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Database: UniProt
Entry: A0A3N6AEP7_9BACL
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ID   A0A3N6AEP7_9BACL        Unreviewed;       568 AA.
AC   A0A3N6AEP7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
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:RPJ97199.1};
GN   ORFNames=CW357_00570 {ECO:0000313|EMBL:RPJ97199.1};
OS   Rummeliibacillus sp. TYF005.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Rummeliibacillus.
OX   NCBI_TaxID=2058214 {ECO:0000313|EMBL:RPJ97199.1, ECO:0000313|Proteomes:UP000271255};
RN   [1] {ECO:0000313|EMBL:RPJ97199.1, ECO:0000313|Proteomes:UP000271255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TYF005 {ECO:0000313|EMBL:RPJ97199.1,
RC   ECO:0000313|Proteomes:UP000271255};
RA   Fan X., Li M., Cui L., Li Y.;
RT   "Rummeliibacillus sp. strain TYF005.";
RL   Submitted (MAY-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};
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:RPJ97199.1}.
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DR   EMBL; QGPZ01000002; RPJ97199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N6AEP7; -.
DR   Proteomes; UP000271255; 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; 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; 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:RPJ97199.1};
KW   Hydrolase {ECO:0000313|EMBL:RPJ97199.1};
KW   Nuclease {ECO:0000313|EMBL:RPJ97199.1};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271255};
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          49..68
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          89..108
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          124..143
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;  63682 MW;  A265B8E34B6A4D9C CRC64;
     MMNKKIIINT LEKIALYLEL QGVNPFKISA FRKAAAALEA DTRSIDEIED ITAIKGIGKG
     TAAVIHDLLE NGQSEVLLQL ENEVPKGLPP LLKLPGLGGK KIAKLYQELG VDSAESLKEA
     CEDGKVSALS GFGKKTEEKI LKELESFGKR AEFHPVWLLE EVVSGIEEIL EQIPEIQQSS
     VAGSFRRVKE QSKDVDFIIA TSKPEVVKEA LLSKLAVKEI IAAGDTKVSV TLQTEDVNVD
     FRLVSQAEYA TALHHFTGSK EHNVRMRQIA KERGEKISEY GVEQQDGSIL TFNTEKDFFA
     HFDLPFIPPT VRAGTHEFER LDDIPNLVQL SDIKSDLHMH TTWSDGANAV REMGEALIAK
     GYQYAVITDH SQYLKVANGL TPERLIEQRK EIWSFNEKHP DFRLLAGTEM DILPDGSLDF
     EDDVMAELDF VIASIHSSFS QPQEKIMERL HNAMKNPHVD MIAHPTGRVI GQRDGYNPDI
     PQLIAWAKEY GKILELNANP YRLDLCVEHL EMAANAGVPI AINTDAHAIE QLRYMEIGTK
     YAQKAWLKKE NIVNTWSFND FVNFLEKK
//
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