ID   TRM1_EHV2               Reviewed;         728 AA.
AC   Q66612;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN   Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014}; OrderedLocusNames=7;
OS   Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX   NCBI_TaxID=82831;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA   Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus 2.";
RL   J. Mol. Biol. 249:520-528(1995).
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}.
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DR   EMBL; U20824; AAC13794.1; -; Genomic_DNA.
DR   PIR; S55601; S55601.
DR   RefSeq; NP_042603.1; NC_001650.2.
DR   SMR; Q66612; -.
DR   GeneID; 1461062; -.
DR   KEGG; vg:1461062; -.
DR   Proteomes; UP000007083; Genome.
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   Reference proteome; Viral genome packaging; Viral release from host cell;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..728
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000406035"
FT   ZN_FING         186..214
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   REGION          239..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..272
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         653..660
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   728 AA;  79676 MW;  30455CF3D696CE23 CRC64;
     MARELAAVYA QVFDLAAEVS LLGYCDPSSI DKRCVMANSN KVFKLCESLL PCLRLQNDTE
     CSPLSLELQH LLQNTREALG VLTDLLSGDP SRSEYFEALH PSRPLEGPCK RHARVRVPFY
     GGAEKTVSLS LLNDVEVFFK RLNSVFYCLP AEGALEALGE TVAFLGRLRG VSPIPPADAY
     VSSVPCASCF AEAAMLPNQG ESVLSMLAAV NCNHVCRQVP SDPVIGVFEN ELRHLGADAR
     AAGRAGGGRE SERRGREDAD DEEDDEEEPR DGQGDAGDGA ALRVLTESSL SVLAGHTIFE
     EEDGRLAEIS NLVYWSSAAD RGGVGGTARA TSSSHMAKLF AHEARMHRSR AWLGRGAPSH
     FFDAHRPSPL ESLFCGGVFN SIDDTIAALQ KDCSATFLKK SNYQTLIQQQ NELYVRLNEV
     LNGAGRDEGG AKGAEAIADA EPLKPDGGAS CDPRDVLSDA RVRRDLYLKK LTRDGLRRLT
     DCIETHGRVL SDTLSLRVWG SALYASAARL VNHFLFRRQF VGLGWADLTA GGEAAFENSK
     YIKNALHGQR LNREHLDSIV VHFYRLITGP LSLQNSHFPV PDNVALAYCL DAAGAMPHQK
     LVITEMIWPG IESKDWIDCN FNSFYSIETG DLNLTQKKTL NYIREAVLSI SLYNRVWEKS
     LSLLSATELR GSCLAESASG ELGEGVYLTY EGTAPLVLVF DSKGYVFKDL YTLLYTHLQL
     SGRRQASV