SitesBLAST

R95 (= R113) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K119 (= K140) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
K168 (= K198) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KVYEE 168:172 (≠ KIHEE 198:202) binding
E171 (= E201) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E172 (= E202) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
E175 (= E205) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K189 (= K219) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KLEE 189:192 (≠ KVQA 219:222) binding
E192 (≠ A222) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E193 (= E223) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
D196 (= D226) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K222 (= K252) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
KFERR 222:226 (= KFERR 252:256) binding
R226 (= R256) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
W253 (= W283) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K257 (= K287) 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)
49% identity, 91% coverage: 25:290/292 of query aligns to 6:225/225 of 3crcA

query
sites
3crcA

L

L

K

T

I

I

M

M

E

Q

K

R

L

L

R

R

D

D

P

P

Q

E

T

N

G

G

C

C

P

P

W

W

D

D

K

K

A

E

Q

Q

T

T

Y

F

Q

A

T

T

I

I

V

A

P

P

F

Y

T

T

L

L

E

E

A

T

Y

Y

E

E

V

V

A

L

D

D

T

A

I

I

E

A

R

R

L

E

A

D

L

F

D

D

E

D

L

L

P

R

D

G

E

E

L

L

G

G

D

D

L

L

F

F

Q

Q

V

V

F

F

Y

Y

C

A

Q

Q

L

M

G

A

K

Q

E

E

Q

E

G

G

R

R

F

F

D

D

F

F

S

N

T

D

V

I

V

C

N

A

K

A

I

I

T

S

D

D

K

K

L

L

T

E

R

R

H

H

P

P

H

-

V

-

F

-

G

-

N

-

E

-

V

-

F

-

E

-

A

-

D

-

A

-

S

-

Q

-

M

-

K

-

A

-

N

-

W

-

E

-

A

-

I

-

K

-

A

-

S

-

E

-

R

-

E

-

Q

-

K

-

A

-

L

-

A

-

G

-

A

-

S

-

L

-

S

-

E

-

V

-

S

S

V

A

L

L

D

D

I

I

P

P

R

R

A

S

Q

L

P

P

A

A

L

L

S

M

R

R

S

A

I

Q

K

K

I

I

Q

Q

Q

K

R

R

V

C

A

A

R

N

V

V

G

G

F

F

D

D

W

W

P

T

E

T

L

L

E

G

P

P

V

V

A

D

K

K

I

V

H

Y

E

E

I

I

D

D

E

E

V

V

F

M

A

Y

E

E

V

A

N

R

Q

Q

P

A

T

V

L

V

D

D

Q

Q

A

A

K

K

V

L

Q

E

A

E

E

E

M

M

G

G

D

D

L

L

F

F

A

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

Q

I

A

A

L

L

R

Q

Q

K

A

A

N

N

V

E

K

K

F
|
F

E

E

R

R

R
|
R

F

F

K

R

G

E

V

V

E

E

A

R

F

I

A

V

R

-

Q

-

N

A

K

R

A

G

L

L

E

E

E

M

H

T

S

D

L

L

E

E

E

T

L

M

D

E

V

E

Y

V

W
|
W

D

Q

K

Q

V

V

K

A

Q

R

G

Q

E

E

binding adenosine-5'-triphosphate: F190 (= F253), R193 (= R256), W218 (= W283)

3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
45% identity, 91% coverage: 25:290/292 of query aligns to 6:219/220 of 3crcB

