DPOL_BPMD2
ID DPOL_BPMD2 Reviewed; 607 AA.
AC O64235;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=DNA polymerase;
DE EC=2.7.7.7;
DE EC=3.1.11.- {ECO:0000250|UniProtKB:P06225};
GN Name=44;
OS Mycobacterium phage D29 (Mycobacteriophage D29).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Fromanvirus.
OX NCBI_TaxID=28369;
OH NCBI_TaxID=1763; Mycobacterium.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9636706; DOI=10.1006/jmbi.1997.1610;
RA Ford M.E., Sarkis G.J., Belanger A.E., Hendrix R.W., Hatfull G.F.;
RT "Genome structure of mycobacteriophage D29: implications for phage
RT evolution.";
RL J. Mol. Biol. 279:143-164(1998).
CC -!- FUNCTION: Replicates viral genomic DNA. This polymerase possesses two
CC enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic
CC activity that degrades single-stranded DNA in the 3'-5' direction.
CC {ECO:0000250|UniProtKB:P06225}.
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 -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR EMBL; AF022214; AAC18485.1; -; Genomic_DNA.
DR PIR; B72805; B72805.
DR RefSeq; NP_046860.1; NC_001900.1.
DR SMR; O64235; -.
DR PRIDE; O64235; -.
DR GeneID; 1261584; -.
DR KEGG; vg:1261584; -.
DR Proteomes; UP000002131; Genome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
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:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10133; PTHR10133; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW Hydrolase; Nuclease; Nucleotidyltransferase; Reference proteome;
KW Transferase; Viral DNA replication.
FT CHAIN 1..607
FT /note="DNA polymerase"
FT /id="PRO_0000101263"
FT DOMAIN 1..213
FT /note="3'-5' exonuclease"
FT REGION 214..607
FT /note="Polymerase"
FT /evidence="ECO:0000250"
SQ SEQUENCE 607 AA; 68184 MW; 4BD15E327B790BFD CRC64;
MIELRHEVQG DLVTINVVEH PEDLDGFRDF IRAHQNCLAV DTETTGLDIY SADFRCRLVQ
FGTQTESWVL PIEDLEMLGR EEVHEALDVL NKIVMQNASY DLQVLDRCFG IKMESLWPKI
LDTQILAKLV DPRPFGAGGF GHSLEELIAE FISKEQAENV KGLMAKLAKE HKTTKAKIWS
TIDLYHPEYL TYAGMDTVFT ARICSALAPL VPDVSRPLVP YEHKISEICS YIDRRGFLLD
VEYSQQLADK WLGEQQVWEA VLLNEYGIEK VNATEDVAEA FEELGHKFTA FTDSGKRKVD
KGFYADMIAA GGEKAHLAEM VQEAKKLGKW RTSWVQTFLD TRDSEDRCHT FVNPLQARTS
RMSITGIPAQ TLPASDWTVR RCFLADPGHV MASIDYQAQE LRVLAALSGD RTMIQAFKDG
ADLHLMTARA AFGDHITKDD PERKYAKTVN FGRVYGGGAN TVAEQTGISI ETAKQVVDGF
DKAYPGVTRY SRKLANEAKR NGYIINPMGR RLPVDRSRTY SALNYQIQST SRDVTCKALI
RLHEAGFTPY LRLPIHDEIV ASLPAEKANW GAREIARLMA EEMGPVLIGT DPEVGKRSWG
SLYGADY