SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_010554469.1 NCBI__GCF_000238395.3:WP_010554469.1 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)
38% identity, 95% coverage: 18:565/577 of query aligns to 20:571/590 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

P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
30% identity, 89% coverage: 63:575/577 of query aligns to 49:561/561 of P69451

query
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P69451

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Y213 (≠ F225) mutation to A: Loss of activity.
T214 (= T226) mutation to A: 10% of wild-type activity.
G216 (= G228) mutation to A: Decreases activity.
T217 (= T229) mutation to A: Decreases activity.
G219 (= G231) mutation to A: Decreases activity.
K222 (= K234) mutation to A: Decreases activity.
E361 (= E371) mutation to A: Loss of activity.

8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
30% identity, 93% coverage: 32:566/577 of query aligns to 1:486/486 of 8wevA

query
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8wevA

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K

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G

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A

A

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M

L

L

T

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H

H

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N

N

I

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x
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binding adenosine monophosphate: G267 (= G343), A268 (≠ S344), Y289 (= Y367), G290 (= G368), M291 (≠ Q369), T292 (= T370), D371 (= D451), R386 (= R466)
binding magnesium ion: R24 (≠ H57), R186 (≠ K261)

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)
29% identity, 90% coverage: 48:566/577 of query aligns to 15:496/503 of P9WQ37

query
sites
P9WQ37

N

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R17 (≠ E50) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
K172 (= K234) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
R195 (≠ T257) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
R197 (≠ D259) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
V209 (≠ C271) 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 (= A273) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
T214 (≠ S278) 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 (≠ G308) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
A302 (≠ G368) 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 (= W446) 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 (= D451) 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 (= R466) mutation to A: Reduction of binding affinity for fatty acids.
S404 (≠ R473) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
G406 (= G475) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
K487 (= K557) 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.

3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
28% identity, 90% coverage: 48:566/577 of query aligns to 18:496/502 of 3r44A

query
sites
3r44A

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x
E

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Q

L

T
|
T

E
|
E

C

S

S

C

P

G

I

G

N

G

N

T

I

L

T

L

E

L

T

S

D

E

S

D

S

A

I

L

E

-

R

R

Q

K

V

A

T

G

T

S

V

A

G

G

R

R

A

A

L

T

A

M

H

F

T

T

E

D

V

V

K

A

I

V

I

R

D

G

E

D

L

D

G

G

N

V

I

I

Q

R

Q

E

I

H

G

G

Q

E

P

-

G

G

E

E

V

V

C

V

S

I

K

K

G

S

A

D

G

I

I

L

M

L

R

K

C

E

Y

Y

W

W

N

N

D

R

D

P

A

E

K

A

T

T

K

R

A

D

T

A

I

F

D

D

E

-

S

N

G

G

W

W

L

F

H

R

S

T

G

G

D

D

L

I

G

G

V

E

M

I

D

D

T

D

E

E

G

G

F

Y

V

L

T

Y

I

I

V

K

G

D

R

R

I

L

K

K

D

D

M

M

I

I

I
|
I

R

S

G

G

E

E

N
|
N

I

V

Y

Y

P

P

R

A

E

E

I

I

E

E

E

S

V

V

L

I

Y

I

T

G

Y

V

P

P

G

G

I

V

Q

S

D

E

A

V

A

A

I

V

F

I

G

G

I

L

T

P

D

D

E

E

R

K

Y

W

G

G

E

E

E

I

V

A

C

A

A

A

W

I

I

V

Q

V

P

A

K

D

E

Q

D

N

A

E

V

V

L

-

D

S

E

E

Q

Q

A

Q

I

I

R

V

E

E

F

Y

L

C

K

G

D

T

K

R

L

L

A

A

Y

R

F

Y

K

K

M

L

P

P

R

K

H

K

I

V

R

I

F

F

V

A

E

E

N

A

Y

I

P

P

M

R

T

N

V

P

T

T

G

G

K
|
K

L

I

Q

L

K

K

F

T

K

V

M

L

R

R

E

E

Q

Q

active site: T167 (= T226), A184 (≠ N246), H208 (= H270), T304 (= T370), E305 (= E371), I403 (= I472), N408 (= N477), K487 (= K557)
binding histidine: E179 (≠ K241), H182 (≠ L244)

