DPO1_MYCLE
ID DPO1_MYCLE Reviewed; 911 AA.
AC P46835;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=DNA polymerase I;
DE Short=POL I;
DE EC=2.7.7.7;
GN Name=polA; OrderedLocusNames=ML1381;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7476188; DOI=10.1111/j.1365-2958.1995.tb02317.x;
RA Fsihi H., Cole S.T.;
RT "The Mycobacterium leprae genome: systematic sequence analysis identifies
RT key catabolic enzymes, ATP-dependent transport systems and a novel polA
RT locus associated with genomic variability.";
RL Mol. Microbiol. 16:909-919(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 3'-5' and 5'-3' exonuclease activity. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- SUBUNIT: Single-chain monomer with multiple functions.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA50927.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z46257; CAA86364.1; -; Genomic_DNA.
DR EMBL; U00021; AAA50927.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL583921; CAC31762.1; -; Genomic_DNA.
DR PIR; S77659; S77659.
DR RefSeq; NP_301982.1; NC_002677.1.
DR RefSeq; WP_049769942.1; NC_002677.1.
DR AlphaFoldDB; P46835; -.
DR SMR; P46835; -.
DR STRING; 272631.ML1381; -.
DR PRIDE; P46835; -.
DR EnsemblBacteria; CAC31762; CAC31762; CAC31762.
DR KEGG; mle:ML1381; -.
DR PATRIC; fig|272631.5.peg.2560; -.
DR Leproma; ML1381; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR HOGENOM; CLU_004675_0_0_11; -.
DR OMA; NRPPMPD; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR CDD; cd09898; H3TH_53EXO; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR020045; DNA_polI_H3TH.
DR InterPro; IPR018320; DNA_polymerase_1.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10133; PTHR10133; 1.
DR Pfam; PF01367; 5_3_exonuc; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00475; 53EXOc; 1.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF47807; SSF47807; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
DR TIGRFAMs; TIGR00593; pola; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Exonuclease; Hydrolase; Nuclease;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..911
FT /note="DNA polymerase I"
FT /id="PRO_0000101246"
FT DOMAIN 186..280
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000255"
FT DOMAIN 320..497
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000255"
SQ SEQUENCE 911 AA; 99792 MW; 12B4EA18B2BC9864 CRC64;
MSAAMTAEVC EDHTKPMLML LDGNSLAFRA FYALPTENFK TRGGLTTNAV YGFTAMLINL
LREEAPTHIA AAFDVSRKTF RSECYAGYKA NRSSIPAEFH GQIDITKEVL GALGITVFAE
AGFEADDLIA TLATQAENEG YRVLVVTGDR DALQLVSNDV TVLYPRKGVS ELTRFTPEAV
IEKYGVTPAQ YPDLAALRGD PSDNLPGIPG VGEKTAAKWI VDYGSLQGLV DNVESVRGKV
GEALRTHLAS VVRNRELTEL VKDVPLVQTS DTLRLQPWDR DRIHRLFDNL EFRVLRDRLF
EALAAAGERV PEVDEGFDVR GGLLESGTVG RWLAKHADDG RRSGLAIVGT HLPHGGDATA
LAVAAADGNG GYIDTAMLTP DDDDALAAWL ADPDNPKALH EAKLAMHDLA GRGWTLGGIT
SDTALAAYLV RPGQRSFTLD DLSLRYLRRE LRAETPEQEQ FSLLDNVDEV DKQAIQTLIL
RARAVVDLAA ALDAELDLID STSLLGEMEL PVQQVLADME KAGIAADLRL LTELQSQFGD
QIRDAAEAAY AVIGKQINLS SPKQLQVVLF EELGMPKTKR TKTGYTTDAD ALQSLFCKTE
HPFLQHLLTH RDVTRLKVTV DGLLNAVAAD GRIHTTFNQT IATTGRLSST EPNLQNIPIR
TNAGRQIRDA FVVGSENNGY TELMTADYSQ IEMRIMAHLS RDEGLIEAFH TGEDLHSFVA
SRAFGIPIED ITPELRRRVK AMSYGLAYGL SAYGLATQLK ISTEEAKLQM EQYFARFGGV
RDYLMDVVEQ ARKDGYTSTV LGRRRYLPEL DSSNRQIREA AERAALNAPI QGSAADIIKV
AMIAVDKSLK QAKLASRMLL QVHDELLFEV AIGEREQIEA MVREQMGSAY PLDVPLEVSV
GFGRSWGAAA H