SitesBLAST

R95 (= R95) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K119 (= K119) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
K168 (= K168) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KVYEE 168:172 (= KVYEE 168:172) binding
E171 (= E171) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E172 (= E172) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
E175 (= E175) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K189 (= K189) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KLEE 189:192 (= KLEE 189:192) binding
E192 (= E192) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E193 (= E193) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
D196 (= D196) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K222 (= K222) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
KFERR 222:226 (= KFERR 222:226) binding
R226 (= R226) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
W253 (= W253) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K257 (= K257) 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)
86% identity, 98% coverage: 2:260/263 of query aligns to 1:225/225 of 3crcA

query
sites
3crcA

N

N

Q

Q

I

I

D

D

R

R

L

L

T

T

I

I

M

M

Q

Q

R

R

L

L

R

R

D

D

P

P

E

E

N

N

G

G

C

C

P

P

W

W

D

D

K

K

E

E

Q

Q

T

T

F

F

A

A

T

T

I

I

A

A

P

P

Y

Y

T

T

L

L

E

E

T

T

Y

Y

E

E

V

V

L

L

D

D

A

A

I

I

A

A

R

R

E

E

D

D

F

F

D

D

L

L

R

R

G

G

E

E

L

L

G

G

D

D

L

L

F

F

Q

Q

V

V

F

F

Y

Y

A

A

Q

Q

M

M

A

A

Q

Q

E

E

G

G

R

R

F

F

D

D

F

F

N

N

D

D

I

I

C

C

A

A

I

I

S

S

D

D

K

K

L

L

E

E

R

R

H

H

P

P

H

-

V

-

F

-

A

-

D

-

S

-

A

-

E

-

N

-

S

-

E

-

V

-

L

-

A

-

R

-

W

-

E

-

Q

-

I

-

K

-

T

-

E

-

R

-

A

-

Q

-

K

-

A

-

Q

-

H

-

S

S

A

A

L

L

D

D

I

I

P

P

R

R

S

S

L

L

P

P

A

A

L

L

M

M

R

R

A

A

Q

Q

K

K

I

I

Q

Q

K

K

R

R

C

C

A

A

N

N

V

V

G

G

F

F

D

D

W

W

T

T

L

L

G

G

P

P

V

V

D

D

K

K

V

V

Y

Y

E

E

I

I

D

D

E

E

V

V

M

M

Y

Y

E

E

A

A

R

R

Q

Q

A

A

V

V

D

D

Q

Q

A

A

K

K

L

L

E

E

M

M

G

G

D

D

L

L

F

F

A

A

T

T

V

V

N

N

L

L

A

A

R

R

H

H

L

L

G

G

T

T

K

K

A

A

E

E

I

I

A

A

L

L

Q

Q

K

K

A

A

N

N

E

E

K

K

F
|
F

E

E

R

R

R
|
R

F

F

R

R

E

E

V

V

E

E

R

R

I

I

V

V

A

A

R

R

G

G

L

L

E

E

M

M

T

T

G

-

V

-

D

D

L

L

E

E

T

T

M

M

E

E

V

V

W
|
W

Q

Q

V

V

K

A

R

R

Q

Q

E

E

binding adenosine-5'-triphosphate: F190 (= F223), R193 (= R226), W218 (= W253)

3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
84% identity, 99% coverage: 2:261/263 of query aligns to 1:220/220 of 3crcB