Sites not aligning to the query:

binding histidine: 5

4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
28% identity, 92% coverage: 41:569/577 of query aligns to 6:503/506 of 4gxqA

query
sites
4gxqA

F

F

D

A

F

R

I

L

V

F

D

D

K

K

-

L

-

D

N

D

P

P

E

H

A

K

L

L

A

A

V

I

V

E

V

T

H

A

H

-

Q

A

G

G

I

D

R

K

L

I

T

S

Y

Y

K

A

E

E

F

L

Q

V

K

A

E

R

V

A

N

G

Q

R

L

V

A

A

M

N

G

V

L

L

L

V

A

A

L

R

G

G

V

L

K

Q

P

V

G

G

E

D

R

R

V

V

G

A

I

A

W

Q

S

T

P

E

N

K

N

S

I

V

E

E

W

A

C

L

L

V

T

L

Q

Y

F

L

A

A

T

T

A

V

K

R

I

A

G

G

A

G

I

V

M

Y

V

L

C

P

I

L

N

N

P

T

A

A

Y

Y

R

T

P

L

N

H

E

E

L

L

Q

D

Y

Y

A

F

L

I

N

T

S

D

V

A

E

E

C

-

S

-

T

-

L

-

I

-

T

-

A

-

S

-

N

-

F

-

K

-

G

-

S

-

D

-

Y

-

L

-

E

-

M

-

L

-

N

-

G

-

L

-

A

-

P

P

E

K

L

I

A

V

T

V

C

C

N

D

-

P

-

S

-

K

K

R

D

D

T

G

L

I

N

A

L

A

K

I

A

A

L

A

P

K

T

V

L

G

K

A

N

T

I

V

I

E

R

T

I

L

G

G

D

P

E

D

A

-

S

-

P

-

G

G

M

R

Y

G

S

S

F

L

N

T

D

D

V

-

I

-

N

-

L

-

P

-

T

-

S

A

A

A

H

A

E

G

L

A

E

S

L

E

K

A

A

F

I

A

G

T

A

I

N

D

L

R

N

G

A

A

E

D

Q

D

D

L

I

A

N

A

I

I

Q

L

F

Y

T
|
T

S
|
S

G
|
G

T
|
T

G

G

N

R

P

S

K

K

G

G

A

A

T

M

L

L

T

S

H

H

K

D

N

N

I

L

L

A

N

S

N
|
N

A

S

L

L

F

T

V

L

A

V

E

D

S

Y

M

W

H

R

F

F

T

T

S

P

D

D

K

V

L

L

C

I

I

H

P

A

I

L

P

P

L

I

Y

Y

H
|
H

C

T

F

H

A

G

M

L

V

F

L

V

G

A

S

S

-

N

L

V

L

T

C

L

V

F

S

A

K

R

G

G

A

S

A

M

A

I

I

F

Y

L

P

P

G

-

D

-

S

K

F

F

D

D

A

P

K

D

T

K

T

I

L

L

D

D

V

L

V

M

Q

A

Q

R

E

-

G

-

C

A

T

T

A

V

L

L

H

M

G

G

V

V

P

P

T

T

M

F

F

Y

I

T

S

R

E

L

L

L

E

Q

L

S

S

P

N

R

F

L

N

T

D

K

Y

E

D

T

L

T

S

G

T

H

L

M

R

