SitesBLAST

R95 (= R96) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K119 (= K120) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
K168 (= K174) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KVYEE 168:172 (≠ KIEEE 174:178) binding
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 ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K189 (≠ R194) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KLEE 189:192 (≠ RVAD 194:197) binding
E192 (≠ D197) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E193 (= E198) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
D196 (= D201) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K222 (= K227) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
KFERR 222:226 (= KFERR 227:231) binding
R226 (= R231) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
W253 (= W258) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K257 (= K262) 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)
45% identity, 97% coverage: 4:265/269 of query aligns to 2:225/225 of 3crcA

query
sites
3crcA

N

Q

I

I

D

D

R

R

L

L

I

L

D

T

V

I

M

M

A

Q

R

R

L

L

R

R

D

D

P

P

N

E

G

N

G

G

C

C

P

P

W

W

D

D

L

K

E

E

Q

Q

T

T

Y

F

A

A

T

T

I

I

A

A

P

P

H

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

K

R

G

E

D

D

M

F

S

D

A

D

L

L

R

R

E

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

M

M

A

A

R

Q

E

E

T

G

L

R

F

F

D

D

F

F

D

N

E

D

V

I

A

C

G

A

V

A

I

I

A

S

D

D

K

K

M

L

I

E

R

R

H

H

P

P

H

-

V

-

F

-

G

-

A

-

E

-

V

-

K

-

G

-

A

-

D

-

M

-

Q

-

T

-

S

-

R

-

W

-

E

-

D

-

H

-

K

-

A

-

E

-

R

-

A

-

K

-

A

-

E

-

G

-

R

-

A

-

P

-

S

S

A

A

L

L

E

D

G

D

V

I

I

P

A

R

G

S

L

L

P

P

A

A

L

L

T

M

R

R

A

A

L

Q

K

K

L

I

Q

Q

N

K

R

R

A

C

A

A

R

N

V

V

G

G

F

F

D

D

W

W

T

T

D

T

A

L

R

G

D

P

I

V

L

V

D

D

K

K

I

V

E

Y

E

E

V

I

R

D

E

E

L

V

R

M

H

Y

E

E

M

A

D

R

S

Q

G

A

S

V

A

V

P

D

D

Q

-

A

R

K

V

L

A

E

D

E

E

E

L

M

G

G

D

D

L

L

F

F

A

A

L

T

V

V

N

N

L

L

A

A

R

R

R

H

L

L

K

G

V

T

E

K

P

A

E

E

S

I

A

A

L

L

R

Q

G

K

T

A

N

N

A

E

K

K

F
|
F

E

E

R

R

R
|
R

F

F

H

R

R

E

I

V

E

E

A

R

L

I

L

V

S

A

E

A

Q

R

G

G

R

L

T

E

P

M

K

T

E

D

A

-

T

-

L

L

D

E

E

T

M

M

E

E

A

E

F

V

W
|
W

Q

Q

A

V

K

A

R

R

E

Q

E

E

binding adenosine-5'-triphosphate: F190 (= F228), R193 (= R231), W218 (= W258)

3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
43% identity, 97% coverage: 4:265/269 of query aligns to 2:219/220 of 3crcB

