ID   TRM1_HHV1A              Reviewed;         785 AA.
AC   P12835;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 70.
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 1 (strain Angelotti) (HHV-1) (Human herpes simplex virus
OS   1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10301;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2823222; DOI=10.1093/nar/15.19.8109;
RA   Knopf C.W.;
RT   "The nucleotide sequence of the herpes simplex virus type 1 late gene
RT   ICP18.5 of strain Angelotti.";
RL   Nucleic Acids Res. 15:8109-8110(1987).
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; Y00453; CAA68508.1; -; Genomic_DNA.
DR   PIR; A26987; WMBEK8.
DR   SMR; P12835; -.
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   Viral genome packaging; Viral release from host cell; Zinc; Zinc-finger.
FT   CHAIN           1..785
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000115875"
FT   ZN_FING         197..225
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   REGION          433..489
FT                   /note="Disordered"
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;  85608 MW;  7E08C7D4B4734D1A CRC64;
     MAAPVSEPTV ARQKLLALLG QVQTYVFQIE LLRRCDPHIG RGKLPQLKLN ALQVRALRRR
     LRPGLEAQAG AFLTPLSVTL ELLLEYAWRE GERLLGSLET FATAGDVAAF FTETMGLARP
     CPYHQRVRLD TYGGTVHMEL CFLHDVENFL KQLNYCHLIT PSRGATAALE RVREFMVGAV
     GSGLIVPPEL SDPSHPCAVC FEELCVTANQ GATIARRLAD RICNHVTQQA QVRLDANELR
     RYLPHAAGLS DADRARALSV LDHALARTAG GDGQPHPSPE NDSVRKEADA LLEAHDVFQA
     TTPGLYAISE LRFWLASGDR AGQTTMDAFA SNLTALARRE LQQETAAVAV ELALFGRRAE
     HFDRAFGSHL AALDMVDALI IGGQATSPDD QIEALIRACY DHHLTTPLLR RLVSPEQCDE
     EALRRVLARM GAGGAADAPK GGAGPDDDGD RVAVEEGTRG LGAPGGGGED EDRRRGPGGQ
     GPETWGDIAT QAAADVRERR RLYADRLTKR SLASLGRCVR EQRGELEKML RVSVHGEVLP
     ATFAAVANGF AARARFCALT AGAGTVIDNR SAPGVFDAHR FMRASLLRHQ VDPALLPSIT
     HRFFELVNGP LFDHSTHSFA QPPNTALYYS VENVGLLPHL KEELARFIMG AGGSGADWAV
     SEFQRFYCFD GISGITPTQR AAWRYIRELI IATTLFASVY RCGELELRRP DCSRPTSEGR
     YRYPPGVYLT YDSDCPLVAI VESAPDGCIG PRSVVVYDRD VFSILYSVLQ HLAPRLPDGG
     HDGPP