SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 5210149 FitnessBrowser__PV4:5210149 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)
40% identity, 96% coverage: 14:562/574 of query aligns to 20:572/590 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)
32% identity, 95% coverage: 17:561/574 of query aligns to 6:551/561 of P69451

query
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P69451

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Y213 (≠ F221) mutation to A: Loss of activity.
T214 (= T222) mutation to A: 10% of wild-type activity.
G216 (= G224) mutation to A: Decreases activity.
T217 (= T225) mutation to A: Decreases activity.
G219 (= G227) mutation to A: Decreases activity.
K222 (= K230) mutation to A: Decreases activity.
E361 (= E367) mutation to A: Loss of 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, 93% coverage: 31:561/574 of query aligns to 2:495/503 of P9WQ37

query
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R9 (≠ D38) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
R17 (≠ D46) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
K172 (= K230) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
R195 (≠ G253) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
R197 (≠ E255) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
V209 (≠ C267) 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 (≠ G269) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
T214 (≠ L272) 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 (= R304) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
A302 (≠ G364) 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 (= W442) 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 (= D447) 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 (= R462) mutation to A: Reduction of binding affinity for fatty acids.
S404 (≠ R469) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
G406 (= G471) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
K487 (= K553) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.

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)
28% identity, 93% coverage: 35:567/574 of query aligns to 40:554/556 of Q9S725

query
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Q9S725

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K211 (= K230) mutation to S: Drastically reduces the activity.
M293 (≠ H309) mutation M->A,P: Affects the substrate specificity.
K320 (≠ V336) mutation K->L,A: Affects the substrate specificity.
E401 (= E414) mutation to Q: Slighlty reduces the substrate specificity.
C403 (= C416) mutation to A: Significantly reduces the substrate specificity.
R449 (= R462) mutation to Q: Drastically reduces the activity.
K457 (≠ G470) mutation to S: Drastically reduces the activity.
K540 (= K553) mutation to N: Abolishes the activity.

4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
29% identity, 91% coverage: 45:569/574 of query aligns to 16:506/506 of 4gxqA

