SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_066742179.1 NCBI__GCF_001701045.1:WP_066742179.1 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 20 (the maximum) hits to proteins with known functional sites (download)

Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
36% identity, 65% coverage: 293:842/844 of query aligns to 33:588/590 of Q4WR83

query
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Q4WR83

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Sites not aligning to the query:

6:14 PTS2-type peroxisomal targeting signal

Q84P21 Peroxisomal OPC-8:0-CoA ligase 1; 4-coumarate--CoA ligase isoform 9; At4CL9; 4-coumarate--CoA ligase-like 5; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 60% coverage: 313:822/844 of query aligns to 46:533/546 of Q84P21

query
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Q84P21

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K530 (= K819) mutation to N: Lossed enzymatic activity.

P9WQ37 Long-chain-fatty-acid--CoA ligase FadD13; Fatty acyl-CoA ligase; FACL; FACL13; Fatty acyl-CoA synthetase; ACS; FACS; Very-long-chain fatty-acyl-CoA synthetase; ACSVL; EC 6.2.1.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
30% identity, 61% coverage: 311:828/844 of query aligns to 16:496/503 of P9WQ37

query
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P9WQ37

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R

R

M

L

I

L

Q

P

V

L

P

P

M

M

F

F

H

H

C
x
V

F

A

G
x
A

M

L

V

T

L
x
T

A

V

M

I

T

F

A

S

S

A

M

M

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-

H

R

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G

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L

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L

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-

V

-

I

I

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Y

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A

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A

N

K

M

N

K

I

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E

I

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Y

Y

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x
A

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A

A

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Q

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N

T

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A

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Q

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Q

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I

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E

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Y

F

C

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A

T

N

R

M

L

A

A

R

R

H

Y

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K

C

L

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P

R

K

Y

K

I

V

D

I

F

F

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A

P

E

A

A

F

I

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P

M

R

N

N

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Q

R17 (≠ D312) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
K172 (= K496) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
R195 (≠ S519) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
R197 (≠ A521) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
V209 (≠ C533) mutation to D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis.
A211 (≠ G535) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
T214 (≠ L538) mutation to W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid).
R244 (= R569) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
A302 (≠ G629) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.; mutation to W: Does not show activity with small, medium or long acyl chains.
W377 (= W708) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis.
D382 (= D713) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced.
R397 (= R728) mutation to A: Reduction of binding affinity for fatty acids.
S404 (≠ R735) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
G406 (= G737) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
K487 (= K819) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.

Sites not aligning to the query:

9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.

3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
29% identity, 60% coverage: 326:828/844 of query aligns to 47:528/528 of 3ni2A

query
sites
3ni2A

T

T

Y

Y

A

A

E

D

F

V

R

E

D

L

D

T

V

A

D

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E

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L

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G

G

A

A

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A

V

A

N

N

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A

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A

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A

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A

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I

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Y

R

I

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F

F

F

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E

A

A

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active site: S182 (≠ T488), S202 (≠ N508), H230 (= H532), T329 (= T631), E330 (= E632), K434 (≠ I734), Q439 (≠ N739), K519 (= K819)
binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F534), S236 (≠ L538), G302 (= G604), A303 (≠ S605), P304 (= P606), G325 (≠ T627), G327 (= G629), T329 (= T631), P333 (= P635), V334 (≠ G636), D413 (= D713), K430 (= K730), K434 (≠ I734), Q439 (≠ N739)

3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 60% coverage: 326:828/844 of query aligns to 47:528/528 of 3a9vA

query
sites
3a9vA

T

T

Y

Y

A

A

E

D

F

V

R

E

D

L

D

T

V

A

D

R

E

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A

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A

T

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H

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G

A

A

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A

V

A

N

N

T

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A

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Y

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A

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A

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E

F

I

V

C

A

I

R

R

G

G

Y

D

N

Q

I

I

M

M

K

K

G

G

Y

Y

Y

L

K

N

M

D

P

P

E

E

A

A

T

T

A

S

A

R

A

T

I

I

D

D

K

K

D

E

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G

W

W

L

L

H

H

S

T

G

G

D
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D

L

I

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G

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Y

R

I

T

D

A

D

D

D

G

D

Y

E

Y

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|
K

D

E

M

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I

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I
x
K

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Y

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K

G

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N
x
Q

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A

P

P

K

A

E

E

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L

E

E

E

A

F

L

L

L

Y

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H

P

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E

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I

K

S

D

D

V

A

Q

A

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V

I

V

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G

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L

P

K

D

D

E

E

A

D

M

A

G

G

E

E

E

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I

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M

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A

A

C

F

V

V

I

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L

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G

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A

A

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T

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E

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D

E

E

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I

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K

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N

Q

M

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A

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C

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I

R

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Y

R

I

V

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F

F

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I

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A

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E

E

E

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active site: S182 (≠ T488), S202 (≠ N508), H230 (= H532), T329 (= T631), E330 (= E632), K434 (≠ I734), Q439 (≠ N739), K519 (= K819)
binding adenosine monophosphate: H230 (= H532), G302 (= G604), A303 (≠ S605), P304 (= P606), Y326 (= Y628), G327 (= G629), M328 (≠ Q630), T329 (= T631), D413 (= D713), K430 (= K730), K434 (≠ I734), Q439 (≠ N739)

