SitesBLAST

L2 (= L2) mutation to A: Loss of in vivo repression and activation, 73-fold decreased affinity for RNA, about 75% wild-type protein levels.
LILTRR 2:7 (= LILTRR 2:7) Region 1, important for regulation and mRNA-binding
I3 (= I3) mutation to A: 80% loss of in vivo repression and activation, about 20% wild-type protein levels.
L4 (= L4) mutation to A: 90% loss of in vivo repression and activation, 60-fold decreased affinity for RNA, about 60% wild-type protein levels.
R6 (= R6) mutation to A: Nearly complete loss of in vivo repression and activation, 30-fold decreased affinity for RNA, about 175% wild-type protein levels.
R7 (= R7) mutation to A: 70% loss of in vivo repression and activation, 12-fold decreased affinity for RNA, about 125% wild-type protein levels.
T19 (= T19) mutation to A: Increased repression and activation in vivo, about 75% wild-type protein levels.
N35 (= N35) mutation to A: Increased repression and activation in vivo, about 75% wild-type protein levels.
V40 (= V40) mutation to A: 90% loss of in vivo repression and activation, 67-fold decreased affinity for RNA, about 75% wild-type protein levels.
40:47 (vs. 40:47, 100% identical) Region 2, important for regulation and mRNA-binding
V42 (= V42) mutation to A: Loss of in vivo repression and activation, 135-fold decreased affinity for RNA, about 40% wild-type protein levels.
R44 (= R44) mutation to A: Loss of in vivo repression and activation, 150-fold decreased affinity for RNA, >500% wild-type protein levels.
I47 (= I47) mutation to A: 90% loss of in vivo repression and activation, 67-fold decreased affinity for RNA, about 150% wild-type protein levels.

O69078 Translational regulator CsrA; Carbon storage regulator; Global translational regulatory protein RsmA from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
85% identity, 100% coverage: 1:61/61 of query aligns to 1:61/61 of O69078

query
sites
O69078

M

M

L

L

I

I

L

L

T

T

R

R

V

V

G

G

E
|
E

T

T

L

L

M

M

I

V

G

G

D

D

E

D

V

V

T

T

V

V

T

T

V

V

L

L

G

G

V

V

K

K

G

G

N

N

Q

Q

V

V

R

R

I

I

G

G

V

V

N

N

A

A

P

P

K

K

E

E

V

V

S

A

V

V

H

H

R
|
R

E

E

I

I

Y

Y

Q

Q

R

R

I

I

Q

Q

A

K

E

E

K

K

S

D

Q

Q

P

E

T

P

S

N

Y

H

E10 (= E10) mutation to A: Behaves like wild-type in swarming, pyocyanine production and lipase biosynthesis assays.
R44 (= R44) mutation to A: Does not complement deletion in swarming, pyocyanine production or lipase biosynthesis assays.

7yr6E Cryo-em structure of pseudomonas aeruginosa rsmz RNA in complex with two rsma protein dimers (see paper)
93% identity, 90% coverage: 1:55/61 of query aligns to 1:55/55 of 7yr6E

query
sites
7yr6E

M
|
M

L
|
L

I
|
I

L
|
L

T

T

R
|
R

R

R

V

V

G

G

E

E

T

T

L

L

M

M

I

V

G

G

D

D

E

D

V

V

T

T

V

V

T

T

V

V

L

L

G

G

V

V

K

K

G

G

N

N

Q

Q

V

V

R
|
R

I

I

G
|
G

V

V

N

N

A

A

P
|
P

K
|
K

E

E

V
|
V

S

A

V
|
V

H
|
H

R
|
R

E

E

I

I

Y
|
Y

Q

Q

R

R

I

I

Q

Q

A

K

E

E

K

K

binding : M1 (= M1), L2 (= L2), I3 (= I3), L4 (= L4), R6 (= R6), R31 (= R31), G33 (= G33), P37 (= P37), K38 (= K38), V40 (= V40), V42 (= V42), H43 (= H43), R44 (= R44), Y48 (= Y48)

2mf0A Structural basis of the non-coding RNA rsmz acting as protein sponge: conformer l of rsmz(1-72)/rsme(dimer) 1to3 complex (see paper)
71% identity, 95% coverage: 1:58/61 of query aligns to 1:58/59 of 2mf0A

query
sites
2mf0A

M
|
M

L
|
L

I
|
I

L
|
L

T
|
T

R

R

R
x
K

V

V

G

G

E

E

T

S

L

I

M

N

I

I

G

G

D

D

E

D

V

I

T

T

V

I

T

T

V

I

L

L

G

G

V

V

K

S

G

G

N
x
Q

Q
|
Q

V

V

R
|
R

I

I

G

G

V

I

N

N

A
|
A

P
|
P

K
|
K

E

D

V
|
V

S

A

V
|
V

H
|
H

R
|
R

E

E

I

I

Y

Y

Q

Q

R

R

I

I

Q

Q

A

A

E

G

K

L

S

T

Q

A

P

P

binding : M1 (= M1), L2 (= L2), I3 (= I3), L4 (= L4), T5 (= T5), K7 (≠ R7), Q28 (≠ N28), Q29 (= Q29), R31 (= R31), A36 (= A36), P37 (= P37), K38 (= K38), V40 (= V40), V42 (= V42), H43 (= H43), R44 (= R44)

