SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing GFF3324 PS417_17010 AMP-binding protein 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, 99% coverage: 7:544/544 of query aligns to 24:581/590 of Q4WR83

query
sites
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, 94% coverage: 26:534/544 of query aligns to 29:551/561 of P69451

query
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P69451

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Y213 (= Y194) mutation to A: Loss of activity.
T214 (= T195) mutation to A: 10% of wild-type activity.
G216 (= G197) mutation to A: Decreases activity.
T217 (= T198) mutation to A: Decreases activity.
G219 (= G200) mutation to A: Decreases activity.
K222 (= K203) mutation to A: Decreases activity.
E361 (= E340) mutation to A: Loss of activity.

4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 90% coverage: 47:534/544 of query aligns to 28:499/506 of 4gxqA

query
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4gxqA

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active site: T163 (= T195), N183 (= N215), H207 (= H239), T303 (= T339), E304 (= E340), I403 (= I441), N408 (= N446), A491 (≠ K526)
binding adenosine-5'-triphosphate: T163 (= T195), S164 (= S196), G165 (= G197), T166 (= T198), T167 (= T199), K171 (= K203), H207 (= H239), S277 (≠ G312), A278 (= A313), P279 (≠ T314), E298 (≠ Q333), R299 (≠ A335), Y300 (= Y336), G301 (= G337), M302 (= M338), T303 (= T339), V322 (= V361), D382 (= D420), I394 (= I432), R397 (= R435)
binding carbonate ion: H207 (= H239), T208 (≠ C240), H209 (≠ F241), S277 (≠ G312), R299 (≠ A335), G301 (= G337), M302 (= M338), M307 (≠ L346)

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, 94% coverage: 22:534/544 of query aligns to 4:495/503 of P9WQ37

query
sites
P9WQ37

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R9 (≠ D27) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
R17 (≠ D35) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
K172 (= K203) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
R195 (≠ T226) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
R197 (≠ Q228) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
V209 (≠ C240) 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 (≠ G242) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
T214 (≠ M245) 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 (≠ H277) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
A302 (≠ G337) 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 (= W415) 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 (= D420) 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 (= R435) mutation to A: Reduction of binding affinity for fatty acids.
S404 (≠ R442) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
G406 (= G444) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
K487 (= K526) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.

3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 92% coverage: 34:534/544 of query aligns to 19:495/502 of 3r44A

query
sites
3r44A

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R

D

G

A

D

D

D

G

G

N

V

T

I

V

R

A

E

R

H

G

G

E

E

I

-

G

G

E

E

L

V

C

V

T

I

R

K

G

S

Y

D

S

I

V

L

M

L

L

K

G

E

Y

Y

W

W

N

N

N

R

P

P

D

E

A

A

T

T

R

R

E

D

A

A

I

F

D

D

D

N

A

-

G

G

W

W

M

F

H

R

T

T

G

G

D

D

L

I

A

G

S

E

M

I

D

D

A

D

H

E

G

G

Y

Y

V

L

C

Y

I

I

A

K

G

D

R

R

N

L

K

K

D

D

M

M

I

I

I
|
I

R

S

G

G

E

E

N
|
N

V

V

Y

Y

P

P

R

A

E

E

L

I

E

E

E

S

F

V

F

I

T

G

H

V

P

P

A

G

V

V

A

S

D

E

V

V

Q

A

V

V

I

I

G

G

I

L

P

P

D

D

E

E

R

K

Y

W

G

G

E

E

A

I

I

A

V

A

A

A

W

I

V

V

K

V

F

A

H

D

P

Q

G

N

H

E

V

V

A

-

N

S

E

E

L

Q

E

Q

L

I

Q

V

T

E

W

Y

C

C

K

G

G

T

R

R

I

L

A

A

H

R

F

Y

K

K

T

L

P

P

K

K

H

K

F

V

K

I

F

F

V

A

E

E

E

A

F

I

P

P

M

R

T

N

V

P

T

T

G

G

K
|
K

I

I

Q

L

K

K

F

T

R

V

M

L

R

R

E

E

active site: T167 (= T195), A184 (≠ N215), H208 (= H239), T304 (= T339), E305 (= E340), I403 (= I441), N408 (= N446), K487 (= K526)
binding histidine: H178 (= H209), E179 (≠ H210), H182 (≠ L213)

