ID   TRM1_GAHVM              Reviewed;         793 AA.
AC   Q77MS2;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN   Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014}; OrderedLocusNames=MDV041;
OS   Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS   disease herpesvirus type 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX   NCBI_TaxID=10389;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA   Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT   "The genome of a very virulent Marek's disease virus.";
RL   J. Virol. 74:7980-7988(2000).
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; AF243438; AAG14221.1; -; Genomic_DNA.
DR   RefSeq; YP_001033957.1; NC_002229.3.
DR   SMR; Q77MS2; -.
DR   GeneID; 4811502; -.
DR   KEGG; vg:4811502; -.
DR   Proteomes; UP000008072; 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..793
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000406559"
FT   ZN_FING         206..234
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   BINDING         697..704
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   793 AA;  90142 MW;  F092E17892F13548 CRC64;
     MLGMSHNRLQ SQGTEHDKFA TQKLFAIWGQ IQSYLFQVEL LKRCDPTVGV RMINRLKLNV
     LMIYYLEKKM VPALKEQREM NLTPLTYGLW LALRRAKLEG ELLLDALCEF KDGGNLRDFF
     RKSMSMCGDC PYHSTVELDT YGGKVSTEIK FLHDVENVLK QLNYCHLILK ADTVENFMVS
     LDNYLLKTLG SGSVVPPELY DPSQPCSVCF EELCVTANSG DSTHKRIVRK ICDHITKQIN
     IRVNSDDMVT HLPHATYVPD DKRTTAQTAL DVIQSTMRDT TTENDSNISV SKAAAAALDA
     HNVFLPASGD LYAISELQFW IASSGRKLHQ PRGNTVESFA DNLEALVSKE RLFDLRTSIV
     ETAVFDRRMD HFERVFAQEI EHMNAADRLL LGGRAAAPDD IIEALIKACY DHHMSAPLLK
     RLLYPDEAAH DALKTVLERV SSHCIGNDIQ CQDGDGTCGE RMNETGHFRT NDSFAMSTTS
     LGHDEWLEMV KSASSDVARR RKMYAERLTK KSLASLDKCI TEQRHELEKM LRVNVYGEVL
     IDSYTALFNG FRSRKRLLEA VKNCCANIID NRNSDDAFDA HRFMQTSLLK HRIDPAMLPS
     LTHKFFQLVN GPMFSHDRHR FAQPSNTALY FSVENVGLLP HLKEEMARFM FHSSRKTDWT
     VSKFRGFYDF STIDNVTAAH RMAWKYIKEL IFATALFSSV FKCGELHICR ADSLQINSNG
     DYVWKNGIYI TYETEYPLIM ILGSESSTSE TQNMTAIIDT DVFSLLYSIL QYMAPVTADQ
     VRVEQITNSH API