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Database: UniProt
Entry: A0A3P5XLX1_9BACL
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ID   A0A3P5XLX1_9BACL        Unreviewed;       568 AA.
AC   A0A3P5XLX1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   Name=polX {ECO:0000313|EMBL:VDC32706.1};
GN   ORFNames=FILTAD_02880 {ECO:0000313|EMBL:VDC32706.1};
OS   Filibacter tadaridae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Filibacter.
OX   NCBI_TaxID=2483811 {ECO:0000313|EMBL:VDC32706.1, ECO:0000313|Proteomes:UP000270468};
RN   [1] {ECO:0000313|EMBL:VDC32706.1, ECO:0000313|Proteomes:UP000270468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATB-66 {ECO:0000313|EMBL:VDC32706.1};
RA   Criscuolo A.;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; UXAV01000044; VDC32706.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P5XLX1; -.
DR   OrthoDB; 9808747at2; -.
DR   Proteomes; UP000270468; 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:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
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; IPR028207; DNA_pol_B_palm_palm.
DR   InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR   InterPro; IPR037160; DNA_Pol_thumb_sf.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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; PF14792; DNA_pol_B_palm; 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   SMART; SM00278; HhH1; 3.
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.
PE   4: Predicted;
KW   DNA synthesis {ECO:0000256|ARBA:ARBA00022634};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Exonuclease {ECO:0000313|EMBL:VDC32706.1};
KW   Hydrolase {ECO:0000313|EMBL:VDC32706.1};
KW   Nuclease {ECO:0000313|EMBL:VDC32706.1};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000270468};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..313
FT                   /note="DNA-directed DNA polymerase X"
FT                   /evidence="ECO:0000259|SMART:SM00483"
FT   DOMAIN          48..67
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          88..107
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          123..142
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          335..414
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   568 AA;  64102 MW;  CA295F7F7C145297 CRC64;
     MNKKTIIRTF EKIALYMELL GENHFKVSAF RKAANVLELD PRSLSEMDDI LTLKGIGKGT
     GAVITDLLEK GESDLQKELE EEVPKGLIPL LKVPGLGGKR IAKLREAIGI DSVESLRAAC
     AAGEVSKLPG FGKKTEENLL NEIDILGTRQ GKFPIWQMEK VVTFLETELQ KITEIKHFSV
     AGSYRRTKEE SSDVDFIIVT DEPSIVREKL LQSLPLLATI AAGDSKLSVT LDLEEAIDAD
     FRFVKDEQFA SAIHHFTGSK DHNVRMRQLA KSKGMKISEY GVESEDGSII TFETEEQFYA
     HFDLPFIPPS LRMDGREIDR TDEIAGLVDL EDIKGDFHMH TTWSDGAYSI REMVDACRVK
     GYSHLVITDH TQYLKVANGL TPERLRDQIA EIRSLNEEYD DIEIFCGTEM DILPDATLDF
     DDDLLKELDF VIASIHSSFS QSQEQIMERL HSAISNPNVD MIAHPTGRII GQREGYNPDV
     PQLIEWAKEY GKILELNASP YRLDLMTEQL IMAQEAGVHI AINTDAHAID QLKYMKTGVN
     YAKKAWLKKE TVVNTWPLDK FIREIVRK
//
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