ID   TRM1_HHV8P              Reviewed;         695 AA.
AC   Q2HRD2;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN   Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014}; OrderedLocusNames=ORF7;
OS   Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS   sarcoma-associated herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=868565;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA   Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT   "Identification of a spliced gene from Kaposi's sarcoma-associated
RT   herpesvirus encoding a protein with similarities to latent membrane
RT   proteins 1 and 2A of Epstein-Barr virus.";
RL   J. Virol. 73:6953-6963(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA   Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT   "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL   J. Gen. Virol. 87:1781-1804(2006).
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; AF148805; ABD28850.1; -; Genomic_DNA.
DR   RefSeq; YP_001129353.1; NC_009333.1.
DR   SMR; Q2HRD2; -.
DR   PRIDE; Q2HRD2; -.
DR   DNASU; 4961505; -.
DR   GeneID; 4961505; -.
DR   KEGG; vg:4961505; -.
DR   Proteomes; UP000000942; 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..695
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000423882"
FT   ZN_FING         182..210
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   BINDING         621..628
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   695 AA;  78386 MW;  A9F42663400AD632 CRC64;
     MAKELAAVYA DVSALAMDLC LLSYADPATL DTKSLALTTG KFQSLHGTLL PLLRRQNAHE
     CSGLSLELEH LLENVADALT TLGVCTSRKL SPEEHFSLLH LDITCNKHRS VRFNFYGNWA
     LELKLSLIND VEIFFKRLSS VFYCIGSGSA LEGLGEVLRF VGKLRGISPV PGPDLYVSNL
     PCLECLQEVC LTPNQGTSLQ AMLPDTACSH ICTPACGEPV RGLFENELKQ LGLQTPESIP
     TTPCQSRVRQ DDEIRQSSLM AVGDHHIFGE VTRSVLEISN LIYWSSGHSD ATCDGDRDCS
     HLASLFTHEA DMHKRRVDLA GCLGERGTPK HFFDCFRPDS LETLFCGGLF SSVEDTIESL
     QKDCSSAFYQ QVNYTTALQK QNEFYVRLSK LLAAGQLNLG KCSTESCPSE ARRQLVGGDK
     PEEVLRDAKH RQELYLQKVA RDGFKKLSDC IRHQGHILSQ TLGLRLWGSV IYNEASALQN
     HFLHRAQFIS LPWQDLTVDC PTRFENSKYI KNSLYCQRLG REHVEILTLE FYKLITGPLS
     KRHTLFPSPP NVTLAQCFEA AGMLPHQKMM VSEMIWPSIE PKDWIEPNFN QFYSFENQDI
     NHLQKRAWEY IRELVLSVSL YNRTWERELK ILLTPQGSPG FKEPKPAGLT TGLYLTFETS
     APLVLVDKKY GWIFKDLYAL LYHHLQLSNH NDSQV