ID A0A1W6DAP0_9BETA Unreviewed; 726 AA. AC A0A1W6DAP0; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 27-SEP-2017, entry version 3. DE RecName: Full=Tripartite terminase subunit 1 {ECO:0000256|HAMAP-Rule:MF_04014}; GN Name=TRM1 {ECO:0000256|HAMAP-Rule:MF_04014}; OS Human herpesvirus 6. OC Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae; OC Betaherpesvirinae; Roseolovirus; 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}; RA Greninger A.L., Hall Sedlak R., Roychoudhury P., Xie H., Guan J., RA Peddu V., Huang M.-L., Cook L., Yoshikawa T., Caserta M., Hill J.A., RA Jerome K.R.; RT "A rash of human herpesvirus 6 genomes."; RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the molecular motor that translocates viral CC genomic DNA in empty capsid during DNA packaging. Forms a CC tripartite terminase complex together with TRM2 and TRM3 in the CC host cytoplasm. Once the complex reaches the host nucleus, it CC interacts with the capsid portal vertex. This portal forms a ring CC in which genomic DNA is translocated into the capsid. TRM1 carries CC an endonuclease activity that plays an important role for the CC cleavage of concatemeric viral DNA into unit length genomes. CC {ECO:0000256|HAMAP-Rule:MF_04014}. CC -!- SUBUNIT: Associates with TRM2 and TRM3 to form the tripartite CC terminase complex. Interacts with portal protein. CC {ECO:0000256|HAMAP-Rule:MF_04014}. CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|HAMAP- CC Rule:MF_04014}. Note=Found associated with the external surface of CC the viral capsid during assembly and DNA packaging, but seems CC absent in extracellular mature virions. {ECO:0000256|HAMAP- CC 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:0008565; F:protein transporter activity; IEA:UniProtKB-UniRule. 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 Virus exit 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 C3H1-type. {ECO:0000256|HAMAP-Rule: FT MF_04014}. FT NP_BIND 626 633 ATP. {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 //