Sites not aligning to the query:

binding histidine: 4, 5, 6, 7

6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
29% identity, 93% coverage: 28:535/544 of query aligns to 29:536/539 of 6k4dA

query
sites
6k4dA

R

K

T

K

V

Y

A

A

Q

Q

F

L

P

P

D

G

G

T

E

I

A

A

L

L

V

T

V

D

R

A

H

H

Q

T

Q

E

R

E

R

N

Y

I

T

S

W

Y

R

A

Q

E

L

L

A

L

E

E

T

L

V

T

D

C

L

R

H

L

A

A

R

E

A

S

F

L

L

K

A

N

L

Y

G

G

M

L

Q

K

T

Q

G

N

D

N

R

T

L

I

G

A

I

V

W

C

A

S

P

E

N

N

C

N

A

L

E

Q

W

F

C

F

I

I

S

P

Q

V

I

I

A

A

S

A

A

L

K

Y

L

I

G

G

V

V

I

A

L

V

V

A

N

P

I

V

N

N

P

D

A

K

Y

Y

R

T

S

E

S

R

E

E

L

L

E

I

Y

N

V

S

L

L

K

N

Q

I

S

S

G

K

C

P

Q

T

W

I

L

I

V

F

C

C

A

-

G

-

S

S

F

K

K

K

T

T

S

L

D

Q

Y

K

H

I

A

L

M

Q

L

V

Q

K

A

K

L

K

N

L

P

S

D

Y

L

I

R

K

G

K

M

I

I

I

S

I

L

L

D

D

P

S

S

K

P

E

P

D

-

I

P

G

G

G

F

Y

L

Q

P

C

W

L

A

N

Q

N

L

F

A

I

A

S

L

Q

G

H

T

S

G

D

I

A

P

N

L

F

E

N

Q

V

L

S

H

N

S

F

R

K

Q

P

T

N

S

S

L

F

H

D

F

R

D

D

Q

E

A

Q

V

V

N

A

-

L

I

I

Q

M

Y

N

T

S

S

S

G

G

T

T

G

G

F

L

P

P

K

K

G

G

A

V

T

M

L

L

S

T

H

H

H

K

N

N

-

L

-

V

-
x
R

-

F

-

S

-

H

-

C

-

R

-

D

-

P

I

I

L

F

N

G

N

N

G

Q

Y

I

M

I

V

P

G

G

E

T

S

A

L

I

G

-

L

L

T

T

A

V

Q

-

D

-

R

-

L

-

V

-

I

-

P

-

V

I

P

P

L

F

Y

H

H
|
H

C
x
G

F
|
F

G

G

M

M

V

-

M

F

G
x
T

N

T

L

L

G

G

C

Y

I

F

T

T

H

C

G

G

T

F

T

R

M

I

I

V

Y

L

P

M

N

H

D

R

G

-

F

F

D

E

P

E

L

E

L

L

T

F

L

L

T

K

A

S

V

L

A

Q

E

D

E

Y

H

K

A

V

T

Q

G

S

L

T

Y
x
L

G

L

V

V

P

P

T

T

M

L

F

M

I

A

A

F

M

F

L

A

D

K

H

S

P

P

Q

L

L

V

G

D

G

K

F

Y

D

D

L

L

S

S

S

N

L

L

R

K

T

E

G

I

I

A

M
x
S

A
x
G

G
|
G

A
|
A

T
x
P

C

L

P

S

I

K

E

E

V

V

M

G

R

E

R

A

V

V

I

A

S

K

E

R

M

F

H

K

M

L

S

P

E

