ID   TRM1_TUHV2              Reviewed;         782 AA.
AC   Q9WRL6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN   Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014};
OS   Tupaiid herpesvirus (strain 2) (TuHV-2) (Herpesvirus tupaia (strain 2)).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae.
OX   NCBI_TaxID=132678;
OH   NCBI_TaxID=37347; Tupaia belangeri (Common tree shrew) (Tupaia glis belangeri).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10392721; DOI=10.1016/s0168-1702(99)00012-x;
RA   Bahr U., Springfeld C., Tidona C.A., Darai G.;
RT   "Structural organization of a conserved gene cluster of Tupaia herpesvirus
RT   encoding the DNA polymerase, glycoprotein B, a probable processing and
RT   transport protein, and the major DNA binding protein.";
RL   Virus Res. 60:123-136(1999).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF084543; AAD42934.1; -; Genomic_DNA.
DR   SMR; Q9WRL6; -.
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..782
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000115886"
FT   ZN_FING         190..218
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   REGION          727..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..741
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         666..673
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   782 AA;  87393 MW;  4DE40314E5BABB9B CRC64;
     MNTLQRLCVV CSKCNECAME LECLKYCDPA IVLVDSAPFK RNALTVVHLY RRLCPALAEQ
     NARYQASLIT LYLEMLLRCL YEDVLLVDEA LGEFERHGDR QRYYRRVLRL DRCACHDTLE
     VTFTERIRLT VDVATLNEVE RLLCKINCVY GVLEPTRGLE LCRRLLSLMG RLCGISPVAA
     PEAYVENLTC LQCYEELAAV PNQGRSILKR LRGLLCDHLT VRKSLVQLET GIQTMEQDIV
     ETVGSRPRLS SLLELLKGLS SSAAVSHAYI SEAEDTLRRY NLFTDIPPRI YSLSDFTYWS
     KTSEVIVQRV NVTVQQLNMY HSLCRTLRNE LGQYLYGDRV EDLFTLSEAQ LGEDERLYVG
     SIYAAPERIV DLMTSLSLQS FENNPVFNKL HENNEIYSKI RSLLEEIRRP LDGAGTRGAA
     AATAAGARGA AEGTGGAAAA GGAAAAAGEA AGGPFQCGDP AARAHDVVRE VHVRKKAYLQ
     KVSELGYNRV MQCIKGQEKL IKKLVNVNLL GTVCFEVLAK VINGFIRRRA YLERVDGVVD
     VDRLLQYDDH LYVVNNLVHR RLPAESLPAL GQEFYRFVNG PVFQHHADRY PLPYNIDMAY
     ACDNAGMLPH LKEDLVRLAE GTVAPSEWMV APYRRFFDLG AALDLNELQK GFWAHVREIV
     FSVALYNEAF GKELRLCRAD EPVDEERERL VVTYNVDGPL FLYAGGGVWK SKDLYLLLYQ
     HLNGAAAPPP PAAPSPPPAE PATTAGASRK RPAVESPGVL LDLVRDADRE SSLVPDCLLY
     DP