DPOL_BPAPS
ID DPOL_BPAPS Reviewed; 993 AA.
AC Q9T1Q3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Probable DNA polymerase;
DE EC=2.7.7.7 {ECO:0000250|UniProtKB:P00581};
DE EC=3.1.11.- {ECO:0000250|UniProtKB:P00581};
DE AltName: Full=P45;
GN Name=45;
OS Acyrthosiphon pisum secondary endosymbiont phage 1 (Bacteriophage APSE-1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Sendosyvirus.
OX NCBI_TaxID=2682836;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10489345; DOI=10.1006/viro.1999.9902;
RA van der Wilk F., Dullemans A.M., Verbeek M., van den Heuvel J.F.J.M.;
RT "Isolation and characterization of APSE-1, a bacteriophage infecting the
RT secondary endosymbiont of acyrthosiphon pisum.";
RL Virology 262:104-113(1999).
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:P00581}.
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:0000250|UniProtKB:P00581};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR EMBL; AF157835; AAF03988.1; -; Genomic_DNA.
DR RefSeq; NP_051006.1; NC_000935.1.
DR GeneID; 1262339; -.
DR KEGG; vg:1262339; -.
DR Proteomes; UP000000853; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR012337; RNaseH-like_sf.
DR Pfam; PF00476; DNA_pol_A; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 2.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-directed DNA polymerase; Hydrolase;
KW Nucleotidyltransferase; Reference proteome; Transferase;
KW Viral DNA replication.
FT CHAIN 1..993
FT /note="Probable DNA polymerase"
FT /id="PRO_0000101262"
SQ SEQUENCE 993 AA; 111764 MW; 82D134031549F04D CRC64;
MQNLLFCDLE TYSDIPINCG THRYAENAEI LLFAYAYNHA PVKVWDVTQD KTMPADLKAY
LDDSEILTVW HNGGMFDTVI LKRVLNIDLP LSRVHDTLVQ ALAHGLPGAL GLLCDIFNVN
SDKAKDKEGK ALISLLCKPR PKNSKIQRAT ALTHAEEWQR FKDYAGSDIL AMREIYQHLP
NWNMNVHETE LWQLDQKINR RGMCMDVELA KSALTAVENE QKRLSTVTQQ LTDNAVQNAT
QRDALLQHIA SAFGITLPDM QASTLQRRIN DPDIPPALRE LLSVRLQSCT TSTSKYKALL
KSVSADGRLR GTKQFCGASR TGRWAGRVFQ PDNLPRPTLD PNTIDNGIEA LKAGCAELIC
DDIMQLTSSA LRGCIIAPPG KKLVISDLSN IEGRMLAWLA GENWKVNAFS EFDNGKGDDL
YKLAYARAFN LLPEDVTKEQ RQIGKVMELG LGYGGGVAAF LTFALAYGLD LDELAEAALP
NIPPGVKREA MRWYQKSVET DKTYGLSEKI FVTCDSLKRM WRNAHPQTVS FWYDIEDAVK
QAIQSPGIAF KCRKLSVRRD KSWLRICLPS GRSLCYPSAR IENGQITYMG TNPYSRKWER
LKTYGGKSCL AKGTLVLTIT GWMPIEIVSQ DAYVWDGIEW VRTDGSVFNG NQEVIQAYGV
GMTADHQVLT EKGWKSASQS KRYNRSSCRL PDGYKLPRFR RKEINLESTL HLWTRNNHSS
NRITKTKKTR YNCLLRMPKG TNNIMQKPKA RNVKTPRFCC MEQHVSQMYS PFPQSMVKLW
WSGNNGLQTL AKKFQQFLGR HGQDIPTRLI FRSHQQQCRL PPQKLPLGYV ASTSSKYSTS
TIRANSPRHN EYTGISSPNR DCSKHALLSP GKKGKSSTTS GAPKHIAEVY DLINCGPRNR
FVIATPDGPL IVHNCENICQ AAARDVLAYN MPPIEKAGYE IVLTVHDEII SEAPDTPQFS
AEGLSKLLSF NSDWAWDLPL SANGFETYRY RKE