query
sites
3crcB

L

L

K

T

I

I

M

M

E

Q

K

R

L

L

R

-

D

-

P

-

Q

-

T

-

G

-

C

-

P

-

W

W

D

D

K

K

A

E

Q

Q

T

T

Y

F

Q

A

T

T

I

I

V

A

P

P

F

Y

T

T

L

L

E

E

A

T

Y

Y

E

E

V

V

A

L

D

D

T

A

I

I

E

A

R

R

L

E

A

D

L

F

D

D

E

D

L

L

P

R

D

G

E

E

L

L

G

G

D

D

L

L

F

F

Q

Q

V

V

F

F

Y

Y

C

A

Q

Q

L

M

G

A

K

Q

E

E

Q

E

G

G

R

R

F

F

D

D

F

F

S

N

T

D

V

I

V

C

N

A

K

A

I

I

T

S

D

D

K

K

L

L

T

E

R

R

R

-

H

-

P

-

H

-

V

-

F

-

G

-

N

-

E

-

V

-

F

-

E

-

A

-

D

-

A

-

S

-

Q

-

M

-

K

-

A

-

N

-

W

-

E

-

A

-

I

-

K

-

A

-

S

-

E

-

R

-

E

-

Q

-

K

-

A

-

L

-

A

-

G

-

A

-

S

-

L

-

S

A

E

Q

V

H

S

S

V

A

L

L

D

D

I

I

P

P

R

R

A

S

Q

L

P

P

A

A

L

L

S

M

R

R

S

A

I

Q

K

K

I

I

Q

Q

Q

K

R

R

V

C

A

A

R

N

V

V

G

G

F
|
F

D

D

W
|
W

P

T

E

T

L

L

E

G

P

P

V

V

A

D

K
|
K

I

V

H

Y

E

E

E
|
E

I

I

D

D

E
|
E

V

V

F

M

A

Y

E

E

V

A

N

R

Q

Q

P

A

T

V

L

V

D

D

Q

Q

A

A

K

K

V

L

Q

E

A

E

E
|
E

M

M

G

G

D
|
D

L

L

F

F

A

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

Q

I

A

A

L

L

R

Q

Q

K

A

A

N

N

V

E

K

K

F

F

E

E

R

R

F

F

K

R

G

E

V

V

E

E

A

R

F

I

A

V

R

A

Q

A

N

R

N

G

K

L

A

E

L

M

E

T

E

G

H

V

S

D

L

L

E

E

E

T

L

M

D

E

V

E

Y

V

W

W

D

Q

K

Q

V

V

K

A

Q

R

G

Q

E

E

binding adenosine-5'-triphosphate: F116 (= F187), W118 (= W189), K127 (= K198), E131 (= E202), E134 (= E205)
binding magnesium ion: E131 (= E202), E134 (= E205), E152 (= E223), D155 (= D226)

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)
41% identity, 91% coverage: 25:290/292 of query aligns to 11:253/255 of Q9X015

