SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing PS417_07145 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 3 hits to proteins with known functional sites (download)

D3RPC0 Sulfur carrier protein TusA from Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D) (Chromatium vinosum) (see paper)
53% identity, 92% coverage: 7:79/79 of query aligns to 4:76/76 of D3RPC0

query
sites
D3RPC0

F

F

D

D

A

Q

E

E

L

L

D

D

A

A

S

S

G

G

L

L

N

N

C
|
C

P

P

L

L

P

P

L

I

L

L

K

R

A

A

K

K

L

K

E

T

L

L

N

N

R

A

L

M

A

S

S

S

G

G

A

Q

V

V

L

L

K

H

V

V

I

I

A

A

T

T

D

D

A

P

G

G

S

S

Q

V

R

K

D

D

F

F

R

D

T

A

F

F

A

A

K

K

L

Q

A

T

G

G

H

N

T

E

L

L

L

M

H

E

E

S

E

K

D

E

A

E

A

G

G

G

V

K

Y

F

R

H

Y

F

W

L

L

I

R

K

K

K

A

S

C15 (= C18) active site, Cysteine persulfide intermediate; mutation to S: Loss of sulfur binding in the presence of sulfide. Loss of interaction with DsrEFH proteins.

P0A890 Sulfur carrier protein TusA; Sulfur mediator TusA; Sulfur transfer protein TusA; tRNA 2-thiouridine synthesizing protein A from Escherichia coli (strain K12) (see 2 papers)
35% identity, 100% coverage: 1:79/79 of query aligns to 1:80/81 of P0A890

query
sites
P0A890

M

M

T

T

D

D

A

L

V

F

A

S

F

S

-

P

D

D

A

H

E

T

L

L

D

D

A

A

S

L

G

G

L

L

N

R

C
|
C

P

P

L
x
E

P

P

L

V

L

M

K

M

A

V

K

R

L

K

E

T

L

V

N

R

R

N

L

M

A

Q

S

P

G

G

A

E

V

T

L

L

K

L

V

I

I

I

A

A

T

D

D

D

A

P

G

A

S

T

Q

T

R

R

D

D

F

I

R

P

T

G

F

F

A
x
C

K

T

L

F

A

M

G

E

H

H

T

E

L

L

L

V

H

A

E

K

E

E

D

T

A

D

A

G

G

L

V

P

Y

Y

R

R

Y

Y

W

L

L

I

R

R

K

K

A

G

C19 (= C18) active site, Cysteine persulfide intermediate; mutation to S: Unable to restore mnm5s2U formation in a tusA-deficient mutant. Unable to accept sulfur from IscS.
E21 (≠ L20) mutation to K: In sirA1; affects the stability of sigma-S during the logarithmic growth phase.
C56 (≠ A55) mutation to S: Able to restore mnm5s2U formation in a tusA-deficient mutant.

P0A892 Sulfur carrier protein TusA; Sulfur mediator TusA; Sulfur transfer protein TusA; tRNA 2-thiouridine synthesizing protein A from Escherichia coli O157:H7 (see paper)
35% identity, 100% coverage: 1:79/79 of query aligns to 1:80/81 of P0A892

query
sites
P0A892

M

M

T

T

D

D

A

L

V

F

A

S

F

S

-

P

D

D

A

H

E

T

L

L

D

D

A

A

S

L

G

G

L

L

N

R

C

C

P

P

L
x
E

P

P

L

V

L
x
M

K

M

A

V

K
x
R

L
x
K

E
x
T

L
x
V

N
x
R

R
x
N

L
x
M

A
x
Q

S
x
P

G

G

A

E

V

T

L

L

K

L

V

I

I

I

A

A

T

D

D
|
D

A

P

G

A

S

T

Q

T

R
|
R

D
|
D

F

I

R

P

T

G

F

F

A

C

K

T

L
x
F

A

M

G

E

H

H

T

E

L

L

L

V

H

A

E

K

E

E

D

T

A

D

A

G

G

L

V

P

Y

Y

R

R

Y

Y

W

L

L

I

R

R

K

K

A

G

E21 (≠ L20) mutation to A: Decreased binding of IscS.
M24 (≠ L23) mutation to R: No binding of IscS, 50% modified tRNA produced.
R27 (≠ K26) mutation R->D,E: No binding of IscS, 19% modified tRNA produced (for R27E).
27:35 (vs. 26:34, 0% identical) mutation to DKTVRNMQS: No modified tRNA produced.
R31 (≠ N30) mutation to A: No binding of IscS, 30% modified tRNA produced.
D45 (= D44) mutation to A: Binds IscS, 56% modified tRNA produced.
R50 (= R49) mutation to A: Binds IscS, 67% modified tRNA produced.
D51 (= D50) mutation to A: Binds IscS, 67% modified tRNA produced.
F58 (≠ L57) mutation to A: No binding of IscS, 67% modified tRNA produced.

Query Sequence

>PS417_07145
MTDAVAFDAELDASGLNCPLPLLKAKLELNRLASGAVLKVIATDAGSQRDFRTFAKLAGH
TLLHEEDAAGVYRYWLRKA

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