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Database: UniProt
Entry: A0A2N5GAH4_9BACI
LinkDB: A0A2N5GAH4_9BACI
Original site: A0A2N5GAH4_9BACI 
ID   A0A2N5GAH4_9BACI        Unreviewed;       571 AA.
AC   A0A2N5GAH4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, 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=CU633_08790 {ECO:0000313|EMBL:PLR77748.1};
OS   Bacillus sp. V3-13.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2053728 {ECO:0000313|EMBL:PLR77748.1, ECO:0000313|Proteomes:UP000234805};
RN   [1] {ECO:0000313|EMBL:PLR77748.1, ECO:0000313|Proteomes:UP000234805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V3-13 {ECO:0000313|EMBL:PLR77748.1,
RC   ECO:0000313|Proteomes:UP000234805};
RA   Seuylemezian A., Cooper K., Vaishampayan P.;
RT   "Comparitive Functional Genomics of Dry Heat Resistant strains isolated
RT   from the Viking Spacecraft.";
RL   Submitted (NOV-2017) 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:PLR77748.1}.
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DR   EMBL; PGUZ01000022; PLR77748.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5GAH4; -.
DR   OrthoDB; 9808747at2; -.
DR   Proteomes; UP000234805; 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.
DR   SUPFAM; SSF158702; Sec63 N-terminal 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:PLR77748.1};
KW   Hydrolase {ECO:0000313|EMBL:PLR77748.1};
KW   Nuclease {ECO:0000313|EMBL:PLR77748.1};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234805};
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   571 AA;  63928 MW;  AD94CF69C40E7A0F CRC64;
     MSVNKKDVVR LLETIAIYLE LKGENPFKVV AFRKAANALE MDDRSLSEFE DLTKLSGIGK
     GTAAVIEEYI ETGNSTVLRE LQEEVPPGLI PLLQLPGLGG KKIAKLHQEL GIEDVSDLLE
     ACMAGKVKGL AGFGKKTEEK IIAAIKNAGT RPERLPVAYM LEIAESIEAE VSKMDGVVKF
     SRAGSLRRLR ETIKDLDFII ATENPLQVKN QLLELPNIKE TIAAGETKVS VTFEYSYEVS
     ADFRLVKPEE FATALHHFTG SKDHNVRMRQ LAKERGEKIS EYGVEVIETG EVLTFDTEHD
     FYKHFGLPFF PPEIREDGRE VDEYSGELDL IMLDAINGDL HMHSTWSDGA HTIEEMIEAC
     RRRGYKYMAI TDHSQYLKIA SGLTPERLRK QKELIKQLND RYDDIEILAG VEMDILPDGS
     LDYDDELLAE MDIVIASIHS AFSQPKEKIM ARLKTALENP HVDIIAHPTG RVIGRREGYE
     VDMDMLIKLA KETNTALELN ANPNRLDLAA ENIRKAHEAG VKIVINTDAH KLDTLVDMEI
     GVAAARKGWT PKSSVLNALS TEELLDFLHR R
//
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