query
sites
Q9X015

L

L

L

V

K

S

I

I

M

M

E

E

K

K

L

L

R

R

D

S

P

P

Q

E

T

-

G

G

C

C

P

E

W

W

D

D

K

R

A

K

Q

Q

T

T

Y

H

Q

E

T

S

I

L

V

K

P

P

F

Y

T

L

L

I

E
|
E

A

C

Y

Y

E
|
E

V

L

A

I

D

E

T

A

I

I

E

D

R

E

L

K

A

N

L

D

D

D

E

M

L

M

P

K

D

E

E
|
E

L

L

G

G

D

D

L

V

L

L

F

L

Q

Q

V

V

F

F

Y

H

C

A

Q

Q

L

I

G

A

K

R

E

E

Q

R

G

G

R

A

F

F

D

T

F

I

S

E

T

D

V

V

V

I

N

R

K

T

I

L

T

N

D

E

K

K

L

L

T

I

R
|
R

H

H

P

P

H

H

V

V

F

F

G

G

N

D

E

-

V

-

F

-

E

-

A

-

D

-

A

-

S

S

S

P

Q

G

Q

Y

M

S

K

Y

A

K

N

Q

W

W

E

E

A

D

I

I

K
|
K

A

A

S

Q

E

E

R

K

E

G

Q

K

K

K

A

K

L

-

A

-

G

-

G

S

A

S

S

R

L

I

S

G

E

E

V

I

S

N

V

P

L

L

D

-

I

-

P

-

R

-

A

-

Q

V

P

P

A

A

L

L

S

S

R

M

S

A

I

R

K

R

I

I

Q

Q

Q

E

R

N

V

A

A

S

R

Q

V

V

G

G

F

F

D

D

W

W

P

K

E

D

L

P

E

E

P

G

V

V

V

Y

A

E

K

K

I

I

H

E

E

E

I

-

D

-

E

-

V

-

F

-

A

L

E

K

V
x
E

N

L

Q

K

P
x
E

T

A

L

K

D

D

Q

P

A

R

K

E

V

L

Q

E

A
x
E

E
|
E

M

F

G

G

D

D

L

L

F

F

A

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

Q

S

A

A

L

L

R

R

Q

K

A

A

N

T

V

R

K

K

F

F

E

V

R

E

R

R

F

F

K

K

G

K

V

M

E

E

A

E

F

L

A

I

R

E

Q

K

N

D

N

G

K

L

A

V

L

L

E

E

H

L

S

P

L

I

E

E

E

K

L

L

D

D

V

E

Y

Y

W

W

D

E

K

K

V

A

K

K

Q

G

G

G

E

D

E41 (= E56) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
E42 (= E57) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
E45 (= E60) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
E61 (= E76) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
R97 (= R112) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
R98 (= R113) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
K118 (= K140) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
E173 (≠ V210) mutation to A: Has little effects on the NTPase activity.
E176 (≠ P213) mutation to A: Has little effects on the NTPase activity.
EE 185:186 (≠ AE 222:223) mutation to AA: Has little effects on the NTPase activity.

P96379 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
35% identity, 55% coverage: 26:187/292 of query aligns to 91:235/325 of P96379

query
sites
P96379

L

V

K

A

I

M

M

M

E

D

K

K

L

L

R

R

D

-

P

-

Q

-

T

T

G

A

C

G

P

P

W

W

D

E

K

S

A

E

Q

Q

T

T

Y

H

Q

D

T

S

I

L

V

R

P

R

F

Y

T

L

L

L

E

E

A

T

Y

Y

E

E

V

L

A

L

D

D

T

A

I

V

E

R

R

S

L

G

A

S

L

V

D

D

E

Q

L

L

P

R

D

E

E

E

L

L

G

G

D

D

L

L

F

L

Q

Q

V

V

V

L

F

F

Y

H

C

A

Q

R

L

I

G

A

K

E

E

D

-

A

-

S

Q

Q

G

S

R

P

F

F

D

T

F

I

S

D

T

D

V

V

V

A

N

D

K

T

I

L

T

M

D

R

K

K

L

L

T

G

R

N

R

R

H

A

P

P

H

G

V

V

F

L

G

A

N

G

E

E

V

S

F

I

E

-

A

-

D

-

A

-

S

S

S

L

Q

E

Q

D

M

Q

K

L

A

A

N

Q

W

W

E

E

A

A

I

A

K

K

A

A

S

S

E

E

R

K

E

A

Q

R

K

K

A

-

L

-

A

-

G

-

A

-

S

-

L

-

S

-

E

-

V

-

S

S

V

V

L

A

D

D

I

V

P

H

R

T

A

G

Q

Q

P

P

A
|
A

L

L

S

A

R

L

S

A

I

Q

K

K

I

V

Q

I

Q

Q

R

R

V

A

A

Q

R

K

V

A

G

G

F

L

A219 (= A171) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.

A0R3C4 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
35% identity, 55% coverage: 26:187/292 of query aligns to 91:238/324 of A0R3C4

