ID   TRM1_VZVD               Reviewed;         770 AA.
AC   P09284;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN   Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014}; OrderedLocusNames=30;
OS   Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10338;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA   Davison A.J., Scott J.E.;
RT   "The complete DNA sequence of varicella-zoster virus.";
RL   J. Gen. Virol. 67:1759-1816(1986).
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; X04370; CAA27913.1; -; Genomic_DNA.
DR   PIR; D27214; WZBE30.
DR   SMR; P09284; -.
DR   PRIDE; P09284; -.
DR   Proteomes; UP000002602; 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..770
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000115887"
FT   ZN_FING         199..227
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   BINDING         675..682
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   770 AA;  86972 MW;  BB0FFD8D6B07ABC0 CRC64;
     MELDINRTLL VLLGQVYTYI FQVELLRRCD PRVACRFLYR LAANCLTVRY LLKLFLRGFN
     TQLKFGNTPT VCALHWALCY VKGEGERLFE LLQHFKTRFV YGETKDSNCI KDYFVSAFNL
     KTCQYHHELS LTTYGGYVSS EIQFLHDIEN FLKQLNYCYI ITSSREALNT LETVTRFMTD
     TIGSGLIPPV ELFDPAHPCA ICFEELCITA NQGETLHRRL LGCICDHVTK QVRVNVDVDD
     IIRCLPYIPD VPDIKRQSAV EALRTLQTKT VVNPMGAKND TFDQTYEIAS TMLDSYNVFK
     PAPRCMYAIS ELKFWLTSNS TEGPQRTLDV FVDNLDVLNE HEKHAELTAV TVELALFGKT
     PIHFDRAFSE ELGSLDAIDS ILVGNRSSSP DSQIEALIKA CYAHHLSSPL MRHISNPSHD
     NEAALRQLLE RVGCEDDLTK EASDSATASE CDLNDDSSIT FAVHGWENLL SKAKIDAAER
     KRVYLEHLSK RSLTSLGRCI REQRQELEKT LRVNVYGEAL LQTFVSMQNG FGARNVFLAK
     VSQAGCIIDN RIQEAAFDAH RFIRNTLVRH TVDAAMLPAL THKFFELVNG PLFNHDEHRF
     AQPPNTALFF TVENVGLFPH LKEELAKFMG GVVGSNWLLS PFRGFYCFSG VEGVTFAQRL
     AWKYIRELVF ATTLFTSVFH CGEVRLCRVD RLGKDPRGCT SQPKGIGSSH GPLDGIYLTY
     EETCPLVAII QSGETGIDQN TVVIYDSDVF SLLYTLMQRL APDSTDPAFS