ID   TRM1_HHV1F              Reviewed;         780 AA.
AC   P06490;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN   Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014}; OrderedLocusNames=UL28;
OS   Human herpesvirus 1 (strain F) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10304;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3023664; DOI=10.1128/jvi.60.3.1134-1140.1986;
RA   Pellett P.E., Jenkins F.J., Ackermann M., Sarmiento M., Roizman B.;
RT   "Transcription initiation sites and nucleotide sequence of a herpes simplex
RT   virus 1 gene conserved in the Epstein-Barr virus genome and reported to
RT   affect the transport of viral glycoproteins.";
RL   J. Virol. 60:1134-1140(1986).
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:0000255|HAMAP-Rule:MF_04014}.
CC   -!- SUBUNIT: Associates with TRM2 and TRM3 to form the tripartite terminase
CC       complex. Interacts with portal protein. {ECO:0000255|HAMAP-
CC       Rule:MF_04014}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|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:0000255|HAMAP-Rule:MF_04014}.
CC   -!- SIMILARITY: Belongs to the herpesviridae TRM1 protein family.
CC       {ECO:0000255|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; M14164; AAA45775.1; -; Genomic_DNA.
DR   PIR; A26101; WMBEH8.
DR   SMR; P06490; -.
DR   PRIDE; P06490; -.
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; Host nucleus; Late protein; Metal-binding; Nucleotide-binding;
KW   Viral genome packaging; Viral release from host cell.
FT   CHAIN           1..780
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000115876"
FT   REGION          41..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         691..698
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   780 AA;  83846 MW;  AD20A1166DF4BCBE CRC64;
     MAAPVSEPTV ARQKLLALLG QVQTYVFQIE LLRRCDPHIG RGNAPPTEAE RASGAGAAAS
     SEAGPGGPAG AFLTPLSVTL ELLLEYAWRE GERLLGSLET FATAGDVAVF FTETMGLARP
     CPYHQRVRLD TYGGTVHMEL CFLHDVENFL KQLNYCHLIT PSRGATALER VREFMVGAVG
     SGLIVPPELS DPSHPCAVCF EELCVTANQG ATIAAAWRTV SVTTSPSRRR CGWTPTSVRR
     YLPHAAGLSD ADRAGALRVG PCAGPDRGGR RAAPPVAEND SVRKEADALL EAHDVFQATT
     PGLYAISELR FWLASGDRAG QTTMDAFASN LTALARELQQ ETAAVAVELA LFGRRAEHFD
     RAFGSHLAAL DMVDALIIGG QATSPDDQIE ALIRACYDHH LTTPLLRRLV SPEQCDEEAL
     RRVLARMGAG AGGPKGGAGP DDDGDRVAVE EGARGLGAPG GGGEDEAPSP RARGTGPETW
     GDIATQAAAD VRERRRLYAD RLTKRSLASL GRCVREQRGE LEKMLRVSVH GEVLPATFAA
     VANGFAARAL LAALTAGAGT VIDNRSAPGV FDAHRFMRAS LLRHQVDPAL LPSITHRFFE
     LVNGPLFDHS THSFAQPPNT ALYYSVENVG LLPHLKEELA RFIMGAGGSG ADWAVSEFQR
     FYCFDGISGI TPTQRAAWRY IRELIIATTL FASVYRCGEL ELRRPDCSRP TSEGRYRYPP
     GVYLTYDSDC PLVAIVESAP DGCIGPRSVV VYDRDVFSIL YSVLQHLAPR LPDGGHDGPP