SitesBLAST

Comparing WP_029133289.1 NCBI__GCF_000428045.1:WP_029133289.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 1 hits to proteins with known functional sites (download)

O53289 Phosphoserine phosphatase SerB2; PSP; PSPase; O-phosphoserine phosphohydrolase; Protein-serine/threonine phosphatase; EC 3.1.3.3; EC 3.1.3.16 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
22% identity, 94% coverage: 3:206/218 of query aligns to 181:368/409 of O53289

query
sites
O53289

L

L

A

I

I

V

F

F

D
|
D

L
x
V

D
|
D

N
x
S

T

T

L

L

L

V

N

Q

G

G

D

E

S

V

D

I

H

E

L

M

W

L

G

A

Q

A

F

R

L

A

A

G

E

A

Q

Q

G

G

I

Q

V

V

D

A

G

A

D

-

W

-

Y

-

E

-

R

-

E

-

N

-

D

-

R

-

F

I

Y

T

Q

E

E

A

Y

A

K

M

E

R

G

G

T

E

L

L

D

D

I

F

H

A

E

E

F

S

L

L

R

Q

F

R

S

R

L

V

K

A

P

T

L

L

S

A

Q

G

H

L

S

P

P

A

E

T

Q

V

L

I

R

D

Q

D

W

-

H

-

Q

-

A

-

F

-

M

V

H

A

E

E

K

Q

I

L

E

E

P

-

I

-

L

L

L

M

P

P

A

G

A

A

Q

R

I

T

L

T

I

I

D

R

K

T

H

L

R

R

A

R

T

L

G

G

D

F

T

R

L

C

M

G

I

V

T
x
S

A

G

T

G

N

F

A

R

F

R

V

I

T

I

A

E

P

P

I

L

A

A

A

R

A

E

F

L

G

M

I

L

E

D

H

F

L

V

I

A

A

S

T

N

D

E

P

L

E

E

M

I

V

V

G

D

G

G

R

I

Y

L

T

T

G

G

E

R

V

V

A

V

G

G

T

P

P

I

C

V

F

D

Q

R

E

P

G

G

K
|
K

V

A

T

K

R

A

L

L

K

R

Q

D

W

F

L

A

E

S

Q

Q

H

Y

R

G

Q

V

N

P

L

M

A

E

G

Q

S

T

S

V

F

A

Y

V

S

G

D
|
D

S

G

H

A

N

N

D
|
D

L

I

P

D

L

M

L

L

R

G

Q

A

V

A

E

G

H

L

P

G

I

I

A

A

V

F

D

N

P

A

D

K

E

P

T

A

L

L

A

R

Q

E

H

V

A

A

D185 (= D7) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.

V186 (≠ L8) mutation to Q: Decreases enzymatic activity by 50%.

D187 (= D9) mutation to N: Decreases enzymatic activity by 15%.

S188 (≠ N10) mutation to A: No effect on enzymatic activity.

S273 (≠ T111) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).

K318 (= K156) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.

D341 (= D179) mutation to G: Decreases enzymatic activity by 80%.; mutation to N: Decreases enzymatic activity by 85%. Completely abolishes enzymatic activity, does not elicit cytoskeletal rearrangements, and does not suppress IL-8 production after TNF-alpha stimulation; when associated with N-345.

D345 (= D183) mutation to N: Decreases enzymatic activity by 55%. Completely abolishes enzymatic activity, does not elicit cytoskeletal rearrangements, and does not suppress IL-8 production after TNF-alpha stimulation; when associated with N-341.

Sites not aligning to the query:

18 G→A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.

108 G→A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.

Query Sequence

>WP_029133289.1 NCBI__GCF_000428045.1:WP_029133289.1
MPLAIFDLDNTLLNGDSDHLWGQFLAEQGIVDGDWYERENDRFYQEYKEGTLDIHEFLRF
SLKPLSQHSPEQLRQWHQAFMHEKIEPILLPAAQILIDKHRATGDTLMIITATNAFVTAP
IAAAFGIEHLIATDPEMVGGRYTGEVAGTPCFQEGKVTRLKQWLEQHRQNLAGSSFYSDS
HNDLPLLRQVEHPIAVDPDETLAQHARKHGWPIITLRE

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

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