Acry_2162 protein (Acidiphilium cryptum) - STRING interaction network

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Acry_2162

Carboxypeptidase Taq; Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues. (504 aa)

Predicted Functional Partners:

Acry_2163

0.818

Acry_2164

0.818

ctaB

0.548

Acry_1482

0.416

Acry_2167

0.412

Your Current Organism:

Acidiphilium cryptum

NCBI taxonomy Id: 349163
Other names: A. cryptum JF-5, Acidiphilium cryptum JF-5, Acidiphilium cryptum str. JF-5, Acidiphilium cryptum strain JF-5, Acidiphilum cryptum JF-5

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Acry_1482	Acry_2162	Acry_1482	Acry_2162	TIGRFAM: oligoendopeptidase, pepF/M3 family; PFAM: peptidase M3A and M3B, thimet/oligopeptidase F; Oligopeptidase F.	Carboxypeptidase Taq; Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.	0.416
Acry_2162	Acry_1482	Acry_2162	Acry_1482	Carboxypeptidase Taq; Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.	TIGRFAM: oligoendopeptidase, pepF/M3 family; PFAM: peptidase M3A and M3B, thimet/oligopeptidase F; Oligopeptidase F.	0.416
Acry_2162	Acry_2163	Acry_2162	Acry_2163	Carboxypeptidase Taq; Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.	Conserved hypothetical protein.	0.818
Acry_2162	Acry_2164	Acry_2162	Acry_2164	Carboxypeptidase Taq; Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.	PFAM: cytochrome c oxidase, subunit III.	0.818
Acry_2162	Acry_2167	Acry_2162	Acry_2167	Carboxypeptidase Taq; Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.	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).	0.412
Acry_2162	ctaB	Acry_2162	Acry_2165	Carboxypeptidase Taq; Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.	Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.	0.548
Acry_2163	Acry_2162	Acry_2163	Acry_2162	Conserved hypothetical protein.	Carboxypeptidase Taq; Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.	0.818
Acry_2163	Acry_2164	Acry_2163	Acry_2164	Conserved hypothetical protein.	PFAM: cytochrome c oxidase, subunit III.	0.931
Acry_2163	Acry_2167	Acry_2163	Acry_2167	Conserved hypothetical 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).	0.808
Acry_2163	ctaB	Acry_2163	Acry_2165	Conserved hypothetical protein.	Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.	0.819
Acry_2164	Acry_2162	Acry_2164	Acry_2162	PFAM: cytochrome c oxidase, subunit III.	Carboxypeptidase Taq; Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.	0.818
Acry_2164	Acry_2163	Acry_2164	Acry_2163	PFAM: cytochrome c oxidase, subunit III.	Conserved hypothetical protein.	0.931
Acry_2164	Acry_2167	Acry_2164	Acry_2167	PFAM: cytochrome c oxidase, subunit III.	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).	0.999
Acry_2164	ctaB	Acry_2164	Acry_2165	PFAM: cytochrome c oxidase, subunit III.	Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.	0.996
Acry_2167	Acry_2162	Acry_2167	Acry_2162	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).	Carboxypeptidase Taq; Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.	0.412
Acry_2167	Acry_2163	Acry_2167	Acry_2163	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).	Conserved hypothetical protein.	0.808
Acry_2167	Acry_2164	Acry_2167	Acry_2164	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).	PFAM: cytochrome c oxidase, subunit III.	0.999
Acry_2167	ctaB	Acry_2167	Acry_2165	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).	Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.	0.997
ctaB	Acry_2162	Acry_2165	Acry_2162	Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.	Carboxypeptidase Taq; Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.	0.548
ctaB	Acry_2163	Acry_2165	Acry_2163	Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.	Conserved hypothetical protein.	0.819

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