SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing IAI46_18455 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 14 hits to proteins with known functional sites (download)

1pohA The 2.0 angstroms resolution structure of escherichia coli histidine- containing phosphocarrier protein hpr: a redetermination (see paper)
99% identity, 100% coverage: 1:85/85 of query aligns to 1:85/85 of 1pohA

query
sites
1pohA

M

M

F

F

Q

Q

E

E

V

V

T

T

I

I

T

T

A

A

P

P

N

N

G

G

L

L

H

H

T

T

R

R

P

P

A

A

Q

Q

F

F

V

V

K

K

E

E

A

A

K

K

G

G

F

F

T

T

S

S

D

E

I

I

T

T

V

V

T

T

S

S

N
|
N

G

G

K
|
K

S

S

A

A

S

S

A

A

K

K

S

S

L

L

F

F

K

K

L

L

Q

Q

T

T

L

L

G

G

L

L

T

T

Q

Q

G

G

T

T

V

V

T

T

I

I

S

S

A

A

E

E

G

G

E

E

D

D

E

E

Q

Q

K

K

A

A

V

V

E

E

H

H

L

L

V

V

K

K

L

L

M

M

A

A

E

E

L

L

E

E

binding sulfate ion: N38 (= N38), K40 (= K40)

1j6tB Complex of enzyme iiamtl and the histidine-containing phosphocarrier protein hpr from escherichia coli nmr, restrained regularized mean structure (see paper)
99% identity, 100% coverage: 1:85/85 of query aligns to 1:85/85 of 1j6tB

query
sites
1j6tB

M

M

F

F

Q

Q

E

E

V

V

T

T

I

I

T

T

A

A

P

P

N

N

G

G

L

L

H
|
H

T
|
T

R

R

P

P

A

A

Q

Q

F

F

V

V

K

K

E

E

A

A

K

K

G

G

F

F

T

T

S

S

D

E

I

I

T

T

V

V

T

T

S

S

N

N

G

G

K

K

S

S

A

A

S

S

A

A

K

K

S

S

L

L

F

F

K

K

L

L

Q

Q

T

T

L

L

G

G

L

L

T

T

Q

Q

G

G

T

T

V

V

T

T

I

I

S

S

A

A

E

E

G

G

E

E

D

D

E

E

Q

Q

K

K

A

A

V

V

E

E

H

H

L

L

V

V

K

K

L

L

M

M

A

A

E

E

L

L

E

E

binding phosphite ion: H15 (= H15), T16 (= T16)

P0AA04 Phosphocarrier protein HPr; Histidine-containing protein from Escherichia coli (strain K12) (see paper)
99% identity, 100% coverage: 1:85/85 of query aligns to 1:85/85 of P0AA04

query
sites
P0AA04

M

M

F

F

Q

Q

E

E

V

V

T

T

I

I

T

T

A

A

P

P

N

N

G

G

L

L

H
|
H

T

T

R

R

P

P

A

A

Q

Q

F

F

V

V

K

K

E

E

A

A

K

K

G

G

F

F

T

T

S

S

D

E

I

I

T

T

V

V

T

T

S

S

N

N

G

G

K

K

S

S

A

A

S

S

A

A

K

K

S

S

L

L

F

F

K

K

L

L

Q

Q

T

T

L

L

G

G

L

L

T

T

Q

Q

G

G

T

T

V

V

T

T

I

I

S

S

A

A

E

E

G

G

E

E

D

D

E

E

Q

Q

K

K

A

A

V

V

E

E

H

H

L

L

V

V

K

K

L

L

M

M

A

A

E

E

L

L

E

E

H15 (= H15) active site, Pros-phosphohistidine intermediate

O06976 HPr-like protein Crh; Catabolite repression HPr from Bacillus subtilis (strain 168) (see 3 papers)
47% identity, 98% coverage: 1:83/85 of query aligns to 1:83/85 of O06976

query
sites
O06976

M

M

F

V

Q

Q

E

K

V

V

T

E

I

V

T

R

A

L

P

K

N

T

G

G

L

L

H
x
Q

T

A

R

R

P

P

A

A

Q

L

F

F

V

V

K

Q

E

E

A

A

K

N

G

R

F

F

T

T

S

S

D

D

I

V

T

F

V

L

T

E

S

K

N

D

G

G

K

K

S

K

A

V

S

N

A

A

K

K

S
|
S

L

I

F

M

K

G

L

L

Q

M

T

S

L

L

G

A

L

V

T

S

Q

T

G

G

T

T

V

E

V

V

T

T

I

L

S

I

A

A

E

Q

G

G

E

E

D

D

E

E

Q

Q

K

E

A

A

V

L

E

E

H

K

L

L

V

A

K

A

L

Y

M

V

A

Q

E

E

Q15 (≠ H15) mutation to H: Cannot fulfill its catalytic role within PTS transport. Does not affect dimerization.
S46 (= S46) modified: Phosphoserine; by HPrK/P

