SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_015798991.1 NCBI__GCF_000023265.1:WP_015798991.1 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)
45% identity, 31% coverage: 222:354/430 of query aligns to 6:131/255 of Q9X015

query
sites
Q9X015

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E41 (= E255) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
E42 (= E256) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
E45 (= E259) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
E61 (= E280) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
R97 (= R316) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
R98 (= R317) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
K118 (= K341) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.

Sites not aligning to the query:

173 E→A: Has little effects on the NTPase activity.
176 E→A: Has little effects on the NTPase activity.
185:186 EE→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, 34% coverage: 224:368/430 of query aligns to 4:152/263 of P0AEY3

query
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P0AEY3

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R95 (= R317) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K119 (= K341) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.

Sites not aligning to the query:

168 K→A: Does not affect nucleotide pyrophosphohydrolysis activity.
168:172 binding ATP
171 E→A: Does not affect nucleotide pyrophosphohydrolysis activity.
172 E→A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
175 binding ATP; E→A: Does not affect nucleotide pyrophosphohydrolysis activity.
189 K→A: Does not affect nucleotide pyrophosphohydrolysis activity.
189:192 binding ATP
192 E→A: Does not affect nucleotide pyrophosphohydrolysis activity.
193 E→A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
196 binding ATP; D→A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
222 K→A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
222:226 binding ATP
226 R→A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
253 binding ATP; W→A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
257 K→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)
33% identity, 34% coverage: 224:368/430 of query aligns to 3:119/225 of 3crcA

query
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3crcA

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Sites not aligning to the query:

binding adenosine-5'-triphosphate: 190, 193, 218

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, 46% coverage: 230:425/430 of query aligns to 93:287/324 of A0R3C4

query
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A0R3C4

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A222 (= A357) 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)
37% identity, 41% coverage: 230:405/430 of query aligns to 93:262/325 of P96379

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P96379

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A219 (= A357) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.

7yh5B Mazg(mycobacterium tuberculosis) (see paper)
43% identity, 20% coverage: 230:317/430 of query aligns to 93:177/177 of 7yh5B

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7yh5B

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binding magnesium ion: E119 (= E256), E122 (= E259), E138 (= E280), D141 (= D283)

3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
31% identity, 41% coverage: 240:417/430 of query aligns to 14:190/220 of 3crcB

query
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3crcB

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E

binding adenosine-5'-triphosphate: F116 (≠ L355), W118 (≠ A357), K127 (vs. gap), E131 (≠ R360), E134 (≠ K363)
binding magnesium ion: E131 (≠ R360), E134 (≠ K363), E152 (vs. gap), D155 (= D382)

2yxhA Crystal structure of mazg-related protein from thermotoga maritima
28% identity, 27% coverage: 226:341/430 of query aligns to 4:113/114 of 2yxhA

query
sites
2yxhA

R

R

L

L

G

L

E

E

V

I

S

E

T

R

L

S

R

L

S

R

A

K

C

C

P

P

W

W

D

L

A

E

S

K

Q

Q

T

S

H

I

R

E

S

T

L

L

A

L

R

E

H

A

L

L

I

A

E

S

E
|
E

A

I

Y

E

E
|
E

A

V

V

A

D

E

A

A

L

V

D

K

A

K

Y

-

E

-

A

-

D

-

G

-

H

N

D

D

R

L

D

A

H

N

V

L

V

E

E

E

E
|
E

L

I

G

G

D
|
D

V

M

L

I

L

Y

Q
x
D

V

A

L

L

M

L

H

V

A

A

T

A

I

V

A

A

D

Q

E

R

D

D

G

Y

S

G

F

I

D

D

L

L

I

E

A

S

I

A

A

I

R

Q

A

K

L

V

T

V

D

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

A

E

V

K

A

I

R

-

S

S

A

L

G

E

E

E

V

A

E

E

Q

K

R

I

W

W

E

K

A

E

I

R

K

K

binding magnesium ion: E34 (= E256), E34 (= E256), E37 (= E259), E53 (= E280), D56 (= D283), D60 (≠ Q287)

Query Sequence

>WP_015798991.1 NCBI__GCF_000023265.1:WP_015798991.1
MKPIVRVVGCGAGRAEAAALGDALEGCVAVVARSLEHPGLAEALGTLDAPILTCDDLYAA
STTFEECYERIVERLRDLAFETGGPVGYVVPGSPQVAERTVVLLRRADDIDVEILAGRGV
LELIIERFGVDPLEGLSVVDAEALHANPWIASGTVVALQVWHEPLARDLVVLAERSGARA
VLAHHLGLDDEVVAEVDSGDERLAAVDHLSSVVLTDFEPPSVALGRLGEVVSTLRSACPW
DASQTHRSLARHLIEEAYEAVDALDAYEADGHDRDHVVEELGDVLLQVLMHATIADEDGS
FDLIAIARALTDKLIRRHPHVFGDAVARSAGEVEQRWEAIKAAEQPGSRPVPVGLPASLR
LAKLARRARARDVRAASLGRGDDLAGVLVEAALSGVDVDEALRDAARRLERALGEVDVDA
GRPGNGDGTS

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