SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_075858468.1 NCBI__GCF_001950255.1:WP_075858468.1 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)

P15029 Fe(3+) dicitrate transport system permease protein FecD; Iron(III) dicitrate transport system permease protein FecD from Escherichia coli (strain K12) (see paper)
37% identity, 92% coverage: 22:316/321 of query aligns to 16:316/318 of P15029

query
sites
P15029

S

C

V

A

L

L

A

S

A

L

N

H

L

M

G

G

A

V

V

I

K

P

I

V

P

P

P

W

A

R

K

A

I

L

L

L

M

T

E

D

-

W

-

Q

-

A

-

G

-

H

P

E

Y

H

K

Y

T

Y

I

V

F

L

F

M

K

E

I

Y

R
|
R

L

L

P

P

R
|
R

I

L

A

L

L

L

G

A

L

L

G

F

V

V

G

G

S

A

A

A

L

L

G

A

L

V

A

A

G

G

T

V

V

L

Y

I

Q

Q

G

G

V

I

L

V

K

R

T

N

P

P

L

L

A

A

D

S

P

P

Y

D

I

I

L

L

G

G

V

V

S

N

S

H

G

A

A

A

A

S

-

L

A

A

A

S

V

V

A

G

L

A

L

L

T

L

L

L

L

M

K

P

S

S

F

L

P

P

Y

V

Y

M

V

V

L

L

P

P

F

L

G

L

A

A

F

F

L

A

G

G

S

G

I

M

I

A

A

G

L

L

L

I

L

L

V

L

F

K

L

M

I

L

A

A

R

K

K

T

P

H

E

Q

P

P

N

M

R

K

L

L

I

A

L

L

A

T

G

G

I

V

I

A

V

L

N

S

S

A

F

C

L

W

G

A

A

S

V

L

V

T

T

D

F

Y

V

L

L

M

A

L

V

S

S

R

R

P

E

Q

N

D

M

V

P

N

R

N

I

A

I

L

Y

L

W

W

L

L

M

T

G

G

G

S

L

L

-

W

-

G

N

R

N

D

K

W

G

S

F

F

K

V

E

K

A

I

G

A

V

I

L

P

G

L

L

M

Y

I

V

L

F

F

A

L

G

P

F

L

I

S

L

L

L

S

F

F

V

-

L

-

A

C

R

R

D

D

L

L

N

D

A

L

M

L

S

A

F

L

G

G

D

D

D

A

T

R

A

A

A

T

Q

T

L

L

G

G

V

V

E

S

V

V

T

P

K

H

K

T

R

R

V

F

L

W

F

A

L

L

M

L

L

L

A

A

S

V

F

A

L

M

T

T

A

S

G

T

A

G

V

V

S

A

F

A

A

C

G

G

T

P

I

I

G

S

F

F

V

I

G

G

L

L

I

V

V

V

P

P

Q

H

V

M

E

R

L

S

I

I

F

T

G

G

K

G

D

R

F

H

R

R

V

R

L

L

I

L

P

P

L

V

S

S

T

A

L

L

A

T

G

G

G

A

V

L

L

L

V

V

I

V

A

A

D

D

A

L

L

L

A

A

R
|
R

S

I

I

I

L

H

A

P

P

P

S

L

E

E

L

L

P

P

V

V

G

G

V

V

I

L

T

T

A

A

F

I

I

I

G

G

A

A

P

P

F

W

F

F

A

V

Y

W

L

L

F

L

I

V

R

R

R51 (= R52) mutation to C: Retains 32% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 14% of wild-type citrate-mediated Fe(3+) transport.
R54 (= R55) mutation to C: Retains 19% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 24% of wild-type citrate-mediated Fe(3+) transport.
R288 (= R288) mutation to C: Retains 65% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 35% of wild-type citrate-mediated Fe(3+) transport.

