Cphy_0002 protein (Lachnoclostridium phytofermentans)

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Cphy_0002

DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] (370 aa)

Predicted Functional Partners:

polA

0.997

dnaX

0.993

Cphy_0335

0.992

Cphy_1729

0.992

Cphy_1962

0.991

Cphy_3913

0.990

dnaA

0.989

Cphy_2148

0.960

dinB

0.960

dinB-2

0.960

Your Current Organism:

Lachnoclostridium phytofermentans

NCBI taxonomy Id: 357809
Other names: Clostridium phytofermentans ISDg, L. phytofermentans ISDg, Lachnoclostridium phytofermentans ISDg

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Cphy_0002	Cphy_0335	Cphy_0002	Cphy_0335	DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]	KEGG: tte:TTE1818 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; DNA polymerase III alpha subunit; SMART: phosphoesterase PHP domain protein.	0.992
Cphy_0002	Cphy_1729	Cphy_0002	Cphy_1729	DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]	TIGRFAM: DNA ligase D; DNA ligase D, 3'-phosphoesterase domain protein; DNA polymerase LigD, polymerase domain protein; DNA polymerase LigD, ligase domain protein; PFAM: mRNA capping enzyme; DNA primase small subunit; ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: dsy:DSY0616 hypothetical protein.	0.992
Cphy_0002	Cphy_1962	Cphy_0002	Cphy_1962	DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]	TIGRFAM: DNA polymerase III, delta subunit; PFAM: DNA polymerase III delta; KEGG: cth:Cthe_1040 DNA polymerase III, delta subunit.	0.991
Cphy_0002	Cphy_2148	Cphy_0002	Cphy_2148	DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]	PFAM: UMUC domain protein DNA-repair protein; KEGG: blo:BL1114 DNA polymerase V.	0.960
Cphy_0002	Cphy_3913	Cphy_0002	Cphy_3913	DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]	TIGRFAM: DNA polymerase III, delta prime subunit; KEGG: amt:Amet_0084 DNA polymerase III, delta prime subunit.	0.990
Cphy_0002	dinB	Cphy_0002	Cphy_2727	DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]	DNA-directed DNA polymerase; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	0.960
Cphy_0002	dinB-2	Cphy_0002	Cphy_3921	DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]	DNA-directed DNA polymerase; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	0.960
Cphy_0002	dnaA	Cphy_0002	Cphy_0001	DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]	Chromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.	0.989
Cphy_0002	dnaX	Cphy_0002	Cphy_0046	DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]	DNA polymerase III, subunits gamma and tau; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.	0.993
Cphy_0002	polA	Cphy_0002	Cphy_2803	DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]	DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.	0.997
Cphy_0335	Cphy_0002	Cphy_0335	Cphy_0002	KEGG: tte:TTE1818 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; DNA polymerase III alpha subunit; SMART: phosphoesterase PHP domain protein.	DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]	0.992
Cphy_0335	Cphy_1962	Cphy_0335	Cphy_1962	KEGG: tte:TTE1818 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; DNA polymerase III alpha subunit; SMART: phosphoesterase PHP domain protein.	TIGRFAM: DNA polymerase III, delta subunit; PFAM: DNA polymerase III delta; KEGG: cth:Cthe_1040 DNA polymerase III, delta subunit.	0.988
Cphy_0335	Cphy_2148	Cphy_0335	Cphy_2148	KEGG: tte:TTE1818 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; DNA polymerase III alpha subunit; SMART: phosphoesterase PHP domain protein.	PFAM: UMUC domain protein DNA-repair protein; KEGG: blo:BL1114 DNA polymerase V.	0.548
Cphy_0335	Cphy_3913	Cphy_0335	Cphy_3913	KEGG: tte:TTE1818 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; DNA polymerase III alpha subunit; SMART: phosphoesterase PHP domain protein.	TIGRFAM: DNA polymerase III, delta prime subunit; KEGG: amt:Amet_0084 DNA polymerase III, delta prime subunit.	0.987
Cphy_0335	dinB	Cphy_0335	Cphy_2727	KEGG: tte:TTE1818 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; DNA polymerase III alpha subunit; SMART: phosphoesterase PHP domain protein.	DNA-directed DNA polymerase; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	0.548
Cphy_0335	dinB-2	Cphy_0335	Cphy_3921	KEGG: tte:TTE1818 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; DNA polymerase III alpha subunit; SMART: phosphoesterase PHP domain protein.	DNA-directed DNA polymerase; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	0.548
Cphy_0335	dnaA	Cphy_0335	Cphy_0001	KEGG: tte:TTE1818 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; DNA polymerase III alpha subunit; SMART: phosphoesterase PHP domain protein.	Chromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.	0.415
Cphy_0335	dnaX	Cphy_0335	Cphy_0046	KEGG: tte:TTE1818 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; DNA polymerase III alpha subunit; SMART: phosphoesterase PHP domain protein.	DNA polymerase III, subunits gamma and tau; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.	0.988
Cphy_0335	polA	Cphy_0335	Cphy_2803	KEGG: tte:TTE1818 DNA polymerase III alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; DNA polymerase III alpha subunit; SMART: phosphoesterase PHP domain protein.	DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.	0.821
Cphy_1729	Cphy_0002	Cphy_1729	Cphy_0002	TIGRFAM: DNA ligase D; DNA ligase D, 3'-phosphoesterase domain protein; DNA polymerase LigD, polymerase domain protein; DNA polymerase LigD, ligase domain protein; PFAM: mRNA capping enzyme; DNA primase small subunit; ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: dsy:DSY0616 hypothetical protein.	DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]	0.992

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