SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_008483296.1 NCBI__GCF_000299915.1:WP_008483296.1 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 4 hits to proteins with known functional sites (download)

P69783 PTS system glucose-specific EIIA component; EIIA-Glc; EIII-Glc; Glucose-specific phosphotransferase enzyme IIA component from Escherichia coli (strain K12) (see 6 papers)
64% identity, 100% coverage: 1:168/168 of query aligns to 1:169/169 of P69783

query
sites
P69783

M
|
M

G

G

L

L

L
x
F

D

D

K

K

L

L

K

K

Q

S

L

L

L

V

G

S

D

D

G

D

P

K

Q

K

G

D

D

T

G

G

-

T

I

I

D

E

I

I

H

I

A

A

P

P

V

L

S

S

G

G

E

E

L

I

V

V

D

N

I

I

E

E

S

D

V

V

P

P

D

D

V

V

F

F

A

A

E

E

K

K

I

I

V

V

G

G

D

D

G

G

I

I

A

A

I

I

K

K

P

P

S

T

S

G

H

N

Q

K

V

M

V

V

A

A

P

P

V

V

N

D

G

G

T

T

I

I

G

G

K

K

I

I

F

F

E

E

T

T

N

N

H
|
H

A

A

F

F

S

S

I

I

E

E

S

S

E

D

Q

S

G

G

V

V

E

E

I

L

F

F

V

V

H
|
H

L

F

G

G

I

I

D

D

T

T

V

V

E

E

L

L

K

K

G

G

E

E

G

G

F

F

L

K

R

R

V

I

A

A

S

E

E

E

G

G

Q

Q

Q

R

V

V

K

K

K

V

G

G

D

D

V

T

V

V

L

I

E

E

C

F

D

D

L

L

K

P

F

L

L

L

E

E

A

E

H

K

A

A

R

K

S

S

T

T

L

L

T

T

P

P

I

V

V

V

V

I

S

S

N

N

M

M

D

D

D

E

F

I

R

K

H

E

I

L

R

I

K

K

K

L

T

S

G

G

K

S

V

V

K

T

A

V

G

G

E

E

D

T

V

P

I

V

L

I

T

R

L

I

Y

K

R

K

M1 (= M1) modified: Initiator methionine, Removed
F4 (≠ L4) mutation to W: Same activity as the wild-type.
H76 (= H75) Important for phospho-donor activity; binding Zn(2+); mutation to Q: Unable to transfer phosphoryl group.
H91 (= H90) active site, Tele-phosphohistidine intermediate; for EIIA activity; binding Zn(2+); modified: Phosphohistidine; by HPr; mutation to Q: Unable to be phosphorylated by Hpr.

1glcF Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
63% identity, 99% coverage: 2:168/168 of query aligns to 1:161/161 of 1glcF

query
sites
1glcF

G

G

L

L

L

F

D

D

K

K

L

L

K

K

Q

S

L

L

L

V

G

S

D

T

G

-

P

-

Q

-

G

-

D

-

G

-

I

I

D

E

I

I

H

I

A

A

P

P

V

L

S

S

G

G

E

E

L

I

V

V

D

N

I

I

E

E

S

D

V

V

P

P

D

D

V

V

F

F

A

A

E

E

K

K

I

I

V

V

G

G

D

D

G

G

I

I

A

A

I

I

K

K

P

P

S

T

S

G

H

N

Q

K

V

M

V

V

A

A

P

P

V

V

N

D

G

G

T

T

I

I

G

G

K

K

I

I

F

F

E

E

T

T

N

N

H
|
H

A

A

F

F

S

S

I

I

E

E

S

S

E

D

Q

S

G

G

V

V

E

E

I

L

F

F

V

V

H
|
H

L

F

G

G

I

I

D

D

T

T

V

V

E

E

L

L

K

K

G

G

E

E

G

G

F

F

L

K

R

R

V

I

A

A

S

E

E

E

G

G

Q

Q

Q

R

V

V

K

K

K

V

G

G

D

D

V

T

V

V

L

I

E

E

C

F

D

D

L

L

K

P

F

L

L

L

E

E

A

E

H

K

A

A

R

K

S

S

T

T

L

L

T

T

P

P

I

V

V

V

V

I

S

S

N

N

M

M

D

D

D

E

F

I

R

K

H

E

I

L

R

I

K

K

K

L

T

S

G

G

K

S

V

V

K

T

A

V

G

G

E

E

D

T

V

P

I

V

L

I

T

R

L

I

Y

K

R

K

binding zinc ion: H68 (= H75), H83 (= H90)

