RMCT_4269 protein (Mycolicibacterium thermoresistibile)

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Score

RMCT_4269

Putative uncharacterized protein. (218 aa)

Predicted Functional Partners:

cobQ

0.774

map-2

0.700

RMCT_4270

0.614

RMCT_4266

0.519

Your Current Organism:

Mycolicibacterium thermoresistibile

NCBI taxonomy Id: 1797
Other names: ATCC 19527, CCUG 28008, CCUG 41353, CIP 105390, DSM 44167, JCM 6362, M. thermoresistibile, Mycobacterium thermoresistibile, NCTC 10409

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
RMCT_4266	RMCT_4269	RMCT_4266	RMCT_4269	Phenylacetic acid degradation-like protein.	Putative uncharacterized protein.	0.519
RMCT_4266	RMCT_4270	RMCT_4266	RMCT_4270	Phenylacetic acid degradation-like protein.	Membrane protein.	0.559
RMCT_4266	cobQ	RMCT_4266	RMCT_4268	Phenylacetic acid degradation-like protein.	Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.	0.567
RMCT_4266	map-2	RMCT_4266	RMCT_4267	Phenylacetic acid degradation-like protein.	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	0.577
RMCT_4269	RMCT_4266	RMCT_4269	RMCT_4266	Putative uncharacterized protein.	Phenylacetic acid degradation-like protein.	0.519
RMCT_4269	RMCT_4270	RMCT_4269	RMCT_4270	Putative uncharacterized protein.	Membrane protein.	0.614
RMCT_4269	cobQ	RMCT_4269	RMCT_4268	Putative uncharacterized protein.	Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.	0.774
RMCT_4269	map-2	RMCT_4269	RMCT_4267	Putative uncharacterized protein.	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	0.700
RMCT_4270	RMCT_4266	RMCT_4270	RMCT_4266	Membrane protein.	Phenylacetic acid degradation-like protein.	0.559
RMCT_4270	RMCT_4269	RMCT_4270	RMCT_4269	Membrane protein.	Putative uncharacterized protein.	0.614
RMCT_4270	cobQ	RMCT_4270	RMCT_4268	Membrane protein.	Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.	0.645
RMCT_4270	map-2	RMCT_4270	RMCT_4267	Membrane protein.	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	0.597
cobQ	RMCT_4266	RMCT_4268	RMCT_4266	Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.	Phenylacetic acid degradation-like protein.	0.567
cobQ	RMCT_4269	RMCT_4268	RMCT_4269	Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.	Putative uncharacterized protein.	0.774
cobQ	RMCT_4270	RMCT_4268	RMCT_4270	Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.	Membrane protein.	0.645
cobQ	map-2	RMCT_4268	RMCT_4267	Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	0.786
map-2	RMCT_4266	RMCT_4267	RMCT_4266	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	Phenylacetic acid degradation-like protein.	0.577
map-2	RMCT_4269	RMCT_4267	RMCT_4269	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	Putative uncharacterized protein.	0.700
map-2	RMCT_4270	RMCT_4267	RMCT_4270	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	Membrane protein.	0.597
map-2	cobQ	RMCT_4267	RMCT_4268	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.	0.786

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