ID A0A0A7HGG1_9CAUD Unreviewed; 904 AA. AC A0A0A7HGG1; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 05-JUN-2019, entry version 23. 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; 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., 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: CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA- CC COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7; CC Evidence={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}. 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 OrthoDB; 8987at10239; -. 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000030717}; 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 369 776 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 //