ID A0A3N8LAY0_9BURK Unreviewed; 792 AA.
AC A0A3N8LAY0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=DID96_13065 {ECO:0000313|EMBL:RQS71644.1};
OS Burkholderia sp. Bp8963.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=2184547 {ECO:0000313|EMBL:RQS71644.1, ECO:0000313|Proteomes:UP000274808};
RN [1] {ECO:0000313|EMBL:RQS71644.1, ECO:0000313|Proteomes:UP000274808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp8963 {ECO:0000313|EMBL:RQS71644.1,
RC ECO:0000313|Proteomes:UP000274808};
RA Hall C., Sahl J., Wagner D.;
RT "Comparative analysis of Burkholderia isolates from Puerto Rico.";
RL Submitted (AUG-2018) 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}.
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:RQS71644.1}.
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DR EMBL; QTQP01000012; RQS71644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N8LAY0; -.
DR OrthoDB; 5807460at2; -.
DR Proteomes; UP000274808; 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 Reference proteome {ECO:0000313|Proteomes:UP000274808};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 80..301
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 382..436
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 495..711
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
SQ SEQUENCE 792 AA; 90195 MW; 21B21125D7D0C28B CRC64;
MTEFEQGFIL TRHWRDTAAG VEIEFWLATG HGPRRVRLRP QEAVAFVPVE QREAAERELA
GESGAELRPL ALRDFRQRPV VGLYCRRYRH LSALQKRLAR AGVDVYEADV QPPERYMMER
FITAPVRFRG VPDGDGVLCD GELKPDASYR PALRCVSLDI ETSAHGELYS IAVEGCGQRQ
VFMLGPANGD ARDVDFAFDY CDSRATLLAR LNDWFEQHDP DVIIGWNLIQ FDLRVLHAHA
HAEQYRVPLR LGRGGSVLDW RAHGQQPDHF FAAAAGRLVI DGIDALKSAT WTFPSFSLEY
VAQALLGEGK SIDNPYQRMD EIQRRFDHDK PALARYNLKD CELVTRIFEK ADLLSFMLER
ATVTGLAADR TGGSVAAFTH LYLPRMHRLG YVAPNVGDVT GQTSPGGFVM DSRPGLYDSV
LVFDYKSLYP SIIRTFLIDP AGLIEGLADP GDDASVPGFL GARFSRTRHC LPDIVRRVWD
SRELAKRERN APLSQALKII MNAFYGVLGS TGCRFFDPRL ASSITMRGHE IMHRTRELIE
SQGYEVIYGD TDSTFVWLKE PHSDDDAARI GRALVEHVNR WWKTHLQQCF GLDSALELQY
ERHYHRFLMP TVRGTDEGSK KRYAGLAVAP DGREDVVFKG LETVRTDWTP LAQQFQRELY
RRVFKREPYQ DFIRDYVRRT LAGELDDLLV YRKRVRRPLG EYQRNVPPHV RAARIADAFN
DTHGRPLQYQ RGGWISYMMT TAGPEPLETM RSPIDYAFYV SRQLQPVADA ILPFVRDDFE
SVVSGQGRLF QG
//