SitesBLAST

371 modified: Glutamate methyl ester (Gln); Q→D: Marked diminution of methanol upon both addition and removal of asparagine. No release of methanol upon asparagine addition but methanol release upon asparagine removal is not affected; when associated with D-630. Release of methanol upon both asparagine addition and removal; when associated with D-637. No methylation; when associated with D-630 and D-637.
595 Q→D: Wild-type production of methanol.
630 modified: Glutamate methyl ester (Glu); E→D: Marked diminution of methanol upon both addition and removal of asparagine; methanol release delayed by about 1 minute compared to wild-type; adapts normally to addition of asparagine but fails to adapt to asparagine removal. No release of methanol upon asparagine addition but methanol release upon asparagine removal is not affected; when associated with D-371. Releases methanol upon asparagine addition but not upon asparagine removal; when associated with D-637. No methylation; when associated with D-371 and D-637.
637 modified: Glutamate methyl ester (Glu); E→D: Marked diminution of methanol upon both addition and removal of asparagine; fails to adapt to addition of asparagine. Release of methanol upon both asparagine addition and removal; when associated with D-371. Releases methanol upon asparagine addition but not upon asparagine removal; when associated with D-630. No methylation; when associated with D-371 and D-630.

P30847 Signal transduction histidine-protein kinase BaeS; EC 2.7.13.3 from Escherichia coli (strain K12) (see paper)
24% identity, 23% coverage: 308:473/710 of query aligns to 70:256/467 of P30847

query
sites
P30847

L

F

L

L

S

R

S

N

T

N

D

D

A

R

T

F

L

V

F

F

S

Q

R

I

F

L

R

R

K

S

F

F

L

E

E

H

S

D

G

N

-

S

-

E

-

D

K

K

S

P

G

G

V

P

L

G

S

M

M

P

P

P

Y

H

N

G

G

W

R

R

D

T

S

Q

L

F

W

W

A

V

F

V

S

D

A

Q

P

N

D

N

K

K

R

V

G

L

V

V

S

G

L

P

V

R

L

A

I

P

L

I

P

P

H

P

D

D

D

G

-

T

-

R

-

P

-

I

-

L

-

V

-

N

-

G

-

A

-

E

-

V

-

G

-

A

-

V

V

I

V

A

A

S

P

P

A

V

N

E

K
x
R

A

L

K

T

S

R

Y

N

V

T

Q

D

L

I

A

N

I

F

N

D

N

K

Q

Q

Y

Q

L

R

H

Q

T

T

V

S

F

W

V

L

L

I

I

V

I

A

V

L

V

A

V

T

L

L

V

L

S

A

V

A

L

L

A

A

F

T

L

F

L

L

S

L

R

A

R

R

-

G

F

L

T

L

E

A

N
x
P

I

V

M

K

I

R

L

L

A

V

R

D

G

G

V

T

K

H

R

K

I

L

S

A

G

G

D

D

F

F

S

T

A

T

R

R

V

V

E

T

V

P

A

T

G

S

E

E

D

D

E

E

V

L

G

G

E

K

L

L

A

A

R

Q

D

D

F

F

N

N

S

Q

M

L

A

A

P

S

A

T

L

L

R

E

E

K

H

N

I

Q

E

Q

I

M

K

R

S

R

A

D

L

F

-

M

-

A

D

D

V

I

A

S

M

H

E

E

V

L

Q

R

T

T

N

P

L

L

R150 (≠ K370) mutation to W: Increased expression of periplasmic chaperone Spy.
P192 (≠ N411) mutation to L: Increased expression of periplasmic chaperone Spy.

Sites not aligning to the query:

264 E→K: Increased expression of periplasmic chaperone Spy.
268 D→N: Increased expression of periplasmic chaperone Spy.
416 R→C: Increased expression of periplasmic chaperone Spy, increased mRNA for mdtA and acrD, target genes of the BaeSR envelope stress response.

