SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_010876500.1 NCBI__GCF_000008645.1:WP_010876500.1 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 6 hits to proteins with known functional sites (download)

Q8YMD9 Bifunctional arginine dihydrolase/ornithine cyclodeaminase AgrE; Arginine-guanidine removing enzyme; EC 3.5.3.27; EC 4.3.1.12 from Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) (see paper)
43% identity, 99% coverage: 1:407/411 of query aligns to 283:695/703 of Q8YMD9

query
sites
Q8YMD9

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N524 (= N236) binding NAD(+)
A525 (= A237) binding NAD(+)
D603 (= D315) binding NAD(+)
S635 (≠ T347) binding NAD(+)
M636 (= M348) binding NAD(+)
L637 (= L349) binding NAD(+)
H638 (= H350) binding NAD(+)
D656 (= D368) binding NAD(+)
D679 (= D391) binding NAD(+)
V680 (= V392) binding NAD(+)

Sites not aligning to the query:

22 binding L-arginine; binding L-ornithine; N→A: Loss of arginine dihydrolase activity.
65 binding L-arginine; D→A: Shows residual arginine dihydrolase activity.
71 binding L-arginine; mutation N->A,D: Shows residual arginine dihydrolase activity.
90 binding L-arginine; binding L-ornithine; R→A: Loss of arginine dihydrolase activity.
118 E→A: Loss of arginine dihydrolase activity.
122 mutation D->A,N: Loss of arginine dihydrolase activity.
139 binding L-arginine; binding L-ornithine; R→A: Shows residual arginine dihydrolase activity.
167 Y→F: Retains 9% of arginine dihydrolase activity.
168 binding L-ornithine; H→A: Loss of arginine dihydrolase activity.
170 binding L-arginine; mutation D->A,N: Loss of arginine dihydrolase activity.
219 N→A: Loss of arginine dihydrolase activity.
258 binding L-arginine
264 binding L-ornithine; C→A: Loss of arginine dihydrolase activity.

P74535 Bifunctional arginine dihydrolase/ornithine cyclodeaminase ArgZ; EC 3.5.3.27; EC 4.3.1.12 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
42% identity, 99% coverage: 1:407/411 of query aligns to 283:696/705 of P74535

query
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P74535

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Sites not aligning to the query:

22 binding L-arginine; binding L-ornithine; N→A: Significant loss of arginine dihydrolase activity.
65 D→A: Significant loss of arginine dihydrolase activity.
68 F→A: Significant loss of arginine dihydrolase activity.
71 binding L-arginine; binding L-ornithine; N→D: Produces equal trace amounts of citrulline and ornithine.; N→S: Transforms the enzyme from a dihydrolase to a deiminase.
90 binding L-arginine; binding L-ornithine; R→A: Significant loss of arginine dihydrolase activity.
118 E→A: Complete loss of arginine dihydrolase activity.
139 binding L-arginine; binding L-ornithine; R→A: Significant loss of arginine dihydrolase activity.
167 Y→A: Significant loss of arginine dihydrolase activity.
168 binding L-arginine; binding L-ornithine; H→F: Complete loss of arginine dihydrolase activity.
170 binding L-arginine
258 binding L-arginine; binding L-ornithine
264 binding covalent; binding L-ornithine; C→S: Complete loss of arginine dihydrolase activity.

6lrgB Crystal structure of the ternary complex of agre with ornithine and NAD+ (see paper)
42% identity, 99% coverage: 1:407/411 of query aligns to 280:681/681 of 6lrgB

query
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6lrgB

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D

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I

N

N

P

P

A

A

T

V

V

V

T

T

K

K

L

L

S

S

D

D

R

R

G

G

S

S

S

I

Q

E

A

S

V

V

S

G

V

V

T

T

D

D

V

V

G

G

A

L

F

F

I

L

P

S

I

L

L

L

L

T

H

Q

E

Q

I

L

K

D

K

K

M

L

N

T

Sites not aligning to the query:

