ID   A0A0A7HGG1_9CAUD        Unreviewed;       904 AA.
AC   A0A0A7HGG1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   10-MAY-2017, entry version 13.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_04100};
DE            EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_04100};
DE            EC=3.1.11.- {ECO:0000256|HAMAP-Rule:MF_04100};
GN   ORFNames=VR25_050 {ECO:0000313|EMBL:AIZ02394.1};
OS   Escherichia phage vB_EcoM_VR25.
OC   Viruses; dsDNA viruses, no RNA stage; Caudovirales; Myoviridae;
OC   Tevenvirinae; Sp18virus.
OX   NCBI_TaxID=1567028 {ECO:0000313|EMBL:AIZ02394.1, ECO:0000313|Proteomes:UP000030717};
RN   [1] {ECO:0000313|EMBL:AIZ02394.1, ECO:0000313|Proteomes:UP000030717}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kaliniene L., Meskys R., Simoliunas E., Zajanckauskaite A.,
RA   Truncaite L.;
RT   "VR bacteriophages - a small but diverse group of low-temperature
RT   viruses.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Replicates the viral genomic DNA. This polymerase
CC       possesses two enzymatic activities: DNA synthesis (polymerase) and
CC       an exonucleolytic activity that degrades single-stranded DNA in
CC       the 3'- to 5'-direction for proofreading purpose.
CC       {ECO:0000256|HAMAP-Rule:MF_04100}.
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1). {ECO:0000256|HAMAP-Rule:MF_04100,
CC       ECO:0000256|RuleBase:RU000442}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_04100};
CC   -!- SUBUNIT: Part of the replicase complex that includes the DNA
CC       polymerase, the polymerase clamp, the clamp loader complex, the
CC       single-stranded DNA binding protein, and the primase/helicase.
CC       Interacts with the polymerase clamp; this interaction constitutes
CC       the polymerase holoenzyme. {ECO:0000256|HAMAP-Rule:MF_04100}.
CC   -!- DOMAIN: The N-terminus contains the 3'-5' exonuclease activity.
CC       The C-terminus contains the polymerase activity and is involved in
CC       binding to the polymerase clamp protein. A beta hairpin structure
CC       is necessary for the proofreading function of the polymerase.
CC       {ECO:0000256|HAMAP-Rule:MF_04100}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|HAMAP-Rule:MF_04100, ECO:0000256|RuleBase:RU000442}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04100}.
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DR   EMBL; KP007361; AIZ02394.1; -; Genomic_DNA.
DR   RefSeq; YP_009209792.1; NC_028925.1.
DR   RefSeq; YP_009209792.1; NC_028925.1.
DR   RefSeq; YP_009209792.1; NC_028925.1.
DR   GeneID; 26636212; -.
DR   KEGG; vg:26636212; -.
DR   KO; K18942; -.
DR   OrthoDB; VOG0900001M; -.
DR   Proteomes; UP000030717; Genome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.90.1600.10; -; 1.
DR   HAMAP; MF_04100; DPOL_T4; 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; IPR023211; DNA_pol_palm_dom.
DR   InterPro; IPR034749; DPOL_T4.
DR   InterPro; IPR012337; RNaseH-like_dom.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000030717};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_04100,
KW   ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_04100,
KW   ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_04100,
KW   ECO:0000256|RuleBase:RU000442};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_04100};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_04100};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_04100};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_04100};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_04100};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_04100};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04100,
KW   ECO:0000256|RuleBase:RU000442};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_04100,
KW   ECO:0000256|RuleBase:RU000442};
KW   Viral DNA replication {ECO:0000256|HAMAP-Rule:MF_04100}.
FT   DOMAIN       96    294       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      369    770       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   REGION      381    904       Polymerase. {ECO:0000256|HAMAP-Rule:
FT                                MF_04100}.
FT   REGION      415    417       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_04100}.
FT   REGION      706    709       Binding of DNA in B-conformation.
FT                                {ECO:0000256|HAMAP-Rule:MF_04100}.
FT   REGION      898    904       Interaction with the polymerase clamp.
FT                                {ECO:0000256|HAMAP-Rule:MF_04100}.
FT   METAL       114    114       Magnesium 1; catalytic; for 3'-5'
FT                                exonuclease activity. {ECO:0000256|HAMAP-
FT                                Rule:MF_04100}.