R

T

L

G

F

V

I

M

S

A

G

G
x
S

S
x
A

T
x
P

C

L

P

L

E

A

Q

D

V

T

M

H

R

R

K

E

V

W

Q

S

T

A

Q

K

M

T

N

G

M

-

H

H

Q

A

V

V

L

L

I
x
E

A
x
R

Y

Y

G
|
G

Q
x
M

T
|
T

E
|
E

C

T

S

N

P

-

I

M

N

N

N

T

I

S

T

N

E

P

T

Y

D

D

S

G

S

-

I

-

E

D

R

R

Q

V

V

P

T

G

T

A

V

V

G

G

R

P

A

A

L

L

A

P

H

G

T

V

E

S

V

A

K

R

I

V

I

T

D

D

-

P

E

E

L

T

G

G

N

K

I

E

Q

L

Q

P

I

R

G

G

Q

D

P

I

G

G

E

M

V

I

C

E

S

V

K

K

G

G

A

P

G

N

I

V

M

F

R

K

C

G

Y

Y

W

W

N

R

D

M

D

P

A

E

K

K

T

T

K

K

A

S

T

E

I

F

D

R

E

D

S

D

G

G

W

F

L

F

H

I

S

T

G

G

D
|
D

L

L

G

G

V

K

M

I

D

D

T

E

E

R

G

G

F

Y

V

V

T

H

I

I

V

L

G

G

R
|
R

I

G

K

K

D

D

M

L

I

V

I
|
I

R

T

G

G

E

F

N
|
N

I

V

Y

Y

P

P

R

K

E

E

I

I

E

E

E

S

V

E

L

I

Y

D

T

A

Y

M

P

P

G

G

I

V

Q

V

D

E

A

S

A

A

I

V

F

I

G

G

I

V

T

P

D

H

E

A

R

D

Y

F

G

G

E

E

E

G

V

V

C

T

A

A

W

F

I

V

Q

V

P

L

K

K

E

R

D

E

A

F

V

A

L

P

D

S

E

E

-

I

-

L

-

A

Q

E

A

E

I

L

R

K

E

A

F

F

L

V

K

K

D

D

K

R

L

L

A

A

Y

K

F

F

K

K

M

M

P

P

R

K

H

K

I

V

R

I

F

F

V

V

E

D

N

D

Y

L

P

P

M

R

T

N

V

T

T

M

G

G

K
x
A

L

V

Q

Q

K

K

F

N

K

V

M

L

R

R

E

E

Q

T

M

Y

Q

K

E

D

active site: T163 (= T226), N183 (= N246), H207 (= H270), T303 (= T370), E304 (= E371), I403 (= I472), N408 (= N477), A491 (≠ K557)
binding adenosine-5'-triphosphate: T163 (= T226), S164 (= S227), G165 (= G228), T166 (= T229), T167 (= T230), H207 (= H270), S277 (≠ G343), A278 (≠ S344), P279 (≠ T345), E298 (≠ I365), M302 (≠ Q369), T303 (= T370), D382 (= D451), R397 (= R466)
binding carbonate ion: H207 (= H270), S277 (≠ G343), R299 (≠ A366), G301 (= G368)

6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
28% identity, 85% coverage: 63:551/577 of query aligns to 31:493/504 of 6qjzA

