ID A0A0G1XRI2_9BACT Unreviewed; 717 AA.
AC A0A0G1XRI2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=UY30_C0013G0002 {ECO:0000313|EMBL:KKU96935.1};
OS Parcubacteria group bacterium GW2011_GWB1_48_6.
OC Bacteria.
OX NCBI_TaxID=1618881 {ECO:0000313|EMBL:KKU96935.1, ECO:0000313|Proteomes:UP000034815};
RN [1] {ECO:0000313|EMBL:KKU96935.1, ECO:0000313|Proteomes:UP000034815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKU96935.1}.
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DR EMBL; LCPM01000013; KKU96935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1XRI2; -.
DR PATRIC; fig|1618881.3.peg.209; -.
DR Proteomes; UP000034815; Unassembled WGS sequence.
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; 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; 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 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.
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|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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 2..271
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
SQ SEQUENCE 717 AA; 79551 MW; 3C31603D75AD5667 CRC64;
MKRLILIDGN ALVHRAFHAL PPNMTAPDGT PTNAIFGFAS ILLKAIKDFK PDYMAAAFDL
AGPTFRHEEF AEYKAHREKA PDTLYEQMEV VKKLLANFGV PVFTQSGYEA DDLIGSLAGQ
ARKLKDLETI ILTGDLDTLQ LVDDAKVKVF TARKGLSDTI LYDQAAVEKR FGLKPEQVAD
FKGLKGDPSD NIPGVPGVGD KTATSLLQAY GTIEKVYTAI EKKNFKPNPV VSAKLLEKLK
HYKDQALFSK KLATIVCDMK LDFSLSQANW QANFNEVAVL ELFRSLGFGS LVTRLSGLGL
AKAASLAGRQ AQPALFAPSE AETAKVYNNR AGPEFKRSLE AVGRLYLLQV SGGVLVTTDG
KSVALISEKD FAQWREIFSD PKIAKHGYYL REVYKSLAER GIILRGIEFD IKLAAYLVKP
DLRDFSLANI FAWQDRSVGQ ANGQEFLPDE ERLLLALPAL ADKLGEQLKE LKLMKVFQEI
ELPLIRVLAE MERQGVKIDL PAIKELSIAV EKEVKDLEKK IYQLAGMEFN INSSQQLGQV
LFERLNINVK VRKTGGGVKS TAASELEKMR EAHPIVELIL RYREVEKLKN TYIDPFPQLV
DPKDGRLHTT FNQVGAVTGR LSSQDPNLQN IPIRSELGGQ FRRAFVAAPG FKLISLDYSQ
IELRIVAHFS QDEKMLGAFK RGEDIHTRTA AEIFDVRPDQ VSPRAARSGQ PQYAAGG
//