P0DPC3 Translational regulator CsrA1; Carbon storage regulator 1; Regulator of secondary metabolites RsmE from Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CFBP 6595 / CHA0) (see paper)
71% identity, 95% coverage: 1:58/61 of query aligns to 1:58/64 of P0DPC3

query
sites
P0DPC3

M
|
M

L
|
L

I
|
I

L
|
L

T
|
T

R
|
R

R
x
K

V

V

G

G

E

E

T

S

L

I

M

N

I

I

G

G

D

D

E

D

V

I

T

T

V

I

T

T

V

I

L

L

G

G

V

V

K

S

G

G

N
x
Q

Q
|
Q

V
|
V

R
|
R

I

I

G

G

V

I

N

N

A

A

P
|
P

K
|
K

E
x
D

V
|
V

S
x
A

V
|
V

H
|
H

R
|
R

E

E

I
|
I

Y
|
Y

Q
|
Q

R
|
R

I

I

Q

Q

A

A

E

G

K

L

S

T

Q

A

P

P

1:7 (vs. 1:7, 86% identical) Contacts 5' UTR of mRNA
L4 (= L4) mutation to A: Partial loss of repression of hcnA in vivo, decreased affinity for mRNA.
R6 (= R6) mutation to A: Complete loss of repression of hcnA in vivo.
QQVR 28:31 (≠ NQVR 28:31) Contacts 5' UTR of mRNA
37:44 (vs. 37:44, 75% identical) Contacts 5' UTR of mRNA
R44 (= R44) mutation to A: Partial loss of repression of hcnA in vivo, decreased affinity for mRNA.
IYQR 47:50 (= IYQR 47:50) Contacts 5' UTR of mRNA

P33911 Translational regulator CsrA from Bacillus subtilis (strain 168) (see 2 papers)
42% identity, 98% coverage: 1:60/61 of query aligns to 1:60/74 of P33911

query
sites
P33911

M

M

L

L

I

V

L

L

T

S

R
|
R

R
x
K

V

I

G

N

E

E

T

A

L

I

M

Q

I
|
I

G

G

D

A

E

D

V

I

T

E

V

V

T

K

V

V

L

I

G

A

V
|
V

K

E

G

G

N

D

Q

Q

V

V

R

K

I
x
L

G
|
G

V

I

N

D

A
|
A

P

P

K

K

E

H

V

I

S

D

V

I

H

H

R

R

E

K

E
|
E

I

I

Y

Y

Q
x
L

R

T

I

I

Q

Q

A

E

E

E

K
x
N

S

N

Q

R

P
x
A

T

A

S

A

R6 (= R6) mutation R->L,W: In sow-2 and sow28; suppresses the motility loss and flagellar assembly defect of an fliW deletion. Binds FliW.
K7 (≠ R7) mutation to E: In sow-12; suppresses the motility loss and flagellar assembly defect of an fliW deletion. Binds FliW.
I14 (= I14) mutation to M: Inhibits motility and flagellar filament assembly, still binds FliW. Binds 5'-UTR of hag mRNA, is not completed by FliW.
V25 (= V25) mutation to G: In sow-20; suppresses the motility loss and flagellar assembly defect of an fliW deletion.
L32 (≠ I32) mutation to P: In sow-10; suppresses the motility loss and flagellar assembly defect of an fliW deletion.
G33 (= G33) mutation to R: In sow-11; suppresses the motility loss and flagellar assembly defect of an fliW deletion. Binds FliW.
A36 (= A36) mutation A->T,V: In sow-8 and sow-4; suppresses the motility loss and flagellar assembly defect of an fliW deletion. Binds FliW.
E46 (= E46) mutation to K: In sow-15; suppresses the motility loss and flagellar assembly defect of an fliW deletion. Binds FliW.
L49 (≠ Q49) mutation to S: Inhibits motility and flagellar filament assembly, reduced binding of FliW.
N55 (≠ K55) mutation to D: Inhibits motility and flagellar filament assembly, greatly reduced binding of FliW. Binds 5'-UTR of hag mRNA, is not completed by FliW.
A58 (≠ P58) mutation to V: Inhibits motility and flagellar filament assembly, reduced binding of FliW.

Query Sequence

>HGI48_RS16340
MLILTRRVGETLMIGDEVTVTVLGVKGNQVRIGVNAPKEVSVHREEIYQRIQAEKSQPTS
Y

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