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Database: UniProt
Entry: A0A158JPD6_9BURK
LinkDB: A0A158JPD6_9BURK
Original site: A0A158JPD6_9BURK 
ID   A0A158JPD6_9BURK        Unreviewed;       788 AA.
AC   A0A158JPD6;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=AWB68_04022 {ECO:0000313|EMBL:SAL70200.1};
OS   Caballeronia choica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326476 {ECO:0000313|EMBL:SAL70200.1, ECO:0000313|Proteomes:UP000054770};
RN   [1] {ECO:0000313|Proteomes:UP000054770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Peeters C.;
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         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; FCON02000045; SAL70200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158JPD6; -.
DR   OrthoDB; 5807460at2; -.
DR   Proteomes; UP000054770; 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; 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; 2.
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          77..299
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          381..439
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          484..764
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
SQ   SEQUENCE   788 AA;  89491 MW;  E113E4C273505DE6 CRC64;
     MNQAQQGFLL TRHWRDTAAG TEVGFWLATD SGPQRIRLTP QPSVAFIPAA QRERAESIIG
     GARSVELRPL PLCDFQHRPV LGLYCQQYRQ LAGLEKALKE GGIQVYEADI RPPERYLMER
     FITAPVSFSG TPNGDGPLLD AEMRPAPDYR PRLAVVSLDI ETSERGDLYS IALEGCGARQ
     VYMLGSPNGD DAPRDFDLEY VATPAQLLER FIDWIRRHDP DAIIGWNLVQ FDLRVLQKEA
     ERYGVALRLG RDGSLVEWRE HGLKQNHFFV SVAGRLIIDG IEALKSATWS FPSFSLEYVA
     QALLGEGKSI ESPYQRMDEI NRRFAEDKPA LARYNLHDCE LVTKIFAKTE LLTFLLERAT
     VTGLAADRSG GSVAAFTHLY MPRMHRVGFV APNLGDVQLE SSPGGFVMDS KPGLYDSVLV
     LDYKSLYPSI IRTFVIDPVG LVEGMRHPDD RDSVPGFLGA RFSRSRHSLP AIVGQVWEGR
     EAAKRQQNKP LSQALKIIMN SFYGVLGSSG CRFFDPRLAS SITMRGHEIM HRTRELIEGA
     GYQVIYGDTD STFVWLKHAH TEDEAQRIGR TLVERVNGWW REHLQQEYGL ASALELEVDT
     HYRRFLMPTI RGAEQGSKKR YAGLTVDAHG ADEMVYKGLE SVRTDWTPLA QQFQQQLYLR
     IFKREPYQDF VRDYIDRTLA GEFDELLVYR KQLRRRLGDY QRNVPPHVRA ARLADEFNRG
     QNRPLQYQNG GWISYVMTIA GPEPVEAQRA AIDYEHYLTR QLQPVADAIL PFLRDDFASL
     MTGQKELF
//
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