SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_010961416.1 NCBI__GCF_000008325.1:WP_010961416.1 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 8 hits to proteins with known functional sites (download)

P48636 Cytokinin riboside 5'-monophosphate phosphoribohydrolase; AMP nucleosidase; PaLOG; EC 3.2.2.n1; EC 3.2.2.4 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
61% identity, 97% coverage: 1:190/195 of query aligns to 1:190/195 of P48636

query
sites
P48636

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E74 (= E74) binding substrate
M89 (= M89) mutation to A: Almost complete loss of activity.
R92 (= R92) mutation to A: Almost complete loss of activity.
RK 92:93 (= RK 92:93) binding substrate
109:115 (vs. 109:115, 71% identical) binding substrate
T112 (= T112) mutation to A: Almost complete loss of activity.
E114 (= E114) mutation to A: Almost complete loss of activity.
E115 (= E115) mutation to A: Almost complete loss of activity.
E118 (= E118) mutation to A: Retains 8% of wild-type activity.

5zbkA Crystal structure of type-i log from pseudomonas aeruginosa pao1 in complex with amp (see paper)
61% identity, 93% coverage: 3:183/195 of query aligns to 2:182/182 of 5zbkA

query
sites
5zbkA

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binding adenosine monophosphate: A11 (≠ S12), E73 (= E74), M88 (= M89), R91 (= R92), K92 (= K93), G108 (= G109), G110 (= G111), T111 (= T112)

Q5ZC82 Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG; Protein LONELY GUY; EC 3.2.2.n1 from Oryza sativa subsp. japonica (Rice) (see paper)
48% identity, 93% coverage: 3:183/195 of query aligns to 35:215/242 of Q5ZC82

query
sites
Q5ZC82

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G73 (= G41) mutation to D: In LOG-4; decreased activity.

5zblD Crystal structure of type-i log from corynebacterium glutamicum in complex with amp (see paper)
49% identity, 93% coverage: 3:183/195 of query aligns to 2:181/181 of 5zblD

query
sites
5zblD

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binding adenosine monophosphate: S11 (= S12), M47 (= M48), R90 (= R92), K91 (= K93), G107 (= G109), G109 (= G111), T110 (= T112), E112 (= E114), E113 (= E115)

5ajuA Crystal structure of ligand-free phosphoribohydroxylase lonely guy from claviceps purpurea in complex with phosphoribose (see paper)
39% identity, 93% coverage: 5:185/195 of query aligns to 4:207/217 of 5ajuA

query
sites
5ajuA

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binding 5-O-phosphono-beta-D-ribofuranose: S11 (= S12), R108 (= R92), G131 (= G109), Y132 (≠ I110), G133 (= G111), T134 (= T112), E137 (= E115)

7w2iA Crystal structure of log (rv1205) from mycobacterium tuberculosis (see paper)
42% identity, 90% coverage: 5:179/195 of query aligns to 8:181/183 of 7w2iA

query
sites
7w2iA

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binding magnesium ion: D120 (≠ E118), D124 (≠ W122)

O05306 Cytokinin riboside 5'-monophosphate phosphoribohydrolase; Protein LONELY GUY homolog; LOG homolog; EC 3.2.2.n1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
42% identity, 90% coverage: 5:179/195 of query aligns to 12:185/187 of O05306

query
sites
O05306

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W

E

E

R
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R

K

K

A

Q

R

I

M

M

A

E

E

D

L

R

S

S

D

D

G

A

F

F

V

I

A

V

L

L

P

P

G

G

I

V

G

G

T
|
T

F

L

E
x
D

E
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E

L

L

F

F

E

D

A

A

W

W

T

T

W

D

A

G

Q

Y

L

L

G

G

I

T

H

H

H

D

K

K

P

P

C

I

A

V

L

M

L

V

N

D

V

P

A

W

G

G

Y

H

Y

F

D

D

R

G

L

L

V

R

A

A

F

W

L

L

E

N

H

G

A

L

A

D

E

T

G

G

F

Y

M

V

R

S

R

P

L

T

H

A

R

M

S

E

M

R

L

L

L

V

V

V

A

V

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D

Q

N

P

V

E

K

E

D

L

A

L

L

E

R

V

A

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C

A

A

M54 (= M48) mutation to A: Large decrease in catalytic activity.
K74 (≠ Q68) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup); mutation to A: Abrogates pupylation. This mutant accumulates in M.tuberculosis with a functional proteasome system and sensitizes M.tuberculosis to NO. Decrease in catalytic activity.
E80 (= E74) mutation to A: Large decrease in catalytic activity.
R98 (= R92) mutation to A: Loss of catalytic activity.
T118 (= T112) mutation to A: Loss of catalytic activity.
DE 120:121 (≠ EE 114:115) mutation to AA: Loss of catalytic activity.

3sbxA Crystal structure of a putative uncharacterized protein from mycobacterium marinum bound to adenosine 5'-monophosphate amp (see paper)
41% identity, 90% coverage: 5:179/195 of query aligns to 3:176/177 of 3sbxA

query
sites
3sbxA

S

T

V

V

C

A

V

V

Y

Y

C

C

G

A

S

A

V

-

G

P

E

T

R

H

P

P

E

E

Y

L

L

L

G

E

E

L

A

A

R

G

R

A

F

V

G

G

R

A

L

A

L

I

A

A

E

A

R

R

G

G

I

W

R

T

L

L

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V

Y

W

G

G

A

G

S

H

V

V

G

S

L

A

M

M

G

G

A

A

V

V

A

S

D

S

A

A

L

R

A

A

A

H

G

G

E

W

V

T

I

V

G

G

V

V

I

I

P

P

Q

K

A

M

L

L

V

V

A

H

K

R

E
|
E

I

L

A

A

H

D

S

H

G

D

L

A

T

D

E

E

L

L

R

V

V

V

T

T

A

E

S

T

M
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M

H

W

E

E

R
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R

K
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K

A

Q

R

V

M

M

A

E

E

D

L

R

S

A

D

N

G

A

F

F

V

I

A

T

L

L

P

P

G

G

G
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G

I

V

G
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G

T
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T

F

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x
D

E
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E

L

L

F

L

E

D

A

V

W

W

T

T

W

E

A

G

Q

Y

L

L

G

G

I

M

H

H

H

D

K

K

P

S

C

I

A

V

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V

L

L

N

D

V

P

A

W

G

G

Y

H

Y

F

D

D

R

G

L

L

V

R

A

A

F

W

L

L

E

S

H

E

A

L

A

A

A

D

E

T

G

G

F

Y

M

V

R

S

R

R

L

T

H

A

R

M

S

E

M

R

L

L

L

I

V

V

A

V

R

D

Q

N

P

L

E

D

L

A

L

L

E

Q

V

A

F

C

A

A

binding adenosine monophosphate: E71 (= E74), M86 (= M89), R89 (= R92), K90 (= K93), G106 (= G109), G108 (= G111), T109 (= T112), D111 (≠ E114), E112 (= E115)

Query Sequence

>WP_010961416.1 NCBI__GCF_000008325.1:WP_010961416.1
MELKSVCVYCGSSVGERPEYLGEARRFGRLLAERGIRLVYGGASVGLMGAVADAALAAGG
EVIGVIPQALVAKEIAHSGLTELRVTASMHERKARMAELSDGFVALPGGIGTFEELFEAW
TWAQLGIHHKPCALLNVAGYYDRLVAFLEHAAAEGFMRRLHRSMLLVARQPEELLEVFAA
YRPPEVETWVRADES

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