binding L-ornithine: 18, 62, 65, 68, 87, 136, 164, 165, 255, 261

6lrgA Crystal structure of the ternary complex of agre with ornithine and NAD+ (see paper)
42% identity, 99% coverage: 1:407/411 of query aligns to 282:675/678 of 6lrgA

query
sites
6lrgA

M

V

N

E

T

S

R

R

E

I

V

I

E

R

L

I

R

E

G

G

H

H

I

L

D

D

S

S

L

G

I

L

L

I

P

N

R

R

A

A

L

L

D

D

I

M

I

I

M

V

D

D

M

T

G

G

D

S

F

F

Q

Q

I

V

L

L

E

N

I

F

D

N

I

L

G

G

K

E

R

Q

K

R

S

Q

D

S

P

T

S

S

H

A

A

A

R

E

I

V

L

K

V

V

E

S

A

A

E

P

T

S

P

H

S

E

L

V

L

M

N

E

Q

E

I

I

L

I

D

S

E

L

L

L

G

I

E

D

I

L

G

G

A

A

S

V

I

D

A

L

E

P

I

Q

K

D

E

E

A

R

E

D

L

A

R

K

R

L

A

E

P

P

M

V

-

I

-

Q

D

D

R

G

V

V

L

A

P

P

D

D

F

F

Y

Y

S

V

T

S

T

T

N

I

H

Y

Q

P

T

T

F

E

I

V

Y

R

H

I

G

N

G

G

E

Q

W

W

V

I

E

K

V

V

E

E

G

N

I

Q

E

R

M

M

D

D

C

G

M

A

I

I

V

A

V

I

D

T

-

Q

-

T

P

P

E

N

S

G

R

L

T

L

A

A

R

Q

C

C

K

K

P

I

I

L

R

R

E

D

I

L

K

K

K

A

G

G

D

E

L

Q

V

V

V

I

V

V

G

D

R

V

E

L

G

G

I

I

K

R

V

T

V

I

P

-

E

-

R

-

P

-

R

-

G

-

K

-

Q

-

G

-

V

-

F

-

E

-

F

-

M

-

G

-

S

-

E

R

V

V

S

S

E

E

K

R

P

R

L

V

V

E

T

L

T

V

I

V

K

E

K

Q

I

V

A

A

S

W

E

E

I

L

T

R

E

K

I

I

K

R

K

D

R

A

G

G

R

K

I

V

G

V

L

V

V

T

G

A

G

G

P
|
P

A
x
V

I

V

V

I

H

H

T

T

G

G

S

G

A

G

P

E

V

H

I

L

A

S

E

R

M

L

I

I

R

R

L

E

G

G

F

Y

I

V

D

Q

V

A

L

L

F

L

A

G

G
|
G

N
|
N

A
|
A

L

I

A

A

T

V

H

H

D

D

I

I

E

E

C

Q

A

N

L

M

Y

M

G

G

T

T

S

S

L

L

G

G

V

V

D

D

I

M

D

K

R

R

G

G

E

V

A

A

V

V

S

R

R

G

G

G

H

H

R

R

H

H

H
|
H

I

L

N

K

A

V

I

I

N

N

E

T

I

I

N

R

R

R

A

H

G

G

S

S

I

I

R

A

D

K

A

G

V

V

E

E

Q

S

G

G

V

I

L

I

T

R

S

S

G

G

I

V

M

M

Y

Y

E

E

C

C

V

V

K

R

N

N

D

Q

V

I

P

P

F

F

V

V

L

L

A

A

G

G

S
|
S

I

I

R
|
R

D
|
D

G

G

P

P

L

L

P

P

D

D

V

T

I

Q

T

M

D

D

V

L

M

I

E

K

A

A

Q

Q

N

E

E

E

M

Y

R

A

K

K

Y

H

V

L

Q

E

D

G

L

A

D

E

M

M

V

I

I

L

M

M

I

L

A
x
S

T
x
S

M
|
M

L

L

H
|
H

S

S

I

I

A

G

T

V

G

G

N

N

I

M

L

T

P

P

S

A

R

G

V

V

K

K

T

M

I

V

C

C

V

V

D
|
D

I
|
I

N

N

P

P

A

A

T

V

V

V

T

T

K

K

L

L

S

S

D

D

R

R

G

G

S

S

S

I

Q

E

A

S

V

V

S

G

V

V

T

T

D
|
D

V
|
V

G

G

A

L

F

F

I

L

P

S

I

L

L

L

L

T

H

Q

E

Q

I

L

K

D

K

K

M

L

N

T

binding nicotinamide-adenine-dinucleotide: P477 (= P209), V478 (≠ A210), G503 (= G235), N504 (= N236), A505 (= A237), H537 (= H269), S579 (= S311), R581 (= R313), D582 (= D314), D583 (= D315), S614 (≠ A346), S615 (≠ T347), M616 (= M348), H618 (= H350), D636 (= D368), I637 (= I369), D659 (= D391), V660 (= V392)

Sites not aligning to the query:

binding L-ornithine: 20, 64, 67, 70, 89, 138, 166, 167, 263

6lrhA Crystal structure of the binary complex of agre c264a mutant with l- arginine (see paper)
42% identity, 99% coverage: 1:407/411 of query aligns to 282:673/675 of 6lrhA

