DPOL_BPML5
ID DPOL_BPML5 Reviewed; 595 AA.
AC Q05254;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 L5 (Mycobacteriophage L5).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Fromanvirus.
OX NCBI_TaxID=31757;
OH NCBI_TaxID=1763; Mycobacterium.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8459766; DOI=10.1111/j.1365-2958.1993.tb01131.x;
RA Hatfull G.F., Sarkis G.J.;
RT "DNA sequence, structure and gene expression of mycobacteriophage L5: a
RT phage system for mycobacterial genetics.";
RL Mol. Microbiol. 7:395-405(1993).
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; Z18946; CAA79420.1; -; Genomic_DNA.
DR PIR; S30989; S30989.
DR RefSeq; NP_039708.1; NC_001335.1.
DR SMR; Q05254; -.
DR GeneID; 2942951; -.
DR KEGG; vg:2942951; -.
DR Proteomes; UP000002123; 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 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..595
FT /note="DNA polymerase"
FT /id="PRO_0000101264"
FT DOMAIN 1..212
FT /note="3'-5' exonuclease"
FT REGION 213..595
FT /note="Polymerase"
FT /evidence="ECO:0000250"
SQ SEQUENCE 595 AA; 66221 MW; EB4AA7DBFBB4DCC6 CRC64;
MIELRHEVQG DLVTVNVVET PEDLEGFRNF IRAHLNCLAV DTETTGLDIY SDTFECRLVQ
FGTQDEAWVV PVELGDVFIE DVRIAIGALK RMVLQNASFD LQVLDQCFGI EMEGLWPRVL
DTQILAKLVD PRPFEAGGFG HSLEELIAKF ISEDQAENVK KLMAKLAAEH KTTKAKIWST
IDLFHPEYLL YAGMDTIFTA RVCKSLTPLV PDVSRSLVPY EHKISEICSY IDRQGFLLDV
EYSRSLAEKW LADQEVWEAI AFTEYGVEKV NSTEDLAEGL EEMGVKITGR TETGKRQVNA
ALLDKLVEDG NELAAIAQEA KKLGKWRKTW VQKFIDTRDS EDRCHTFINP LQARTSRMSI
TGIPAQTLPS SDWIVRRCFI AEPGDVMASV DYQAQELRVL AALSGDRNMI EAFENGADLH
QMTADAAQVP RKVGKTANFQ KVYGGGAKAL AEAVGISIPV AKRVHEAFSA TYPGVERLSK
KLAMEAGRNG YIVNAMGRRL PVDSSRTYSA LNYMIQSSSR DVTCRALIRL HEAGYTPYLR
LPIHDEIVAS LPASEAERAA AHIGHLMQEQ MGPVLVGTDP EVGKRSWGSL YGADY