query
sites
3crcB

N

Q

I

I

D

D

R

R

L

L

I

L

D

T

V

I

M

M

A

Q

R

R

L

L

R

-

D

-

P

-

N

-

G

-

C

-

P

-

W

W

D

D

L

K

E

E

Q

Q

T

T

Y

F

A

A

T

T

I

I

A

A

P

P

H

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

K

R

G

E

D

D

M

F

S

D

A

D

L

L

R

R

E

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

M

M

A

A

R

Q

E

E

T

G

L

R

F

F

D

D

F

F

D

N

E

D

V

I

A

C

G

A

V

A

I

I

A

S

D

D

K

K

M

L

I

-

R

-

H

-

P

-

H

-

V

-

F

-

G

-

A

-

E

-

V

-

K

-

G

-

A

-

D

-

M

-

Q

-

T

-

S

-

R

-

W

-

E

-

D

-

H

-

K

-

A

-

E

E

R

R

A

A

A

Q

K

H

A

-

E

-

G

-

R

-

A

-

P

-

S

S

A

A

L

L

E

D

G

D

V

I

I

P

A

R

G

S

L

L

P

P

A

A

L

L

T

M

R

R

A

A

L

Q

K

K

L

I

Q

Q

N

K

R

R

A

C

A

A

R

N

V

V

G

G

F
|
F

D

D

W
|
W

T

T

D

T

A

L

R

G

D

P

I

V

L

V

D

D

K
|
K

I

V

E

Y

E

E

E
|
E

V

I

R

D

E
|
E

L

V

R

M

H

Y

E

E

M

A

D

R

S

Q

G

A

S

V

A

V

P

D

D

Q

-

A

R

K

V

L

A

E

D

E

E
|
E

L

M

G

G

D
|
D

L

L

F

F

A

A

L

T

V

V

N

N

L

L

A

A

R

R

R

H

L

L

K

G

V

T

E

K

P

A

E

E

S

I

A

A

L

L

R

Q

G

K

T

A

N

N

A

E

K

K

F

F

E

E

R

R

F

F

H

R

R

E

I

V

E

E

A

R

L

I

L

V

S

A

E

A

Q

R

G

G

R

L

T

E

P

M

K

T

E

G

A

V

T

D

L

L

D

E

E

T

M

M

E

E

A

E

F

V

W

W

Q

Q

A

V

K

A

R

R

E

Q

E

E

binding adenosine-5'-triphosphate: F116 (= F163), W118 (= W165), K127 (= K174), E131 (= E178), E134 (= E181)
binding magnesium ion: E131 (= E178), E134 (= E181), E152 (= E198), D155 (= D201)

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, 96% coverage: 5:262/269 of query aligns to 8:250/255 of Q9X015

query
sites
Q9X015

I

F

D

E

R

E

L

L

I

V

D

S

V

I

M

M

A

E

R

K

L

L

R

R

D

S

P

P

N

E

G

G

G

-

C

C

P

E

W

W

D

D

L

R

E

K

Q

Q

T

T

Y

H

A

E

T

S

I

L

A

K

P

P

H

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

K

E

G

K

D

N

M

D

S

D

A

M

L

M

R

K

E

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

M

I

A

A

R

R

E

E

E

R

T

G

L

A

F

F

D

T

F

I

D

E

E

D

V

V

A

I

G

R

V

T

I

L

A

N

D

E

K

K

M

L

I

I

R
|
R

H

H

P

P

H

H

V

V

F

F

G

G

A

-

E

-

V

-

K

D

G

S

A

P

D

G

M

Y

Q

S

T

Y

S

K

R

Q

W

W

E

E

D

D

H

I

K
|
K

A

A

A

Q

E

E

R

K

A

-

K

-

A

-

E

-

G

G

R

K

A

K

P

K

S

S

A

S

L

R

E

I

G

G

V

E

I

I

A

N

G

P

L

L

-

V

P

P

A

A

L

L

T

S

R

M

A

A

L

R

K

R

L

I

Q

Q

N

E

R

N

A

A

A

S

R

Q

V

V

G

G

F

F

D

D

W

W

T

K

D

D

A

P

R

E

D

G

I

V

L

Y

D

E

K

K

I

I

E

E

V

L

R

K

E
|
E

L

L

R

K

H
x
E

E

A

M

K

D

D

S

-

G

-

S

-

A

-

P

P

D

R

R

E

V

L

A

E

D
x
E

E
|
E

L

F

G

G

D

D

L

L

F

F

A

S

L

I

V

V

N

N

L

L

A

S

R

R

R

F

L

L

K

N

V

V

E

D

P

P

E

E

S

S

A

A

L

L

R

R

G

K

T

A

N

T

A

R

K

K

F

F

E

V

R

E

R

R

F

F

H

K

R

K

I

M

E

E

A

E

L

L

L

I

S

E

E

K

Q

D

G

G

R

L

T

V

P

L

K

E

E

E

A

L

T

P

L

I

D

E

E

K

M

L

E

D

A

E

F

Y

W

W

Q

E

Q

K

A

A

K

K

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 (= K120) 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 (≠ H184) mutation to A: Has little effects on the NTPase activity.
EE 185:186 (≠ DE 197:198) 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)
36% identity, 59% coverage: 6:163/269 of query aligns to 85:235/325 of P96379

query
sites
P96379

D

E

R

R

L

L

I

V

D

D

V

A

M

V

A

A

R

M

L

M

R

D

D

K

P

L

N

R

G

T

G

A

C

G

P

P

W

W

D

E

L

S

E

E

Q

Q

T

T

Y

H

A

D

T

S

I

L

A

R

P

R

H

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

K

S

G

G

D

S

M

V

S

D

A

Q

L

L

R

R

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

M

I

A

A

R

E

E

D

-

A

-

S

E

Q

T

S

L

P

F

F

D

T

F

I

D

D

E

D

V

V

A

A

G

D

V

T

I

L

A

M

D

R

K

K

M

L

I

G

R

N

R

R

H

A

P

P

H

G

V

V

F

L

G

A

A

G

E

E

E

S

V

I

K

S

G

L

A

E

D

D

M

-

Q

Q

T

L

S

A

R

Q

W

W

E

E

D

A

H

A

K

K

A

A

A

S

E

E

R

K

A

A

A

R

K

K

A

-

E

-

G

-

R

-

A

-

P

-

S

S

A

V

L

A

E

D

G

D

V

V

I

H

A

T

G

G

L

Q

P

P

A
|
A

L

L

T

A

R

L

A

A

L

Q

K

K

L

V

Q

I

N

Q

R

R

A

A

A

Q

R

K

V

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.

