mcrA protein (Legionella quateirensis) - STRING interaction network

Nodes:

Network nodes represent proteins

splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.

Node Color

colored nodes:
query proteins and first shell of interactors

white nodes:
second shell of interactors

Node Content

empty nodes:
proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

Edges:

Edges represent protein-protein associations

associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.

Known Interactions

from curated databases

experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

gene co-occurrence

Others

textmining

co-expression

protein homology

Your Input:

Neighborhood

Gene Fusion

Cooccurrence

Coexpression

Experiments

Databases

Textmining

[Homology]

Score

mcrA

FAD linked oxidase. (589 aa)

Predicted Functional Partners:

coxB

0.937

plsB

0.811

cycA

0.800

pdhB_1

0.767

Lqua_0342

0.764

etfA

0.758

etfB

0.755

afr

0.737

baeB

0.730

ahlD

0.718

Your Current Organism:

Legionella quateirensis

NCBI taxonomy Id: 45072
Other names: ATCC 49507, CCUG 44899, CIP 105271, L. quateirensis, NCTC 12376

Send network to Cytoscape

Export your current network:

... as a bitmap image:

download

file format is 'PNG': portable network graphic

... as a high-resolution bitmap:

download

same PNG format, but at higher resolution

... as a vector graphic:

download

SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc

... as short tabular text output:

download

TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)

... as tabular text output:

download

TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)

... as an XML summary:

download

structured XML interaction data, according to the 'PSI-MI' data standard

... protein node degrees:

download

node degree of proteins in your network (given the current score cut-off)

... network coordinates:

download

a flat-file format describing the coordinates and colors of nodes in the network

... protein sequences:

download

MFA: multi-fasta format - containing the aminoacid sequences in the network

... protein annotations:

download

a tab-delimited file describing the names, domains and descriptions of proteins in your network

... functional annotations:

download

a tab-delimited file containing all known functional terms of proteins in your network

Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Lqua_0342	afr	Lqua_0342	Lqua_1936	Putative S-isoprenylcysteine methyltransferase.	Oxidoreductase.	0.403
Lqua_0342	baeB	Lqua_0342	Lqua_2024	Putative S-isoprenylcysteine methyltransferase.	Putative glyoxalase II family protein.	0.446
Lqua_0342	coxB	Lqua_0342	Lqua_1762	Putative S-isoprenylcysteine methyltransferase.	Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	0.607
Lqua_0342	cycA	Lqua_0342	Lqua_1763	Putative S-isoprenylcysteine methyltransferase.	Cytochrome c.	0.411
Lqua_0342	mcrA	Lqua_0342	Lqua_1014	Putative S-isoprenylcysteine methyltransferase.	FAD linked oxidase.	0.764
afr	Lqua_0342	Lqua_1936	Lqua_0342	Oxidoreductase.	Putative S-isoprenylcysteine methyltransferase.	0.403
afr	mcrA	Lqua_1936	Lqua_1014	Oxidoreductase.	FAD linked oxidase.	0.737
ahlD	baeB	Lqua_1242	Lqua_2024	Zn-dependent hydrolase GumP.	Putative glyoxalase II family protein.	0.673
ahlD	mcrA	Lqua_1242	Lqua_1014	Zn-dependent hydrolase GumP.	FAD linked oxidase.	0.718
baeB	Lqua_0342	Lqua_2024	Lqua_0342	Putative glyoxalase II family protein.	Putative S-isoprenylcysteine methyltransferase.	0.446
baeB	ahlD	Lqua_2024	Lqua_1242	Putative glyoxalase II family protein.	Zn-dependent hydrolase GumP.	0.673
baeB	coxB	Lqua_2024	Lqua_1762	Putative glyoxalase II family protein.	Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	0.751
baeB	cycA	Lqua_2024	Lqua_1763	Putative glyoxalase II family protein.	Cytochrome c.	0.424
baeB	mcrA	Lqua_2024	Lqua_1014	Putative glyoxalase II family protein.	FAD linked oxidase.	0.730
coxB	Lqua_0342	Lqua_1762	Lqua_0342	Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Putative S-isoprenylcysteine methyltransferase.	0.607
coxB	baeB	Lqua_1762	Lqua_2024	Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Putative glyoxalase II family protein.	0.751
coxB	cycA	Lqua_1762	Lqua_1763	Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Cytochrome c.	0.992
coxB	etfA	Lqua_1762	Lqua_2634	Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Electron transfer flavoprotein subunit alpha.	0.436
coxB	mcrA	Lqua_1762	Lqua_1014	Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	FAD linked oxidase.	0.937
coxB	pdhB_1	Lqua_1762	Lqua_2834	Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	2-oxoisovalerate dehydrogenase, E1 component, alpha and beta fusion.	0.790