ID   TRM1_ELHVK              Reviewed;         692 AA.
AC   Q9DKU0;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN   Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014};
OS   Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998) (EIHV-1)
OS   (Elephant endotheliotropic herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Proboscivirus.
OX   NCBI_TaxID=654902;
OH   NCBI_TaxID=9783; Elephas maximus (Indian elephant).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=99490; Loxodonta cyclotis (African forest elephant).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17507487; DOI=10.1128/jvi.00255-07;
RA   Ehlers B., Kuchler J., Yasmum N., Dural G., Voigt S., Schmidt-Chanasit J.,
RA   Jakel T., Matuschka F.R., Richter D., Essbauer S., Hughes D.J., Summers C.,
RA   Bennett M., Stewart J.P., Ulrich R.G.;
RT   "Identification of novel rodent herpesviruses, including the first
RT   gammaherpesvirus of Mus musculus.";
RL   J. Virol. 81:8091-8100(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11172087; DOI=10.1099/0022-1317-82-3-475;
RA   Ehlers B., Burkhardt S., Goltz M., Bergmann V., Ochs A., Weiler H.,
RA   Hentschke J.;
RT   "Genetic and ultrastructural characterization of a European isolate of the
RT   fatal endotheliotropic elephant herpesvirus.";
RL   J. Gen. Virol. 82:475-482(2001).
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; AF322977; AAG41997.2; -; Genomic_DNA.
DR   SMR; Q9DKU0; -.
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..692
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000408161"
FT   ZN_FING         190..218
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   BINDING         634..641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   692 AA;  80149 MW;  D8E3A839284ED399 CRC64;
     MNKLQLLGVV FAKVNECSLE LSCVRYCDPN LLLTKRKEFL HNAFVCKYLC DSLLSELQHF
     SCTNGLTACK HLAIILENLC EHFYVINKAL CSFEIHKDHQ QYYRTLFDVD QCSLHDPIKI
     SFVNKQDLEI TLTDFNEIER FLCKLNLIFP LIDARSGMRI ISQIYDRLRK FTGISPLARL
     EFYKSACGGC YLCYEELQMT PNNGSSVQKR LNGVLCEHVT YTKDLVFQEN EYLEVLREDL
     KRDNLLREDM RTELDDMKKI LSNKKERGFY VPEAEQLLHR YDVFTDDIPN YIYTLSDLTY
     WSKTSEKIIK TMNMTMQQLN VYNNNMIKLK RSISRALNDI EVRDCFDVFE KVVDKRHCMF
     LGSMFTSSAK IISLLATQCL TAFEEKAVFE RLNECDALCS TVNTILERLK SASGDGKEGI
     TKQDFQADEL IKGYNVSDEV SVRKKTYLNK VADKGYSKIV ASLSTEERSI KKLIDINFLG
     TLCIDMMVKL EKMFYKRSQI GQMVENGVHL LALCNYDNHL YIRNNLSRQS ISTENVNGVI
     QHILSFLCGP IFTHRHDIFP MPPNIDMAYA CDNANVLPHR KEELMQCVND ITSVHGWSIS
     SYNTFFKIDS VDLNTAHAHV WGYVKEFIVA VTLYNELYGQ RLRAFRVDEN TIRECGLYLT
     YNSDIPLVLK TDKNVIYGSD IYSILYAHMH HA