ID A0A1G1W8J2_9BACT Unreviewed; 575 AA.
AC A0A1G1W8J2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-NOV-2023, entry version 17.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=A2172_04015 {ECO:0000313|EMBL:OGY24003.1};
OS Candidatus Woykebacteria bacterium RBG_13_40_15.
OC Bacteria; Candidatus Woykebacteria.
OX NCBI_TaxID=1802593 {ECO:0000313|EMBL:OGY24003.1, ECO:0000313|Proteomes:UP000176631};
RN [1] {ECO:0000313|EMBL:OGY24003.1, ECO:0000313|Proteomes:UP000176631}
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 -!- 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:OGY24003.1}.
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DR EMBL; MHCP01000016; OGY24003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1W8J2; -.
DR STRING; 1802593.A2172_04015; -.
DR Proteomes; UP000176631; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00141; NT_POLXc; 1.
DR CDD; cd07436; PHP_PolX; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1.
DR Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR InterPro; IPR010996; DNA_pol_b-like_N.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR037160; DNA_Pol_thumb_sf.
DR InterPro; IPR022312; DNA_pol_X.
DR InterPro; IPR002008; DNA_pol_X_beta-like.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR029398; PolB_thumb.
DR InterPro; IPR022311; PolX-like.
DR InterPro; IPR047967; PolX_PHP.
DR PANTHER; PTHR36928; PHOSPHATASE YCDX-RELATED; 1.
DR PANTHER; PTHR36928:SF1; PHOSPHATASE YCDX-RELATED; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF14716; HHH_8; 1.
DR Pfam; PF02811; PHP; 1.
DR PIRSF; PIRSF005047; UCP005047_YshC; 1.
DR PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00870; DNAPOLXBETA.
DR SMART; SM00481; POLIIIAc; 1.
DR SMART; SM00483; POLXc; 1.
DR SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..325
FT /note="DNA-directed DNA polymerase X"
FT /evidence="ECO:0000259|SMART:SM00483"
FT DOMAIN 349..420
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 575 AA; 64688 MW; C09B442EFCD42F7B CRC64;
MEKKFSNKDI AQLLRNVSAA YQVKGGANSF QIRAYDLAAD AVEHASSDAR ALWETGDLDK
IPGVGANIAN YLDELYTTGE VKHFKQVFKQ IPCSMFEFLK ISGIGPKTAY KLADTGVKSI
NHLETKIKDG SLKREGFGEK TLANILEGIE EFRRKSDRIL LPVAWDVASQ VIEYLKKNKD
VTSADPLGSL RRKVATVGDI DISVASKDPK SVVEHFLKFP GKERVVEAGE RTATISVGGG
IRIDLMVQPP ERYGSLLQHF TGSKHHNIHI RKLAREKSLS LSEYGIKKIE QSGKQFSEDT
FIKCQNEQEF YRRLGMSYIE PELREDQGEI EAALSNKLPK LIALEDIKGD LHTHSFWSDG
KDSIADMAKA AMSLGREYIA LTDHSYPSLN YSKRSKEIEQ FNYSQDNIRV ISGLEVNINA
DSTLQIPDNI LAKHDIVFAS VHTSFRQSKD EMTKRIIRAM ESPHVDALAH PTGRLLLERE
GIDVDWEEVF KRVAELGKFI EINSFPNRLD LPDTLVREAK KFGIKFTIDT DSHQVGHLGL
MEYGISVARR GWLEKVDVIN TLPYPKLKDI LGIRD
//