6k4eB Siaa-pp2c domain of pseudomonas aeruginosa (see paper)
24% identity, 34% coverage: 458:701/710 of query aligns to 7:244/246 of 6k4eB

query
sites
6k4eB

E

K

I

I

K

G

S

D

A

S

L

L

D

D

V

Y

A

A

M

S

E

L

V

I

Q

Q

T

R

N

A

L

I

L

L

P

P

Q

D

H

R

S

Q

P

L

H

S

I

A

R

-

G

-

Y

-

D

-

I

T

Y

L

G

G

E

E

S

H

R

H

Y

F

C

I

-

L

-

W

-

K

-

P

-

R

D

D

E

V

L

V

G

G

D

D

Y

F

F

Y

D

V

Y

Y

I

-

R

R

P

E

D

Q

R

A

D

D

G

G

E

-

N

-

M

Y

R

L

I

I

A

G

I

V

G

V

D
|
D

V
x
C

S

A

G
|
G

H

H

G

G

V

V

P

P

A

G

A

A

M

L

L

M

M

T

G

-

S

-

V

-

R

-

G

-

Y

-

L

-

R

-

A

-

R

-

T

M

L

L

S

A

G

R

G

A

Q

A

L

I

D

D

E

H

I

A

I

I

S

E

D

A

V

V

N

G

S

S

-

R

-

D

-

P

-

A

L

I

V

L

A

G

Q

E

D

T

T

D

Y

Q

K

A

T

M

G

R

Q

S

F

M

M

L

T

S

M

A

L

L

M

A

V

T

E

N

L

M

D

D

P

-

A

-

K

-

S

A

E

G

L

L

R

V

W

W

V

V

R

D

A

R

G

R

H

R

E

R

P

Q

G

-

L

L

I

A

F

F

D

A

P

G

A

A

E

K

K

I

D

S

F

L

I

Y

R

A

L

S

E

D

G

G

E

E

G

E

I

V

-

Q

-

E

-

L

-

K

-

G

V

A

L

R

G

R

A

A

F

I

E

G

D

D

V

G

E

D

Y

Y

S

-

E

R

N

N

C

I

C

E

A

V

D

P

L

L

E

A

E

P

G

G

Q

W

I

T

L

F

V

Y

L

L

G

S

T

T

D
|
D

G

G

I

F

W

L

-

D

E

Q

A

A

S

G

N

G

K

E

N

H

G

G

E

F

F

G

F

F

G

G

K

S

Q

R

R

R

L

F

W

A

D

D

L

M

I

L

N

R

L

D

K

H

K

A

N

R

S

Q

S

P

A

L

E

P

S

E

I

Q

V

A

S

E

G

A

I

F

F

V

A

A

A

T

V

L

Q

A

D

E

F

Y

T

Q

G

G

R

E

S

H

K

P

Q

Q

E

R

D
|
D

D

D

L

I

T

T

V

I

V

L

V

S

I

F

K

R

binding magnesium ion: D66 (= D519), D66 (= D519), C67 (≠ V520), G69 (= G522), D183 (= D641), D236 (= D693)

O34206 Alginate biosynthesis sensor protein KinB; EC 2.7.13.3 from Pseudomonas aeruginosa (see paper)
38% identity, 10% coverage: 388:456/710 of query aligns to 177:245/595 of O34206

query
sites
O34206

F

L

V

V

L

G

I

V

I

A

V

I

V

L

L

I

V

G

S

F

V

V

L

T

A

A

F

H

L

S

L

I

S

A

R

R

F

F

T

G

E

A

N

P

I

I

M

E

I

T

L

L

A

A

R

R

G

A

V

A

K

D

R

R

I

I

S

G

S

E

G

G

D

D

F

F

S

D

A

V

R

T

V

L

E

P

V

M

A

T

G

N

E

V

D

A

E

E

V

V

G

G

E

Q

L

L

A

T

R

R

D

R

F

F

N

G

S

L

M

M

A

A

P

E

A

A

L

L

R

R

E

Q

H

Y

Sites not aligning to the query:

385 modified: Phosphohistidine; by autocatalysis; mutation H->K,Q: Loss of autophosphorylation.
504 N→Q: Loss of autophosphorylation.
532 D→E: Loss of autophosphorylation.; D→N: Residual autophosphorylation.
560 G→A: Loss of autophosphorylation.

P39214 Methyl-accepting chemotaxis protein McpA; H1 from Bacillus subtilis (strain 168) (see 2 papers)
40% identity, 8% coverage: 403:457/710 of query aligns to 300:354/661 of P39214

query
sites
P39214

L

L

L

I

S

I

R

R

R

S

F

I

T

T

E

T

N

P

I

L

M

K

I

Q

L

L

A

V

R

G

G

S

V

S

K

K

R

R

I

I

S

S

S

E

G

G

D

D

F

L

S

T

A

E

R

T

V

I

E

D

V

I

A

R

G

S

E

K

D

D

E

E

V

L

G

G

E

E

L

L

A

G

R

K

D

S

F

F

N

N

S

N

M

M

A

A

P

S

A

S

L

L

R

R

E

S

H

L

I

I

Sites not aligning to the query:

593 modified: Deamidated glutamine; Q→A: No CheD modification at Q-593 and Q-594 but modification possible at the unidentified second site; when associated with A-594.
594 modified: Deamidated glutamine; modified: Glutamate methyl ester (Gln); Q→A: No CheD modification at Q-593 and Q-594 but modification possible at the unidentified second site; when associated with A-593.

