ID   TRM1_MUHVS              Reviewed;         798 AA.
AC   P30674;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN   Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014};
OS   Murid herpesvirus 1 (strain Smith) (MuHV-1) (Mouse cytomegalovirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Muromegalovirus.
OX   NCBI_TaxID=10367;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1329325; DOI=10.1016/0042-6822(92)90198-x;
RA   Messerle M., Keil G.M., Schneider K., Koszinowski U.H.;
RT   "Characterization of the murine cytomegalovirus genes encoding the major
RT   DNA binding protein and the ICP18.5 homolog.";
RL   Virology 191:355-367(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8971012; DOI=10.1128/jvi.70.12.8833-8849.1996;
RA   Rawlinson W.D., Farrell H.E., Barrell B.G.;
RT   "Analysis of the complete DNA sequence of murine cytomegalovirus.";
RL   J. Virol. 70:8833-8849(1996).
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; X67021; CAA47415.1; -; Genomic_DNA.
DR   EMBL; U68299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; B44051; B44051.
DR   SMR; P30674; -.
DR   PRIDE; P30674; -.
DR   Proteomes; UP000008774; 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..798
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000115891"
FT   ZN_FING         191..219
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   REGION          416..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         674..681
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   798 AA;  89101 MW;  CF6CE8BEF6752533 CRC64;
     MAMNTLQKLC VVCSKCNECA MDVECLKYCD PNIVSMDSTA FRRNGVMVIH LYRTLYPALV
     SQNAVQTSVL TLYMEMLLQG LYDTMREIDM ALTDFGTHRD RQRYYRRVLK LDSCNRHESI
     TITFAPELAL TIDLATLNDV ERLLCKINCV YGAVDASQGV AVCRRLLSLL ARLCDICPVA
     GPEIYRETVT CFQCYEELMA VPNQGRSINR RMQGLLCDHI TIKKVLVQLD MDAQAVEQDM
     GDIAIRAPSV KGIIRAIKSL ASFSPASYAY INDAEEALRG YNLFSEIPDR IYSLSDYTYW
     SKTSEAIVRH VGITMRQLNV SHSLWKTLRT ELSRYHYGED LEDVFTLGEG RFGGDERIYV
     GSIFAAPGKV VDMITSMSIK SFENNPLFNR LHESNEIYAK IKSLIEEIRG VGDGPAAGAA
     RSRAEAASGA GAGGEEGAGA AAGRGNTGGD EGAGTTTAMS SALECGDPLL RVHDVNKEVN
     VRKRAYLKKV SEMGYNKVMA CIRNQEHLVT KLVNVNLVGT VCLEAVSKIM NGFLSRQRSI
     TEAETYPDVA ESLGYDEHLY VINNLVHKRL PSELLPQLGQ QIYRFINGPM FTHYLDRHPL
     PYNVNMAYAC DNAGILPHVK EDLVRCADGT VVPSDWMTVG YMGFFRFADI RELNDLQKMV
     WAHIRELVLS VALYNETFGK QLALWRVEDG DEIGDGIILT YNPESPLILR RGDRSYRSRD
     LYLLLYKHLS VDSETLADAG SRASVADLCQ VERPGPIAEQ RSSTQNVKKK RKRMSLLELV
     RDVDGAGGDD LVPPCLYK