SitesBLAST

Q9HW91 Methyl-accepting chemotaxis protein PctB from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
20% identity, 34% coverage: 115:376/768 of query aligns to 95:360/629 of Q9HW91

query
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Q9HW91

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Y109 (≠ L126) binding
S115 (≠ L132) binding ; binding
Y121 (= Y138) binding ; binding
RPW 126:128 (≠ QAW 141:143) binding ; binding
YME 144:146 (≠ FFS 159:161) binding
E146 (≠ S161) binding
D173 (= D188) binding ; binding

Q9HW93 Methyl-accepting chemotaxis protein PctC from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
23% identity, 34% coverage: 115:376/768 of query aligns to 101:363/632 of Q9HW93

query
sites
Q9HW93

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Y124 (= Y138) binding
RAW 129:131 (≠ QAW 141:143) binding
A150 (≠ Q162) binding
D176 (= D188) binding

P9WLZ7 Multidomain regulatory protein Rv1364c; Anti-sigma-F factor Rv1364c; Anti-SigF factor; Protein-serine/threonine phosphatase; Putative multidomain regulator of SigF; MursiF; Serine/threonine-protein kinase; EC 3.1.3.16; EC 2.7.11.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
27% identity, 26% coverage: 487:683/768 of query aligns to 256:453/653 of P9WLZ7

query
sites
P9WLZ7

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T299 (= T530) modified: Phosphothreonine; by PknD
D328 (= D560) binding ; mutation to A: Leads to the accumulation of the autophosphorylated protein. 10-fold decrease in phosphatase activity.
D387 (= D612) binding
T390 (= T615) modified: Phosphothreonine; by PknD
E444 (= E674) mutation to A: Strong decrease in ATPase activity. Abolishes autophosphorylation.; mutation to K: Abolishes autophosphorylation.
N448 (= N678) mutation to A: Strong decrease in ATPase activity. Abolishes autophosphorylation.; mutation to K: Abolishes autophosphorylation.
H452 (= H682) mutation to A: Abolishes autophosphorylation.

Sites not aligning to the query:

54 modified: Phosphothreonine; by PknD
81 modified: Phosphothreonine; by PknD
211 binding ; binding ; D→A: Does not affect autophosphorylation. 10-fold decrease in phosphatase activity.
212 binding
506 modified: Phosphoserine; by PknD
520 modified: Phosphothreonine; by PknD
568 modified: Phosphothreonine; by PknD
600 modified: Phosphoserine; by autocatalysis; S→A: Decreases ATPase activity. Abolishes autophosphorylation. Can still be phosphorylated by PknD.; S→E: Does not affect ATPase activity. Abolishes autophosphorylation.

3ke6A The crystal structure of the rsbu and rsbw domains of rv1364c from mycobacterium tuberculosis
28% identity, 28% coverage: 487:701/768 of query aligns to 96:301/354 of 3ke6A

query
sites
3ke6A

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binding manganese (ii) ion: D168 (= D560), D217 (= D612)

Sites not aligning to the query:

binding manganese (ii) ion: 51, 51, 52, 53

B0R470 Transducer protein Htr4 from Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) (see paper)
33% identity, 15% coverage: 265:378/768 of query aligns to 268:376/778 of B0R470

query
sites
B0R470

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Q

Sites not aligning to the query:

522 modified: Glutamate methyl ester (Glu)
739 modified: Glutamate methyl ester (Glu)

Q88NI1 Methyl-accepting chemotaxis protein McpU from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
26% identity, 30% coverage: 143:370/768 of query aligns to 186:413/688 of Q88NI1

