ID A0A1G1WH24_9BACT Unreviewed; 720 AA.
AC A0A1G1WH24;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGY26740.1};
GN ORFNames=A2Z11_00280 {ECO:0000313|EMBL:OGY26740.1};
OS Candidatus Woykebacteria bacterium RBG_16_43_9.
OC Bacteria; Candidatus Woykebacteria.
OX NCBI_TaxID=1802596 {ECO:0000313|EMBL:OGY26740.1, ECO:0000313|Proteomes:UP000176389};
RN [1] {ECO:0000313|EMBL:OGY26740.1, ECO:0000313|Proteomes:UP000176389}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGY26740.1}.
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DR EMBL; MHCS01000011; OGY26740.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1WH24; -.
DR STRING; 1802596.A2Z11_00280; -.
DR Proteomes; UP000176389; 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 2..263
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 474..680
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 720 AA; 80594 MW; DE85C9914E2A9A94 CRC64;
MKKLVLVDGH AVFHRAYHAL PPLTTSKGEL VNAVFGFTSM LLRAIADIKP DYIAVAFDRA
EPTFRHQAYT AYKAQRVAAP EELHEQMPRS KEVLNVLNIP IFELAGYEAD DIIGTLVKQA
TENGIADLET IIVTGDRDTL QLVRPHVKIY TPGKSFSDVV YFDEKIVGEK YKLEPEQLID
FKALAGDPSD NIPGVRGIGD KGATKLLQEF GSVEEIYKNL DKVPEKTRKL LEADPEAAVM
SKKLATIDQN TPIKLDLSKC VLSDYDKEAA VGLFKELEFR SLISKLPGIE QKIASKETKA
AGQTGLFDKE NEEKSGKSNE LDVVLRQMEG WGVLIDQKKL SALSKEINTE VNSLEKKIYK
EVGHEFNLNS PKQLATVLYD ELNLVPDRST RIKTHKSTDE ATLSTLIDAH PVIELILQYR
ELFKLKSTYV DALPSQIGAD GRIHTHYHAD ATRTGRLSSK NPNLQNIPAR GAWGEKIRSA
FVAPKGCVLL SADYNQIELR VMAHMSGDKE LKRVFEEGED IHTQAAAAAF NKKTTQVTKE
DRRIAKIINF GIMYGISPFG LAKQLKIQPS EAKEIIDRYY ERFPAVKEWM GTILAAAYEK
GFVETLGGFK RYVLELRSNN QTVRKLGERI AVNSPIQGTA ADIIKKAMVD LNEELRIKNL
ETKMILQVHD ELVFEVAEKE LKEVALVIKD LMENSFPLSV PLVVELKAGK NWGQMKPLKI
//
