SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012409247.1 NCBI__GCF_000020025.1:WP_012409247.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 8 hits to proteins with known functional sites (download)

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)
39% identity, 93% coverage: 12:266/273 of query aligns to 8:251/255 of Q9X015

query
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Q9X015

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E41 (= E46) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
E42 (= E47) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
E45 (= E50) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
E61 (= E66) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
R97 (= R102) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
R98 (= R103) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
K118 (= K127) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
E173 (≠ Q191) mutation to A: Has little effects on the NTPase activity.
E176 (≠ A194) mutation to A: Has little effects on the NTPase activity.
EE 185:186 (≠ AE 203:204) mutation to AA: Has little effects on the NTPase activity.

P0AEY3 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Escherichia coli (strain K12) (see paper)
40% identity, 94% coverage: 12:267/273 of query aligns to 4:259/263 of P0AEY3

query
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P0AEY3

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R95 (= R103) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K119 (= K127) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
K168 (= K181) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KVYEE 168:172 (≠ KFHEE 181:185) binding ATP
E171 (= E184) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E172 (= E185) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
E175 (= E188) binding ATP; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K189 (≠ R200) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KLEE 189:192 (≠ RQQA 200:203) binding ATP
E192 (≠ A203) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E193 (= E204) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
D196 (= D207) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K222 (≠ R233) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
KFERR 222:226 (≠ RFVQR 233:237) binding ATP
R226 (= R237) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
W253 (= W261) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K257 (= K265) 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)
36% identity, 94% coverage: 12:267/273 of query aligns to 3:224/225 of 3crcA

query
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3crcA

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binding adenosine-5'-triphosphate: F190 (= F234), R193 (= R237), W218 (= W261)

3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
33% identity, 87% coverage: 31:267/273 of query aligns to 14:218/220 of 3crcB

query
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3crcB

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binding adenosine-5'-triphosphate: F116 (= F170), W118 (= W172), K127 (= K181), E131 (= E185), E134 (= E188)
binding magnesium ion: E131 (= E185), E134 (= E188), E152 (= E204), D155 (= D207)

P96379 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
36% identity, 58% coverage: 13:170/273 of query aligns to 85:235/325 of P96379

query
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P96379

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Q

N

-

W

W

E

E

Q

A

I

A

K

K

A

A

Q

S

E

E

K

K

G

-

E

-

P

-

S

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P

-

D

-

A

A

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R

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L

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S

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A

A

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D

L

D

G

V

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H

Y

T

G

G

R

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T

-

L

-

P

P

P
x
A

L

L

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A

A

L

A

A

M

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K

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I

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A

A

A

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A

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A

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A219 (≠ P154) 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)
39% identity, 44% coverage: 13:131/273 of query aligns to 85:204/324 of A0R3C4

query
sites
A0R3C4

Q

E

E

R

L

L

I

V

E

D

V

A

V

V

A

A

K

L

L

M

R

D

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L

D

R

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G

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C

G

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W

D

E

L

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A

E

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Q

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T

A

H

E

D

T

S

L

L

T

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R

Y

Y

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L

I

L

E

E

A

T

Y

Y

E

E

V

L

V

F

D

D

A

A

I

V

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R

S

S

G

G

D

N

Q

A

K

D

A

E

I

L

A

R

E

E

L

L

G

G

D

D

L

V

L

L

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Q

V

V

V

L

L

F

Q

H

A

A

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I

I

A

A

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E

D

S

A

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H

-

H

-

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F

F

S

S

L

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D

E

D

I

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T

A

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D

G

A

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K

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L

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R

N

R

R

H

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P

H

A

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F

L

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A

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G

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E

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S

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A

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S

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D

E

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L

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W

E

E

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A

A

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E

E

K

K

Sites not aligning to the query:

222 A→E: Pyrophosphohydrolase activity is reduced 30-fold.

7yh5B Mazg(mycobacterium tuberculosis) (see paper)
38% identity, 33% coverage: 13:103/273 of query aligns to 85:177/177 of 7yh5B

query
sites
7yh5B

Q

E

E

R

L

L

I

V

E

D

V

A

V

V

A

A

K

M

L

M

R

D

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K

P

L

D

R

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G

A

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W

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E

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E

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L

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Y

Y

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L

I

L

E

E

E
|
E

A

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Y

Y

E
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E

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L

D

D

A

A

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G

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E

E
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E

L

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D
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D

L

L

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V

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L

F

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H

A

A

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I

I

A

A

S

E

E

D

S

A

G

S

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Q

-

S

-

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F

F

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D

E

D

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A

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D

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L

L

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binding magnesium ion: E119 (= E47), E122 (= E50), E138 (= E66), D141 (= D69)

2yxhA Crystal structure of mazg-related protein from thermotoga maritima
29% identity, 42% coverage: 12:127/273 of query aligns to 2:113/114 of 2yxhA

query
sites
2yxhA

L

V

Q

E

E

R

L

L

I

L

E

E

V

I

A

E

K

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-

S

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L

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-

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-

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-

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E

Y

A

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A

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E
|
E

A

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Y

E

E
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E

V

V

V

A

D

E

A

A

I

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N

D

D

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A

A

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A

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E

E

E
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E

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D

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x
D

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A

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L

L

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A

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A

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A

A

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E

R

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Y

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G

F

I

S

D

L

L

K

E

E

S

I

A

T

I

Q

Q

G

K

I

V

S

V

Q

E

K

K

L

I

I

S

R

H

R

R

H

K

P

P

H

W

V

L

F

F

G

W

D

E

V

E

S

K

V

I

A

-

S

S

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L

D

E

E

E

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A

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E

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N

I

W

W

E

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binding magnesium ion: E34 (= E47), E34 (= E47), E37 (= E50), E53 (= E66), D56 (= D69), D60 (≠ Q73)

Query Sequence

>WP_012409247.1 NCBI__GCF_000020025.1:WP_012409247.1
MTSDKVETLAALQELIEVVAKLRSPDGGCPWDLAQTAETLTPYVIEEAYEVVDAIKSGDQ
KAIAEELGDLLLQVVLQAQIASESGQFSLKEITQGISQKLIRRHPHVFGDVSVASVDEVR
QNWEQIKAQEKGEPSPDAQKLSAKLGRYGRTLPPLTAAMKISQKAAAIGFEWENIQGVWD
KFHEELGEFQQALAEETPARQQAELGDLLFAVIQLARWHNLDPSAGLQGTNQRFVQRLEK
MEAVCDRPLSDYSLDELENLWQQAKAQLAKEGL

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