ID A0A1W6GAI0_9BETA Unreviewed; 1012 AA. AC A0A1W6GAI0; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 24-JUL-2024, entry version 25. DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442}; DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442}; OS Human betaherpesvirus 6. OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Betaherpesvirinae; Roseolovirus. OX NCBI_TaxID=10368 {ECO:0000313|EMBL:ARM09815.1}; RN [1] {ECO:0000313|EMBL:ARM09815.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HP23A7 {ECO:0000313|EMBL:ARM07012.1}, HP73F12 RC {ECO:0000313|EMBL:ARM08003.1}, HP94B11 {ECO:0000313|EMBL:ARM09097.1}, RC and JHPT-D12 {ECO:0000313|EMBL:ARM09815.1}; RX PubMed=29554870; DOI=.1186/s12864-018-4604-2; RA Greninger A.L., Knudsen G.M., Roychoudhury P., Hanson D.J., Sedlak R.H., RA Xie H., Guan J., Nguyen T., Peddu V., Boeckh M., Huang M.L., Cook L., RA Depledge D.P., Zerr D.M., Koelle D.M., Gantt S., Yoshikawa T., Caserta M., RA Hill J.A., Jerome K.R.; RT "Comparative genomic, transcriptomic, and proteomic reannotation of human RT herpesvirus 6."; RL BMC Genomics 19:204-204(2018). 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 -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}. 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; KY315531; ARM07012.1; -; Genomic_DNA. DR EMBL; KY315540; ARM08003.1; -; Genomic_DNA. DR EMBL; KY315549; ARM09097.1; -; Genomic_DNA. DR EMBL; KY315555; ARM09815.1; -; Genomic_DNA. DR GO; GO:0008296; F:3'-5'-DNA exonuclease activity; IEA:TreeGrafter. 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:0006287; P:base-excision repair, gap-filling; IEA:TreeGrafter. DR GO; GO:0045004; P:DNA replication proofreading; IEA:TreeGrafter. DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IEA:TreeGrafter. DR GO; GO:0009432; P:SOS response; IEA:TreeGrafter. 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; IPR050240; DNA_pol_type-B. 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 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 Host nucleus {ECO:0000256|ARBA:ARBA00022562}; 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 159..444 FT /note="DNA-directed DNA polymerase family B exonuclease" FT /evidence="ECO:0000259|Pfam:PF03104" FT DOMAIN 509..979 FT /note="DNA-directed DNA polymerase family B FT multifunctional" FT /evidence="ECO:0000259|Pfam:PF00136" SQ SEQUENCE 1012 AA; 115803 MW; 08D0F4E21546D949 CRC64; MDSVSFFNPY LEANRLKKKS RSSYIRILPR GIMHDGAAGL IKDVCDSEPR MFYRDRQYLL SKEMTWPSLD IARSKDYDHM RMKFHIYDAV ETLMFTDSIE NLPFQYRHFV IPSGTVIRMF GRTEDGEKIC VNVFGQEQYF YCECVDGKSL KATINNLMLT GEVKMSCSFV IEPADKLSLY GYNANTVVNL FKVSFGNFYV SQRIGKILQN EGFVVYEIDV DVLTRFFVDN GFLSFGWYNV KKYIPQDMGK GSNLEVEINC HVSDLVSLED VNWPLYGCWS FDIECLGQNG NFPDAENLGD IVIQISVISF DTEGDRDERH LFTLGTCEKI DGVHIYEFAS EFELLLGFFI FLRIESPEFI TGYNINNFDL KYLCIRMDKI YHYDIGCFSK LKNGKIGISV PHEQYRKGFL QAQTKVFTSG VLYLDMYPVY SSKITAQNYK LDTIAKICLQ QEKEQLSYKE IPKKFISGPS GRAVVGKYCL QDSVLVVRLF KQINYHYEVV EVARLAHVTA RCVVFEGQQK KIFPCILTEA KRRNMILPSM VSSHNRQGIG YKGATVLEPK TGYYAVPTVV FDFQSLYPSI MMAHNLCYST LVLDERQIAG LSESDILTVK LGDETHRFVK PCIRESVLGS LLKDWLAKRR EVKAEMQNCS DPMMKLLLDK KQLALKTTCN SVYGVTGAAH GLLPCVAIAA SVTCLGREML CSTVDYVNSK MQSEQFFCEE FGLTSSDFTG DLKVEVIYGD TDSIFMSVRN MVNQSLRRIA PMIAKHITDR LFKSPIKLEF EKILCPLILI CKKRYIGRQD DSLLIFKGVD LVRKTSCDFV KGVVKDIVDL LFFDEEVQTA AVEFSHMTQT QLREQGVPVG IHKILRRLCE AREELFQNRA DVRHLMLSSV LSKEMAAYKQ PNLAHLSVIR RLAQRKEEIP NVGDRIMYVL IAPSIGNKQT HNYELAEDPN YVIEHKIPIH AEKYFDQIIK AVTNAISPIF PKTDIKKEKL LLYLLPVKVY LDETFSAIAE VM //