ID   DPOL_BPT5               Reviewed;         855 AA.
AC   P19822; Q38546; Q5DMI1; Q66LU3; Q6QGG5;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   06-JUL-2016, sequence version 3.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=DNA polymerase {ECO:0000255|RuleBase:RU004460};
DE            EC=2.7.7.7 {ECO:0000269|PubMed:773933};
DE            EC=3.1.11.- {ECO:0000269|PubMed:15377656};
GN   ORFNames=T5.122 {ECO:0000312|EMBL:AAS77168.1},
GN   T5p120 {ECO:0000312|EMBL:AAU05259.1};
OS   Escherichia phage T5 (Enterobacteria phage T5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Demerecviridae; Markadamsvirinae; Tequintavirus.
OX   NCBI_TaxID=2695836;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2660138; DOI=10.1073/pnas.86.12.4465;
RA   Leavitt M.C., Ito J.;
RT   "T5 DNA polymerase: structural -- functional relationships to other DNA
RT   polymerases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:4465-4469(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RA   Ksenzenko V.N., Kaliman A.V., Krutilina A.I., Shlyapnikov M.G.;
RT   "Bacteriophage T5 complete genome.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11303-B5;
RX   PubMed=15661140; DOI=10.1016/j.virol.2004.10.049;
RA   Wang J., Jiang Y., Vincent M., Sun Y., Yu H., Wang J., Bao Q., Kong H.,
RA   Hu S.;
RT   "Complete genome sequence of bacteriophage T5.";
RL   Virology 332:45-65(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=St0 deletion mutant;
RX   PubMed=24198424; DOI=10.1128/jvi.02262-13;
RA   Zivanovic Y., Confalonieri F., Ponchon L., Lurz R., Chami M., Flayhan A.,
RA   Renouard M., Huet A., Decottignies P., Davidson A.R., Breyton C.,
RA   Boulanger P.;
RT   "Insights into bacteriophage T5 structure from analysis of its
RT   morphogenesis genes and protein components.";
RL   J. Virol. 88:1162-1174(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-163.
RX   PubMed=1995424; DOI=10.1016/0378-1119(91)90004-u;
RA   Chatterjee D.K., Fujimura R.K., Campbell J.H., Gerard G.F.;
RT   "Cloning and overexpression of the gene encoding bacteriophage T5 DNA
RT   polymerase.";
RL   Gene 97:13-19(1991).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-10, FUNCTION, DOMAIN, AND CATALYTIC ACTIVITY.
RX   PubMed=15377656; DOI=10.1074/jbc.m408428200;
RA   Andraos N., Tabor S., Richardson C.C.;
RT   "The highly processive DNA polymerase of bacteriophage T5. Role of the
RT   unique N and C termini.";
RL   J. Biol. Chem. 279:50609-50618(2004).
RN   [7]
RP   CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=773933; DOI=10.1016/s0021-9258(17)33671-2;
RA   Fujimura R.K., Roop B.C.;
RT   "Characterization of DNA polymerase induced by bacteriophage T5 with DNA
RT   containing single strand breaks.";
RL   J. Biol. Chem. 251:2168-2174(1976).
CC   -!- FUNCTION: Replicates the viral genomic DNA. This polymerase possesses
CC       two enzymatic activities: DNA synthesis (polymerase) and an
CC       exonucleolytic activity that degrades single-stranded DNA in the 3'-5'
CC       direction for proofreading purpose. The DNA synthesis very likely
CC       occurs by strand displacement. {ECO:0000269|PubMed:15377656,
CC       ECO:0000269|PubMed:773933}.
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; Evidence={ECO:0000269|PubMed:773933};
CC   -!- SUBUNIT: Single-chain monomer with multiple functions.
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC       {ECO:0000305|PubMed:15661140}.
CC   -!- DOMAIN: The C-terminus seems to increase the affinity of the DNA for
CC       the polymerase active site, and thus increase processivity and decrease
CC       the accessibility of the DNA to the exonuclease active site.
CC       {ECO:0000269|PubMed:15377656}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA32558.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
CC       Sequence=AAA32561.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAX12050.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR   EMBL; M24354; AAA32561.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AY543070; AAS77168.1; -; Genomic_DNA.
DR   EMBL; AY587007; AAX12050.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AY692264; AAU05259.1; -; Genomic_DNA.
DR   EMBL; M64047; AAA32558.1; ALT_INIT; Genomic_DNA.
DR   PIR; A33923; DJBPT5.
DR   RefSeq; YP_006950.1; NC_005859.1.
DR   SMR; P19822; -.
DR   GeneID; 2777603; -.
DR   KEGG; vg:2777603; -.
DR   Proteomes; UP000002107; Genome.
DR   Proteomes; UP000002141; Genome.
DR   Proteomes; UP000002503; Genome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Direct protein sequencing; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Early protein; Exonuclease; Hydrolase;
KW   Nuclease; Nucleotidyltransferase; Reference proteome; Transferase;
KW   Viral DNA replication.
FT   CHAIN           1..855
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000101267"
FT   DOMAIN          107..332
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000255"
FT   REGION          333..833
FT                   /note="Polymerase"
FT                   /evidence="ECO:0000269|PubMed:15377656"
SQ   SEQUENCE   855 AA;  97589 MW;  86E504E0D612A7CF CRC64;
     MKIAVVDKAL NNTRYDKHFQ LYGEEVDVFH MCNEKLSGRL LKKHITIGTP ENPFDPNDYD
     FVILVGAEPF LYFAGKKGIG DYTGKRVEYN GYANWIASIS PAQLHFKPEM KPVFDATVEN
     IHDIINGREK IAKAGDYRPI TDPDEAEEYI KMVYNMVIGP VAFDSETSAL YCRDGYLLGV
     SISHQEYQGV YIDSDCLTEV AVYYLQKILD SENHTIVFHN LKFDMHFYKY HLGLTFDKAH
     KERRLHDTML QHYVLDERRG THGLKSLAMK YTDMGDYDFE LDKFKDDYCK AHKIKKEDFT
     YDLIPFDIMW PYAAKDTDAT IRLHNFFLPK IEKNEKLCSL YYDVLMPGCV FLQRVEDRGV
     PISIDRLKEA QYQLTHNLNK AREKLYTYPE VKQLEQDQNE AFNPNSVKQL RVLLFDYVGL
     TPTGKLTDTG ADSTDAEALN ELATQHPIAK TLLEIRKLTK LISTYVEKIL LSIDADGCIR
     TGFHEHMTTS GRLSSSGKLN LQQLPRDESI IKGCVVAPPG YRVIAWDLTT AEVYYAAVLS
     GDRNMQQVFI NMRNEPDKYP DFHSNIAHMV FKLQCEPRDV KKLFPALRQA AKAITFGILY
     GSGPAKVAHS VNEALLEQAA KTGEPFVECT VADAKEYIET YFGQFPQLKR WIDKCHDQIK
     NHGFIYSHFG RKRRLHNIHS EDRGVQGEEI RSGFNAIIQS ASSDSLLLGA VDADNEIISL
     GLEQEMKIVM LVHDSVVAIV REDLIDQYNE ILIRNIQKDR GISIPGCPIG IDSDSEAGGS
     RDYSCGKMKK QHPSIACIDD DEYTRYVKGV LLDAEFEYKK LAAMDKEHPD HSKYKDDKFI
     AVCKDLDNVK RILGA