WL94_30580 protein (Burkholderia cepacia) - STRING interaction network

Nodes:

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second shell of interactors

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Known Interactions

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experimentally determined

Predicted Interactions

gene neighborhood

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textmining

co-expression

protein homology

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[Homology]

Score

WL94_30580

annotation not available (110 aa)

Predicted Functional Partners:

WI67_15935

0.959

WL94_16540

0.776

WI67_11985

0.753

WI67_11995

0.706

DM42_5619

0.546

WL94_04045

0.531

WL94_13805

0.517

aauA

0.499

DM42_5538

0.479

WI67_26090

0.479

Your Current Organism:

Burkholderia cepacia

NCBI taxonomy Id: 292
Other names: ATCC 25416, B. cepacia, Burkholderia cepacia, Burkholderia cepacia genomovar I, CCUG 12691, CCUG 13226, CFBP 2227, CIP 80.24, DSM 7288, ICMP 5796, IFO 14074, JCM 5964, NBRC 14074, NCCB 76047, NCPPB 2993, NCTC 10743, NRRL B-14810, Pseudomonas cepacia, Pseudomonas kingii, Pseudomonas multivorans, strain 717-ICPB 25, strain Ballard 717

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
DM42_5538	WL94_13805	DM42_5538	DM42_2222	annotation not available	Cytochrome c oxidase subunit 2; 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)	0.572
DM42_5538	WL94_30580	DM42_5538	DM42_2021	annotation not available	annotation not available	0.479
DM42_5619	WL94_13805	DM42_5619	DM42_2222	annotation not available	Cytochrome c oxidase subunit 2; 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)	0.713
DM42_5619	WL94_30580	DM42_5619	DM42_2021	annotation not available	annotation not available	0.546
WI67_11985	WI67_11995	DM42_2860	DM42_2858	annotation not available	annotation not available	0.954
WI67_11985	WL94_04045	DM42_2860	DM42_2546	annotation not available	annotation not available	0.717
WI67_11985	WL94_16540	DM42_2860	DM42_2861	annotation not available	annotation not available	0.968
WI67_11985	WL94_30580	DM42_2860	DM42_2021	annotation not available	annotation not available	0.753
WI67_11995	WI67_11985	DM42_2858	DM42_2860	annotation not available	annotation not available	0.954
WI67_11995	WI67_15935	DM42_2858	DM42_2022	annotation not available	annotation not available	0.779
WI67_11995	WL94_16540	DM42_2858	DM42_2861	annotation not available	annotation not available	0.937
WI67_11995	WL94_30580	DM42_2858	DM42_2021	annotation not available	annotation not available	0.706
WI67_15935	WI67_11995	DM42_2022	DM42_2858	annotation not available	annotation not available	0.779
WI67_15935	WL94_04045	DM42_2022	DM42_2546	annotation not available	annotation not available	0.750
WI67_15935	WL94_16540	DM42_2022	DM42_2861	annotation not available	annotation not available	0.528
WI67_15935	WL94_30580	DM42_2022	DM42_2021	annotation not available	annotation not available	0.959
WI67_26090	WL94_13805	DM42_6978	DM42_2222	annotation not available	Cytochrome c oxidase subunit 2; 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)	0.572
WI67_26090	WL94_30580	DM42_6978	DM42_2021	annotation not available	annotation not available	0.479
WL94_04045	WI67_11985	DM42_2546	DM42_2860	annotation not available	annotation not available	0.717
WL94_04045	WI67_15935	DM42_2546	DM42_2022	annotation not available	annotation not available	0.750

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