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Database: UniProt
Entry: A0A150MQY9_9BACI
LinkDB: A0A150MQY9_9BACI
Original site: A0A150MQY9_9BACI 
ID   A0A150MQY9_9BACI        Unreviewed;       574 AA.
AC   A0A150MQY9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=B4113_0747 {ECO:0000313|EMBL:KYD26871.1};
OS   Geobacillus sp. B4113_201601.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1586290 {ECO:0000313|EMBL:KYD26871.1, ECO:0000313|Proteomes:UP000075654};
RN   [1] {ECO:0000313|EMBL:KYD26871.1, ECO:0000313|Proteomes:UP000075654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4113_201601 {ECO:0000313|EMBL:KYD26871.1,
RC   ECO:0000313|Proteomes:UP000075654};
RA   Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA   Eijlander R.T., Kuipers O.P.;
RT   "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT   Foods.";
RL   Submitted (JAN-2016) 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:KYD26871.1}.
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DR   EMBL; LQYX01000074; KYD26871.1; -; Genomic_DNA.
DR   RefSeq; WP_033844270.1; NZ_LQYX01000074.1.
DR   AlphaFoldDB; A0A150MQY9; -.
DR   PATRIC; fig|1586290.3.peg.811; -.
DR   OrthoDB; 9808747at2; -.
DR   Proteomes; UP000075654; 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: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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..316
FT                   /note="DNA-directed DNA polymerase X"
FT                   /evidence="ECO:0000259|SMART:SM00483"
FT   DOMAIN          50..69
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          90..109
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          125..144
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          338..417
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   574 AA;  64438 MW;  4C1EA86EFA7D8926 CRC64;
     MSVHKKEVIR LLETIALYME IKGENPFKVT AFRKAANALE TDERSLTEIG DFTAIPGIGK
     STAAIITEFV ETGSSSVLEE LKRDIPETLL ALLTIPGLGG KKIAKLHQEL GIVDMDGLKE
     ACLAGKVRAL PGFGAKTEEK LLMAIEEAGK RPERLPLARV LPISADIERR LAEMDGVIRF
     SRAGSLRRWN ETVKDLDYVI ATARPMEVRE ALLRLPHIHE VIAAGETKVS LLFRYEDEIA
     ADFRLVSEAQ FATALHHFTG SKDHNVRMRQ LAKERGEKIS EYGVEDQTTG KVKTFPNEAA
     FYAHFGLPYI PPELREDGTE VERFSADWPL VRLEDVRGDL HMHSAWSDGA CSLEELAEAC
     RRRGYRYIAI TDHSRYLKVA NGLTPERLRR QREEIERLNA RYSDLTILAG VEMDILPDGT
     LDYDDDVLEE LDFVIAAIHS GFKQPRATIM KRLEAALFHP YVDVIAHPTG RLIGQRAGYD
     VDIERLIELA AETETILELN ANPNRLDLSA AYVKKAEEAG AYIAINTDAH HLDMLDDMAV
     GVATARKGWI KKDTVVNTWP LEKLQQFLRA KRKK
//
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