ID   TRM1_BHV2B              Reviewed;         664 AA.
AC   P17587;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 68.
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   Bovine herpesvirus 2 (strain BMV) (BoHV-2) (Bovine mammillitis virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10296;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2841793; DOI=10.1016/0042-6822(88)90583-1;
RA   Hammerschmidt W., Conraths F., Mankertz J., Pauli G., Ludwig H.,
RA   Buhk H.-J.;
RT   "Conservation of a gene cluster including glycoprotein B in bovine
RT   herpesvirus type 2 (BHV-2) and herpes simplex virus type 1 (HSV-1).";
RL   Virology 165:388-405(1988).
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   PIR; B29242; WMBEBH.
DR   SMR; P17587; -.
DR   PRIDE; P17587; -.
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..664
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000115878"
FT   ZN_FING         205..233
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   REGION          273..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..461
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   664 AA;  72368 MW;  A84F7ED8EBE24D29 CRC64;
     MADAFDPSDT RPDELAAVAR QKLLVVLGQL QTYIFQVELL KRCDPQVARH QIGKLKLNAL
     QVRAVSRHFM EGMSSQAATL ITPLTLALEL SLEYARREGE KLLEALNDLG ERSSPVAYFE
     GTMGLARGCP HHQAVKLATY GGEIDKELCF LHDVENFLKQ MNYCHLITPA SAAAEALVSV
     KAFLARTVGS ELIVPPEISD PSHPCHVCFE ELCVTANQGA TASRRLAGKI CDHVTQQARV
     RLDADEMRRN LPHVVGLSEA RRARALHALE VSSKMTEANS GGPAEAPGPA AAQEREASAL
     LDAHHVFKSA PPGLYAVSEL RFWLSSGDRT SGSTVDAFAD NLSALAERER RYETGAVAVE
     LAAFGRRGEH FDRTFGDRVA SLDMVDALFV GGQSAAPDDQ IEALVRACYN HHLSAPVLRQ
     LAGSEHGDAE ALRSALEGLH AAEDPPGDGN AEKEARRAPS LGGGPEDDWA ALAARAAADV
     GARRRLYADR LTKRSLASLG RCVREQRGEL EKMLRVSTYG EVLPTVFAAV CNGFAARTRF
     CELTARAGTV IDNRGNPDTF DTHRFMRASL MRHRVDPALL PGITHQFFEL VNGPLFDHAT
     HGFAQPPNTA LYFSVENVGL LPHLKEELAR FMMGKADSDW AISEFQKFYH FDGTSGITPT
     QRIA