MPER_06533 protein (Moniliophthora perniciosa)

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second shell of interactors

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proteins of unknown 3D structure

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Known Interactions

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experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

gene co-occurrence

Others

textmining

co-expression

protein homology

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[Homology]

Score

MPER_06533

Uncharacterized protein. (188 aa)

Predicted Functional Partners:

MPER_03115

0.949

MPER_04531

0.934

MPER_03384

0.800

MPER_08484

0.745

MPER_12722

0.666

MPER_02624

0.580

MPER_02160

0.491

Your Current Organism:

Moniliophthora perniciosa

NCBI taxonomy Id: 554373
Other names: M. perniciosa FA553, Moniliophthora perniciosa FA553

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
MPER_02160	MPER_03115	E2L8A4	E2LAK9	Uncharacterized protein.	Uncharacterized protein.	0.439
MPER_02160	MPER_06533	E2L8A4	E2LIY0	Uncharacterized protein.	Uncharacterized protein.	0.491
MPER_02624	MPER_04531	E2L9E4	E2LE02	Flavodoxin-like domain-containing protein.	MFS domain-containing protein.	0.408
MPER_02624	MPER_06533	E2L9E4	E2LIY0	Flavodoxin-like domain-containing protein.	Uncharacterized protein.	0.580
MPER_03115	MPER_02160	E2LAK9	E2L8A4	Uncharacterized protein.	Uncharacterized protein.	0.439
MPER_03115	MPER_03384	E2LAK9	E2LB79	Uncharacterized protein.	T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	0.654
MPER_03115	MPER_06533	E2LAK9	E2LIY0	Uncharacterized protein.	Uncharacterized protein.	0.949
MPER_03115	MPER_08484	E2LAK9	E2LNS0	Uncharacterized protein.	T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	0.678
MPER_03384	MPER_03115	E2LB79	E2LAK9	T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	Uncharacterized protein.	0.654
MPER_03384	MPER_04531	E2LB79	E2LE02	T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	MFS domain-containing protein.	0.812
MPER_03384	MPER_06533	E2LB79	E2LIY0	T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	Uncharacterized protein.	0.800
MPER_03384	MPER_08484	E2LB79	E2LNS0	T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	0.954
MPER_04531	MPER_02624	E2LE02	E2L9E4	MFS domain-containing protein.	Flavodoxin-like domain-containing protein.	0.408
MPER_04531	MPER_03384	E2LE02	E2LB79	MFS domain-containing protein.	T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	0.812
MPER_04531	MPER_06533	E2LE02	E2LIY0	MFS domain-containing protein.	Uncharacterized protein.	0.934
MPER_04531	MPER_08484	E2LE02	E2LNS0	MFS domain-containing protein.	T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	0.767
MPER_06533	MPER_02160	E2LIY0	E2L8A4	Uncharacterized protein.	Uncharacterized protein.	0.491
MPER_06533	MPER_02624	E2LIY0	E2L9E4	Uncharacterized protein.	Flavodoxin-like domain-containing protein.	0.580
MPER_06533	MPER_03115	E2LIY0	E2LAK9	Uncharacterized protein.	Uncharacterized protein.	0.949
MPER_06533	MPER_03384	E2LIY0	E2LB79	Uncharacterized protein.	T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.	0.800