query
sites
Q88NI1

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E

A

G

A

S

G

A

L

L

L

A

A

G

G

Q

N

R

S

A

R

Q

D

D

D

E

S

L

V

I

L

A

-

L

-

R

-

G

G

D

K

P

P

A

M

E

D

P

K

I

S

R

V

H

A

T

D

G

G

L

L

-

R

A

V

T

A

H

H

A

P

N

F

A

T

P

P

V

I

W

-

I

-

Y

-

H

-

A

-

P

P

I

-

D

D

G

T

T

A

H

P

W

W

Q

Q

F

V

G

V

L

L

V

E

V

L

P

P

E

E

-

S

-

V

-

L

-

Q

-

A

-

P

-

A

-

V

-

A

-

L

-

N

E

Q

R

R

I

L

Y

D

G

A

G

H

V

N

R

Q

R

N

T

A

F

N

S

L

V

T

A

S

L

L

S

L

V

I

G

G

A

L

L

G

A

T

L

A

L

I

S

A

L

G

T

L

L

L

T

V

L

W

V

L

V

T

T

A

R

R

R

G

V

V

L

T

S

R

P

P

L

I

G

L

V

A

L

V

T

A

E

A

R

R

A

L

E

E

Q

D

V

I

A

A

K

S

G

G

A

E

L

G

D

D

F

L

E

-

L

-

P

-

R

-

V

T

R

R

-

L

-

D

-

Y

-

A

-

H

R

Q

D

D

E

E

V

L

G

G

R

Q

L

L

T

T

H

G

A

W

F

F

D

N

R

R

M

F

R

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L

L

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A

A

E

Q

L

V

W186 (= W143) mutation to A: Does not bind putrescine. 100-fold decrease in affinity for spermidine. 36-fold decrease in affinity for cadaverine.
Y202 (≠ F159) mutation to A: Does not bind putrescine. 24-fold decrease in affinity for spermidine. 16-fold decrease in affinity for cadaverine.
YLD 202:204 (≠ FFS 159:161) binding
D204 (≠ S161) mutation to A: Does not bind putrescine and spermidine. 12-fold decrease in affinity for cadaverine.
D233 (= D188) binding ; mutation to A: Does not bind putrescine, spermidine and cadaverine.

Sites not aligning to the query:

164 E→A: 20-fold decrease in affinity for putrescine. 7-fold decrease in affinity for spermidine. Increases affinity for cadaverine.
170 M→A: Does not bind putrescine. Does not affect affinity for spermidine. 3-fold decrease in affinity for cadaverine.

G3XD24 Methyl-accepting chemotaxis protein PctA from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 3 papers)
21% identity, 33% coverage: 123:376/768 of query aligns to 106:360/629 of G3XD24

query
sites
G3XD24

D

D

G

G

S

V

L

F

S

T

V
x
M

R

R

D

P

L

D

L

S

K

P

D

M

P

P

A

A

P

G

Y
|
Y

-

D

-

P

W

R

T

S

Q
x
R

A
x
P

W
|
W

F

Y

A

K

T

D

G

A

L

V

A

A

C

A

A

G

T

G

G

L

C

T

W

L

Q

T

Q

E

P

P

F
x
Y

F
x
V

S
x
D

Q
x
A

S

A

R

T

Q

Q

R

E

R

L

L

I

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I

N

T

Y

A

S

A

A

T

A

P

I

V

E

K

A

A

G

A

G

G

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N

P

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L

G

G

V

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L

V

N

G

A

G

D
|
D

V

L

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S

L

L

E

K

W

T

L

L

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G

Q

V

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I

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N

A

S

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L

N

D

K

F

P

S

R

G

D

M

T

G

E

Y

A

A

F

F

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Q

D

G

G

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Y

I

L

L

A

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V

H

E

P

G

D

-

K

-

E

-

Q

-

V

-

M

S

K

A

T

L

L

A

S

G

E

Q

V

R

Y

A

P

Q

Q

D

N

E

T

L

P

I

K

A

I

A

A

L

T

R

G

G

F

D

S

P

E

A

A

E

E

P

L

I

H

R

G

H

H

T

T

G

R

L

I

L

L

A

A

T

-

H

-

A

-

N

-

A

-

P

-

V

-

W

-

I

-

Y

-

H

F

A

T

P

P

I

I

D

K

G

G

-

L

-

P

-

S

T

V

H

T

W

W

Q

Y

F

L

G

A

L

L

V

S

V

I

P

D

E

K

E

D

R

K

I

A

Y

Y

G

A

G

M

V

L

R

S

R

K

T

F

F

R

S

V

V

S

A

A

L

I

S

A

V

A

G

A

A

L

L

I

A

S

L

I

L

V

S

A

L

I

T

L

L

V

L

L

T

L

L

G

V

L

T

I

R

R

R

L

V

L

L

M

S

Q

P

P

L

L

G

H

V

L

L

M

T

G

E

R

R

A

A

M

E

Q

Q

D

V

I

A

A

K

Q

G

G

A

E

L

G

D

D

F

L

-

T

E

K

L

R

P

L

R

A

V

V

R

T

R

S

R

R

D

D

E

E

V

F

G

G

R

V

L

L

T

G

H

D

A

A

F

F

D

N

R

Q

M

F

R

V

H

E

E

R

L

I

A

H

D

R

H

S

L

I

A

R

E

E

L

V

G

A

R

G

V

T

A

A

R

H

E

K

M111 (≠ V128) mutation to A: 120-fold reduction in AI-2 binding affinity.
Y121 (= Y138) binding ; binding ; binding ; mutation to A: 150-fold reduction in AI-2 binding affinity.
R126 (≠ Q141) mutation to A: Fails to recognize L-Ala, L-Arg, L-Thr, L-Trp and L-Pro. 290-fold reduction in AI-2 binding affinity.
RPW 126:128 (≠ QAW 141:143) binding ; binding ; binding
W128 (= W143) mutation to A: Fails to recognize L-Trp. Decreases affinity for L-Ala, L-Arg, L-Thr and L-Pro. 160-fold reduction in AI-2 binding affinity.
Y144 (≠ F159) mutation to A: Binds L-Trp, but not L-Ala, L-Arg, L-Thr and L-Pro. 100-fold reduction in AI-2 binding affinity.
YVDA 144:147 (≠ FFSQ 159:162) binding ; binding ; binding
D146 (≠ S161) mutation to A: Fails to recognize L-Ala, L-Arg, L-Thr, L-Trp and L-Pro. 240-fold reduction in AI-2 binding affinity.
A147 (≠ Q162) mutation to F: 80-fold reduction in AI-2 binding affinity.
D173 (= D188) binding ; binding ; binding ; mutation to A: Binds L-Trp, but not L-Ala, L-Arg, L-Thr and L-Pro. 85-fold reduction in AI-2 binding affinity.

