ID A0A1W6DAP0_9BETA Unreviewed; 726 AA. AC A0A1W6DAP0; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 26-FEB-2020, entry version 9. DE RecName: Full=Tripartite terminase subunit 1 {ECO:0000256|HAMAP-Rule:MF_04014}; GN Name=TRM1 {ECO:0000256|HAMAP-Rule:MF_04014}; OS Human betaherpesvirus 6. OC Viruses; Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus; OC unclassified Roseolovirus. OX NCBI_TaxID=10368 {ECO:0000313|EMBL:ARJ99730.1}; RN [1] {ECO:0000313|EMBL:ARJ99730.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Japan-a11 {ECO:0000313|EMBL:ARJ99730.1}, Japan-a3 RC {ECO:0000313|EMBL:ARJ98948.1}, and Japan-b9 RC {ECO:0000313|EMBL:ARK00636.1}; 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 -!- FUNCTION: Component of the molecular motor that translocates viral CC genomic DNA in empty capsid during DNA packaging. Forms a tripartite CC terminase complex together with TRM2 and TRM3 in the host cytoplasm. CC Once the complex reaches the host nucleus, it interacts with the capsid CC portal vertex. This portal forms a ring in which genomic DNA is CC translocated into the capsid. TRM1 carries an endonuclease activity CC that plays an important role for the cleavage of concatemeric viral DNA CC into unit length genomes. {ECO:0000256|HAMAP-Rule:MF_04014}. CC -!- SUBUNIT: Associates with TRM2 and TRM3 to form the tripartite terminase CC complex. Interacts with portal protein. {ECO:0000256|HAMAP- CC Rule:MF_04014}. CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|HAMAP-Rule:MF_04014}. CC Note=Found associated with the external surface of the viral capsid CC during assembly and DNA packaging, but seems absent in extracellular CC mature virions. {ECO:0000256|HAMAP-Rule:MF_04014}. CC -!- SIMILARITY: Belongs to the herpesviridae TRM1 protein family. CC {ECO:0000256|HAMAP-Rule:MF_04014}. 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; KY274488; ARJ98948.1; -; Genomic_DNA. DR EMBL; KY274495; ARJ99730.1; -; Genomic_DNA. DR EMBL; KY274503; ARK00636.1; -; Genomic_DNA. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016485; P:protein processing; IEA:UniProtKB-UniRule. DR GO; GO:0019069; P:viral capsid assembly; IEA:UniProtKB-UniRule. DR GO; GO:0019073; P:viral DNA genome packaging; IEA:InterPro. DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule. DR HAMAP; MF_04014; HSV_TRM1; 1. DR InterPro; IPR000501; UL28/UL56. DR Pfam; PF01366; PRTP; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_04014}; KW Host nucleus {ECO:0000256|HAMAP-Rule:MF_04014}; KW Late protein {ECO:0000256|HAMAP-Rule:MF_04014}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04014}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04014}; KW Viral genome packaging {ECO:0000256|HAMAP-Rule:MF_04014}; KW Viral release from host cell {ECO:0000256|HAMAP-Rule:MF_04014}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_04014}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_04014}. FT ZN_FING 189..217 FT /note="C3H1-type" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04014" FT NP_BIND 626..633 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04014" SQ SEQUENCE 726 AA; 83019 MW; F72E47D201EAE473 CRC64; MNSLQSLCVL CARLNECALD LECLKFCDPV IVLSDMANFK KNGIVILHLY QTFFEGIKEQ NLLCASALTV YMQVLLKAMY EQVLLLDAAL ESFMVDQDRK KYFEKVLCLK RCAEHLSINI SLNNGVEFIV QLSTLNDIEQ LISKINSVYA LLLPQEGLQI CGKIIDLLTI MCGACMVAKP ESYLETKTCM KCYEELTLTP NQGKSLRKRL HGKFCNHLTE QKAFFNIEKN IETIEKDLGE AILNYGTIQS VVTEIKKIFK QQRSAESLHV SDAEKTLKKY NIFSKVPDVI YSLSEFTYWS KISETIVRNV AITLQQLNSC HTLYKQLQND VSLYLYGEVS EDFLALSENL LTHDERLYVG SIYVSPSRLI DLVTGLSIKN LEESPIFKRL AEEDEVQHKI KSLLHDIRDP QTTETPGRLN TINCMLQTHN LQQEVLARKK AYFQKVSESG YNRVMACIRE QESLINKVVS VNVYGNFIFE ALSKIMNGLV LRKMYLDGSL RVDSCTYDEH LYIKNNLMPK KLPLELLPDL SEIMYTLLTG PLSDFHKSAY PLPANISMAY GCDHAEMLPH MKEDLARCIE GTIHPSVWMV CEYNEFFNFS GVTDVNDMQK KMWNFIRELT LSVALYNDVF GKRLKIVRID EEEDLNGNVV LTFNHESPLL FHTSGGMTKF KDVYSLLYCD LQAQLSRETV DVPEGVSYSV RTPNLLDLVR ENEQDDSIIP GCLFDE //