O69250 Phosphocarrier protein HPr; Histidine-containing protein from Priestia megaterium (Bacillus megaterium) (see 2 papers)
42% identity, 98% coverage: 1:83/85 of query aligns to 1:83/88 of O69250

query
sites
O69250

M

M

F

A

Q

Q

Q

K

E

T

V

F

T

T

I

V

T

T

A

A

P

D

N

S

G

G

L

I

H

H

T

A

R

R

P

P

A

A

A

T

Q

T

F

L

V

V

K

Q

E

A

A

A

K

S

G

K

F

F

T

D

S

S

D

D

I

I

T

N

V

L

T

E

S

F

N

N

G

G

K

K

S

T

A

V

S

N

A

L

K

K

S
|
S

L

I

F

M

K

G

L

V

Q

M

T

S

L

L

G

G

L

I

T

Q

Q

K

G

G

T

A

V

T

V

I

T

T

I

I

S

S

A

A

E

E

G

G

E

S

D

D

E

E

Q

A

K

D

A

A

V

L

E

A

H

A

L

L

V

E

K

D

L

T

M

M

A

S

E

K

S46 (= S46) modified: Phosphoserine; by HPrK/P

Q84F84 Phosphocarrier protein HPr; Histidine-containing protein from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
42% identity, 99% coverage: 1:84/85 of query aligns to 1:84/88 of Q84F84

query
sites
Q84F84

M

M

F

K

Q

T

Q

Q

E

Q

V

F

T

T

I

V

T

I

A

D

P

P

N

L

G

G

L

I

H
|
H

T

A

R

R

P

P

A

A

A

S

Q

Q

F

L

V

V

K

A

E

K

A

A

K

T

G

P

F

F

T

A

S

S

D

A

I

I

T

E

V

V

T

R

S

T

N

E

G

E

K

K

S

A

A

A

S

N

A

L

K

K

S
|
S

L

I

F

L

K

G

L

V

Q

M

T

G

L

L

G

A

L

L

T

K

Q

Q

G

G

T

S

V

Q

V

F

T

T

I

L

S

Y

A

V

E

E

G

G

E

E

D

D

E

E

Q

D

K

Q

A

A

V

F

E

E

H

A

L

L

V

A

K

T

L

L

M

L

A

T

E

E

L

M

H15 (= H15) active site, Pros-phosphohistidine intermediate
S46 (= S46) modified: Phosphoserine; by HPrK/P; mutation to Q: No phosphorylation by HPrK/P.

P24366 Phosphocarrier protein HPr; Histidine-containing protein from Streptococcus salivarius (see paper)
41% identity, 95% coverage: 1:81/85 of query aligns to 1:81/87 of P24366

query
sites
P24366

M

M

F

A

Q

S

Q

K

E

D

V

F

T

H

I

I

T

V

A

A

P

E

N

T

G

G

L

I

H

H

T

A

R

R

P

P

A

A

A

T

Q

L

F

L

V

V

K

Q

E

T

A

A

K

S

G

K

F

F

T

A

S

S

D

D

I

I

T

T

V

L

T

D

S

Y

N

K

G

G

K

K

S

A

A

V

S

N

A

L

K

K

S
|
S

L

I

F

M

K

G

L

V

Q

M

T

S

L

L

G

G

L

V

T

G

Q

Q

G

G

T

A

V

D

V

V

T

T

I

I

S

S

A

A

E

E

G

G

E

A

D

D

E

A

Q

D

K

D

A

A

V

I

E

V

H

A

L

I

V

A

K

E

L

T

M

M

S46 (= S46) modified: Phosphoserine; by HPrK/P

Q9CJ83 Phosphocarrier protein HPr; Histidine-containing protein from Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) (see paper)
42% identity, 95% coverage: 1:81/85 of query aligns to 1:81/88 of Q9CJ83

