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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//