FT   METAL       116    116       Magnesium 1; catalytic; for 3'-5'
FT                                exonuclease activity. {ECO:0000256|HAMAP-
FT                                Rule:MF_04100}.
FT   METAL       222    222       Magnesium 2; catalytic; for 3'-5'
FT                                exonuclease activity. {ECO:0000256|HAMAP-
FT                                Rule:MF_04100}.
FT   METAL       328    328       Magnesium 1; catalytic; for 3'-5'
FT                                exonuclease activity. {ECO:0000256|HAMAP-
FT                                Rule:MF_04100}.
FT   METAL       328    328       Magnesium 2; catalytic; for 3'-5'
FT                                exonuclease activity. {ECO:0000256|HAMAP-
FT                                Rule:MF_04100}.
FT   METAL       412    412       Magnesium 3; catalytic; for polymerase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_04100}.
FT   METAL       412    412       Magnesium 4; catalytic; for polymerase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_04100}.
FT   METAL       413    413       Magnesium 4; catalytic; via carbonyl
FT                                oxygen; for polymerase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_04100}.
FT   METAL       623    623       Magnesium 3; catalytic; for polymerase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_04100}.
FT   METAL       623    623       Magnesium 4; catalytic; for polymerase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_04100}.
FT   BINDING     483    483       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04100}.
FT   BINDING     560    560       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04100}.
FT   SITE        621    621       Optimization of metal coordination by the
FT                                polymerase active site.
FT                                {ECO:0000256|HAMAP-Rule:MF_04100}.
FT   SITE        707    707       Optimization of metal coordination by the
FT                                polymerase active site.
FT                                {ECO:0000256|HAMAP-Rule:MF_04100}.
FT   SITE        715    715       Essential for viral replication.
FT                                {ECO:0000256|HAMAP-Rule:MF_04100}.
SQ   SEQUENCE   904 AA;  103716 MW;  1231F65A374D4AC9 CRC64;
     MQEFYLTIEQ IGDNLHERYI DKNGNERTRE IPYTPCLFMH AREGQATKYS DIYNKGCVKK
     EFDSMRDASQ WMKRMNDMGL EAMGMDDFKL AYLSDRYPHE IKYDSSKIRV ANFDIEVTSP
     DGFPEPSEAR HPIDALTHYD SVDDKFYVFD LLGSPYATVE QWSIDIAAKL QEDGGDEVPS
     EILEKIVYMA FDSEEEMLQQ YLVFWNEKTP VMLTGWNIEK FDIPYIYNRL KNVFGEATAK
     RLSPHRRTKV KVINNGFGEE QEIIQILGVS VLDYLDLYKK FSFTNQPSYS LDYVAESELG
     VGKLPYDGPI SKLRESNHQR YISYNIIDVY RVVQIDRKRQ FINLSQSMGY YAKMQIQSVF
     SPIKTWDAII FNSLKTQNKV IPETKSHVRQ SFPGAFVKEP IPNAYKYVMS CDLTSLYPSI
     IRQINISPET IAGSFAPAHM HEYIAGTADR PSDAFSCAPN GMMYFKDVAG IIPTEVTKVF
     NQRKEHKGYM LAAQRNGELI KEALSNPGTG TTEPEVDYRH DFDDNMKTTL HGLNQTVLNG
     MLYKAQMEEV AGMTAQINRK LLINSCYGAL GNIWFRYFDL RNATAITSFG QLALQWIERK
     VNEYFDGVCG TQGQTYVFYG DTDSIYIQCD NLIKKVGGES KFRDTNHLVD FMDKFAKDRL
     EPAIDKAFRE LAEYMNNKQH LMFMDREAIA CPPLGSKGVG GFWTAKKRYA LNVYDMEGTR
     YAVPKLKIMG LETQKSSTPK ACQKALKECI RRMLQEGEES LQTYFKEFNK EFNELNYMTI
     AGVSSVNNIQ KYNEGGFPGF KCPAHIKGVL AYMRATKGLK TVPQIMEGEK VYVLPLKVGN
     PFGETVIAWP SGIELPIEIR DQVLQWMDYN TLFQKTFVKP LTGFSEAAKV DYEKKATLFD
     MFDF
//