dinB protein (Gillisia limnaea) - STRING interaction network

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dinB

DNA polymerase IV; 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. (349 aa)

Predicted Functional Partners:

EHQ04044.1

0.825

EHQ03888.1

0.816

recA

0.713

EHQ03108.1

0.688

EHQ01984.1

0.663

polA

0.607

EHQ04409.1

0.572

EHQ03669.1

0.568

EHQ04007.1

0.535

EHQ02638.1

0.520

Your Current Organism:

Gillisia limnaea

NCBI taxonomy Id: 865937
Other names: G. limnaea DSM 15749, Gillisia limnaea DSM 15749, Gillisia limnaea R-8282, Gillisia limnaea str. DSM 15749, Gillisia limnaea strain DSM 15749

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
EHQ01984.1	dinB	Gilli_1318	Gilli_2001	KEGG: gfo:GFO_0399 hypothetical protein; SPTR: Putative uncharacterized protein.	DNA polymerase IV; 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.	0.663
EHQ02638.1	dinB	Gilli_2000	Gilli_2001	PFAM: Semialdehyde dehydrogenase, NAD binding domain; InterPro IPR000534; KEGG: cao:Celal_1270 nucleoside-diphosphate-sugar epimerase; PFAM: Semialdehyde dehydrogenase, NAD-binding; SPTR: Nucleoside-diphosphate-sugar epimerase.	DNA polymerase IV; 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.	0.520
EHQ03108.1	EHQ04007.1	Gilli_2483	Gilli_3407	PFAM: PHP domain; Bacterial DNA polymerase III alpha subunit; Exonuclease; TIGRFAM: DNA-directed DNA polymerase III (polc); COGs: COG0587 DNA polymerase III alpha subunit; InterProIPR004805:IPR006055:IPR003141:IPR013520:IPR 004013:IPR011708:IPR004365; KEGG: zpr:ZPR_4431 DNA polymerase III subunit alpha-1; PFAM: Bacterial DNA polymerase III, alpha subunit; PHP, C-terminal; Exonuclease, RNase T/DNA polymerase III; Nucleic acid binding, OB-fold, tRNA/helicase-type; SMART: Exonuclease; Polymerase/histidinol phosphatase, N-terminal; SPTR: DNA polymerase III subunit alpha-1; TIGRFAM: DNA pol [...]	PFAM: PHP domain; Bacterial DNA polymerase III alpha subunit; TIGRFAM: DNA-directed DNA polymerase III (polc); COGs: COG0587 DNA polymerase III alpha subunit; InterPro IPR004805:IPR003141:IPR004013:IPR011708; KEGG: gfo:GFO_3078 DNA polymerase III subunit alpha-2; PFAM: Bacterial DNA polymerase III, alpha subunit; PHP, C-terminal; SMART: Polymerase/histidinol phosphatase, N-terminal; SPTR: DNA polymerase III subunit alpha-2; TIGRFAM: DNA polymerase III, alpha subunit.	0.955
EHQ03108.1	EHQ04044.1	Gilli_2483	Gilli_3445	PFAM: PHP domain; Bacterial DNA polymerase III alpha subunit; Exonuclease; TIGRFAM: DNA-directed DNA polymerase III (polc); COGs: COG0587 DNA polymerase III alpha subunit; InterProIPR004805:IPR006055:IPR003141:IPR013520:IPR 004013:IPR011708:IPR004365; KEGG: zpr:ZPR_4431 DNA polymerase III subunit alpha-1; PFAM: Bacterial DNA polymerase III, alpha subunit; PHP, C-terminal; Exonuclease, RNase T/DNA polymerase III; Nucleic acid binding, OB-fold, tRNA/helicase-type; SMART: Exonuclease; Polymerase/histidinol phosphatase, N-terminal; SPTR: DNA polymerase III subunit alpha-1; TIGRFAM: DNA pol [...]	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 [...]	0.993
EHQ03108.1	dinB	Gilli_2483	Gilli_2001	PFAM: PHP domain; Bacterial DNA polymerase III alpha subunit; Exonuclease; TIGRFAM: DNA-directed DNA polymerase III (polc); COGs: COG0587 DNA polymerase III alpha subunit; InterProIPR004805:IPR006055:IPR003141:IPR013520:IPR 004013:IPR011708:IPR004365; KEGG: zpr:ZPR_4431 DNA polymerase III subunit alpha-1; PFAM: Bacterial DNA polymerase III, alpha subunit; PHP, C-terminal; Exonuclease, RNase T/DNA polymerase III; Nucleic acid binding, OB-fold, tRNA/helicase-type; SMART: Exonuclease; Polymerase/histidinol phosphatase, N-terminal; SPTR: DNA polymerase III subunit alpha-1; TIGRFAM: DNA pol [...]	DNA polymerase IV; 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.	0.688
