ID A0A0A7HGG1_9CAUD Unreviewed; 904 AA. AC A0A0A7HGG1; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-OCT-2020, entry version 28. 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; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Caudovirales; Myoviridae; Tevenvirinae; Gaprivervirus. 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., 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 possesses CC two enzymatic activities: DNA synthesis (polymerase) and an CC exonucleolytic activity that degrades single-stranded DNA in the 3'- to CC 5'-direction for proofreading purpose. {ECO:0000256|HAMAP- CC Rule:MF_04100}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130, CC Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, CC ChEBI:CHEBI:83828; EC=2.7.7.7; CC Evidence={ECO:0000256|ARBA:ARBA00001680, ECO:0000256|HAMAP- CC Rule:MF_04100, ECO:0000256|RuleBase:RU000442}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_04100}; CC -!- SUBUNIT: Part of the replicase complex that includes the DNA CC polymerase, the polymerase clamp, the clamp loader complex, the single- CC stranded DNA binding protein, and the primase/helicase. Interacts with CC the polymerase clamp; this interaction constitutes the polymerase CC holoenzyme. {ECO:0000256|HAMAP-Rule:MF_04100}. CC -!- DOMAIN: The N-terminus contains the 3'-5' exonuclease activity. The C- CC terminus contains the polymerase activity and is involved in binding to CC the polymerase clamp protein. A beta hairpin structure is necessary for CC the proofreading function of the polymerase. {ECO:0000256|HAMAP- CC Rule:MF_04100}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|HAMAP-Rule:MF_04100, CC ECO:0000256|RuleBase:RU000442}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04100}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KP007361; AIZ02394.1; -; Genomic_DNA. DR RefSeq; YP_009209792.1; NC_028925.1. DR GeneID; 26636212; -. DR KEGG; vg:26636212; -. DR KO; K18942; -. DR Proteomes; UP000030717; Genome. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IEA:UniProtKB-UniRule. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 3.30.420.10; -; 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; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR034749; DPOL_T4. DR InterPro; IPR012337; RNaseH-like_sf. DR InterPro; IPR036397; RNaseH_sf. 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 SUPFAM; SSF56672; SSF56672; 1. DR PROSITE; PS00116; DNA_POLYMERASE_B; 1. PE 3: Inferred from homology; KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP- KW Rule:MF_04100, ECO:0000256|RuleBase:RU000442}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_04100, ECO:0000256|RuleBase:RU000442}; KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932, KW ECO:0000256|HAMAP-Rule:MF_04100, ECO:0000256|RuleBase:RU000442}; KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP- KW Rule:MF_04100}; 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|ARBA:ARBA00023109, ECO:0000256|HAMAP- KW Rule:MF_04100}. FT DOMAIN 96..294 FT /note="DNA_pol_B_exo1" FT /evidence="ECO:0000259|Pfam:PF03104" FT DOMAIN 369..776 FT /note="DNA_pol_B" FT /evidence="ECO:0000259|Pfam:PF00136" FT REGION 381..904 FT /note="Polymerase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT REGION 415..417 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT REGION 706..709 FT /note="Binding of DNA in B-conformation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT REGION 898..904 FT /note="Interaction with the polymerase clamp" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT METAL 114 FT /note="Magnesium 1; catalytic; for 3'-5' exonuclease FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT METAL 116 FT /note="Magnesium 1; catalytic; for 3'-5' exonuclease FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT METAL 222 FT /note="Magnesium 2; catalytic; for 3'-5' exonuclease FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT METAL 328 FT /note="Magnesium 1; catalytic; for 3'-5' exonuclease FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT METAL 328 FT /note="Magnesium 2; catalytic; for 3'-5' exonuclease FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT METAL 412 FT /note="Magnesium 3; catalytic; for polymerase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT METAL 412 FT /note="Magnesium 4; catalytic; for polymerase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT METAL 413 FT /note="Magnesium 4; catalytic; via carbonyl oxygen; for FT polymerase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT METAL 623 FT /note="Magnesium 3; catalytic; for polymerase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT METAL 623 FT /note="Magnesium 4; catalytic; for polymerase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT BINDING 483 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT BINDING 560 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT SITE 621 FT /note="Optimization of metal coordination by the polymerase FT active site" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT SITE 707 FT /note="Optimization of metal coordination by the polymerase FT active site" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04100" FT SITE 715 FT /note="Essential for viral replication" FT /evidence="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 //