P15030 Fe(3+) dicitrate transport system permease protein FecC; Iron(III) dicitrate transport system permease protein FecC from Escherichia coli (strain K12) (see paper)
36% identity, 83% coverage: 50:317/321 of query aligns to 58:331/332 of P15030

query
sites
P15030

K

N

I

L

R
|
R

L

L

P

P

R
|
R

I

S

A

L

L

V

G

A

L

V

G

L

V

I

G

G

S

A

A

S

L

L

G

A

L

L

A

A

G

G

T

T

V

L

Y

L

Q

Q

G

T

V

L

L

T

K

H

T

N

P

P

L

M

A

A

D

S

P

P

Y

S

I

L

L

L

G

G

V

I

S

N

S

S

G

G

A

A

A

L

A

A

V

M

A

A

L

L

L

T

T

S

L

A

L

L

K

S

S

P

F

T

P

P

Y

I

-

A

-

G

Y

Y

V

S

L

L

P

S

F

F

G

I

A

A

F

A

L

C

G

G

S

G

I

G

I

V

A

S

L

W

L

L

V

V

F

M

L

T

I

A

A

G

-

G

-

F

-

R

R

H

K

T

P

H

E

D

P

R

N

N

R

K

L

L

I

I

L

L

A

A

G

G

I

I

I

A

V

L

N

S

S

A

F

F

L

C

G

M

A

G

V

L

V

T

T

R

F

I

V

T

L

L

A

L

V

L

S

A

R

E

E

D

N

H

M

A

P

Y

R

G

I

I

I

F

Y

Y

W

W

L

L

M

A

G

G

L

V

N

S

N

H

K

A

G

R

F

W

K

Q

E

D

A

V

G

W

V

Q

L

L

G

L

L

P

Y

V

V

V

F

V

A

T

G

A

F

V

I

P

L

V

F

L

V

L

L

L

A

A

R

N

D

Q

L

L

N

N

A

L

M

L

S

N

F

L

G

S

D

D

D

S

T

T

A

A

A

H

Q

T

L

L

G

G

V

V

E

N

V

L

T

T

K

R

K

L

R

R

V

L

L

V

F

I

L

N

M

M

L

L

A

V

S

L

F

L

L

L

T

V

A

G

G

A

A

C

V

V

S

S

F

V

A

A

G

G

T

P

I

V

G

A

F

F

V

I

G

G

L

L

I

L

V

V

P

P

Q

H

V

L

V

A

E

R

L

F

I

W

F

A

G

G

K

F

D

D

F

Q

R

R

V

N

L

V

I

L

P

P

L

V

S

S

T

M

L

L

A

L

G

G

G

A

V

T

L

L

L

M

V

L

I

L

A

A

D

D

A

V

L

L

A

A

R
|
R

S

A

I

L

L

A

A

F

P

P

S

G

E

D

L

L

P

P

V

A

G

G

V

A

I

V

T

L

A

A

F

L

I

I

G

G

A

S

P

P

F

C

F

F

A

V

Y

W

L

L

F

V

I

R

R

R

R60 (= R52) mutation to C: Retains 33% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 29% of wild-type citrate-mediated Fe(3+) transport.
R63 (= R55) mutation to C: Retains 74% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 30% of wild-type citrate-mediated Fe(3+) transport.
R302 (= R288) mutation to C: Retains 24% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 28% of wild-type citrate-mediated Fe(3+) transport.

P06972 Iron(3+)-hydroxamate import system permease protein FhuB; Ferric hydroxamate uptake protein B; Ferrichrome transport system permease protein FhuB; Ferrichrome uptake protein FhuB; Iron(III)-hydroxamate import system permease protein FhuB from Escherichia coli (strain K12) (see paper)
31% identity, 97% coverage: 9:319/321 of query aligns to 352:660/660 of P06972