query
sites
4gxqA

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P

P

L

D

T

K

T

I

L

L

E

D

V

L

V

M

E

A

A

-

E

-

R

R

C

A

T

T

A

V

L

L

H

M

G

G

V

V

P

P

T

T

M

F

F

Y

I

T

A

R

Q

L

L

L

E

Q

H

S

P

P

E

R

F

L

K

T

R

K

F

E

D

T

L

T

S

G

S

H

L

M

R

R

T

L

G

F

V

I

M

S

A

G

G
x
S

A
|
A

T
x
P

C

L

P

L

E

A

E

D

V

T

M

H

R

R

R

E

V

-

Q

W

D

S

L

A

M

K

Y

T

M

G

K

H

E

A

V

V

L

L

I
x
E

G
x
R

Y
|
Y

G
|
G

Q
x
M

T
|
T

E
|
E

C

T

S

-

P

-

I

-

N

-

N

N

M
|
M

T

N

E

T

I

S

G

N

S

P

S

Y

L

D

E

G

K

D

R

R

V

V

T

P

-

G

T

A

V
|
V

G

G

R

P

A

A

L

L

A

P

H

G

T

V

Q

S

V

A

K

R

I

V

V

T

D

D

-

P

E

E

F

T

G

G

E

K

V

E

L

L

P

P

V

R

G

G

Q

D

P

I

G

G

E

M

V

I

C

E

S

V

R

K

G

G

Y

P

C

N

V

V

M

F

Q

K

F

G

Y

Y

W

W

N

R

D

M

A

P

E

E

K

K

T

T

A

K

A

S

T

E

I

F

D

R

S

D

E

D

G

G

W

F

L

F

H

I

S

T

G

G

D
|
D

L

L

G

G

E

K

M

I

D

D

S

E

E

R

G

G

Y

Y

V

V

K

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

K

E

L

I

Y

D

T

A

H

M

P

P

D

G

V

V

Q

V

D

E

A

S

A

A

I

V

F

I

G

G

V

V

K

P

S

H

E

A

K

D

Y

F

G

G

E

E

E

G

V

V

C

T

A

A

W

F

I

V

K

V

V

L

Q

K

-

R

-

E

-

F

P

A

G

P

A

S

S

E

V

I

T

L

E

A

E

E

I

L

R

K

H

A

F

F

L

V

T

K

E

D

K

R

F

L

A

A

Y

K

F

F

K

K

V

M

P

P

R

K

Y

K

I

V

K

I

F

F

V

V

E

D

Q

D

Y

L

P

P

M

R

T

N

V

T

T

M

G

G

K
x
A

I

V

Q

Q

K

K

F

N

K

V

M

L

R

R

E

E

M

-

M

T

Y

Y

Q

K

E

D

L

I

Y

Y

E

K

active site: T163 (= T222), N183 (= N242), H207 (= H266), T303 (= T366), E304 (= E367), I403 (= I468), N408 (= N473), A491 (≠ K553)
binding adenosine-5'-triphosphate: T163 (= T222), S164 (= S223), G165 (= G224), T166 (= T225), T167 (= T226), K171 (= K230), H207 (= H266), S277 (≠ G339), A278 (= A340), P279 (≠ T341), E298 (≠ I361), R299 (≠ G362), Y300 (= Y363), G301 (= G364), M302 (≠ Q365), T303 (= T366), V322 (= V388), D382 (= D447), I394 (= I459), R397 (= R462)
binding carbonate ion: H207 (= H266), T208 (≠ C267), H209 (≠ F268), S277 (≠ G339), R299 (≠ G362), G301 (= G364), M302 (≠ Q365), M307 (= M374)

3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 93% coverage: 31:561/574 of query aligns to 5:495/502 of 3r44A