query
sites
6qjzA

L

L

T

T

Y

H

K

S

E

H

F

L

Q

N

K

E

E

L

V

V

N

E

Q

S

L

A

A

A

M

D

G

H

L

L

L

I

A

S

L

A

G

G

V

I

K

K

P

P

G

N

E

D

R

V

V

V

G

A

I

L

W

T

S

F

P

P

N

N

N

T

I

V

E

E

W

Y

C

V

L

I

T

L

Q

F

F

L

A

A

T

V

A

I

K

R

I

V

G

R

A

A

I

T

M

A

V

A

C

P

I

L

N

N

P

A

A

A

Y

Y

R

T

P

A

N

E

E

E

L

F

Q

E

Y

F

A

Y

L

L

N

S

S

D

V

S

E

E

C

S

S

K

T

L

L

L

I

L

T

T

A

P

S

-

N

-

F

-

K

-

G

-

S

-

D

-

Y

-

L

-

E

-

M

-

L

L

N

E

G

G

L

N

A

K

P

P

E

A

L

Q

A

D

T

A

C

A

N

S

K

K

D

L

T

S

L

I

N

P

L

L

K

-

A

-

L

-

P

-

T

-

L

-

K

-

N

-

I

-

R

-

I

-

G

-

D

-

E

-

A

G

S

S

P

A

G

S

M

L

Y

T

S

K

F

S

N

E

D

E

V

E

I

T

N

K

L

L

P

T

T

I

S

S

A

L

H

K

E

H

L

P

E

E

L

S

K

G

A

S

I

V

G

A

A

K

N

L

L

I

N

N

A

E

E

P

Q

S

D

D

I

V

N

A

I

L

Q

F

F

L

-

H

T
|
T

S

S

G

G

T

T

G

S

N

R

P

P

K

K

G

G

A

V

T

P

L

L

T

T

H

Q

K

H

N

N

I

L

L

V

N

S

N
x
S

A

V

L

K

F

N

V

I

A

Q

E

S

S

V

M

Y

H

Q

F

L

T

T

S

E

D

S

D

D

K

S

L

T

C

V

I

I

P

V

I

L

P

P

L

L

Y

F

H
|
H

C

V

F

H

A

G

M

L

V

I

L

A

G

G

S

L

L

L

L

S

C

S

V

L

S

G

K

S

G

G

A

A

A

V

I

V

Y

L

P

P

G

A

-

A

D

G

S

R

F

F

D

S

A

A

K

S

T

T

T

F

L

W

D

K

V

D

V

M

Q

I

Q

Q

E

Y

G

N

C

A

T

T

A

W

L

Y

H

T

G

A

V

V

P

P

T

T

M

I

-

H

-

Q

F

I

I

I

S

L

E

D

L

R

E

H

L

L

S

N

N

N

F

-

N

P

D

E

Y

P

D

A

L

Y

S

P

T

K

L

L

R

R

T

F

G

I

V

R

M

S

A

C

G
x
S

S
x
A

T
x
S

C

L

P

A

E

P

Q

V

V

I

M

L

R

G

K

R

V

L

Q

E

T

E

Q

S

M

F

N

G

M

A

H

-

Q

P

V

V

L

L

I

E

A

A

Y

Y

G
x
A

Q
x
M

T
|
T

E
|
E

C

A

S

S

P

H

I

L

N

M

N

S

I

S

T

N

E

P

T

L

D

P

S

Q

S

N

I

G

E

P

R

H

Q

K

V

A

T

G

T

S

V

V

G

G

R

K

A

P

L

V

A

G

H

Q

T

-

E

E

V

M

K

A

I

I

I

L

D

D

E

E

L

S

G

G

N

R

I

V

Q

L

Q

E

I

A

G

G

Q

V

P

N

G

G

E

E

V

V

C

C

S

I

K

R

G

G

A

E

G

N

I

V

M

T

R

K

C

G

Y

Y

W

K

N

N

D

N

D

E

A

A

K

A

T

N

K

T

A

A

T

A

I

F

D

-

E

L

S

F

G

G

W

W

L

F

H

H

S

T

G

G

D
|
D

L

I

G

G

V

Y

M

F

D

D

T

S

E

D

G

G

F

Y

V

L

T

H

I
x
L

V

V

G

G

R

R

I

I

K
|
K

D

E

M

L

I

I

I
x
N

R

R

G

G

E

E

N
x
K

I

I

Y

S

P

P

R

I

E

E

I

V

E

D

E

A

V

V

L

L

Y

L

T

S

Y

H

P

P

G

D

I

V

Q

A

D

Q

A

A

A

V

I

A

F

F

G

G

I

I

T

P

D

D

E

Q

R

K

Y

Y

G

G

E

E

V

I

C

H

A

C

W

A

I

I

Q

I

P

P

K

R

E

E

D

G

A

S

V

N

L

I

D

D

E

A

Q

E

A

E

I

V

R

L

E

T

F

F

L

C

K

K

D

K

K

N

L

L

A

A

Y

S

F

F

K

K

M

V

P

P

R

K

H

K

I

V

R

F

F

I

V

T

E

D

N

S

Y

L

P

P

active site: T169 (= T226), S189 (≠ N246), H213 (= H270), T314 (= T370), E315 (= E371), N414 (≠ I472), K419 (≠ N477)
binding adenosine monophosphate: H213 (= H270), S288 (≠ G343), A289 (≠ S344), S290 (≠ T345), A312 (≠ G368), M313 (≠ Q369), T314 (= T370), D393 (= D451), L405 (≠ I463), K410 (= K468), K419 (≠ N477)

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)
26% identity, 97% coverage: 15:571/577 of query aligns to 34:554/556 of Q9S725

query
sites
Q9S725

N

N

H

H

L

L

P

P

L

L

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K211 (= K234) mutation to S: Drastically reduces the activity.
M293 (≠ H313) mutation M->A,P: Affects the substrate specificity.
K320 (≠ V340) mutation K->L,A: Affects the substrate specificity.
E401 (= E418) mutation to Q: Slighlty reduces the substrate specificity.
C403 (= C420) mutation to A: Significantly reduces the substrate specificity.
R449 (= R466) mutation to Q: Drastically reduces the activity.
K457 (≠ G474) mutation to S: Drastically reduces the activity.
K540 (= K557) mutation to N: Abolishes the activity.

O74976 Oxalate--CoA ligase; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 88% coverage: 51:560/577 of query aligns to 16:497/512 of O74976

query
sites
O74976

A

A

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