query
sites
P06972

L

L

L

A

G

G

V

V

L

L

L

M

L

A

L

V

I

V

F

V

S

A

V

L

L

S

L

F

A

G

A

R

N

D

L

A

G

H

A

G

V

W

K

T

I

W

P

A

P

S

A

G

K

A

I

L

L

L

M

E

E

D

P

-

Y

-

K

-

T

-

I

-

F

L

F

M

K

P

I

W

R
|
R

L

W

P

P

R

R

I

I

A

M

L

A

G

A

L

L

G

F

V

A

G

G

S

V

A

M

L

L

G

A

L

V

A

A

G

G

T

C

V

I

Y

I

Q

Q

G

R

V

L

L

T

K

G

T

N

P

P

L

M

A

A

D

S

P

P

Y

E

I

V

L

L

G

G

V

I

S

S

G

G

A

A

A

F

A

G

V

V

A

V

L

L

L

M

T

L

L

F

L

L

-

V

-

P

-

G

K

N

S

A

F

F

P

G

Y

W

Y

-

V

L

L

L

P

P

F

A

G

G

A

S

F

-

L

L

G

G

S

A

I

A

I

V

A

T

L

L

L

I

V

I

F

M

L

I

I

A

A

A

R

G

K

R

P

G

-

G

-

F

E

S

P

P

N

H

R

R

L

M

I

L

L

L

A

A

G

G

I
x
M

I

A

V

L

N

S

S

T

F

A

L

F

G

T

A
x
M

V

L

T
x
M

F

M

V

L

L

Q

A

A

V

S

S

G

R

D

E

P

N

R

M

M

P

A

R
x
Q

I

V

I

L

Y
x
T

W

W

L

I

M

S

G

G

G
x
S

L

T

N
x
Y

N

N

K

A

G

T

F

D

K

A

E

Q

A

V

G

W

V

R

L

T

G

G

L

I

Y

V

V

M

F

V

A

I

G

L

F

L

I

A

L

I

L

T

F

P

V

L

L

C

A

R

R

R

D

W

L

L

N

T

A

I

M

L

S

P

F

L

G

G

D

G

D

D

T

T

A

A

A

R

Q

A

L

V

G

G

V

M

E

A

V

L

T

T

K

P

K

T

R

R

V

I

L

A

F

L

L

L

M

L

L

L

A

A

S

A

F

C

L

L

T

T

A

A

G

T

A

A

V

T

S

M

F

T

A

I

G

G

T

P

I

L

G

S

F

F

V

V

G

G

L

L

I

M

V

A

P

P

Q

H

V

I

V

A

E

R

L

M

I

M

F

-

G

-

K

-

D

G

F

F

R

R

V

R

L

T

I

M

P

P

-

H

-

I

-

V

L

I

S

S

T

A

L

L

A

V

G

G

V

L

L

L

V

V

I

F

A

A

D

D

A

W

L

C

A

G

R

R

S

M

I

V

L

L

A

F

P

P

S

F

E
x
Q

L

I

P

P

V

A

G

G

V

L

I

L

T

S

A

T

F

F

I

I

G

G

A

A

P

P

F

Y

F

F

A

I

Y

Y

L

L

F

L

I

R

R

K

R

Q

D

S

H

R

R390 (= R52) Interaction with FhuD; mutation to A: Decreased binding to ferrichrome-FhuD.
M484 (≠ I143) mutation to A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-175; A-492 and A-495.; mutation to L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-175; L-492 and L-495.
M492 (≠ A151) mutation to A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-175; A-484 and A-495.; mutation to L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-175; L-484 and L-495.
M495 (≠ T154) mutation to A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-175; A-484 and A-492.; mutation to L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-175; L-484 and L-492.
Q507 (≠ R166) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-510.
T510 (≠ Y169) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-507.
S515 (≠ G174) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-517.
Y517 (≠ N176) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-515.
Q636 (≠ E295) mutation to A: Decreased binding to ferrichrome-FhuD.

Sites not aligning to the query:

57 S→A: Decreased binding to ferrichrome-FhuD.
170 D→A: Loss of binding to ferrichrome-FhuD; when associated with A-171.
171 Q→A: Loss of binding to ferrichrome-FhuD; when associated with A-170.
175 M→A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-484; A-492 and A-495.; M→L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-484; L-492 and L-495.
182 Interaction with FhuD; T→A: Loss of binding to ferrichrome-FhuD; when associated with A-184.
184 Interaction with FhuD; T→A: Loss of binding to ferrichrome-FhuD; when associated with A-182.
304 Interaction with FhuD; E→A: Decreased binding to ferrichrome-FhuD.

