ID   TRM2_HCMVM              Reviewed;         157 AA.
AC   F5HGI9;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   23-FEB-2022, entry version 33.
DE   RecName: Full=Tripartite terminase subunit 2 {ECO:0000255|HAMAP-Rule:MF_04015};
GN   Name=TRM2 {ECO:0000255|HAMAP-Rule:MF_04015}; OrderedLocusNames=UL51;
OS   Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=295027;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA   Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA   Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA   Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT   "Genetic content of wild-type human cytomegalovirus.";
RL   J. Gen. Virol. 85:1301-1312(2004).
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 TRM1 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. {ECO:0000255|HAMAP-Rule:MF_04015}.
CC   -!- SUBUNIT: Associates with TRM1 and TRM3 to form the tripartite terminase
CC       complex. {ECO:0000255|HAMAP-Rule:MF_04015}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04015}.
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_04015}.
CC   -!- SIMILARITY: Belongs to the herpesviridae TRM2 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04015}.
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DR   EMBL; AY446894; AAR31615.1; -; Genomic_DNA.
DR   RefSeq; YP_081510.1; NC_006273.2.
DR   SMR; F5HGI9; -.
DR   DrugBank; DB12070; Letermovir.
DR   DrugCentral; F5HGI9; -.
DR   PRIDE; F5HGI9; -.
DR   DNASU; 3077482; -.
DR   GeneID; 3077482; -.
DR   KEGG; vg:3077482; -.
DR   Reactome; R-HSA-9610379; HCMV Late Events.
DR   Proteomes; UP000000938; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019073; P:viral DNA genome packaging; IEA:UniProtKB-UniRule.
DR   GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04015; HSV_TRM2; 1.
DR   InterPro; IPR005208; Herpes_TT2.
DR   Pfam; PF03581; Herpes_UL33; 1.
PE   3: Inferred from homology;
KW   Host nucleus; Reference proteome; Viral genome packaging;
KW   Viral release from host cell.
FT   CHAIN           1..157
FT                   /note="Tripartite terminase subunit 2"
FT                   /id="PRO_0000418249"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   157 AA;  16978 MW;  5999035AC484517D CRC64;
     MSWAKQRVPF LDDDDGEEEN DVQDDVDSPV PTRPLVIDED AEPAAGTSGG LEGGGGDDED
     GEDGHALPDL DDDLLLQFEP MLPRVYDLLL PSLDARLNFV NAGQKYAAFL KYVHGDCATC
     SHGEILREKT QLLTAIVSKL MDINGILEGK DEPAPGK