Sites not aligning to the query:

101 Y→A: 260-fold reduction in AI-2 binding affinity.

P39215 Methyl-accepting chemotaxis protein McpB; H3 from Bacillus subtilis (strain 168) (see 2 papers)
19% identity, 30% coverage: 137:363/768 of query aligns to 139:351/662 of P39215

query
sites
P39215

P

P

Y

W

W

Y

T

Q

Q

D

A

A

W

M

F

K

A

A

T

G

G

G

L

E

A

I

C

V

A

V

T

T

G

-

C

-

W

-

Q

-

Q

D

P

P

F

Y

F

V

S

A

Q

A

S

S

R

D

Q

G

R

S

R

M

L

V

V

I

N

T

Y

I

S

A

A

Q

A

E

I

L

E

K

A

D

G

G

G

S

R

-

P

-

V

-

G

G

V

V

L

V

N

A

A

M

D

D

V

I

T

T

L

I

E

D

W

K

L

L

Q

L

G

E

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Q

L

M

Q

K

A

Q

L

I

N

K

K

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P

G

R

K

D

E

T

G

E

Y

A

A

F

F

V

I

I

A

D

T

Q

K

Q

N

G

K

V

T

Y

Y

L

V

A

A

V

H

E

K

G

N

S

H

A

K

L

-

A

A

G

G

Q

E

R

K

A

L

Q

S

D

G

E

D

L

W

I

V

A

A

A

K

L

M

R

Y

G

A

D

N

P

D

A

S

E

G

P

E

I

L

R

Q

H

Y

T

-

G

-

L

-

A

-

T

T

H

L

A

N

N

N

A

E

P

D

V

K

W

K

I

M

Y

T

H

Y

A

T

P

T

I

N

D

E

G

L

T

T

H

G

W

W

Q

K

F

I

G

A

L

G

V

T

V

M

P

Y

E

M

E

D

R

E

I

I

Y

K

G

D

G

A

V

S

R

K

R

S

T

V

F

L

S

T

V

T

A

G

L

M

S

I

V

V

G

L

A

I

L

A

A

S

L

I

L

V

S

A

L

G

T

G

L

I

L

L

T

I

L

L

V

F

V

I

T

V

R

R

R

S

V

I

L

T

S

K

P

P

L

L

G

K

V

R

L

L

T

V

E

Q

R

S

A

S

E

K

Q

T

V

I

A

S

K

R

G

G

A

D

L

L

D

T

F

-

E

E

L

T

P

I

R

E

V

I

R

H

R

S

R

K

D

D

E

E

V

L

G

G

R

E

L

L

T

G

H

E

A

S

F

F

D

N

R

E

M

M

R

G

H

Q

E

S

L

L

Sites not aligning to the query:

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.

Query Sequence

>N515DRAFT_0975 FitnessBrowser__Dyella79:N515DRAFT_0975
MVLRSIASRLAVWVLAGTLLVVVAGGLLLFRVVRQQILEQTHRESAVLAGDVSHRIQHRL
DKVADTAQMLAALIGPRPDDAEPLIRDALAHNADLDGLAAAYVPASIDARAPVRSPFVSR
HLDGSLSVRDLLKDPAPYWTQAWFATGLACATGCWQQPFFSQSRQRRLVNYSAAIEAGGR
PVGVLNADVTLEWLQGVLQALNKPRDTEAFVIDQQGVYLAVEGSALAGQRAQDELIAALR
GDPAEPIRHTGLLATHANAPVWIYHAPIDGTHWQFGLVVPEERIYGGVRRTFSVALSVGA
LALLSLTLLTLVVTRRVLSPLGVLTERAEQVAKGALDFELPRVRRRDEVGRLTHAFDRMR
HELADHLAELGRVAREQQRLASELEIAQQIQTALLPGAHFLDARCNNFELHAVLKPARTV
GGDLYSYFMLHDQRFYIMVGDVSDKGIPAALFMARAITLAKALAPRAQSPQQLLQLLNQE
LCRNNDGCMFVSLLCGLLDTATGHFSMASAGHEPPVLWGEGAPQLLEIETGPALGLDDEA
TYSSRRVRLRPGETLLMYTDGITEATDAELRMYGPERMLDCLGRYAAHGDGDPAGYLLAD
VEAFAAGHGQADDITVLALRWHHAGADGGASMLELTMPASIEAVFDALARCEEQLAAAGV
AQGVRGDVRLVLEELMVNMAEHGRPHTGAARIELRMTLATDAVLVDLHHDGVPFNPLLSP
EPLLTGDVADREIDGGLGIHLVRAMASDFSYAHDEEGNHLQLRFILPT

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