3f79E Structure of pseudo-centered cell crystal form of thE C-terminal phosphatase domain of p. Aeruginosa rssb
27% identity, 26% coverage: 468:652/710 of query aligns to 15:195/236 of 3f79E

query
sites
3f79E

E

Q

V

V

Q

Q

T

M

N

N

L

M

L

L

P

P

Q

V

H

T

S

P

P

W

H

S

I

I

R

E

G

G

Y

L

D

E

I

F

Y

S

G

H

E

R

S

I

R

I

Y

P

C

S

D

L

E

Y

L

L

G

S

G

G

D
|
D

Y

F

F

V

D

D

Y

Y

I

F

R

R

P

V

D

D

R

E

D

-

G

-

E

R

N

R

M

V

R

A

I

F

A

Y

I

L

G

A

D
|
D

V

V

S

S

G
|
G

H

H

G

G

V

A

P

S

A

S

A

A

M

F

L

V

M

T

G

V

S

L

V

L

R

K

G

-

Y

F

L

M

R

T

A

T

R

R

T

L

L

L

-

Y

-

E

-

S

-

R

S

R

G

N

G

G

Q

T

L

L

-

P

-

F

-

K

-

P

D

S

E

E

I

V

I

L

S

A

D

H

V

I

N

N

S

R

L

G

V

L

A

I

Q

N

D

T

T

-

Y

-

K

K

T

L

G

G

Q

K

F

H

M

V

T

T

M

M

L

L

M

G

V

G

E

V

L

I

D

D

P

L

A

E

K

K

S

N

E

S

L

L

R

T

W

Y

V

S

R

I

A

G

G

G

H

H

E

L

P

P

-

L

G

P

L

V

I

L

F

F

D

V

P

E

A

G

E

Q

K

A

D

G

F

Y

I

-

R

-

L

L

E

E

G

G

E

R

G

-

I

-

V

-

L

V

G

G

A

L

F

F

E

D

D

D

V

Y

E

-

Y

-

S

-

E

D

N

D

C

R

C

V

A

M

D

E

L

L

E

P

G

S

Q

F

I

S

L

L

V

S

L

L

G

F

T

S

D

D

G

G

I

I

W

L

E

D

A

V

S

T

N

L

K

K

N

E

G

K

E

E

binding magnesium ion: D46 (= D499), D64 (= D519), G67 (= G522)

Query Sequence

>WP_027720854.1 NCBI__GCF_000425265.1:WP_027720854.1
MKIRFKLLLLLLTVSIFPLVLVQAGVLDSLRSLSDNVGEEVRRELVSKSSVELKRLVEDH
ARVLSKQRRIVELNLQQISAEFSAWIEDGNEFSLPEVFLGSSAGQGDIERLEKKYEQRDQ
TMMHGAYVLDFDAVRYNADGGSDQNAMLPYGTSDAVLPLLKAVELKSPELTLWIRAVFNS
GESLTYPATTGMRMNMHKTVSVINGSTVPTWSLPQKDILTGRTILTASLGVFVDRDAVGS
VSIDVPLDTLLHGYNHLDVFSHNIDSLLVHLEPNGNGTSGVEVVAKEVAASSRKSMMHMW
EPPSTQMLLSSTDATLFSRFRKFLESGKSGVLSMPYNGRDSLWAFSAPDKRGVSLVLILP
HDDVVAPANKAKSYVQLAINNQYLHTVFVLIIVVVLVSVLAFLLSRRFTENIMILARGVK
RISSGDFSARVEVAGEDEVGELARDFNSMAPALREHIEIKSALDVAMEVQTNLLPQHSPH
IRGYDIYGESRYCDELGGDYFDYIRPDRDGENMRIAIGDVSGHGVPAAMLMGSVRGYLRA
RTLSGGQLDEIISDVNSLVAQDTYKTGQFMTMLMVELDPAKSELRWVRAGHEPGLIFDPA
EKDFIRLEGEGIVLGAFEDVEYSENCCADLEEGQILVLGTDGIWEASNKNGEFFGKQRLW
DLINLKKNSSAESIVSGIFAAVQDFTGRSKQEDDLTVVVIKKENNTPEEL

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