query
sites
3crcB

N

N

Q

Q

I

I

D

D

R

R

L

L

T

T

I

I

M

M

Q

Q

R

R

L

L

R

-

D

-

P

-

E

-

N

-

G

-

C

-

P

-

W

W

D

D

K

K

E

E

Q

Q

T

T

F

F

A

A

T

T

I

I

A

A

P

P

Y

Y

T

T

L

L

E

E

T

T

Y

Y

E

E

V

V

L

L

D

D

A

A

I

I

A

A

R

R

E

E

D

D

F

F

D

D

L

L

R

R

G

G

E

E

L

L

G

G

D

D

L

L

F

F

Q

Q

V

V

F

F

Y

Y

A

A

Q

Q

M

M

A

A

Q

Q

E

E

G

G

R

R

F

F

D

D

F

F

N

N

D

D

I

I

C

C

A

A

I

I

S

S

D

D

K

K

L

L

E

E

R

R

R

-

H

-

P

-

H

-

V

-

F

-

A

-

D

-

S

-

A

-

E

-

N

-

S

-

E

-

V

-

L

-

A

-

R

-

W

-

E

-

Q

-

I

-

K

-

T

-

E

-

R

-

A

-

Q

-

K

-

A

A

Q

Q

H

H

S

S

A

A

L

L

D

D

I

I

P

P

R

R

S

S

L

L

P

P

A

A

L

L

M

M

R

R

A

A

Q

Q

K

K

I

I

Q

Q

K

K

R

R

C

C

A

A

N

N

V

V

G

G

F
|
F

D

D

W
|
W

T

T

L

L

G

G

P

P

V

V

D

D

K
|
K

V

V

Y

Y

E

E

E
|
E

I

I

D

D

E
|
E

V

V

M

M

Y

Y

E

E

A

A

R

R

Q

Q

A

A

V

V

D

D

Q

Q

A

A

K

K

L

L

E

E

E
|
E

M

M

G

G

D
|
D

L

L

F

F

A

A

T

T

V

V

N

N

L

L

A

A

R

R

H

H

L

L

G

G

T

T

K

K

A

A

E

E

I

I

A

A

L

L

Q

Q

K

K

A

A

N

N

E

E

K

K

F

F

E

E

R

R

F

F

R

R

E

E

V

V

E

E

R

R

I

I

V

V

A

A

R

R

G

G

L

L

E

E

M

M

T

T

G

G

V

V

D

D

L

L

E

E

T

T

M

M

E

E

V

V

W

W

Q

Q

V

V

K

A

R

R

Q

Q

E

E

I

I

binding adenosine-5'-triphosphate: F116 (= F157), W118 (= W159), K127 (= K168), E131 (= E172), E134 (= E175)
binding magnesium ion: E131 (= E172), E134 (= E175), E152 (= E193), D155 (= D196)

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, 97% coverage: 4:257/263 of query aligns to 8:250/255 of Q9X015

query
sites
Q9X015

I

F

D

E

R

E

L

L

L

V

T

S

I

I

M

M

Q

E

R

K

L

L

R

R

D

S

P

P

E

E

N

-

G

G

C

C

P

E

W

W

D

D

K

R

E

K

Q

Q

T

T

F

H

A

E

T

S

I

L

A

K

P

P

Y

Y

T

L

L

I

E
|
E

T

C

Y

Y

E
|
E

V

L

L

I

D

E

A

A

I

I

A

D

R

E

E

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

F

L

Q

Q

V

V

F

F

Y

H

A

A

Q

Q

M

I

A

A

Q

R

E

E

E

R

G

G

R

A

F

F

D

T

F

I

N

E

D

D

I

V

C

I

A

R

A

T

I

L

S

N

D

E

K

K

L

L

E

I

R
|
R

H

H

P

P

H

H

V

V

F

F

A

G

D

D

S

S

S

P

A

G

E

Y

N

S

S

Y

S

K

E

Q

V

-

L

-

A

-

R

-

W

W

E

E

Q

D

I

I

K
|
K

T

A

E

Q

E

E

R

K

A

G

Q

K

K

K

A

-

Q

K

H

S

S

S

A

R

L

I

D

G

D

E

I

I

P

N

R

P

S

L

L

V

P

P

A

A

L

L

M

S

R

M

A

A

Q

R

K

R

I

I

Q

Q

K

E

R

N

C

A

A

S

N

Q

V

V

G

G

F

F

D

D

W

W

T

K

T

D

L

-

G

-

P

-

V

-

V

P

D

E

K

G

V

V

Y

Y

E

E

E

K

I

-

D

I

E

E

V

E

M

E

Y

L

E

K

A
x
E

R

L

Q

K

A
x
E

V

A

V

K

D

D

Q

P

A

R

K

E

L

L

E

E

E
|
E

M

F

G

G

D

D

L

L

F

F

A

S

T

I

V

V

N

N

L

L

A

S

R

R

H

F

L

L

G

N

T

V

K

D

A

P

E

E

I

S

A

A

L

L

Q

R

K

K

A

A

N

T

E

R

K

K

F

F

E

V

R

E

R

R

F

F

R

K

E

K

V

M

E

E

R

E

I

L

V

I

A

E

A

K

R

D

G

G

L

L

E

V

M

L

T

E

G

E

V

L

D

P

L

I

E

E

T

K

M

L

E

D

E

E

V

Y

W

W

Q

E

Q

K

V

A

K

K

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 (= K119) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
E173 (≠ A180) mutation to A: Has little effects on the NTPase activity.
E176 (≠ A183) mutation to A: Has little effects on the NTPase activity.
EE 185:186 (= EE 192:193) 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)
40% identity, 57% coverage: 8:157/263 of query aligns to 91:238/324 of A0R3C4

