ID   A0A0K1JU13_9BURK        Unreviewed;       788 AA.
AC   A0A0K1JU13;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=ACZ75_01960 {ECO:0000313|EMBL:AKU20468.1};
OS   Massilia sp. NR 4-1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1678028 {ECO:0000313|EMBL:AKU20468.1, ECO:0000313|Proteomes:UP000056897};
RN   [1] {ECO:0000313|EMBL:AKU20468.1, ECO:0000313|Proteomes:UP000056897}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NR 4-1 {ECO:0000313|EMBL:AKU20468.1,
RC   ECO:0000313|Proteomes:UP000056897};
RA   Sul W.J.;
RT   "Massilia sp. NR 4-1 isolated from rhizosphere of Torreya nucifera in
RT   national heritage Bijarim forest, volcanic Jeju Island, Korea.";
RL   Submitted (JUN-2015) 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         ECO:0000256|RuleBase:RU000442};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; CP012201; AKU20468.1; -; Genomic_DNA.
DR   RefSeq; WP_050407181.1; NZ_CP012201.1.
DR   AlphaFoldDB; A0A0K1JU13; -.
DR   STRING; 1678028.ACZ75_01960; -.
DR   KEGG; mnr:ACZ75_01960; -.
DR   PATRIC; fig|1678028.3.peg.387; -.
DR   OrthoDB; 5807460at2; -.
DR   Proteomes; UP000056897; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd05784; DNA_polB_II_exo; 1.
DR   CDD; cd05537; POLBc_Pol_II; 1.
DR   Gene3D; 2.40.50.590; -; 2.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 2.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF21474; DNApolII_N; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000056897};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          75..299
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          388..767
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
SQ   SEQUENCE   788 AA;  90036 MW;  7064057361163830 CRC64;
     MVQAQQGFLL TRHWRDTSAG TEVEFWLATD QGPRHVRLPP QTSVAFIPAE QQEAAQALLR
     GERGCELRPL ALSDFQHRPV LGLYCAKYRH LLKLEKRLRQ AGIDVYEADV RPPERYLMER
     FITAPISFEG EAGDDGTIVL QAPLKPSPDY RPALRLVSLD IETSPHGELY SIALEGCGQR
     QVYMLGQRAE NAEEVDFDLE YCSSHAQMLE RLNAWMAQHD PDAIIGWNLV QFDLRVLLRH
     AEQVKVPLLL GRDGGEMEWR EHAHHEHFFA AAAGRLIIDG IEALRSATWN FPSFSLESVA
     QTLLGEGKSI DNPYQRMAEI ERRFHEDKPA LARYNLKDCE LVTRIFAKTE LLSFLLERAS
     MTGLAADRSG GSVAAFEHLY MPMMHRLGHV APNLGDVVGE NSPGGFVMDS RSGLYDSVLV
     LDYKSLYPSI IRTFLIDPVG LVEGMRDPDS AATVPGFRGA RFSRGKHCLP AIVRQIWQGR
     DAAKREKNAP LSQALKIIMN AFYGVLGSSG CRFFDPRLAS SITMRGHEIM HRTRELIEAQ
     GYQVIYGDTD STFVWLKSAR EEAEAEQIGR QLVLHVNGWW GKHLREEFGL ENALELEYEA
     HYRRFLMPTI RGSEEGSKKR YAGLISRADG SDEIVYKGLE TVRTDWTPLA QQFQRDLYER
     IFKGQPYRDY VRDYVERTVS GEFDEMLVYR KRLRRPLEEY QRNVPPHVRA ARIADEFNQR
     QGRPLQYQNG GWIRYVITTA GPEPLETQRS PIDYEHYLSR QLQPVADAIL PFLRDDFSAL
     VSRQRTLF
//