ECOLI:DPO1

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	polA (synonyms: resA)
Protein Name(s)	DNA polymerase I POL I
External Links
UniProt	P00582
EMBL	V00317 L19201 U00096 AP009048 J01663 J01664
PIR	A92360
RefSeq	NP_418300.1 YP_491586.1
PDB	1D8Y 1D9D 1D9F 1DPI 1KFD 1KFS 1KLN 1KRP 1KSP 1QSL 2KFN 2KFZ 2KZM 2KZZ
PDBsum	1D8Y 1D9D 1D9F 1DPI 1KFD 1KFS 1KLN 1KRP 1KSP 1QSL 2KFN 2KFZ 2KZM 2KZZ
ProteinModelPortal	P00582
SMR	P00582
DIP	DIP-10524N
IntAct	P00582
MINT	MINT-1225247
STRING	511145.b3863
BindingDB	P00582
ChEMBL	CHEMBL4298
DrugBank	DB00548
SWISS-2DPAGE	P00582
PaxDb	P00582
PRIDE	P00582
EnsemblBacteria	AAC76861 BAE77445
GeneID	12933188 948356
KEGG	ecj:Y75_p3322 eco:b3863
PATRIC	32123225
EchoBASE	EB0739
EcoGene	EG10746
eggNOG	COG0258
HOGENOM	HOG000020998
InParanoid	P00582
KO	K02335
OMA	KANRPPM
OrthoDB	EOG6SJJH7
PhylomeDB	P00582
BioCyc	EcoCyc:EG10746-MONOMER ECOL316407:JW3835-MONOMER MetaCyc:EG10746-MONOMER RETL1328306-WGS:GSTH-159-MONOMER
SABIO-RK	P00582
EvolutionaryTrace	P00582
PRO	PR:P00582
Proteomes	UP000000318 UP000000625
Genevestigator	P00582
GO	GO:0005737 GO:0008408 GO:0008409 GO:0003677 GO:0003887 GO:0006284 GO:0071897 GO:0006281 GO:0006260 GO:0006261 GO:0090305
Gene3D	3.30.420.10 3.40.50.1010
InterPro	IPR002562 IPR020046 IPR020045 IPR002421 IPR019760 IPR001098 IPR018320 IPR002298 IPR008918 IPR003583 IPR029060 IPR012337
Pfam	PF01367 PF02739 PF00476 PF01612
PRINTS	PR00868
SMART	SM00474 SM00475 SM00278 SM00279 SM00482
SUPFAM	SSF47807 SSF53098 SSF88723
TIGRFAMs	TIGR00593
PROSITE	PS00447

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
enables	GO:0008409	5'-3' exonuclease activity	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10746 PANTHER:PTN000015249	F	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10746 PANTHER:PTN000015328	P	Seeded From UniProt	complete
involved_in	GO:0006261	DNA-dependent DNA replication	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10746 PANTHER:PTN000015249	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10746 PANTHER:PTN000015249	C	Seeded From UniProt	complete
enables	GO:0003887	DNA-directed DNA polymerase activity	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10746 MGI:MGI:2155399 PANTHER:PTN000015249 UniProtKB:O75417 UniProtKB:P52027 UniProtKB:Q6Z4T5 UniProtKB:Q7Z5Q5	F	Seeded From UniProt	complete
enables	GO:0003887	DNA-directed DNA polymerase activity	PMID:381283^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008409	5'-3' exonuclease activity	PMID:4890763^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008409	5'-3' exonuclease activity	PMID:4552925^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008408	3'-5' exonuclease activity	PMID:4890763^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008408	3'-5' exonuclease activity	PMID:4552924^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	PMID:23630273^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:169227^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006261	DNA-dependent DNA replication	PMID:6262323^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	PMID:4552924^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16858726^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003887	DNA-directed DNA polymerase activity	PMID:13563462^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:4890764^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0071897	DNA biosynthetic process	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003887	P	Seeded From UniProt	complete
involved_in	GO:0071897	DNA biosynthetic process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003887	P	Seeded From UniProt	complete
involved_in	GO:0071897	DNA biosynthetic process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003887	P	Seeded From UniProt	complete
involved_in	GO:0071897	DNA biosynthetic process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003887	P	Seeded From UniProt	complete
involved_in	GO:0071897	DNA biosynthetic process	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003887	P	Seeded From UniProt	complete
involved_in	GO:0071897	DNA biosynthetic process	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003887	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0008408	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008408	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008409	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008409	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008409	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004527	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004518	P	Seeded From UniProt	complete
enables	GO:0003676	nucleic acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002562 InterPro:IPR036397	F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001098 InterPro:IPR002421 InterPro:IPR008918 InterPro:IPR020045 InterPro:IPR020046	F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008918 InterPro:IPR020045	F	Seeded From UniProt	complete
enables	GO:0003887	DNA-directed DNA polymerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001098 InterPro:IPR002298 InterPro:IPR018320 InterPro:IPR019760	F	Seeded From UniProt	complete
involved_in	GO:0006139	nucleobase-containing compound metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002562	P	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001098 InterPro:IPR018320 InterPro:IPR019760	P	Seeded From UniProt	complete
involved_in	GO:0006261	DNA-dependent DNA replication	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002298	P	Seeded From UniProt	complete
enables	GO:0008408	3'-5' exonuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002562	F	Seeded From UniProt	complete
enables	GO:0003887	DNA-directed DNA polymerase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.7.7	F	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
enables	GO:0016779	nucleotidyltransferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0548	F	Seeded From UniProt	complete
enables	GO:0004527	exonuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0269	F	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0540	F	Seeded From UniProt	complete
enables	GO:0003887	DNA-directed DNA polymerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0239	F	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0235	P	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Rhodes, G et al. (1979) A simple and rapid purification method for Escherichia coli DNA polymerase I. J. Biol. Chem. 254 7465-7 PubMed GONUTS page
↑ ^3.0 ^3.1 Deutscher, MP & Kornberg, A (1969) Enzymatic synthesis of deoxyribonucleic acid. XXIX. Hydrolysis of deoxyribonucleic acid from the 5' terminus by an exonuclease function of deoxyribonucleic acid polymerase. J. Biol. Chem. 244 3029-37 PubMed GONUTS page
↑ Setlow, P & Kornberg, A (1972) Deoxyribonucleic acid polymerase: two distinct enzymes in one polypeptide. II. A proteolytic fragment containing the 5' leads to 3' exonuclease function. Restoration of intact enzyme functions from the two proteolytic fragments. J. Biol. Chem. 247 232-40 PubMed GONUTS page
↑ ^5.0 ^5.1 Setlow, P et al. (1972) Deoxyribonucleic acid polymerase: two distinct enzymes in one polypeptide. I. A proteolytic fragment containing the polymerase and 3' leads to 5' exonuclease functions. J. Biol. Chem. 247 224-31 PubMed GONUTS page
↑ Uphoff, S et al. (2013) Single-molecule DNA repair in live bacteria. Proc. Natl. Acad. Sci. U.S.A. 110 8063-8 PubMed GONUTS page
↑ Sharon, R et al. (1975) Two modes of excision repair in toluene-treated Escherichia coli. J. Bacteriol. 123 1107-14 PubMed GONUTS page
↑ Shlomai, J et al. (1981) Replication of phi X174 dna with purified enzymes. I. Conversion of viral DNA to a supercoiled, biologically active duplex. J. Biol. Chem. 256 5233-8 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
↑ LEHMAN, IR et al. (1958) Enzymatic synthesis of deoxyribonucleic acid. I. Preparation of substrates and partial purification of an enzyme from Escherichia coli. J. Biol. Chem. 233 163-70 PubMed GONUTS page
↑ Englund, PT et al. (1969) Enzymatic synthesis of deoxyribonucleic acid. XXXI. Binding of deoxyribonucleic acid to deoxyribonucleic acid polymerase. J. Biol. Chem. 244 3045-52 PubMed GONUTS page

