ID   TRM1_EBVB9              Reviewed;         685 AA.
AC   P25939; Q777A8;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   11-MAY-2016, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN   Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014}; ORFNames=BALF3;
OS   Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=10377;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6087149; DOI=10.1038/310207a0;
RA   Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA   Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA   Tuffnell P.S., Barrell B.G.;
RT   "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL   Nature 310:207-211(1984).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=24554665; DOI=10.1128/jvi.00063-14;
RA   Chiu S.H., Wu M.C., Wu C.C., Chen Y.C., Lin S.F., Hsu J.T., Yang C.S.,
RA   Tsai C.H., Takada K., Chen M.R., Chen J.Y.;
RT   "Epstein-Barr virus BALF3 has nuclease activity and mediates mature virion
RT   production during the lytic cycle.";
RL   J. Virol. 88:4962-4975(2014).
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       ECO:0000269|PubMed:24554665}.
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       ECO:0000269|PubMed:24554665}. Note=Found associated with the external
CC       surface of the viral capsid during assembly and DNA packaging, but
CC       seems absent in extracellular mature virions. {ECO:0000255|HAMAP-
CC       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; V01555; CAA24807.1; -; Genomic_DNA.
DR   EMBL; AJ507799; CAD53465.1; -; Genomic_DNA.
DR   PIR; S33056; S33056.
DR   RefSeq; YP_401715.2; NC_007605.1.
DR   SMR; P25939; -.
DR   IntAct; P25939; 16.
DR   MINT; P25939; -.
DR   PRIDE; P25939; -.
DR   DNASU; 3783679; -.
DR   GeneID; 3783679; -.
DR   KEGG; vg:3783679; -.
DR   Proteomes; UP000153037; 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..685
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000115889"
FT   ZN_FING         173..201
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   REGION          231..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..410
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         619..626
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   685 AA;  74764 MW;  24F8371F54D16635 CRC64;
     MSGLLAAAYS QVYALAVELS VCTRLDPRSL DVAAVVRNAG LLAELEAILL PRLRRQNDRA
     CSALSLELVH LLENSREASA ALLAPGRKGT RVPPLRTPSV AYSVEFYGGH KVDVSLCLIN
     DIEILMKRIN SVFYCMSHTM GLESLERALD LLGRFRGVSP IPDPRLYITS VPCWRCVGEL
     MVLPNHGNPS TAEGTHVSCN HLAVPVNPEP VSGLFENEVR QAGLGHLLEA EEKARPGGPE
     EGAVPGPGRP EAEGATRALD TYNVFSTVPP EVAELSELLY WNSGGHAIGA TGQGEGGGHS
     RLSALFARER RLALVRGACE EALAGARLTH LFDAVAPGAT ERLFCGGVYS SSGDAVEALK
     ADCAAAFTAH PQYRAILQKR NELYTRLNRA MQRLGRGEEE ASRESPEVPR PAGAREPGPS
     GALSDALKRK EQYLRQVATE GLAKLQSCLA QQSETLTETL CLRVWGDVVY WELARMRNHF
     LYRRAFVSGP WEDRRAGEGA AFENSKYIKT HLFTQTLSSE HLHALTHSLY TFITGPLAEE
     SGLFPPPSNV ALARCCDAAG TLPHQKAFLT SLIWPGIEPS DWIETSFNSF YSVPGGSLAS
     SQQILCRALR EAVLTVSLYN KTWGRSLILR RADAVSPGQA LPPDGLYLTY DSDRPLILLY
     KGRGWVFKDL YALLYLHLQM RDDSA