EHQ03108.1	polA	Gilli_2483	Gilli_2638	PFAM: PHP domain; Bacterial DNA polymerase III alpha subunit; Exonuclease; TIGRFAM: DNA-directed DNA polymerase III (polc); COGs: COG0587 DNA polymerase III alpha subunit; InterProIPR004805:IPR006055:IPR003141:IPR013520:IPR 004013:IPR011708:IPR004365; KEGG: zpr:ZPR_4431 DNA polymerase III subunit alpha-1; PFAM: Bacterial DNA polymerase III, alpha subunit; PHP, C-terminal; Exonuclease, RNase T/DNA polymerase III; Nucleic acid binding, OB-fold, tRNA/helicase-type; SMART: Exonuclease; Polymerase/histidinol phosphatase, N-terminal; SPTR: DNA polymerase III subunit alpha-1; TIGRFAM: DNA pol [...]	DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.	0.719
EHQ03108.1	recA	Gilli_2483	Gilli_2155	PFAM: PHP domain; Bacterial DNA polymerase III alpha subunit; Exonuclease; TIGRFAM: DNA-directed DNA polymerase III (polc); COGs: COG0587 DNA polymerase III alpha subunit; InterProIPR004805:IPR006055:IPR003141:IPR013520:IPR 004013:IPR011708:IPR004365; KEGG: zpr:ZPR_4431 DNA polymerase III subunit alpha-1; PFAM: Bacterial DNA polymerase III, alpha subunit; PHP, C-terminal; Exonuclease, RNase T/DNA polymerase III; Nucleic acid binding, OB-fold, tRNA/helicase-type; SMART: Exonuclease; Polymerase/histidinol phosphatase, N-terminal; SPTR: DNA polymerase III subunit alpha-1; TIGRFAM: DNA pol [...]	Protein recA; 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.	0.630
EHQ03669.1	EHQ04409.1	Gilli_3059	Gilli_0259	PFAM: FKBP-type peptidyl-prolyl cis-trans isomerase; Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; COGs: COG0652 Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family; InterPro IPR002130:IPR001179; KEGG: zpr:ZPR_0846 cyclophilin/FKBP-type peptidyl-prolyl cis-trans isomerase; PFAM: Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; Peptidyl-prolyl cis-trans isomerase, FKBP-type; SPTR: Cyclophilin/FKBP-type peptidyl-prolyl cis-trans isomerase.	PFAM: FKBP-type peptidyl-prolyl cis-trans isomerase; Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; COGs: COG0652 Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family; InterPro IPR002130:IPR001179; KEGG: gfo:GFO_0786 cyclophilin/FKBP-type peptidyl-prolyl cis-trans isomerase; PFAM: Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; Peptidyl-prolyl cis-trans isomerase, FKBP-type; SPTR: Cyclophilin/FKBP-type peptidyl-prolyl cis-trans isomerase.	0.932
EHQ03669.1	dinB	Gilli_3059	Gilli_2001	PFAM: FKBP-type peptidyl-prolyl cis-trans isomerase; Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; COGs: COG0652 Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family; InterPro IPR002130:IPR001179; KEGG: zpr:ZPR_0846 cyclophilin/FKBP-type peptidyl-prolyl cis-trans isomerase; PFAM: Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; Peptidyl-prolyl cis-trans isomerase, FKBP-type; SPTR: Cyclophilin/FKBP-type peptidyl-prolyl cis-trans isomerase.	DNA polymerase IV; 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.	0.568
EHQ03888.1	EHQ04044.1	Gilli_3282	Gilli_3445	KEGG: rbi:RB2501_15324 hypothetical protein; SPTR: Putative uncharacterized 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 [...]	0.946
EHQ03888.1	dinB	Gilli_3282	Gilli_2001	KEGG: rbi:RB2501_15324 hypothetical protein; SPTR: Putative uncharacterized protein.	DNA polymerase IV; 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.	0.816
EHQ03888.1	polA	Gilli_3282	Gilli_2638	KEGG: rbi:RB2501_15324 hypothetical protein; SPTR: Putative uncharacterized protein.	DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.	0.937
EHQ03888.1	recA	Gilli_3282	Gilli_2155	KEGG: rbi:RB2501_15324 hypothetical protein; SPTR: Putative uncharacterized protein.	Protein recA; 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.	0.813