query
sites
3r44A

Q
x
K

T
x
N

I
|
I

G

G

D

W

Y

M

L

L

D

R

Q

Q

M

R

A

A

A

T

S

V

H

S

P

P

D

R

Q

L

L

Q

A

A

I

Y

V

V

M

E

H

P

H

S

Q

T

G

D

I

V

R

R

W

M

S

T

Y

Y

Q

A

E

Q

Y

M

Q

N

S

A

H

L

I

A

D

N

E

R

L

C

A

A

A

D

G

V

L

L

L

T

A

A

I

L

G

G

I

I

K

A

P

K

G

G

D

D

R

R

V

V

G

A

I

L

W

L

S

M

P

P

N

N

N

S

I

V

E

E

W

F

C

C

L

C

T

L

Q

F

F

Y

A

G

T

A

A

A

K

K

I

L

G

G

A

A

I

V

M

A

V

V

C

P

I

I

N

N

P

T

A

R

Y

L

R

A

P

A

E

P

E

E

L

V

Q

S

Y

F

A

I

L

L

N

S

N

D

V

S

G

G

C

S

R

K

A

V

I

V

I

I

C

Y

A

G

E

-

K

-

F

-

K

-

S

-

H

-

Y

-

L

-

S

-

M

-

L

-

Y

-

E

-

L

-

A

A

P

P

E

-

L

-

K

-

Q

-

C

-

L

-

P

-

G

-

Q

-

L

-

E

-

S

-

A

-

N

S

L

A

P

P

S

V

L

I

E

D

F

A

V

I

I

R

R

A

M

Q

G

A

D

D

E

-

A

-

S

P

P

P

G

G

M

T

L

V

N

T

F

D

N

W

H

I

L

G

K

A

R

D

P

S

L

L

T

A

E

E

S

R

D

L

R

R

K

S

A

A

L

A

K

A

D

D

T

E

-

P

A

A

A

V

Q

E

L

C

S

G

P

G

F

D

D

D

A

N

I

L

N

F

I

I

Q

M

F

Y

T
|
T

S

S

G

G

T

-

G

-

S

H

P

P

K

K

G

G

A

V

T

V

L

H

S

T

H
|
H

H
x
E

N

S

I

V

L
x
H

N

S

N
x
A

G

A

L

S

V

W

A

A

K

S

A

T

M

I

R

D

L

V

G

R

L

Y

E

R

D

D

R

R

L

L

C

L

I

L

P

P

V

L

P

P

L

M

Y

F

H
|
H

C

V

F

A

G

A

M

L

V

T

L

T

G

V

N

I

L

F

S

S

C

A

I

M

S

R

V

-

G

-

A

G

S

V

A

T

I

L

Y

I

P

S

S

M

D

P

S

Q

F

F

D

D

P

A

L

T

T

K

T

V

L

W

E

S

V

L

V

I

E

V

A

E

E

E

R

R

C

V

T

C

A

I

L

G

H

G

G

A

V

V

P

P

T

A

M

I

F

L

I

N

A

F

Q

M

L

R

E

Q

H

V

P

P

E

E

F

F

K

A

R

E

F

L

D

D

L

A

S

P

S

D

L

F

R

R

T

Y

G

F

V

I

M

T

A

G

G

G

A

A

T

P

C

M

P

P

E

E

E

A

V

L

M

I

R

K

R

-

V

-

Q

-

D

-

L

-

M

I

Y

Y

M

A

K

A

-

K

-

N

-

I

E

E

V

V

L

V

I

Q

G

G

Y

Y

G

A

Q

L

T
|
T

E
|
E

C

S

S

C

P

G

I

G

N

G

N

T

M

L

T

L

E

L

I

S

G

E

S

D

S

A

L

L

E

R

K

K

R

-

V

A

T

G

T

S

V

A

G

G

R

R

A

A

L

T

A

M

H

F

T

T

Q

D

V

V

K

A

I

V

V

R

D

G

E

D

F

D

G

G

E

V

V

I

L

R

P

E

V

H

G

G

Q

E

P

-

G

G

E

E

V

V

C

V

S

I

R

K

G

S

Y

D

C

I

V

L

M

L

Q

K

F

E

Y

Y

W

W

N

N

D

R

A

P

E

E

K

A

T

T

A

R

A

D

T

A

I

F

D

D

S

N

E

-

G

G

W

W

L

F

H

R

S

T

G

G

D

D

L

I

G

G

E

E

M

I

D

D

S

D

E

E

G

G

Y

Y

V

L

K

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

K

V

L

I

Y

I

T

G

H

V

P

P

D

G

V

V

Q

S

D

E

A

V

A

A

I

V

F

I

G

G

V

L

K

P

S

D

E

E

K

K

Y

W

G

G

E

-

E

E

V

I

C

A

A

A

W

A

I

I

K

V

V

V

Q

A

P

D

G

Q

A

N

S

E

V

V

T

S

E

E

E

Q

I

I

R

V

H

E

F

Y

L

C

T

G

E

T

K

R

F

L

A

A

Y

R

F

Y

K

K

V

L

P

P

R

K

Y

K

I

V

K

I

F

F

V

A

E

E

Q

A

Y

I

P

P

M

R

T

N

V

P

T

T

G

G

K
|
K

I

I

Q

L

K

K

F

T

K

V

M

L

R

R

E

E

active site: T167 (= T222), A184 (≠ N242), H208 (= H266), T304 (= T366), E305 (= E367), I403 (= I468), N408 (= N473), K487 (= K553)
binding histidine: K5 (≠ Q31), N6 (≠ T32), I7 (= I33), H178 (= H236), E179 (≠ H237), H182 (≠ L240)

Sites not aligning to the query:

binding histidine: 4

6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
29% identity, 90% coverage: 32:547/574 of query aligns to 5:493/504 of 6qjzA

