ID   TRM1_HHV2H              Reviewed;         785 AA.
AC   P89451;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN   Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014}; OrderedLocusNames=UL28;
OS   Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1662697; DOI=10.1099/0022-1317-72-12-3057;
RA   McGeoch D.J., Cunningham C., McIntyre G., Dolan A.;
RT   "Comparative sequence analysis of the long repeat regions and adjoining
RT   parts of the long unique regions in the genomes of herpes simplex viruses
RT   types 1 and 2.";
RL   J. Gen. Virol. 72:3057-3075(1991).
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; Z86099; CAB06753.1; -; Genomic_DNA.
DR   RefSeq; YP_009137180.1; NC_001798.2.
DR   SMR; P89451; -.
DR   PRIDE; P89451; -.
DR   GeneID; 1487313; -.
DR   KEGG; vg:1487313; -.
DR   Proteomes; UP000001874; 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..785
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000406175"
FT   ZN_FING         201..229
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   REGION          439..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         696..703
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   785 AA;  85241 MW;  246988E41997DF62 CRC64;
     MAAAPPAAVS EPTAARQKLL ALLGQVQTYV FQLELLRRCD PQIGLGKLAQ LKLNALQVRV
     LRRHLRPGLE AQAAAFLTPL SVTLELLLEY AWREGERLLG HLETFATTGD VSAFFTETMG
     LARPCPYHQQ IRLQTYGGDV RMELCFLHDV ENFLKQLNYC HLITPPSGAT AALERVREFM
     VAAVGSGLIV PPELSDPSHP CAVCFEELCV TANQGATIAR RLADRICNHV TQQAQVRLDA
     NELRRYLPHA AGLSDAARAR ALCVLDQALA RTAAGGGARA GPPPADSSSV REEADALLEA
     HDVFQATTPG LYAISELRFW LASGDRARHS TMDAFADNLN ALAQRELQQE TAAVAVELAL
     FGRRAEHFDR AFGGHLAALD MVDALIIGGQ ATSPDDQIEA LIRACYDHHL TTPLLRRLVS
     PEQCDEEALR RVLARLGAGG ATGGAEEEEP RAAAEEGGRR RGAGTPASED GERGPEPGAQ
     GPESWGDIAT RAAADVRERR RLYADRLTKR SLASLGRCVR EQRGELEKML RVSVHGEVLP
     ATFAAVANGF AARARFCALT AGAGTVIDNR AAPGVFDAHR FMRASLLRHQ VDPALLPSIT
     HRFFELVNGP LFDHSTHSFA QPPNTALYYS VENVGLLPHL KEELARFIMG AGGSGADWAV
     SEFQKFYCFD GVSGITPTQR AAWRYIRELI IATTLFASVY RCGELELRRP DCSRPTSEGL
     YRYPPGVYLT YNSDCPLVAI VESGPDGCIG PRSVVVYDRD VFSILYSVLQ HLAPRLAGGG
     SDAPP