query
sites
Q9CJ83

M

M

F

A

Q

S

Q

K

E

E

V

F

T

H

I

I

T

V

A

V

P

E

N

T

G

G

L

I

H

H

T

A

R

R

P

P

A

A

A

T

Q

L

F

L

V

V

K

H

E

T

A

A

K

S

G

K

F

F

T

T

S

S

D

E

I

I

T

T

V

L

T

E

S

Y

N

K

G

G

K

K

S

S

A

V

S

N

A

L

K

K

S
|
S

L

I

F

M

K

G

L

V

Q

M

T

S

L

L

G

G

L

V

T

G

Q

Q

G

G

T

A

V

D

V

V

T

T

I

I

S

S

A

A

E

E

G

G

E

A

D

D

E

A

Q

D

K

D

A

A

V

I

E

S

H

T

L

I

V

A

K

E

L

T

M

M

S46 (= S46) modified: Phosphoserine; by HPrK/P; mutation to A: Abolished S-46 phosphorylation.

P08877 Phosphocarrier protein HPr; Histidine-containing protein from Bacillus subtilis (strain 168) (see 5 papers)
37% identity, 95% coverage: 1:81/85 of query aligns to 1:81/88 of P08877

query
sites
P08877

M
|
M

F

A

Q

Q

Q

K

E

T

V

F

T

K

I

V

T

T

A

A

P

D

N
x
S

G

G

L

I

H
|
H

T

A

R

R

P

P

A

A

A

T

Q

V

F

L

V

V

K

Q

E

T

A

A

K

S

G

K

F

Y

T

D

S

A

D

D

I

V

T

N

V

L

T

E

S

Y

N

N

G

G

K

K

S

T

A

V

S

N

A

L

K

K

S
|
S

L

I

F

M

K

G

L

V

Q

M

T

S

L

L

G

G

L

I

T

A

Q

K

G

G

T

A

V

E

V

I

T

T

I

I

S

S

A

A

E

S

G

G

E

A

D

D

E

E

Q

N

K

D

A

A

V

L

E

N

H

A

L

L

V

E

K

E

L

T

M

M

M1 (= M1) modified: Initiator methionine, Removed
S12 (≠ N12) modified: Phosphoserine
H15 (= H15) active site, Pros-phosphohistidine intermediate; alternate; modified: Tele-phosphohistidine; alternate
S46 (= S46) modified: Phosphoserine; by HPrK/P; mutation to A: No phosphorylation by HPrK/P; abolishes the catabolite repressive effects of glucose on gluconate kinase, glucitol dehydrogenase, and the mannitol-specific catabolic enzymes.

Q9WXK8 Phosphocarrier protein HPr; Histidine-containing protein from Streptococcus equinus (Streptococcus bovis) (see paper)
45% identity, 79% coverage: 1:67/85 of query aligns to 1:67/87 of Q9WXK8

query
sites
Q9WXK8

M

M

F

A

Q

S

Q

K

E

D

V

F

T

H

I

I

T

V

A

A

P

E

N

T

G

G

L

I

H

H

T

A

R

R

P

P

A

A

A

T

Q

L

F

L

V

V

K

Q

E

T

A

A

K

S

G

K

F

F

T

A

S

S

D

D

I

I

T

T

V

L

T

D

S

Y

N

K

G

G

K

K

S

A

A

V

S

N

A

L

K

K

S
|
S

L

I

F

M

K

G

L

V

Q

M

T

S

L

L

G

G

L

V

T

G

Q

Q

G

G

T

A

V

D

V

V

T

T

I

I

S

S

A

A

E

E

G

G

S46 (= S46) mutation to A: No phosphorylation by HPrK/P.