EHQ04007.1	EHQ03108.1	Gilli_3407	Gilli_2483	PFAM: PHP domain; Bacterial DNA polymerase III alpha subunit; TIGRFAM: DNA-directed DNA polymerase III (polc); COGs: COG0587 DNA polymerase III alpha subunit; InterPro IPR004805:IPR003141:IPR004013:IPR011708; KEGG: gfo:GFO_3078 DNA polymerase III subunit alpha-2; PFAM: Bacterial DNA polymerase III, alpha subunit; PHP, C-terminal; SMART: Polymerase/histidinol phosphatase, N-terminal; SPTR: DNA polymerase III subunit alpha-2; TIGRFAM: DNA polymerase III, alpha subunit.	PFAM: PHP domain; Bacterial DNA polymerase III alpha subunit; Exonuclease; TIGRFAM: DNA-directed DNA polymerase III (polc); COGs: COG0587 DNA polymerase III alpha subunit; InterProIPR004805:IPR006055:IPR003141:IPR013520:IPR 004013:IPR011708:IPR004365; KEGG: zpr:ZPR_4431 DNA polymerase III subunit alpha-1; PFAM: Bacterial DNA polymerase III, alpha subunit; PHP, C-terminal; Exonuclease, RNase T/DNA polymerase III; Nucleic acid binding, OB-fold, tRNA/helicase-type; SMART: Exonuclease; Polymerase/histidinol phosphatase, N-terminal; SPTR: DNA polymerase III subunit alpha-1; TIGRFAM: DNA pol [...]	0.955
EHQ04007.1	EHQ04044.1	Gilli_3407	Gilli_3445	PFAM: PHP domain; Bacterial DNA polymerase III alpha subunit; TIGRFAM: DNA-directed DNA polymerase III (polc); COGs: COG0587 DNA polymerase III alpha subunit; InterPro IPR004805:IPR003141:IPR004013:IPR011708; KEGG: gfo:GFO_3078 DNA polymerase III subunit alpha-2; PFAM: Bacterial DNA polymerase III, alpha subunit; PHP, C-terminal; SMART: Polymerase/histidinol phosphatase, N-terminal; SPTR: DNA polymerase III subunit alpha-2; TIGRFAM: DNA polymerase III, alpha subunit.	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 [...]	0.967
EHQ04007.1	dinB	Gilli_3407	Gilli_2001	PFAM: PHP domain; Bacterial DNA polymerase III alpha subunit; TIGRFAM: DNA-directed DNA polymerase III (polc); COGs: COG0587 DNA polymerase III alpha subunit; InterPro IPR004805:IPR003141:IPR004013:IPR011708; KEGG: gfo:GFO_3078 DNA polymerase III subunit alpha-2; PFAM: Bacterial DNA polymerase III, alpha subunit; PHP, C-terminal; SMART: Polymerase/histidinol phosphatase, N-terminal; SPTR: DNA polymerase III subunit alpha-2; TIGRFAM: DNA polymerase III, alpha subunit.	DNA polymerase IV; 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.	0.535
EHQ04007.1	polA	Gilli_3407	Gilli_2638	PFAM: PHP domain; Bacterial DNA polymerase III alpha subunit; TIGRFAM: DNA-directed DNA polymerase III (polc); COGs: COG0587 DNA polymerase III alpha subunit; InterPro IPR004805:IPR003141:IPR004013:IPR011708; KEGG: gfo:GFO_3078 DNA polymerase III subunit alpha-2; PFAM: Bacterial DNA polymerase III, alpha subunit; PHP, C-terminal; SMART: Polymerase/histidinol phosphatase, N-terminal; SPTR: DNA polymerase III subunit alpha-2; TIGRFAM: DNA polymerase III, alpha subunit.	DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.	0.515
EHQ04044.1	EHQ03108.1	Gilli_3445	Gilli_2483	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: PHP domain; Bacterial DNA polymerase III alpha subunit; Exonuclease; TIGRFAM: DNA-directed DNA polymerase III (polc); COGs: COG0587 DNA polymerase III alpha subunit; InterProIPR004805:IPR006055:IPR003141:IPR013520:IPR 004013:IPR011708:IPR004365; KEGG: zpr:ZPR_4431 DNA polymerase III subunit alpha-1; PFAM: Bacterial DNA polymerase III, alpha subunit; PHP, C-terminal; Exonuclease, RNase T/DNA polymerase III; Nucleic acid binding, OB-fold, tRNA/helicase-type; SMART: Exonuclease; Polymerase/histidinol phosphatase, N-terminal; SPTR: DNA polymerase III subunit alpha-1; TIGRFAM: DNA pol [...]	0.993
EHQ04044.1	EHQ03888.1	Gilli_3445	Gilli_3282	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: rbi:RB2501_15324 hypothetical protein; SPTR: Putative uncharacterized protein.	0.946
EHQ04044.1	EHQ04007.1	Gilli_3445	Gilli_3407	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: PHP domain; Bacterial DNA polymerase III alpha subunit; TIGRFAM: DNA-directed DNA polymerase III (polc); COGs: COG0587 DNA polymerase III alpha subunit; InterPro IPR004805:IPR003141:IPR004013:IPR011708; KEGG: gfo:GFO_3078 DNA polymerase III subunit alpha-2; PFAM: Bacterial DNA polymerase III, alpha subunit; PHP, C-terminal; SMART: Polymerase/histidinol phosphatase, N-terminal; SPTR: DNA polymerase III subunit alpha-2; TIGRFAM: DNA polymerase III, alpha subunit.	0.967

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