ID   TRM1_HHV6U              Reviewed;         726 AA.
AC   P52384;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN   Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014}; OrderedLocusNames=U40;
OS   Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS   lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=10370;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA   Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA   Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT   "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT   genome evolution.";
RL   Virology 209:29-51(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; X83413; CAA58374.1; -; Genomic_DNA.
DR   EMBL; X92436; CAA63166.1; -; Genomic_DNA.
DR   RefSeq; NP_042933.1; NC_001664.2.
DR   SMR; P52384; -.
DR   PRIDE; P52384; -.
DR   DNASU; 1487918; -.
DR   GeneID; 1487918; -.
DR   KEGG; vg:1487918; -.
DR   Proteomes; UP000009295; 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..726
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000115882"
FT   ZN_FING         189..217
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   BINDING         626..633
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   726 AA;  82878 MW;  B735E3F0EAD597B5 CRC64;
     MNSLQSLCVL CARLNECALD LECLKFCDPV IVLSDMANFK KNGIVILHLY QTFFEGIKEQ
     NLLCASALTV YMQVLLKAMY EQVLLLDAAL ESFMVDQDRK KYFEKVLCLR RCAETLSINI
     SLNNGVEFIV QLSTLNDIEQ LISKINSVYA LLLPQEGLQI CGKIIDLLTI MCGACMVAKP
     ESYLETKTCM KCYEELTLTP NQGKSLRRRL HGKFCNHLTE QKAFFNIEKN IETIEKDLGE
     AILNYGTVQS VATEIKKIFK QQRSAESLHV SDAEKTLKKY NIFSKVPDVI YSLSEFTYWS
     KISETIVRNV AITLQQLNSC HTLYKQLQND VSLYLYGEVS EDFLALSENL LTHDERLYVG
     SIYVSPSRLI DLVTGLSIKN LEESPIFKRL AEEDEVQHKI KSLLHDIRDP QTTETPGRLN
     TINCMLQTHN LQQEVLARKK AYFQKVSESG YNRVMACIRE QESLINKVVS VNVYGNFIFE
     ALSKIMNGFV LRKMYLDGSF RVDSCTYDEH LYIKNNLMPK KLPLELLPDL SEIMYTLLTG
     PLSDFHKSAY PLPANISMAY GCDHAEMLPH MKEDLARCIE GTIHPSVWMV CEYNEFFNFS
     GVTDVNDMQK KMWNFIRELT LSVALYNDVF GKRLKIVRID EEGDLSGNVV LTFNHESPLL
     FHTGGGMTKF KDVYSLLYCD LQAQLSRETV DVPEGVSYSV RTPNLLDLVR ENEQDGSIIP
     GCLFDE