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Database: UniProt
Entry: A0A1Q7AJ48_9CHLR
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ID   A0A1Q7AJ48_9CHLR        Unreviewed;       584 AA.
AC   A0A1Q7AJ48;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   08-NOV-2023, entry version 20.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=AUH94_05395 {ECO:0000313|EMBL:OLB62086.1};
OS   Ktedonobacter sp. 13_2_20CM_2_54_8.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Ktedonobacteraceae; Ktedonobacter.
OX   NCBI_TaxID=1805234 {ECO:0000313|EMBL:OLB62086.1, ECO:0000313|Proteomes:UP000186751};
RN   [1] {ECO:0000313|EMBL:OLB62086.1, ECO:0000313|Proteomes:UP000186751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(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:OLB62086.1}.
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DR   EMBL; MNDO01000339; OLB62086.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7AJ48; -.
DR   Proteomes; UP000186751; 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; 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   InterPro; IPR010994; RuvA_2-like.
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; 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; SSF47781; RuvA domain 2-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          2..324
FT                   /note="DNA-directed DNA polymerase X"
FT                   /evidence="ECO:0000259|SMART:SM00483"
FT   DOMAIN          348..428
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   584 AA;  65091 MW;  1AA87059ECFEC471 CRC64;
     MDKNQIAAIF EEVAVLLALK EDSNPFEGRA YENAARAINA LDGDIEQLVR TGKLKGTPGL
     GSTIIKRIEE LVNTGHLAFY DELRASTPQI KLQMLRIPGV GPKKINVIYD KLHINSIAEL
     EQACREDKIA HLPGFGKKTQ DNIMQGLAFL AQHADRFLYP VAEEEAERIR SALAELPEIV
     RLQVAGSLRR RRETIGDIDM VASVADDAGE KARNRIMDFF TKQPSVEAIT GKGETKSSVV
     LGTGIAMDLR VVKDSQFPAT LHHFTGSKEH HIPLRRRALS MNMTINDYGL FKGKEPNLEP
     VPCKTEADIY AALGMEYVEP ELREDMGEIE AAVHGTLPVL VQESDLRGVL HVHSTWSDGQ
     NTIREIAEEC IARGYQYLGI TDHSKAAAYA GGLTEDRLRL QHEEIDHLNK EFAGDLRILK
     GTECDILKDG VLDYADEVLA ELDFVVASIH SNFNLSQEEQ TRRMLRAISN PYVDIIGHPT
     GRLLLERAGY ALDMEAVIDA AVEHGVCIEI NAHPSRLDMD WRFVKRARDR GMKIPIDPDA
     HVLAGLDVIR YGIGVARKGW LSAGDVLNTM ETEALLDFFR RRRT
//
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