query
sites
6lrhA

M

V

N

E

T

S

R

R

E

I

V

I

E

R

L

I

R

E

G

G

H

H

I

L

D

D

S

S

L

G

I

L

L

I

P

N

R

R

A

A

L

L

D

D

I

M

I

I

M

V

D

D

M

T

G

G

D

S

F

F

Q

Q

I

V

L

L

E

N

I

F

D

N

I

L

G

G

K

E

R

Q

K

R

S

Q

D

S

P

T

S

S

H

A

A

A

R

E

I

V

L

K

V

V

E

S

A

A

E

P

T

S

P

H

S

E

L

V

L

M

N

E

Q

E

I

I

L

I

D

S

E

L

L

L

G

I

E

D

I

L

G

G

A

A

S

V

I

D

A

L

E

P

I

Q

K

D

E

E

A

R

E

D

L

A

R

K

R

L

A

E

P

P

M

V

-

I

-

Q

D

D

R

G

V

V

L

A

P

P

D

D

F

F

Y

Y

S

V

T

S

T

T

N

I

H

Y

Q

P

T

T

F

E

I

V

Y

R

H

I

G

N

G

G

E

Q

W

W

V

I

E

K

V

V

E

E

G

N

I

Q

E

R

M

M

D

D

C

G

M

A

I

I

V

A

V

I

D

T

-

Q

-

T

P

P

E

N

S

G

R

L

T

L

A

A

R

Q

C

C

K

K

P

I

I

L

R

R

E

D

I

L

K

K

K

A

G

G

D

E

L

Q

V

V

V

I

V

V

G

D

R

V

E

L

G

G

I

I

K

R

V

T

V

I

P

-

E

-

R

-

P

-

R

-

G

-

K

-

Q

-

G

-

V

-

F

-

E

-

F

-

M

-

G

-

S

-

E

R

V

V

S

S

E

E

K

R

P

R

L

V

V

E

T

L

T

V

I

V

K

E

K

Q

I

V

A

A

S

W

E

E

I

L

T

R

E

K

I

I

K

R

K

D

R

A

G

G

R

K

I

V

G

V

L

V

V

T

G

A

G

G

P

P

A

V

I

V

V

I

H

H

T

T

G

G

S

G

A

G

P

E

V

H

I

L

A

S

E

R

M

L

I

I

R

R

L

E

G

G

F

Y

I

V

D

Q

V

A

L

L

F

L

A

G

G

G

N

N

A

A

L

I

A

A

T

V

H

H

D

D

I

I

E

E

C

Q

A

N

L

M

Y

M

G

G

T

T

S

S

L

L

G

G

V

V

D

D

I

M

D

K

R

R

G

G

E

V

A

A

V

V

S

R

R

G

G

G

H

H

R

R

H

H

I

L

N

K

A

V

I

I

N

N

E

T

I

I

N

R

R

R

A

H

G

G

S

S

I

I

R

A

D

K

A

G

V

V

E

E

Q

S

G

G

V

I

L

I

T

R

S

S

G

G

I

V

M

M

Y

Y

E

E

C

C

V

V

K

R

N

N

D

Q

V

I

P

P

F

F

V

V

L

L

A

A

G

G

S

S

I

I

R

R

D

D

G

G

P

P

L

L

P

P

D

D

V

T

I

Q

T

M

D

D

V

L

M

I

E

K

A

A

Q

Q

N

E

E

E

M

Y

R

A

K

K

Y

H

V

L

Q

E

D

G

L

A

D

E

M

M

V

I

I

L