query
sites
A0R3C4

L

V

T

A

I

L

M

M

Q

D

R

K

L

L

R

R

D

-

P

-

E

-

N

T

G

S

C

G

P

P

W

W

D

E

K

S

E

E

Q

Q

T

T

F

H

A

D

T

S

I

L

A

R

P

R

Y

Y

T

L

L

L

E

E

T

T

Y

Y

E

E

V

L

L

F

D

D

A

A

I

V

A

R

R

S

E

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

F

L

Q

Q

V

V

V

L

F

F

Y

H

A

A

Q

R

M

I

A

A

Q

E

E

D

E

A

G

P

R

H

-

H

-

P

F

F

D

S

F

I

N

D

D

D

I

V

C

A

A

D

A

A

I

L

S

V

D

R

K

K

L

L

E

G

R

N

R

R

H

V

P

P

H

A

V

V

F

L

A

A

D

G

S

E

S

S

A

I

E

-

N

S

S

L

S

D

E

E

V

Q

L

L

A

A

R

Q

W

W

E

E

Q

E

I

R

K

K

T

A

E

Q

E

E

R

K

A

K

Q

V

K

K

A

A

Q

R

H

A

S

S

A

S

L

M

D

D

I

V

P

P

R

T

S

G

L

Q

P

P

A
|
A

L

L

M

A

R

L

A

A

Q

Q

K

K

I

V

Q

L

K

A

R

R

C

V

A

S

N

Q

V

A

G

G

F

L

A222 (= A141) 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: 8:157/263 of query aligns to 91:235/325 of P96379

query
sites
P96379

L

V

T

A

I

M

M

M

Q

D

R

K

L

L

R

R

D

-

P

-

E

-

N

T

G

A

C

G

P

P

W

W

D

E

K

S

E

E

Q

Q

T

T

F

H

A

D

T

S

I

L

A

R

P

R

Y

Y

T

L

L

L

E

E

T

T

Y

Y

E

E

V

L

L

L

D

D

A

A

I

V

A

R

R

S

E

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

F

L

Q

Q

V

V

V

L

F

F

Y

H

A

A

Q

R

M

I

A

A

Q

E

E

D

-

A

-

S

E

Q

G

S

R

P

F

F

D

T

F

I

N

D

D

D

I

V

C

A

A

D

A

T

I

L

S

M

D

R

K

K

L

L

E

G

R

N

R

R

H

A

P

P

H

G

V

V

F

L

A

A

D

G

S

E

S

S

A

I

E

S

N

L

S

E

S

D

E

Q

V

-

L

L

A

A

R

Q

W

W

E

E

Q

A

I

A

K

K

T

A

E

S

E

E

R

K

A

A

Q

R

K

K

A

-

Q

-

H

-

S

S

A

V

L

A

D

D

I

V

P

H

R

T

S

G

L

Q

P

P

A
|
A

L

L

M

A

R

L

A

A

Q

Q

K

K

I

V

Q

I

K

Q

R

R

C

A

A

Q

N

K

V

A

G

G

F

L

A219 (= A141) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.

7yh5B Mazg(mycobacterium tuberculosis) (see paper)
41% identity, 33% coverage: 8:95/263 of query aligns to 91:177/177 of 7yh5B

query
sites
7yh5B

L

V

T

A

I

M

M

M

Q

D

R

K

L

L

R

R

D

-

P

-

E

-

N

T

G

A

C

G

P

P

W

W

D

E

K

S

E

E

Q

Q

T

T

F

H

A

D

T

S

I

L

A

R

P

R

Y

Y

T

L

L

L

E

E

E
|
E

T

T

Y

Y

E
|
E

V

L

L

L

D

D

A

A

I

V

A

R

R

S

E

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

F

L

Q

Q

V

V

V

L

F

F

Y

H

A

A

Q

R

M

I

A

A

Q

E

E

D

-

A

-

S

E

Q

G

S

R

P

F

F

D

T

F

I

N

D

D

D

I

V

C

A

A

D

A

T

I

L

S

M

D

R

K

K

L

L

E

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
30% identity, 37% coverage: 4:100/263 of query aligns to 2:95/114 of 2yxhA

query
sites
2yxhA

I

V

D

E

R

R

L

L

T

E

I

I

M

I

Q

E

R

R

-

S

L

L

R

R

D

-

P

-

E

-

N

-

G

K

C

C

P

P

W

W

D

L

K

E

E

K

Q

Q

T

S

F

I

A

E

T

T

I

L

A

L

P

E

Y

A

T

L

L

A

E

S

E
|
E

T

I

Y

E

E
|
E

V

V

L

A

D

E

A

A

I

V

A

K

R

K

E

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

F

Y

Q
x
D

V

A

V

L

F

L

Y

V

A

A

Q

A

M

V

A

A

Q

Q

E

R

E

D

G

Y

R

G

F

I

D

D

F

L

N

E

D

S

I

A

C

I

A

Q

A

K

I

V

S

V

D

E

K

K

L

I

E

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

>16865 FitnessBrowser__Keio:16865
MNQIDRLLTIMQRLRDPENGCPWDKEQTFATIAPYTLEETYEVLDAIAREDFDDLRGELG
DLLFQVVFYAQMAQEEGRFDFNDICAAISDKLERRHPHVFADSSAENSSEVLARWEQIKT
EERAQKAQHSALDDIPRSLPALMRAQKIQKRCANVGFDWTTLGPVVDKVYEEIDEVMYEA
RQAVVDQAKLEEEMGDLLFATVNLARHLGTKAEIALQKANEKFERRFREVERIVAARGLE
MTGVDLETMEEVWQQVKRQEIDL

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