Arth_2004 protein (Arthrobacter sp. FB24) - STRING interaction network

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Arth_2004

PFAM: 5'-3' exonuclease; SMART: Helix-hairpin-helix domain protein, class 2; KEGG: sco:SCO1622 putative 5'-3' exonuclease. (312 aa)

Predicted Functional Partners:

Arth_2753

0.952

Arth_0002

0.931

recA

0.893

Arth_4083

0.880

Arth_3798

0.868

Arth_0294

0.850

Arth_2573

0.850

Arth_1467

0.814

Arth_0672

0.800

Arth_1254

0.798

Your Current Organism:

Arthrobacter sp. FB24

NCBI taxonomy Id: 290399
Other names: A. sp. FB24

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Arth_0002	Arth_0294	Arth_0002	Arth_0294	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 [...]	Bifunctional non-homologous end joining protein LigD; PFAM: ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: mbo:Mb0963 DNA ligase.	0.928
Arth_0002	Arth_0672	Arth_0002	Arth_0672	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: ATP-dependent DNA helicase, RecQ family; PFAM: helicase domain protein; DEAD/DEAH box helicase domain protein; KEGG: pac:PPA0921 ATP-dependent DNA helicase.	0.716
Arth_0002	Arth_1254	Arth_0002	Arth_1254	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: rpd:RPD_3941 hypothetical protein.	0.437
Arth_0002	Arth_1467	Arth_0002	Arth_1467	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 [...]	SMART: helicase c2; DEAD/DEAH box helicase domain protein; KEGG: sma:SAV2464 putative ATP-dependent helicase.	0.821
Arth_0002	Arth_2004	Arth_0002	Arth_2004	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: 5'-3' exonuclease; SMART: Helix-hairpin-helix domain protein, class 2; KEGG: sco:SCO1622 putative 5'-3' exonuclease.	0.931
Arth_0002	Arth_2573	Arth_0002	Arth_2573	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: SMC domain protein; KEGG: sma:SAV7056 putative exonuclease.	0.558
Arth_0002	Arth_2753	Arth_0002	Arth_2753	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 [...]	ATP-dependent DNA helicase, Rep family; PFAM: UvrD/REP helicase; HRDC domain protein; KEGG: sco:SCO5188 putative ATP-dependent DNA helicase.	0.987
Arth_0002	Arth_3798	Arth_0002	Arth_3798	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: SNF2-related protein; helicase domain protein; zinc finger, SWIM domain protein; SMART: DEAD/DEAH box helicase domain protein; KEGG: fra:Francci3_2408 SNF2-related.	0.902
Arth_0002	Arth_4083	Arth_0002	Arth_4083	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: ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: mpa:MAP0341 putative DNA ligase.	0.927
Arth_0002	recA	Arth_0002	Arth_1460	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 [...]	recA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.	0.920
Arth_0294	Arth_0002	Arth_0294	Arth_0002	Bifunctional non-homologous end joining protein LigD; PFAM: ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: mbo:Mb0963 DNA ligase.	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 [...]	0.928
Arth_0294	Arth_1254	Arth_0294	Arth_1254	Bifunctional non-homologous end joining protein LigD; PFAM: ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: mbo:Mb0963 DNA ligase.	KEGG: rpd:RPD_3941 hypothetical protein.	0.541
Arth_0294	Arth_1467	Arth_0294	Arth_1467	Bifunctional non-homologous end joining protein LigD; PFAM: ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: mbo:Mb0963 DNA ligase.	SMART: helicase c2; DEAD/DEAH box helicase domain protein; KEGG: sma:SAV2464 putative ATP-dependent helicase.	0.632
Arth_0294	Arth_2004	Arth_0294	Arth_2004	Bifunctional non-homologous end joining protein LigD; PFAM: ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: mbo:Mb0963 DNA ligase.	PFAM: 5'-3' exonuclease; SMART: Helix-hairpin-helix domain protein, class 2; KEGG: sco:SCO1622 putative 5'-3' exonuclease.	0.850
Arth_0294	Arth_2573	Arth_0294	Arth_2573	Bifunctional non-homologous end joining protein LigD; PFAM: ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: mbo:Mb0963 DNA ligase.	PFAM: SMC domain protein; KEGG: sma:SAV7056 putative exonuclease.	0.747
Arth_0294	Arth_2753	Arth_0294	Arth_2753	Bifunctional non-homologous end joining protein LigD; PFAM: ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: mbo:Mb0963 DNA ligase.	ATP-dependent DNA helicase, Rep family; PFAM: UvrD/REP helicase; HRDC domain protein; KEGG: sco:SCO5188 putative ATP-dependent DNA helicase.	0.435
Arth_0294	Arth_3798	Arth_0294	Arth_3798	Bifunctional non-homologous end joining protein LigD; PFAM: ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: mbo:Mb0963 DNA ligase.	PFAM: SNF2-related protein; helicase domain protein; zinc finger, SWIM domain protein; SMART: DEAD/DEAH box helicase domain protein; KEGG: fra:Francci3_2408 SNF2-related.	0.614
Arth_0294	Arth_4083	Arth_0294	Arth_4083	Bifunctional non-homologous end joining protein LigD; PFAM: ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: mbo:Mb0963 DNA ligase.	PFAM: ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: mpa:MAP0341 putative DNA ligase.	0.407
Arth_0294	recA	Arth_0294	Arth_1460	Bifunctional non-homologous end joining protein LigD; PFAM: ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: mbo:Mb0963 DNA ligase.	recA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.	0.543
Arth_0672	Arth_0002	Arth_0672	Arth_0002	TIGRFAM: ATP-dependent DNA helicase, RecQ family; PFAM: helicase domain protein; DEAD/DEAH box helicase domain protein; KEGG: pac:PPA0921 ATP-dependent DNA helicase.	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 [...]	0.716