M

M

I

L

A

S

T

S

M

M

L

L

H

H

S

S

I

I

A

G

T

V

G

G

N

N

I

M

L

T

P

P

S

A

R

G

V

V

K

K

T

M

I

V

C

C

V

V

D

D

I

I

N

N

P

P

A

A

T

-

V

-

T

T

K

K

L

L

S

S

D

D

R

R

G

G

S

S

S

I

Q

E

A

S

V

V

S

G

V

V

T

T

D

D

V

V

G

G

A

L

F

F

I

L

P

S

I

L

L

L

L

T

H

Q

E

Q

I

L

K

D

K

K

M

L

N

T

Sites not aligning to the query:

binding arginine: 20, 64, 67, 70, 89, 138, 166, 167, 169, 257, 263

Q9SMZ4 Alpha-aminoadipic semialdehyde synthase; cAt-LKR/SDH; LKR/SDH; EC 1.5.1.8; EC 1.5.1.9 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 16% coverage: 6:72/411 of query aligns to 482:548/1064 of Q9SMZ4

query
sites
Q9SMZ4

V

V

E

S

L

L

R

S

G

G

H

H

I

L

I

F

D

D

S

K

L

F

I

L

L

I

P

N

R

E

A

A

L

L

D

D

I

M

I

I

M

E

D

A

M

A

G

G

D

S

F

F

Q

H

I

L

L

A

E

K

I

C

D

E

I

L

G

G

K

Q

R

S

K

A

S

D

D

A

P

E

S

S

H

Y

A

S

R

E

I

L

L

E

V

V

E

G

A

A

E

D

T

D

P

K

S

R

L

V

L

L

N

D

Q

Q

I

I

L

I

D

D

E

S

L

L

G

T

E

R

I

L

G

A

Sites not aligning to the query:

238 modified: Phosphothreonine; mutation T->A,D: No effect on LKR and SDH activity.
407 S→A: No effect on LKR and SDH activity.; S→D: No LKR activity, but no effect on SDH activity.
458 modified: Phosphoserine; S→A: Reduced LKR activity, but no effect on SDH activity.; S→D: No effect on LKR and SDH activity.
551:554 NEDY→IEGR: Loss of LKR activity stimulation by NaCl.

Query Sequence

>WP_010876500.1 NCBI__GCF_000008645.1:WP_010876500.1
MNTREVELRGHIIDSLILPRALDIIMDMGGDFQILEIDIGKRKSDPSHARILVEAETPSL
LNQILDELGEIGASIAEIKEAELRRAPMDRVLPDDFYSTTNHQTFIYHGGEWVEVEGIEM
DCMIVVDPESRTARCKPIREIKKGDLVVVGREGIKVVPPERPRGKQGVFEFMGSEVSSEK
PLVTTIKKIASEITEIKKRGGRIGLVGGPAIVHTGSAPVIAEMIRLGFIDVLFAGNALAT
HDIECALYGTSLGVDIDRGEAVSRGHRHHINAINEINRAGSIRDAVEQGVLTSGIMYECV
KNDVPFVLAGSIRDDGPLPDVITDVMEAQNEMRKYVQDLDMVIMIATMLHSIATGNILPS
RVKTICVDINPATVTKLSDRGSSQAVSVVTDVGAFIPILLHEIKKMNGLGD

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