G

V

I

Q
x
R

I
x
Q

A
x
G

Y
|
Y

G
|
G

M
x
L

T
|
T

E

E

T

T

S

T

P
x
S

V
x
A

S

I

L

I

Q

I

T

T

G

P

A

E

D

G

D

D

D

-

L

-

E

-

R

V

R

K

V

P

T

G

T

S

V
x
T

G

G

R

K

T

V

Q

V

P

P

Q

F

L

F

E

S

N

A

K

K

I

V

D

D

A

L

D

D

-

T

G

G

N

K

T

T

V

L

A

G

R

P

G

N

E

Q

I

R

G

G

E

E

L

L

C

C

T

F

R

K

G

G

Y

D

S

M

V

I

M

M

L

K

G

G

Y

Y

W

V

N

N

P

P

D

E

A

A

T

T

R

K

E

E

A

I

I

I

D

D

D

K

A

D

G

G

W

W

M

L

H

H

T

S

G

G

D
|
D

L

I

A

G

S

Y

M

Y

D

D

A

E

H

D

G

G

Y

H

V

F

C

F

I
|
I

A

V

G

D

R
|
R

N

L

K

K

D

S

M

L

I

I

I

K

R

Y

G

K

G

G

E

Y

N

Q

V

V

Y

A

P

P

R

A

E

E

L

L

E

E

E

S

F

I

F

L

T

Q

H

H

P

P

A

S

V

I

A

I

D

D

V

A

Q

G

V

V

I

T

G

G

I

I

P

P

D

D

E

E

R

D

Y

A

G

G

E

E

A

L

I

P

V

A

A

A

W

C

V

V

K

V

F

L

H

Q

P

P

G

G

H

K

V

H

A

L

N

T

E

E

L

K

E

E

L

V

Q

I

T

D

W

Y

C

V

K

A

G

S

R

Q

I

V

A

S

H

S

F

A

K

K

T

R

P

L

K

R

-

G

H

G

F

V

K

R

F

F

V

V

E

D

E

E

F

I

P

P

M

K

T

G

V

S

T

T

G

G

K
|
K

I

I

Q

D

K

R

F

K

R

A

M

L

R

R

E

Q

I

I

binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (4S)-2-(6-oxidanyl-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylate: H243 (= H239), G244 (≠ C240), F245 (= F241), T249 (≠ G246), L284 (≠ Y282), S312 (≠ M310), G313 (≠ A311), G314 (= G312), A315 (= A313), P316 (≠ T314), Q336 (≠ I334), G337 (≠ A335), Y338 (= Y336), G339 (= G337), L340 (≠ M338), T341 (= T339), S345 (≠ P343), A346 (≠ V344), T360 (≠ V361), D420 (= D420), I432 (= I432), R435 (= R435), K527 (= K526)
binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: R216 (vs. gap), F245 (= F241), T249 (≠ G246), L284 (≠ Y282), S312 (≠ M310), G313 (≠ A311), G314 (= G312), R335 (≠ Q333), G337 (≠ A335), G339 (= G337), L340 (≠ M338), T341 (= T339), S345 (≠ P343), A346 (≠ V344)

6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
29% identity, 93% coverage: 28:535/544 of query aligns to 29:536/538 of 6k4cA