query
sites
A0R3C4

L

V

K

A

I

L

M

M

E

D

K

K

L

L

R

R

D

-

P

-

Q

-

T

T

G

S

C

G

P

P

W

W

D

E

K

S

A

E

Q

Q

T

T

Y

H

Q

D

T

S

I

L

V

R

P

R

F

Y

T

L

L

L

E

E

A

T

Y

Y

E

E

V

L

A

F

D

D

T

A

I

V

E

R

R

S

L

G

A

N

L

A

D

D

E

E

L

L

P

R

D

E

E

E

L

L

G

G

D

D

L

V

L

L

F

L

Q

Q

V

V

V

L

F

F

Y

H

C

A

Q

R

L

I

G

A

K

E

E

D

Q

A

G

P

R

H

F

H

D

P

F

F

S

S

T

I

-

D

V

V

V

A

N

D

K

A

I

L

T

V

D

R

K

K

L

L

T

G

R

N

R

R

H

V

P

P

H

A

V

V

F

L

G

A

N

G

E

E

V

S

F

I

E

S

A

L

D

D

A

-

S

-

Q

-

Q

E

M

Q

K

L

A

A

N

Q

W

W

E

E

A

E

I

R

K

K

A

A

S

Q

E

E

R

K

E

K

Q

V

K

K

A

A

L

R

A

A

A

-

G

-

A

-

S

-

L

-

S

-

E

-

V

-

S

S

V

S

L

M

D

D

I

V

P

P

R

T

A

G

Q

Q

P

P

A
|
A

L

L

S

A

R

L

S

A

I

Q

K

K

I

V

Q

L

Q

A

R

R

V

V

A

S

R

Q

V

A

G

G

F

L

A222 (= A171) mutation to E: Pyrophosphohydrolase activity is reduced 30-fold.

7yh5B Mazg(mycobacterium tuberculosis) (see paper)
34% identity, 33% coverage: 26:120/292 of query aligns to 91:176/177 of 7yh5B

query
sites
7yh5B

L

V

K

A

I

M

M

M

E

D

K

K

L

L

R

R

D

-

P

-

Q

-

T

T

G

A

C

G

P

P

W

W

D

E

K

S

A

E

Q

Q

T

T

Y

H

Q

D

T

S

I

L

V

R

P

R

F

Y

T

L

L

L

E

E

E
|
E

A

T

Y

Y

E
|
E

V

L

A

L

D

D

T

A

I

V

E

R

R

S

L

G

A

S

L

V

D

D

E

Q

L

L

P

R

D

E

E
|
E

L

L

G

G

D
|
D

L

L

F

L

Q

Q

V

V

V

L

F

F

Y

H

C

A

Q

R

L

I

G

A

K

E

E

D

Q

A

G

S

R

Q

F

S

D

P

F

F

S

T

T

-

V

-

V

I

N

D

K

D

I

V

T

A

D

D

K

T

L

L

T

M

R

R

R

K

H

-

P

-

H

-

V

-

F

L

G

G

N

N

binding magnesium ion: E119 (= E57), E122 (= E60), E138 (= E76), D141 (= D79)

2yxhA Crystal structure of mazg-related protein from thermotoga maritima
28% identity, 34% coverage: 22:121/292 of query aligns to 2:98/114 of 2yxhA

query
sites
2yxhA

V

V

A

E

P

R

L

L

K

E

I

I

M

I

E

E

K

R

-

S

L

L

R

R

D

-

P

-

Q

-

T

-

G

K

C

C

P

P

W

W

D

L

K

E

A

K

Q

Q

T

S

Y

I

Q

E

T

T

I

L

V

L

P

E

F

A

T

L

L

A

E

S

E
|
E

A

I

Y

E

E
|
E

V

V

A

A

D

E

T

A

I

V

E

K

R

K

L

N

A

D

L

L

D

A

E

N

L

L

P

E

D

E

E
|
E

L

I

G

G

D
|
D

L

M

L

I

F

Y

Q
x
D

V

A

V

L

F

L

Y

V

C

A

Q

A

L

V

G

A

K

Q

E

R

Q

D

G

Y

R

G

F

I

D

D

F

L

S

E

T

S

V

A

V

I

N

Q

K

K

I

V

T

V

D

E

K

K

L

I

T

S

R

H

R

R

H

K

P

P

H

W

V

L

F

F

G

W

N

E

E

E

binding magnesium ion: E34 (= E57), E34 (= E57), E37 (= E60), E53 (= E76), D56 (= D79), D60 (≠ Q83)

Query Sequence

>7023894 FitnessBrowser__ANA3:7023894
MTSHITPSITELPATALSATDVAPLLKIMEKLRDPQTGCPWDKAQTYQTIVPFTLEEAYE
VADTIERLALDELPDELGDLLFQVVFYCQLGKEQGRFDFSTVVNKITDKLTRRHPHVFGN
EVFEADASSQQMKANWEAIKASEREQKALAAGGASLSEVSVLDDIPRAQPALSRSIKIQQ
RVARVGFDWPELEPVVAKIHEEIDEVFAEVNQPTLDQAKVQAEMGDLLFAVVNLARHLKV
DPEQALRQANVKFERRFKGVEAFARQNNKALEEHSLEELDVYWDKVKQGESR

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