ID A0A1L7D381_9CORY Unreviewed; 872 AA.
AC A0A1L7D381;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA polymerase I {ECO:0000256|RuleBase:RU004460};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU004460};
GN Name=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=CPHO_06550 {ECO:0000313|EMBL:APT92609.1};
OS Corynebacterium phocae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=161895 {ECO:0000313|EMBL:APT92609.1, ECO:0000313|Proteomes:UP000185491};
RN [1] {ECO:0000313|EMBL:APT92609.1, ECO:0000313|Proteomes:UP000185491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M408/89/1 {ECO:0000313|EMBL:APT92609.1,
RC ECO:0000313|Proteomes:UP000185491};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium phocae M408/89/1(T)(=DSM
RT 44612(T)), isolated from the common seal (Phoca vitulina).";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 5'-3' exonuclease activity. {ECO:0000256|RuleBase:RU004460}.
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 Evidence={ECO:0000256|ARBA:ARBA00024632,
CC ECO:0000256|RuleBase:RU004460};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR EMBL; CP009249; APT92609.1; -; Genomic_DNA.
DR RefSeq; WP_075734251.1; NZ_VXKJ01000039.1.
DR AlphaFoldDB; A0A1L7D381; -.
DR STRING; 161895.CPHO_06550; -.
DR KEGG; cpho:CPHO_06550; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000185491; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR CDD; cd06140; DNA_polA_I_Bacillus_like_exo; 1.
DR CDD; cd09898; H3TH_53EXO; 1.
DR CDD; cd09859; PIN_53EXO; 1.
DR Gene3D; 3.30.70.370; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
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 NCBIfam; TIGR00593; pola; 1.
DR PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 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; SM00475; 53EXOc; 1.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004460};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU004460};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU004460};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004460};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU004460};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000185491};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 1..256
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 630..835
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 872 AA; 96194 MW; F7662DF2DBC81C4C CRC64;
MLIDGHSMAF RAFYALPAEN FSTTGGQHTN AVYGFLSMLA NIVGQQRPEY LAVAFDVGRK
TFRTEMFPEY KAQREAAPEP FKGQVELIRE VLETLGITTL SRENFEADDI LATLATQATD
FDTVLVTGDR DYLQLVNDTT TVLYPMKGVS TMHTFTPEAV EEKYGLTPQQ YPDFAALRGD
PSDNLPGIPK VGEKTATKWI KQYGSLDELI ANADKIKGVV GENFRERLDQ VKMNRQLTQM
ITDMDLEVGP EDLDLKGADV TALAAKFDEL EFGPNLRERV LAVIPHDGQE SNTEPASPAL
ELNIAEPGES LAGWLEGKSE VAVYVQGDGQ PGRGDASAMA FVDSEGNAIQ VELPELSAED
DKALAAWWES DAIKFLHGSK AVFHMLAGRG IGLNGVAHDT ELAAYLLRPG QRSYALGDIY
QRHLEKTLGA ADDQLSLLDD CTLVDQASAI MELALSLTQD LMDIESLQLY TDMELPLALV
LARMESTGIA VDMDRLEEQL EVLAGKVQEQ EQAARDLAGD NSLNLHSPKQ LQVVLFETFD
MPKTKKTKTG YSTAAKEIEQ LAVTNPHPFL DHLLAHREYQ KLKSTLEGLI KTVQPDGRIH
TTFNQTAAST GRLSSTDPNL QNIPVRTEAG RKIREAFVVG EGYETLLTAD YSQIEMRVMA
HLSEDPGLIK AYHEGEDLHN YVGSQVFNVP VNEVTPELRR RVKAMSYGLV YGLSAFGLAQ
QLSIPNGEAK QIMEAYFDRF GGVKQYLDDV VVKARKDVYT ATIFGRRRYL PELNSDKRLA
RENAERAALN APIQGTAADI IKVAMIRVDK ALEGFKSRVL LQVHDELVVE VAKGELEQVR
EVIEKEMDSA ISLTVPLEVS VGAGENWDAA AH
//