A0R3C4 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
36% identity, 59% coverage: 6:163/269 of query aligns to 85:238/324 of A0R3C4

query
sites
A0R3C4

D

E

R

R

L

L

I

V

D

D

V

A

M

V

A

A

R

L

L

M

R

D

D

K

P

L

N

R

G

T

G

S

C

G

P

P

W

W

D

E

L

S

E

E

Q

Q

T

T

Y

H

A

D

T

S

I

L

A

R

P

R

H

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

K

S

G

G

D

N

M

A

S

D

A

E

L

L

R

R

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

M

I

A

A

R

E

E

D

E

A

T

P

-

H

L

P

F

F

D

S

F

I

D

D

E

D

V

V

A

A

G

D

V

A

I

L

A

V

D

R

K

K

M

L

I

G

R

N

R

R

H

V

P

P

H

A

V

V

F

L

G

A

A

G

E

E

E

S

V

I

K

-

G

S

A

L

D

D

M

E

Q

Q

T

L

S

A

R

Q

W

W

E

E

D

E

H

R

K

K

A

A

A

Q

E

E

R

K

A

K

A

V

K

K

A

A

A

-

E

-

G

-

R

R

A

A

P

-

S

S

A

S

L

M

E

D

G

D

V

V

I

P

A

T

G

G

L

Q

P

P

A
|
A

L

L

T

A

R

L

A

A

L

Q

K

K

L

V

Q

L

N

A

R

R

A

V

A

S

R

Q

V

A

G

G

F

L

A222 (= A147) mutation to E: Pyrophosphohydrolase activity is reduced 30-fold.

7yh5B Mazg(mycobacterium tuberculosis) (see paper)
37% identity, 34% coverage: 6:96/269 of query aligns to 85:177/177 of 7yh5B

query
sites
7yh5B

D

E

R

R

L

L

I

V

D

D

V

A

M

V

A

A

R

M

L

M

R

D

D

K

P

L

N

R

G

T

G

A

C

G

P

P

W

W

D

E

L

S

E

E

Q

Q

T

T

Y

H

A

D

T

S

I

L

A

R

P

R

H

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

K

S

G

G

D

S

M

V

S

D

A

Q

L

L

R

R

E

E

E
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E

L

L

G

G

D
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D

L

L

F

L

Q

Q

V

V

V

L

Y

F

Y

H

S

A

Q

R

M

I

A

A

R

E

E

D

-

A

-

S

E

Q

T

S

L

P

F

F

D

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I

D

D

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D

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A

G

D

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T

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K

M

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R

R

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

2yxhA Crystal structure of mazg-related protein from thermotoga maritima
28% identity, 38% coverage: 5:106/269 of query aligns to 2:100/114 of 2yxhA

query
sites
2yxhA

I

V

D

E

R

R

L

L

I

L

D

E

V

I

M

I

A

E

R

R

-

S

L

L

R

R

D

-

P

-

N

-

G

-

G

K

C

C

P

P

W

W

D

L

L

E

E

K

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Q

T

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Y

I

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E

T

T

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L

A

L

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E

H

A

T

L

I

A

E

S

E
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E

A

I

Y

E

E
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E

V

V

A

A

D

E

A

A

I

V

E

K

K

K

G

N

D

D

M

L

S

A

A

N

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L

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E

E

E

E
|
E

L

I

G

G

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D

L

M

L

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F

Y

Q
x
D

V

A

V

L

Y

L

Y

V

S

A

Q

A

M

V

A

A

R

Q

E

R

E

D

T

Y

L

G

F

I

D

D

F

L

D

E

E

S

V

A

A

I

G

Q

V

K

I

V

A

V

D

E

K

K

M

I

I

S

R

H

R

R

H

K

P

P

H

W

V

L

F

F

G

W

A

E

E

E

E

K

V

I

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

Query Sequence

>AZOBR_RS14500 FitnessBrowser__azobra:AZOBR_RS14500
MARNIDRLIDVMARLRDPNGGCPWDLEQTYATIAPHTIEEAYEVADAIEKGDMSALREEL
GDLLFQVVYYSQMAREETLFDFDEVAGVIADKMIRRHPHVFGAEEVKGADMQTSRWEDHK
AAERAAKAAEEGRAPSALEGVIAGLPALTRALKLQNRAARVGFDWTDARDILDKIEEEVR
ELRHEMDSGSAPDRVADELGDLLFALVNLARRLKVEPESALRGTNAKFERRFHRIEALLS
EQGRTPKEATLDEMEAFWQQAKREERGES

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