ID X2FCQ4_CHV16 Unreviewed; 1240 AA. AC X2FCQ4; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 27-MAR-2024, entry version 39. DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442}; DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442}; GN Name=UL30 {ECO:0000313|EMBL:AHM96079.1}; OS Cercopithecine herpesvirus 16 (CeHV-16) (Herpesvirus papio 2). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus; OC Simplexvirus papiinealpha2. OX NCBI_TaxID=340907 {ECO:0000313|EMBL:AHM96079.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9541; Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OH NCBI_TaxID=90387; Macaca leonina (Northern pig-tailed macaque) (Macaca nemestrina leonina). OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque). OH NCBI_TaxID=9545; Macaca nemestrina (Pig-tailed macaque). RN [1] {ECO:0000313|EMBL:AHM96079.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=OU1-76 {ECO:0000313|EMBL:AHM96079.1}; RX PubMed=24606686; DOI=10.1016/j.virol.2013.12.038; RA Black D., Ohsawa K., Tyler S., Maxwell L., Eberle R.; RT "A single viral gene determines lethal cross-species neurovirulence of RT baboon herpesvirus HVP2."; RL Virology 452-453:86-94(2014). CC -!- FUNCTION: Replicates viral genomic DNA. The replication complex is CC composed of six viral proteins: the DNA polymerase, processivity CC factor, primase, primase-associated factor, helicase, and ssDNA-binding CC protein. Additionally, the polymerase contains an intrinsic CC ribonuclease H (RNase H) activity that specifically degrades RNA/DNA CC heteroduplexes or duplex DNA substrates in the 5' to 3' direction. CC Therefore, it can catalyze the excision of the RNA primers that CC initiate the synthesis of Okazaki fragments at a replication fork CC during viral DNA replication. {ECO:0000256|ARBA:ARBA00025601}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; CC Evidence={ECO:0000256|ARBA:ARBA00000077}; 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:0000256|ARBA:ARBA00024632, CC ECO:0000256|RuleBase:RU000442}; CC -!- SUBUNIT: Forms a complex with the ssDNA-binding protein UL29, the DNA CC polymerase processivity factor, and the alkaline exonuclease. Interacts CC with the putative helicase-primase complex subunit UL8; this CC interaction may coordinate leading and lagging strand DNA synthesis at CC the replication fork. {ECO:0000256|ARBA:ARBA00025814}. CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}. CC Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}. 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; KF908240; AHM96079.1; -; Genomic_DNA. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW. DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1. DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1. DR Gene3D; 1.10.287.690; Helix hairpin bin; 1. DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR042087; DNA_pol_B_thumb. DR InterPro; IPR023211; DNA_pol_palm_dom_sf. DR InterPro; IPR021639; DNAPolymera_Pol_C. DR InterPro; IPR012337; RNaseH-like_sf. DR InterPro; IPR036397; RNaseH_sf. DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1. DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1. DR Pfam; PF00136; DNA_pol_B; 1. DR Pfam; PF03104; DNA_pol_B_exo1; 1. DR Pfam; PF11590; DNAPolymera_Pol; 1. DR PRINTS; PR00106; DNAPOLB. DR SMART; SM00486; POLBc; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 1. DR PROSITE; PS00116; DNA_POLYMERASE_B; 1. PE 3: Inferred from homology; KW DNA replication {ECO:0000256|ARBA:ARBA00022705, KW ECO:0000256|RuleBase:RU000442}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442}; KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932, KW ECO:0000256|RuleBase:RU000442}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759}; KW Host nucleus {ECO:0000256|ARBA:ARBA00022562}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, KW ECO:0000256|RuleBase:RU000442}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}; KW Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}. FT DOMAIN 243..543 FT /note="DNA-directed DNA polymerase family B exonuclease" FT /evidence="ECO:0000259|Pfam:PF03104" FT DOMAIN 607..1180 FT /note="DNA-directed DNA polymerase family B FT multifunctional" FT /evidence="ECO:0000259|Pfam:PF00136" FT DOMAIN 1208..1240 FT /note="DNA polymerase catalytic subunit Pol C-terminal" FT /evidence="ECO:0000259|Pfam:PF11590" FT REGION 22..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 646..698 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1104..1138 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1106..1126 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1240 AA; 135777 MW; 4F0A1484582626F6 CRC64; MGPVGRGGPG AGAAARAAAA GFFGPPAGRG SAPPPRPREN FYNPYLAAGR RSGAAGRGAQ PAPHSYCSEC DEFRFVAPRA LDEDAAPEMR VGVHDGRLRR APRVYCGGEE RDVLDFGRDA FWPRRARLWA GVDRAPAEAA PPVDLFHVYD IVENVEHAQH GGCAGRTHGR FLDAITPSGT VVTLLGLTPE GRRVAVHVYG TRQYFYMNRA EVDRRLGCRA PRDLCERMAT ALRESPGGSF RNISADHFEV DVVDRADVYY YETPRVPYYR VYARNGRALA YLCDNFCPGI RKYEGGVDAT TRFVLDNPGF VTFGWYRLGP GRDGAPPHPR PAEAFVTSSD VEVDCTADNL AVERERGDLP GYKLMCFDIE CKAGGEDEAA FPVAANAEDL VIQISCLLYD LAAARLEHIL LFSLGSCDLP EAFVADLGAR GLPAPTVLEF DSEFEMLLAF VTFVKQYGPE FATGYNIINF DWPFLIAKLT DVYKVPLDGY GRMNRRGVFR VWDIGQSHFQ KRSKIKMNGV VNIDMYGIVC DKVKLSSYKL NAVAEAVLKD KKKDLSYRDI PRYYAAGPAQ RGVIGEYCVQ DSLLVGQLFF KFLPHLELSA VARLAGITLT RTIYDGQQIR VYTCLLRLAG QKGFLLPDNP GRFAGAAAAR AGGDGGQEEE DAAGAEEDGG GADAGEGGGD EDASGGGAEP AAREGGAGRH VGYQGAKVLD PASGFHVDPV VVFDFASLYP SIIQAHNLCF STLSLSADAV AGLEPERDYL AIEVGGRRLF FVKAHVRESL LSILLRDWLA MRKQIRSRIP HSAPEEAVLL DKQQAAIKVV CNSVYGFTGV QHGLLPCLHV AATVTTIGRD MLLATREYVH ARWTTFDRLE ADFPEAATMR APGPFSMRII YGDTDSIFVL SRGLTAEGLT AMGDRMAAHI SRALFPPPIK LECEKTFAKL LLIAKKKYIG VICGGKMLIK GVDLVRKNNC AFINRTSRAL VDLLFYDDAV SAAAAALAAR PPEEWLAHPL PEGLDAFGRV LVDAHRRITD PDRDVRDFVL TSELSRHPRA YANKRLPHLT VYYKLLARRD QVPSIKDRIP YVIVAQTREV EETVARIDAL RELDAAPPAP PEPPPPPASA PAPPKRPRGR HPGDPEPKRR RLLVSELAED PAHAVAHRVP LNTDYYFSHL LGAACVTFKA LFGNNAKITE NLLKRFIPEV WHPEEETAVR LRAAGFRAAG AGATEAETRR RLRTAFDILA //