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Database: UniProt
Entry: A0A1X7L9K6_9BURK
LinkDB: A0A1X7L9K6_9BURK
Original site: A0A1X7L9K6_9BURK 
ID   A0A1X7L9K6_9BURK        Unreviewed;       794 AA.
AC   A0A1X7L9K6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=SAMN06265784_105291 {ECO:0000313|EMBL:SMG50501.1};
OS   Paraburkholderia susongensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1515439 {ECO:0000313|EMBL:SMG50501.1, ECO:0000313|Proteomes:UP000193228};
RN   [1] {ECO:0000313|Proteomes:UP000193228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29540 {ECO:0000313|Proteomes:UP000193228};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-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         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; FXAT01000005; SMG50501.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7L9K6; -.
DR   STRING; 1515439.SAMN06265784_105291; -.
DR   OrthoDB; 5807460at2; -.
DR   Proteomes; UP000193228; Unassembled WGS sequence.
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; 6.10.140.1130; -; 1.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          76..305
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          387..769
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
SQ   SEQUENCE   794 AA;  90890 MW;  581E5EF37090AF75 CRC64;
     MTEFEQGFIL TRHWRDTPAG TEIEFWLATD SGPRHIRLRP QPSVAFIPAE HRERAETILR
     DEKQYDLRPL ELCDFQHRPV MGLYCPQYRQ LKSFEKRLKQ GDVDVYEADI QPHERYMMER
     FITAPVWFSG EPQQKGPLSN GELKPASGYR PPLKLVSLDI ETSAHAELYS IALEGCGERQ
     VYMLGPPNGV DGGDGDGSSL DFKLEYCETR AQLLEKLIEW MERHDPDAII GWNLVQFDLK
     VLQQHSEQYR VPLRIGRGGA VMEWREHSVT RNHFFAGAAG RLIIDGIEAL RSATWSFPSF
     SLEYVSRSVL GEGKAIDNPY QRMDEIQRRF DEAKPELARY NLKDCELVTR IFAKTELLPF
     LLERANVTGL PADRSGGSVA AFTHLYMPRM HRQGYVAPNL GDVAGAASPG GFVMDSRPGL
     YDSVLVLDYK SLYPSIIRTF LIDPLGLVEG MLHPDDEHSV PGFLGARFSR TRHCLPSVVA
     QVWQARETAK REHDKPLSQA LKIIMNAFYG VLGSTGCRFF DPRLASSITM RGHEIMHTTR
     ELIEAQGYEV IYGDTDSTFV WLKHAHSEDD AARVGRALVE HINAAWRQKL QERFGLDSAL
     ELQFERHYRR FFMPTVRGAE EGSKKRYAGL IMLPDGSEEV VYKGLETVRT DWTPLAQQFQ
     QGLYLRIFRQ QPYQDYVRDY VSDTLAGRLD DQLVYRKQLR RPLAAYERNV PPHVRAARVA
     DEFNRAQGRP LQYQNGGWIS YVMTIAGPEP LETLRSAIDY EHYLTRQLQP VADAILPLLR
     DDFTTLMSGQ RQLF
//
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