[PMID:21873635-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:381283-2] Rhodes, G et al. (1979) A simple and rapid purification method for Escherichia coli DNA polymerase I. J. Biol. Chem. 254 7465-7 PubMed GONUTS page

[PMID:4890763-3] 3.0 ^3.1 Deutscher, MP & Kornberg, A (1969) Enzymatic synthesis of deoxyribonucleic acid. XXIX. Hydrolysis of deoxyribonucleic acid from the 5' terminus by an exonuclease function of deoxyribonucleic acid polymerase. J. Biol. Chem. 244 3029-37 PubMed GONUTS page

[PMID:4552925-4] Setlow, P & Kornberg, A (1972) Deoxyribonucleic acid polymerase: two distinct enzymes in one polypeptide. II. A proteolytic fragment containing the 5' leads to 3' exonuclease function. Restoration of intact enzyme functions from the two proteolytic fragments. J. Biol. Chem. 247 232-40 PubMed GONUTS page

[PMID:4552924-5] 5.0 ^5.1 Setlow, P et al. (1972) Deoxyribonucleic acid polymerase: two distinct enzymes in one polypeptide. I. A proteolytic fragment containing the polymerase and 3' leads to 5' exonuclease functions. J. Biol. Chem. 247 224-31 PubMed GONUTS page

[PMID:23630273-6] Uphoff, S et al. (2013) Single-molecule DNA repair in live bacteria. Proc. Natl. Acad. Sci. U.S.A. 110 8063-8 PubMed GONUTS page

[PMID:169227-7] Sharon, R et al. (1975) Two modes of excision repair in toluene-treated Escherichia coli. J. Bacteriol. 123 1107-14 PubMed GONUTS page

[PMID:6262323-8] Shlomai, J et al. (1981) Replication of phi X174 dna with purified enzymes. I. Conversion of viral DNA to a supercoiled, biologically active duplex. J. Biol. Chem. 256 5233-8 PubMed GONUTS page

[PMID:18304323-9] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:16858726-10] Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page

[PMID:13563462-11] LEHMAN, IR et al. (1958) Enzymatic synthesis of deoxyribonucleic acid. I. Preparation of substrates and partial purification of an enzyme from Escherichia coli. J. Biol. Chem. 233 163-70 PubMed GONUTS page

[PMID:4890764-12] Englund, PT et al. (1969) Enzymatic synthesis of deoxyribonucleic acid. XXXI. Binding of deoxyribonucleic acid to deoxyribonucleic acid polymerase. J. Biol. Chem. 244 3045-52 PubMed GONUTS page

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ECOLI:DPO1

Contents

Annotations

Notes

References

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