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Database: UniProt
Entry: A0A0G2ASN0_9BACT
LinkDB: A0A0G2ASN0_9BACT
Original site: A0A0G2ASN0_9BACT 
ID   A0A0G2ASN0_9BACT        Unreviewed;       754 AA.
AC   A0A0G2ASN0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Polymerase protein {ECO:0000313|EMBL:KKW44462.1};
GN   ORFNames=UY94_C0023G0004 {ECO:0000313|EMBL:KKW44462.1};
OS   Parcubacteria group bacterium GW2011_GWA2_56_21.
OC   Bacteria.
OX   NCBI_TaxID=1618859 {ECO:0000313|EMBL:KKW44462.1, ECO:0000313|Proteomes:UP000034417};
RN   [1] {ECO:0000313|EMBL:KKW44462.1, ECO:0000313|Proteomes:UP000034417}
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   -!- 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   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705}.
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:KKW44462.1}.
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DR   EMBL; LCRZ01000023; KKW44462.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2ASN0; -.
DR   PATRIC; fig|1618859.3.peg.271; -.
DR   Proteomes; UP000034417; Unassembled WGS sequence.
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:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR   CDD; cd08637; DNA_pol_A_pol_I_C; 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; 2.
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; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR036397; RNaseH_sf.
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   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          11..240
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          504..712
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   754 AA;  85252 MW;  C983E4CDD52783B2 CRC64;
     MAKTLHSKQK KRIVLLDTHA IIHRAYHALP EFTGPTGAPT GALYGLVAML LKIVAELKPD
     YLAACYDLPK PTIRHEAYAG YKATRVHMLK ANTEVDVIIA SGDMDTLQLV DDERVRVYTL
     KKGINDTILY DEKAVIERFG FPPTLIPDWK GLRGDPSDNI KGVAGIGEKT ATELIMAFGS
     IEKIYAALRK SEKKLVEKGV KARMVALLKE HEEDARFSKS LATIRLDAPI AFSLPTQPWR
     ENIDVPKMLA LCDEFGFRTL RERIKAMFTN KPDAEETIEL MPEEKVDSTR LREAQAMLWL
     ISSEFTNPSI DDLRAFTKER TFDAAYATLE KQIAELGRVR EVYEKIEKPL IPVIARMEQR
     GVLINPAVLK ALAKEYRAEL ERIEKRIHKT AGREFNVSSP KQLGEVLFDE LKIIPERQKK
     TAGGQRSTRE SELEKIRDAH PIVSDILEYR ELKKLLSTYI ETLPPLLDAG NRLHAEFIQT
     GSTTGRMASQ NPNLQNIPLR SERGKAIRNA FIAPKGFSLV ALDYSQIELR LAAILSGDEK
     LCDIFKKGRD VHQEVAAQVF HVAPEAVDYE MRRRAKVINF GILYGMGVNA LRAQLDSTTA
     EAHAFLEEYF STFKTLSEYL ESTRGFARKH GYTETLFGRR RQFPEMKSSL PYVRAQAERM
     AINAPIQGTE ADIIKLAMTR VDEMLAKEKA LADAYLLLQV HDELVYEIRR EREKELGTEI
     QKIMESVLPA TETRGVPIIV TMKSGATWGD MHQT
//
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