L

L

V

G

R

N

R

R

binding magnesium ion: E119 (= E40), E122 (= E43), E138 (= E59), D141 (= D62)

2yxhA Crystal structure of mazg-related protein from thermotoga maritima
29% identity, 29% coverage: 22:103/285 of query aligns to 16:97/114 of 2yxhA

query
sites
2yxhA

C

C

P

P

W

W

D

L

T

E

R

K

Q

Q

S

S

Y

I

R

E

T

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

R

K

E

N

D

D

Y

L

P

A

H

N

L

L

K

E

D

E

E
|
E

L

I

G

G

D
|
D

L

M

L

I

F

Y

Q
x
D

V

A

I

L

F

L

Y

V

T

A

Q

A

L

V

G

A

R

Q

E

R

D

D

G

Y

H

G

F

I

D

D

F

L

D

E

G

S

V

A

V

I

D

Q

H

K

L

V

V

V

R

E

K

K

L

I

V

S

R

H

R

R

H

K

P

P

H

W

V

L

F

F

P

W

E

E

binding magnesium ion: E34 (= E40), E34 (= E40), E37 (= E43), E53 (= E59), D56 (= D62), D60 (≠ Q66)

Query Sequence

>GFF813 FitnessBrowser__Marino:GFF813
MSYTIEDLKTLMARLRDPETGCPWDTRQSYRTIVPHTLEEAYEVADAIEREDYPHLKDEL
GDLLFQVIFYTQLGREDGHFDFDGVVDHLVRKLVRRHPHVFPEGTLESSIDPDNRPDEAW
IKESWERIKAEERAMKPAPEASAPVSRLDGIARTLPAMARAEKLQKRAARHGFDWPNVGP
VFDKLHEEIDELKEAWEAAQTGAGDPDAVEDELGDLLFVCVNLARFMKVNPEQALNRTNH
KFDARFRAIERVLEREGRDMDEESLEALDAVWQAVKGVERGENEH

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