ID   TRM1_EHV1B              Reviewed;         766 AA.
AC   Q6DLH9; P28973; P33549;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-NOV-2004, sequence version 2.
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=32;
OS   Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31520;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA   Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus-1.";
RL   Virology 189:304-316(1992).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAT67289.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY665713; AAT67289.1; ALT_INIT; Genomic_DNA.
DR   PIR; F36798; WZBEC5.
DR   RefSeq; YP_053077.1; NC_001491.2.
DR   SMR; Q6DLH9; -.
DR   GeneID; 1487544; -.
DR   KEGG; vg:1487544; -.
DR   Proteomes; UP000001189; 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..766
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000115880"
FT   ZN_FING         191..219
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   BINDING         683..690
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   766 AA;  84384 MW;  D5B501A161ACCE03 CRC64;
     MGSAQARQRL LAIFGQVQAY IFQVEMLKRC DPSALLPLVG SLKLNALTIR MLRRKLGGAL
     IEQAQHQQTP LACALTMALE YAEVEGERVL RAVDDVNLAG PEGFFRATMR LDEPCEYHVR
     VHLDTYGGPI DAEVQFLHDA ENFLKQLNYC HLITGFEAGL DALESVARFL TRTVGSGIVV
     PPELCDPTHP CSVCFEELCV TANQGEAVHR RLLECTCDHI TRQMAVRVAN IDIARHLPHA
     LSVASERRAA AEAALRALEA RRVQGHNGKS AGTEDPTQQV ASRLLESHHV FKPASRCLYA
     VSELKFWLAS TKHGDMGQPR AIDTFTENLE TLDKQEKFFH LQAATVELAL FGRTLDHFDR
     LFADQLLGLD VIDGMLVGSC AVSPDDHIEA LIKACYTHHM SAPLLQRLTD PDTSNREALK
     QLLGRIGVDT DDGAGELGDA LDVDLDNLGG APPVNSTPCG EDALCRTVSE ERPWDKLLER
     ATADASQRRR MYAERLSKRS IASLGRCVRE QRRELEKTLR VNVYGEVLLH TYVSSYNGFC
     ARRGFCAAVS RAGTIIDNRS STSAFDSHQF MKAALLRHPI DQSLMPSITH KFFELINGPV
     FDNAGHNFAQ PPNTALYYSV ENVGLLPHLK EELARFMITA AKGDWSISEF QRFYCFEGVT
     GVTATQRLAW KYIGELILAA AVFSSVFHCG EVRLLRADRT YPDSSGAQRC VSGIYITYEA
     SCPLVAVLSA APHGAIGAET VVIYDSDVFS LLYAVLQQLA PGSGAN