4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
29% identity, 62% coverage: 305:827/844 of query aligns to 8:499/506 of 4gxqA

query
sites
4gxqA

R

R

I

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D

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A

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E

T

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A

N

A

Y

G

T

D

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-

I

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Y

A

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E

E

F

L

R

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D

A

D

R

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A

D

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E

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A

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E

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T

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K

R

I

A

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G

A

G

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P

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L

N

N

T

T

A

A

Y

Y

K

T

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E

A

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Y

Y

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-

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L

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E

E

T

T

A

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A

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P

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G

P

-

L

-

A

-

C

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-

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G

A

A

A

-

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T

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P

S

K

K

G

G

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A

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N

N

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N

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|
H

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N

A

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T

P

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S

I

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A

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I

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M

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x
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x
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E

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I

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|
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Y

P

P

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K

E

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I

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P

P

D

H

E

A

A

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G

G

E

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T

A

A

C

F

V

V

I

V

L

L

K

K

E

R

G

E

E

F

T

A

A

P

T

S

E

E

-

I

-

L

-

A

K

E

E

E

I

L

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K

D

A

H

F

F

V

L

K

A

D

N

R

M

L

A

A

R

K

H

F

K

K

C

M

P

P

R

K

Y

K

I

V

D

I

F

F

V

V

P

D

A

D

F

L

P

P

M

R

N

N

A

T

A

M

G

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x
A

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Q

K

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Y

N

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L

R

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E

E

active site: T163 (= T488), N183 (= N508), H207 (= H532), T303 (= T631), E304 (= E632), I403 (= I734), N408 (= N739), A491 (≠ K819)
binding adenosine-5'-triphosphate: T163 (= T488), S164 (= S489), G165 (= G490), T166 (= T491), T167 (= T492), H207 (= H532), S277 (≠ G604), A278 (≠ S605), P279 (= P606), E298 (≠ I626), M302 (≠ Q630), T303 (= T631), D382 (= D713), R397 (= R728)
binding carbonate ion: H207 (= H532), S277 (≠ G604), R299 (≠ T627), G301 (= G629)

Q9S725 4-coumarate--CoA ligase 2; 4CL 2; 4-coumarate--CoA ligase isoform 2; At4CL2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; EC 6.2.1.12; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
30% identity, 59% coverage: 326:826/844 of query aligns to 65:547/556 of Q9S725

query
sites
Q9S725

T

T

Y

Y

A

A

E

D

F

V

R

H

D

V

D

T

V

S

D

R

E

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F

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A

A

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A

A

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N

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Q

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H

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L

A

A

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F

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G

A

A

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A

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N

T

P

A

F

Y

F

K

T

I

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H

A

E

E

A

I

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Y

K

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Q

L

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K

Q

A

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A

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A

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M

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R

Y

Y

R

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D

S

-

H

-

Y

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D

-

I

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M

-

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E

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L

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E

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T

-

A

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G

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-

P

-

L

-

A

-

C

-

R

-

R

K

L

I

P

K

F

N

L

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N

N

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-

L

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M

A

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E

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N

C

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A

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-

A

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A

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E

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A

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K

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x
M

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E

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x
K

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A

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F

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A

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E

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Y

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R

K211 (= K496) mutation to S: Drastically reduces the activity.
M293 (≠ H574) mutation M->A,P: Affects the substrate specificity.
K320 (≠ A603) mutation K->L,A: Affects the substrate specificity.
E401 (= E680) mutation to Q: Slighlty reduces the substrate specificity.
C403 (≠ V682) mutation to A: Significantly reduces the substrate specificity.
R449 (= R728) mutation to Q: Drastically reduces the activity.
K457 (≠ G736) mutation to S: Drastically reduces the activity.
K540 (= K819) mutation to N: Abolishes the activity.

Q67W82 4-coumarate--CoA ligase 4; 4CL 4; Os4CL4; (E)-ferulate--CoA ligase; 4-coumaroyl-CoA synthase 4; Protein RESISTANCE TO ALUMINUM 1; EC 6.2.1.12; EC 6.2.1.34 from Oryza sativa subsp. japonica (Rice) (see paper)
30% identity, 59% coverage: 326:826/844 of query aligns to 61:542/559 of Q67W82

query
sites
Q67W82

T

S

Y

Y

A

G

E

E

F

V

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E

D

E

D

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D

R

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R

F

A

A

A

R

A

A

G

L

L

I

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S

R

L

L

G

G

V

V

G

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G395 (= G679) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.

3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 61% coverage: 311:828/844 of query aligns to 19:496/502 of 3r44A

query
sites
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