query
sites
6k4cA

R

K

T

K

V

Y

A

A

Q

Q

F

L

P

P

D

G

G

T

E

I

A

A

L

L

V

T

V

D

R

A

H

H

Q

T

Q

E

R

E

R

N

Y

I

T

S

W

Y

R

A

Q

E

L

L

A

L

E

E

T

L

V

T

D

C

L

R

H

L

A

A

R

E

A

S

F

L

L

K

A

N

L

Y

G

G

M

L

Q

K

T

Q

G

N

D

N

R

T

L

I

G

A

I

V

W

C

A

S

P

E

N

N

C

N

A

L

E

Q

W

F

C

F

I

I

S

P

Q

V

I

I

A

A

S

A

A

L

K

Y

L

I

G

G

V

V

I

A

L

V

V

A

N

P

I

V

N

N

P

D

A

K

Y

Y

R

T

S

E

S

R

E

E

L

L

E

I

Y

N

V

S

L

L

K

N

Q

I

S

S

G

K

C

P

Q

T

W

I

L

I

V

F

C

C

A

-

G

-

S

S

F

K

K

K

T

T

S

L

D

Q

Y

K

H

I

A

L

M

Q

L

V

Q

K

A

K

L

K

N

L

P

S

D

Y

L

I

R

K

G

K

M

I

I

I

S

I

L

L

D

D

P

S

S

K

P

E

P

D

-

I

P

G

G

G

F

Y

L

Q

P

C

W

L

A

N

Q

N

L

F

A

I

A

S

L

Q

G

H

T

S

G

D

I

A

P

N

L

F

E

N

Q

V

L

S

H

N

S

F

R

K

Q

P

T

N

S

S

L

F

H

D

F

R

D

D

Q

E

A

Q

V

V

N

A

-

L

I

I

Q

M

Y

N

T

S

S

S

G

G

T

T

G

G

F

L

P

P

K

K

G

G

A

V

T

M

L

L

S

T

H

H

H

K

N

N

-

L

-

V

-

R

-

F

-

S

-

H

-

C

-

R

-

D

-

P

I

I

L

F

N

G

N

N

G

Q

Y

I

M

I

V

P

G

G

E

T

S

A

L

I

G

-

L

L

T

T

A

V

Q

-

D

-

R

-

L

-

V

-

I

-

P

-

V

I

P

P

L

F

Y

H

H
|
H

C

G

F
|
F

G

G

M

M

V

-

M

F

G
x
T

N

T

L

L

G

G

C

Y

I

F

T

T

H

C

G

G

T

F

T

R

M

I

I

V

Y

L

P

M

N

H

D

R

G

-

F

F

D

E

P

E

L

E

L

L

T

F

L

L

T

K

A

S

V

L

A

Q

E

D

E

Y

H

K

A

V

T

Q

G

S

L

T

Y

L

G

L

V

V

P

P

T

T

M

L

F

M

I

A

A

F

M

F

L

A

D

K

H

S

P

P

Q

L

L

V

G

D

G

K

F

Y

D

D

L

L

S

S

S

N

L

L

R

K

T

E

G

I

I

A

M

S

A
x
G

G
|
G

A
|
A

T
x
P

C

L

P

S

I

K

E

E

V

V

M

G

R

E

R

A

V

V

I

A

S

K

E

R

M

F

H

K

M

L

S

P

E

G

V

I

Q
x
R

I

Q

A
x
G

Y
|
Y

G
|
G

M
x
L

T
|
T

E

E

T

T

S

T

P
x
S

V
x
A

S

I

L

I

Q

I

T

T

G

P

A

E

D

G

D

D

D

-

L

-

E

-

R

V

R

K

V

P

T

G

T

S

V

T

G

G

R

K

T

V

Q

V

P

P

Q

F

L

F

E

S

N

A

K

K

I

V

D

D

A

L

D

D

-

T

G

G

N

K

T

T

V

L

A

G

R

P

G

N

E

Q

I

R

G

G

E

E

L

L

C

C

T

F

R

K

G

G

Y

D

S

M

V

I

M

M

L

K

G

G

Y

Y

W

V

N

N

P

P

D

E

A

A

T

T

R

K

E

E

A

I

I

I

D

D

D

K

A

D

G

G

W

W

M

L

H

H

T

S

G

G

D
|
D

L

I

A

G

S

Y

M

Y

D

D

A

E

H

D

G

G

Y

H

V

F

C

F

I
|
I

A

V

G

D

R
|
R

N

L

K

K

D

S

M

L

I

I

I

K

R

Y

G

K

G

G

E

Y

N

Q

V

V

Y

A

P

P

R

A

E

E

L

L

E

E

E

S

F

I

F

L

T

Q

H

H

P

P

A

S

V

I

A

I

D

D

V

A

Q

G

V

V

I

T

G

G

I

I

P

P

D

D

E

E

R

D

Y

A

G

G

E

E

A

L

I

P

V

A

A

A

W

C

V

V

K

V

F

L

H

Q

P

P

G

G

H

K

V

H

A

L

N

T

E

E

L

K

E

E

L

V

Q

I

T

D

W

Y

C

V

K

A

G

S

R

Q

I

V

A

S

H

S

F

A

K

K

T

R

P

L

K

R

-

G

H

G

F

V

K

R

F

F

V

V

E

D

E

E

F

I

P

P

M

K

T

G

V

S

T

T

G

G

K
|
K

I

I

Q

D

K

R

F

K

R

A

M

L

R

R

E

Q

I

I

binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H239), F245 (= F241), T249 (≠ G246), G313 (≠ A311), G314 (= G312), A315 (= A313), P316 (≠ T314), R335 (≠ Q333), G337 (≠ A335), Y338 (= Y336), G339 (= G337), L340 (≠ M338), T341 (= T339), S345 (≠ P343), A346 (≠ V344), D420 (= D420), I432 (= I432), R435 (= R435), K527 (= K526)

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)
26% identity, 91% coverage: 49:541/544 of query aligns to 59:545/546 of Q84P21

query
sites
Q84P21

T

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K530 (= K526) mutation to N: Lossed enzymatic activity.

2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
29% identity, 90% coverage: 48:535/544 of query aligns to 47:534/539 of 2d1sA

query
sites
2d1sA

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