ID   TRM1_SHV21              Reviewed;         679 AA.
AC   P24911;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   23-FEB-2022, entry version 75.
DE   RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN   Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014}; OrderedLocusNames=7;
OS   Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=10383;
OH   NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2154888; DOI=10.1016/0042-6822(90)90107-3;
RA   Albrecht J.-C., Fleckenstein B.;
RT   "Structural organization of the conserved gene block of Herpesvirus saimiri
RT   coding for DNA polymerase, glycoprotein B, and major DNA binding protein.";
RL   Virology 174:533-542(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA   Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA   Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA   Honess R.W.;
RT   "Primary structure of the herpesvirus saimiri genome.";
RL   J. Virol. 66:5047-5058(1992).
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; X64346; CAA45630.1; -; Genomic_DNA.
DR   EMBL; M31122; AAA46163.1; -; Genomic_DNA.
DR   RefSeq; NP_040209.1; NC_001350.1.
DR   SMR; P24911; -.
DR   GeneID; 1682494; -.
DR   KEGG; vg:1682494; -.
DR   Proteomes; UP000000587; 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..679
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000115885"
FT   ZN_FING         180..208
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   679 AA;  77597 MW;  D6A14C408B2A9BCB CRC64;
     MAQHLAAVYS QIYGLTLDVS ILTFVDPAHI NWKTVTKNTE KINKIYLQIM PLLHNQNNIE
     STSLSVELQH LLHNLKIVLE TFSAHLSDYN MYFENIHSLS APCSRHKSIV FQFYNNCCVS
     VKMCIINDIE IFSKRLSSVF YCIRSCDALR GINHVIDFLG HLRGVSPIPL PDTYLSNIPC
     IYCLNEHMML PNQGESLPSL MMCVNCKHVC KQLNPEPIQG MFENELLQRH IIVESNKQKE
     QNQTCSIDNQ IRDASLSKLN QHTIFENISA PVLELSNLIY WSSGAHKKCA NVENTSEMAK
     LLSYEAKMQN YRKYICKNST HFFDKYKPYP IESIFCGGIF SSVDDTVKSL KSDCSLAFMK
     RANYQQLIKK QNELFVRLNK ILQGEDTVSH AASAVPLSDK ATIVNPDQVL HDAHARKDAY
     LQKVTKDGLK SLYTCLETQG AVLSNTLSMR VWGGAVYDEI VKLKNHFLFR DQFISLDWIH
     CETDSVTGFE NSKYIKNLIY SQKLSSEHIS SLTLQFYKLI TGPLSQNVSF FPLPSNIALA
     HCLDAAGALP HHKLLLTEMI WPSIEPKDWV SQTYNKFYTI TSTDLNSIQK EAWFFIRELV
     LSVSLYNEVL EKNLLVFSAL NFEKNCVNLS PNQFCSGIYL TYEDSSPLIF VYENQGWVFK
     DLYALLYHHL QLSGKNHGT