5b57A Inward-facing conformation of abc heme importer bhuuv from burkholderia cenocepacia (see paper)
38% identity, 84% coverage: 42:310/321 of query aligns to 48:320/330 of 5b57A

query
sites
5b57A

E

Q

P

Q

Y

A

K

R

T

A

I

V

F

L

K
x
D

I

I

R

R

L

A

P

P

R

R

I

V

A

V

L

L

G

A

L

L

G
x
L

V

V

G

G

S

G

A

G

L

F

G

G

L

A

A

T

G

G

T

A

V

A

Y

M

Q

Q

G

A

V

L

L

F

K

R

T

N

P

P

L

L

A

A

D

D

P

P

Y

G

I

L

L

V

G

G

V

V

S

S

G

G

A

A

A

L

A

G

V

A

A

T

L

T

L

L

T

I

L

V

L

L

K

G

S

P

F

A

P

S

Y

A

V

A

L

L

P

P

F

V

G

A

A

A

F

F

L

A

G

G

S

G

I

L

I

A

A

V

L

A

L

L

V

V

F

Y

L

R

I

L

A

A

R

A

-

S

-

R

-

G

K

R

P

L

E

A

P

L

N

P

R

L

L

L

I

L

L

L

A

A

G

G

I

I

I

A

V

I

N

N

S

A

F

L

L

V

G

G

A

A

V

A

V

I

T

G

F

L

V

L

L

T

A

F

V

V

S

A

R

D

E

D

N

A

M

Q

P

L

R

R

-

S

I

L

I

T

Y

F

W

W

L

S

M

L

G

G

G

S

L

L

N

G

K

A

G

Q

F
x
W

K

P

E

T

A

L

G
x
A

V

A

L

V

G
x
A

L

P

Y

C

V

V

F

A

A

L

G

G

F

G

I

V

L

L

F

-

V

V

L

R

A

E

R

R

D

D

-

A

L

L

N

N

A

A

M

L

S

Q

F

L

G

G

D

E

D

T

T

E

A

A

A

L

Q

H

L

L

G

G

V

V

E

P

V

V

T

Q

-

R

-

L

K

K

K

R

R

R

V

V

L

L

F

-

L

-

M

-

L

V

A

A

S

V

F

A

L

L

T

A

A

V

G

G

A

A

-

L

V

V

S

S

F

C

A

A

G

G

T

I

I

I

G

G

F

F

V

I

G

G

L

L

I

V

V

A

P

P

Q

H

V

C

V

V

E

R

L

L

I

A

F

C

G

G

K

P

D

D

F

Q

R

R

V

I

L

V

I

L

P

P

L

G

S

A

T

A

L

L

A

L

G

G

G

A

V

L

L

L

L

T

V

L

I

A

A

A

D

D

A

L

L

A

A

A

R

R

S

T

I

V

L

A

A

A

P

P

S

A

E

D

L

I

P

P

V

L

G

G

V

V

I

L

T

T

A

A

F

L

I

L

G

G

A

A

P

P

F

F

binding decyl-beta-d-maltopyranoside: D56 (≠ K50), L67 (≠ G61), W190 (≠ F180), A194 (≠ G184), A197 (≠ G187)

Query Sequence

>WP_075858468.1 NCBI__GCF_001950255.1:WP_075858468.1
MKSWWAKLLLGGVLLLLLLIFSVLLAANLGAVKIPPAKILMEPYKTIFFKIRLPRIALGL
GVGSALGLAGTVYQGVLKTPLADPYILGVSSGAAAAVALLTLLKSFPYYVLPFGAFLGSI
IALLLVFLIARKPEPNRLILAGIIVNSFLGAVVTFVLAVSRENMPRIIYWLMGGLNNKGF
KEAGVLGLYVFAGFILLFVLARDLNAMSFGDDTAAQLGVEVTKKRVLFLMLASFLTAGAV
SFAGTIGFVGLIVPQVVELIFGKDFRVLIPLSTLAGGVLLVIADALARSILAPSELPVGV
ITAFIGAPFFAYLFIRRDHHA

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