1o2fA Complex of enzyme iiaglc and iibglc phosphocarrier protein hpr from escherichia coli nmr, restrained regularized mean structure (see paper)
66% identity, 89% coverage: 20:168/168 of query aligns to 2:150/150 of 1o2fA

query
sites
1o2fA

I

I

D

E

I

I

H

I

A

A

P

P

V

L

S

S

G

G

E

E

L

I

V

V

D

N

I

I

E

E

S

D

V

V

P

P

D

D

V

V

F

F

A

A

E

E

K

K

I

I

V

V

G

G

D

D

G

G

I

I

A

A

I

I

K

K

P

P

S

T

S

G

H

N

Q

K

V

M

V

V

A

A

P

P

V

V

N

D

G

G

T

T

I

I

G

G

K

K

I

I

F

F

E

E

T
|
T

N

N

H
|
H

A

A

F

F

S

S

I

I

E

E

S

S

E

D

Q

S

G

G

V

V

E

E

I

L

F

F

V

V

H
|
H

L

F

G

G

I

I

D
|
D

T

T

V

V

E

E

L

L

K

K

G

G

E

E

G

G

F

F

L

K

R

R

V

I

A

A

S

E

E

E

G

G

Q

Q

Q

R

V

V

K

K

K

V

G

G

D

D

V

T

V

V

L

I

E

E

C

F

D

D

L

L

K

P

F

L

L

L

E

E

A

E

H

K

A

A

R

K

S

S

T

T

L

L

T

T

P

P

I

V

V

V

V

I

S

S

N

N

M

M

D

D

D

E

F

I

R

K

H

E

I

L

R

I

K

K

K

L

T

S

G

G

K

S

V

V

K

T

A

V

G

G

E

E

D

T

V

P

I

V

L

I

T

R

L

I

Y

K

R

K

active site: T55 (= T73), H57 (= H75), H72 (= H90)
binding phosphite ion: H72 (= H90), D76 (= D94)

P09323 PTS system N-acetylglucosamine-specific EIICBA component; EIICBA-Nag; EII-Nag; EC 2.7.1.193 from Escherichia coli (strain K12) (see paper)
53% identity, 82% coverage: 24:160/168 of query aligns to 503:640/648 of P09323

query
sites
P09323

A

S

P

P

V

I

S

T

G

G

E

D

L

V

V

V

D

A

I

L

E

D

S

Q

V

V

P

P

D

D

V

E

V

A

F

F

A

A

E

S

K

K

I

A

V

V

G

G

D

D

G

G

I

V

A

A

I

V

K

K

P

P

S

T

S

D

H

K

Q

I

V

V

A

S

P

P

V

A

N

A

G

G

T

T

I

I

G

V

K

K

I

I

F

F

E

N

T

T

N

N

H

H

A

A

F

F

S

C

I

L

E

E

S

T

E

E

Q

K

G

G

V

A

E

E

I

I

F

V

V

V

H

H

L

M

G

G

I

I

D

D

T

T

V

V

E

A

L

L

K

E

G

G

E

K

G

G

F

F

L

K

R

R

V

L

A

V

S

E

E

E

G

G

Q

A

Q

Q

V

V

K

S

K

A

G

G

D

Q

V

P

V

I

L

L

E

E

C

M

D

D

L

L

K

D

F

Y

L

L

E

N

A

A

H

N

A

A

R

R

S

S

T

M

L

I

T

S

P

P

I

V

V

V

V

C

S

S

N

N

M

I

D

D

F

F

R

S

H

G

-

L

I

I

R

I

K

K

K

A

T

Q

G

G

K

H

V

I

K

V

A

A

G

G

E

Q

Sites not aligning to the query:

1 modified: N-formylmethionine

Query Sequence

>WP_008483296.1 NCBI__GCF_000299915.1:WP_008483296.1
MGLLDKLKQLLGDGPQGDGIDIHAPVSGELVDIESVPDVVFAEKIVGDGIAIKPSSHQVV
APVNGTIGKIFETNHAFSIESEQGVEIFVHLGIDTVELKGEGFLRVASEGQQVKKGDVVL
ECDLKFLEAHARSTLTPIVVSNMDDFRHIRKKTGKVKAGEDVILTLYR

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