query
sites
6qjzA

T

T

I

L

G

T

D

G

Y

L

L

L

D

Q

Q

S

M

V

A

A

A

K

S

T

H

F

P

P

D

S

Q

R

L

R

A

G

I

I

V

-

M

-

H

-

Q

-

G

S

I

L

R

A

W

G

S

K

Y

F

Q

D

E

L

Y

T

Q

H

S

S

H

H

I

L

D

N

E

E

L

L

-

V

-

E

-

S

-

A

A

A

A

D

G

H

L

L

L

I

A

S

I

A

G

G

I

I

K

K

P

P

G

N

D

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

E

E

L

F

Q

E

Y

F

A

Y

L

L

N

S

N

D

V

S

G

E

C

S

R

K

A

L

I

L

C

T

A

P

E

L

K

E

F

G

K

N

S

K

S

P

H

-

Y

-

L

-

S

-

M

-

L

-

Y

-

E

-

L

-

A

A

P

Q

E

D

L

A

K

A

Q

S

C

K

L

L

P

S

G

I

Q

P

L

L

E

G

S

S

A

A

N

S

L

L

P

T

S

K

L

S

E

E

F

E

V

E

I

T

R

K

M

L

G

T

D

I

E

S

A

-

S

-

P

-

G

-

M

-

L

-

N

-

F

-

N

-

H

-

L

L

K

K

R

H

P

P

L

E

T

S

E

G

S

S

D

V

R

A

K

K

A

L

L

I

K

N

D

E

T

-

A

-

Q

-

L

-

S

-

P

P

F

S

D

D

A

V

I

A

N

L

I

F

Q

L

F

H

T
|
T

S

S

G

G

T

T

G

S

S

R

P

P

K

K

G

G

A

V

T

P

L

L

S

T

H

Q

H

H

N

N

I

L

L

V

N

S

N
x
S

G

V

L

K

L

N

V

I

A

Q

K

S

A

V

M

Y

R

Q

L

L

G

T

L

E

E

S

D

D

R

S

L

T

C

V

I

I

P

V

V

L

P

P

L

L

Y

F

H
|
H

C

V

F

H

G

G

M

L

V

I

L

A

G

G

N

L

L

L

S

S

C

S

I

L

S

G

V

S

G

G

A

A

S

A

A

V

I

V

Y

L

P

P

S

A

D

A

S

G

-

R

F

F

D

S

P

A

L

S

T

T

T

F

L

W

E

K

V

D

V

M

E

I

A

Q

E

Y

R

N

C

A

T

T

A

W

L

Y

H

T

G

A

V

V

P

P

T

T

M

I

-

H

-

Q

-

I

F

L

I

D

A

R

Q

H

L

L

E

N

H

N

P

P

E

E

F

P

K

A

R

Y

F

P

D

K

L

L

S

R

S

F

L

I

R

R

T

S

G

-

V

-

M

-

A

C

G
x
S

A
|
A

T
x
S

C

L

P

A

E

P

E

V

V

I

M

L

R

G

R

R

V

L

Q

E

D

E

L

-

M

S

Y

F

M

G

K

A

E

P

V

V

L

L

I
x
E

G
x
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

M

S

T

N

E

P

I

L

G

P

S

Q

S

N

L

G

E

P

K

H

R

K

V

A

T

G

T

S

V
|
V

G

G

R

K

A

P

L

V

A

G

H

Q

T

-

Q

E

V

M

K

A

I

I

V

L

D

D

E

E

F

S

G

G

E

R

V

V

L

L

P

E

V

A

G

G

Q

V

P

N

G

G

E

E

V

V

C

C

S

I

R

R

G

G

Y

E

C

N

V

V

M

T

Q

K

F

G

Y

Y

W

K

N

N

D

N

-

E

A

A

E

A

K

N

T

T

A

A

T

F

I

L

D

F

S

-

E

-

G

G

W

W

L

F

H

H

S

T

G

G

D
|
D

L

I

G

G

E

Y

M

F

D

D

S

S

E

D

G

G

Y

Y

V

L

K

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

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active site: T169 (= T222), S189 (≠ N242), H213 (= H266), T314 (= T366), E315 (= E367), N414 (≠ I468), K419 (≠ N473)
binding adenosine monophosphate: H213 (= H266), S288 (≠ G339), A289 (= A340), S290 (≠ T341), E309 (≠ I361), A310 (≠ G362), Y311 (= Y363), A312 (≠ G364), M313 (≠ Q365), T314 (= T366), V336 (= V388), D393 (= D447), L405 (≠ I459), K410 (= K464), N414 (≠ I468), K419 (≠ N473)

Q9SMT7 Oxalate--CoA ligase; 4-coumarate--CoA ligase isoform 8; At4CL8; 4-coumarate--CoA ligase-like 10; Acyl-activating enzyme 3; Adenosine monophosphate binding protein 3; AtMPBP3; Oxalyl-CoA synthetase; EC 6.2.1.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 94% coverage: 31:569/574 of query aligns to 4:512/514 of Q9SMT7

query
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TSGTT 170:174 (= TSGTT 222:226) binding
H214 (= H266) binding ; mutation to A: Abolished activity.
S289 (≠ G339) binding ; mutation to A: Abolished activity.
SAS 289:291 (≠ GAT 339:341) binding
EA 310:311 (≠ IG 361:362) binding
M314 (≠ Q365) binding
T315 (= T366) binding
H319 (≠ P370) binding ; mutation to A: Abolished activity.
D394 (= D447) binding
R409 (= R462) binding ; mutation to A: Abolished activity.
K500 (= K553) binding ; binding ; mutation to A: Abolished activity.

6e97B Implication of mbth-like proteins in crystallization of the independent nrps a domains. Crystal structure of fscc: supporting rationale for revised mechanism of freestanding aryl acid adenylating enzymes.
29% identity, 94% coverage: 31:567/574 of query aligns to 22:536/537 of 6e97B

query
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6e97B

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