Q9F166 Phosphocarrier protein HPr from Bacillus thuringiensis subsp. israelensis (see 2 papers)
37% identity, 79% coverage: 8:74/85 of query aligns to 7:73/87 of Q9F166

query
sites
Q9F166

I

V

T

T

A

S

P

D

N

S

G

G

L

I

H
|
H

T

A

R

R

P

P

A

A

A

T

Q

L

F

L

V

V

K

N

E

T

A

A

K

S

G

K

F

F

T

G

S

S

D

D

I

I

T

N

V

L

T

E

S

Y

N

N

G

G

K

K

S

N

A

V

S

N

A

L

K

K

S
|
S

L

I

F

M

K

G

L

V

Q

M

T

S

L

L

G

G

L

I

T

Q

Q

Q

G

N

T

A

V

E

V

I

T

K

I

I

S

T

A

A

E

N

G

G

E

D

D

D

E

A

Q

A

K

Q

A

A

V

L

H14 (= H15) modified: Tele-phosphohistidine; alternate; mutation to A: Not histidine-phosphorylated.
S45 (= S46) modified: Phosphoserine; by HPrK/P; mutation to A: Not serine-phosphorylated. Absence of glucose-induced cry4A expression repression. 60 to 70% reduction in the sporulation efficiency.

P75061 Phosphocarrier protein HPr; Histidine-containing protein from Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae) (see paper)
37% identity, 87% coverage: 1:74/85 of query aligns to 1:75/88 of P75061

query
sites
P75061

M

M

F

K

Q

K

Q

I

E

Q

V

V

T

V

I

V

T

K

A

D

P

P

N

V

G

G

L

I

H

H

T

A

R

R

P

P

A

A

A

S

Q

I

F

I

V

A

K

G

E

E

A

A

K

N

G

K

F

F

T

K

S

S

D

E

I

L

T

K

V

L

T

V

S

S

-

P

N

S

G

G

K

V

S

E

A

G

S

N

A

I

K

K

S
|
S

L

I

F

I

K

N

L

L

Q

M

T

S

L

L

G

G

L

I

T

K

Q

Q

G

N

T

D

V

H

V

I

T

T

I

I

S

K

A

A

E

E

G

G

E

T

D

D

E

E

Q

E

K

E

A

A

V

L

S47 (= S46) modified: Phosphoserine; by HPrK/P

O50515 Phosphocarrier protein HPr; Histidine-containing protein from Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) (see paper)
31% identity, 98% coverage: 1:83/85 of query aligns to 1:84/93 of O50515

query
sites
O50515

M
|
M

F

A

Q

E

Q

R

E

R

V

V

T

N

I

V

T

G

A

W

P

A

N

E

G

G

L

L

H
|
H

T

A

R

R

P

P

A

A

A

S

Q

I

F

F

V

V

K

R

E

A

A

A

K

T

G

A

F

T

T

G

S

V

D

P

I

V

T

T

V

I

T

A

-

K

S

A

N

D

G

G

K

S

S

P

A

V

S

N

A

A

K

A

S

S

L

M

F

L

K

A

L

V

Q

L

T

G

L

L

G

G

L

A

T

Q

Q

G

G

G

T

E

V

E

V

I

T

V

I

L

S

A

A

S

E

D

G

A

E

E

D

G

E

A

Q

E

K

A

A

A

V

L

E

E

H

R

L

L

V

A

K

K

L

L

M

V

A

A

E

E

M1 (= M1) modified: Initiator methionine, Removed
H15 (= H15) mutation to A: Loss of phosphorylation.

P37349 PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM; Dihydroxyacetone kinase subunit M; EC 2.7.1.121 from Escherichia coli (strain K12) (see paper)
29% identity, 81% coverage: 6:74/85 of query aligns to 160:228/472 of P37349

query
sites
P37349

V

V

T

V

I

I

T

K

A

N

P

R

N

N

G

G

L

L

H
|
H

T

V

R

R

P

P

A

A

A

S

Q

R

F

L

V

V

K

Y

E

T

A

L

K

S

G

T

F

F

T

N

S

A

D

D

I

M

T

L

V

L

T

E

S

K

N

N

G

G

K

K

S

C

A

V

S

T

A

P

K

E

S

S

L

I

F

N

K

Q

L

I

Q

A

T

L

L

L

G

Q

L

V

T

R

Q

Y

G

N

T

D

V

T

V

L

T

R

I

L

S

I

A

A

E

K

G

G

E

P

D

E

E

A

Q

E

K

E

A

A

V

L

H169 (= H15) mutation to A: Loss of phosphotransfer activity.

Sites not aligning to the query:

9 H→A: Loss of phosphotransfer activity.
430 H→A: Loss of phosphotransfer activity.

Query Sequence

>IAI46_18455
MFQQEVTITAPNGLHTRPAAQFVKEAKGFTSDITVTSNGKSASAKSLFKLQTLGLTQGTV
VTISAEGEDEQKAVEHLVKLMAELE

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