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Database: UniProt
Entry: A0A0G1YME1_9BACT
LinkDB: A0A0G1YME1_9BACT
Original site: A0A0G1YME1_9BACT 
ID   A0A0G1YME1_9BACT        Unreviewed;       797 AA.
AC   A0A0G1YME1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Polymerase protein {ECO:0000313|EMBL:KKW07534.1};
GN   ORFNames=UY42_C0011G0013 {ECO:0000313|EMBL:KKW07534.1};
OS   Parcubacteria group bacterium GW2011_GWA2_49_16.
OC   Bacteria.
OX   NCBI_TaxID=1618851 {ECO:0000313|EMBL:KKW07534.1, ECO:0000313|Proteomes:UP000034608};
RN   [1] {ECO:0000313|EMBL:KKW07534.1, ECO:0000313|Proteomes:UP000034608}
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:KKW07534.1}.
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DR   EMBL; LCPY01000011; KKW07534.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1YME1; -.
DR   PATRIC; fig|1618851.3.peg.369; -.
DR   Proteomes; UP000034608; 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; 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   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          7..277
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          541..749
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   797 AA;  89174 MW;  9B9ED5CFFC913B7C CRC64;
     MKKKDSQKTL ILLDAHAILH RAYHALPGFT SSTGEPTGAT YGLSTMLMKI IKDLKPDYIA
     GCFDLPQPTF RHEAYEAYKQ GRAKTEDDLV HQIKRARDVF AALAIPSYEL PGFEADDLLA
     TIVEKMKDKK DLRIIIASGD MDTLQLVDDD RVLVYTLKKG INDTILYDEK AVVERFGFVP
     KLLPDYKGLR GDPSDNIIGI KGIGEKTATT LITMFGSVEN MYKKLKKDPE KFRAAGVSPR
     IITLLEEGEE EALFSKTLAT VRRDAPIEFS LPEKEWRENF DLARAETLFA ELEFRALRGR
     LNELNGGANK ATLFPEEEKN ESVIDPTEFK HAQLALWLLN SDLTTPSLED MLHYTKKKNF
     VDAFVALEAE IGKQGLGSVY RDIELPLIPI IEEAQTYGIL VDTKHLKKLS ETYHKTLDEI
     TTRIYTHAGG EFNMNSPKQL GEVLFDKMGL ATKGLKKTEG GARSTRESEL VKLREVHPII
     AEILLYRELQ KLLSTYIDNL PQLTLEDGRL HTTLNQAGTT TGRMSSSNPN LQNIPVRGEM
     GAAIRSAFVA PEGSTLLACD YSQIEMRVLA ALSGDENLFE IFKTGADVHT SVASRVFHVS
     PQDVTAEMRR RAKVINFGIV YGMGVNALKD NLGSTRVEAQ EFYNNYFVTF PKIARYFEDV
     KSRAKKDGFT TTYFGRRRFF AGLKSPIPYI RASAERMAMN APLQGTAADI IKIAMKRAHD
     GLAGAKLLDK AHLLLQIHDE LLYEVEEGVV KKARTIIEDA MEHAVDFPVP ITVSVKEGPR
     WGSMEGVERN GIENVEL
//
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