AEB85388.1 protein (Alicycliphilus denitrificans)

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AEB85388.1

KEGG: dia:Dtpsy_2251 DNA ligase; PFAM: DNA ligase, ATP-dependent, central. (304 aa)

Predicted Functional Partners:

polA

0.949

AEB82442.1

0.939

AEB85415.1

0.829

AEB83015.1

0.775

AEB85536.1

0.744

AEB83834.1

0.600

AEB82551.1

0.579

AEB85387.1

0.578

AEB82989.1

0.561

AEB85659.1

0.561

Your Current Organism:

Alicycliphilus denitrificans

NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
AEB82442.1	AEB82551.1	Alide2_0002	Alide2_0113	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 helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain.	0.865
AEB82442.1	AEB82989.1	Alide2_0002	Alide2_0573	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 [...]	Metallophosphoesterase; PFAM: Metallo-dependent phosphatase; KEGG: dia:Dtpsy_0522 metallophosphoesterase.	0.464
AEB82442.1	AEB83834.1	Alide2_0002	Alide2_1434	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: Exodeoxyribonuclease III xth; AP endonuclease, family 1; KEGG: dia:Dtpsy_1114 exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase.	0.878
AEB82442.1	AEB85388.1	Alide2_0002	Alide2_3041	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: dia:Dtpsy_2251 DNA ligase; PFAM: DNA ligase, ATP-dependent, central.	0.939
AEB82442.1	AEB85415.1	Alide2_0002	Alide2_3069	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: vap:Vapar_6015 DNA polymerase II; PFAM: DNA-directed DNA polymerase, family B, conserved region; DNA-directed DNA polymerase, family B, exonuclease domain; SMART: DNA-directed DNA polymerase, family B.	0.947
AEB82442.1	AEB85536.1	Alide2_0002	Alide2_3195	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: ajs:Ajs_1718 DNA-directed DNA polymerase.	0.997
AEB82442.1	AEB85659.1	Alide2_0002	Alide2_3318	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 [...]	Metallophosphoesterase; PFAM: Metallo-dependent phosphatase; KEGG: ajs:Ajs_1567 metallophosphoesterase.	0.464
AEB82442.1	polA	Alide2_0002	Alide2_3637	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; Belongs to the DNA polymerase type-A family.	0.974
AEB82551.1	AEB82442.1	Alide2_0113	Alide2_0002	TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain.	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 [...]	0.865
AEB82551.1	AEB82989.1	Alide2_0113	Alide2_0573	TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain.	Metallophosphoesterase; PFAM: Metallo-dependent phosphatase; KEGG: dia:Dtpsy_0522 metallophosphoesterase.	0.874
AEB82551.1	AEB85388.1	Alide2_0113	Alide2_3041	TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain.	KEGG: dia:Dtpsy_2251 DNA ligase; PFAM: DNA ligase, ATP-dependent, central.	0.579
AEB82551.1	AEB85415.1	Alide2_0113	Alide2_3069	TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain.	KEGG: vap:Vapar_6015 DNA polymerase II; PFAM: DNA-directed DNA polymerase, family B, conserved region; DNA-directed DNA polymerase, family B, exonuclease domain; SMART: DNA-directed DNA polymerase, family B.	0.634
AEB82551.1	AEB85536.1	Alide2_0113	Alide2_3195	TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain.	KEGG: ajs:Ajs_1718 DNA-directed DNA polymerase.	0.871
AEB82551.1	AEB85659.1	Alide2_0113	Alide2_3318	TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain.	Metallophosphoesterase; PFAM: Metallo-dependent phosphatase; KEGG: ajs:Ajs_1567 metallophosphoesterase.	0.874
AEB82551.1	polA	Alide2_0113	Alide2_3637	TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain.	DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.	0.951
AEB82989.1	AEB82442.1	Alide2_0573	Alide2_0002	Metallophosphoesterase; PFAM: Metallo-dependent phosphatase; KEGG: dia:Dtpsy_0522 metallophosphoesterase.	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 [...]	0.464
AEB82989.1	AEB82551.1	Alide2_0573	Alide2_0113	Metallophosphoesterase; PFAM: Metallo-dependent phosphatase; KEGG: dia:Dtpsy_0522 metallophosphoesterase.	TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain.	0.874
AEB82989.1	AEB85388.1	Alide2_0573	Alide2_3041	Metallophosphoesterase; PFAM: Metallo-dependent phosphatase; KEGG: dia:Dtpsy_0522 metallophosphoesterase.	KEGG: dia:Dtpsy_2251 DNA ligase; PFAM: DNA ligase, ATP-dependent, central.	0.561
AEB82989.1	AEB85415.1	Alide2_0573	Alide2_3069	Metallophosphoesterase; PFAM: Metallo-dependent phosphatase; KEGG: dia:Dtpsy_0522 metallophosphoesterase.	KEGG: vap:Vapar_6015 DNA polymerase II; PFAM: DNA-directed DNA polymerase, family B, conserved region; DNA-directed DNA polymerase, family B, exonuclease domain; SMART: DNA-directed DNA polymerase, family B.	0.627
AEB82989.1	AEB85536.1	Alide2_0573	Alide2_3195	Metallophosphoesterase; PFAM: Metallo-dependent phosphatase; KEGG: dia:Dtpsy_0522 metallophosphoesterase.	KEGG: ajs:Ajs_1718 DNA-directed DNA polymerase.	0.695

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