ID   TRM1_ALHV1              Reviewed;         680 AA.
AC   O36361;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 70.
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   Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal fever
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Macavirus.
OX   NCBI_TaxID=654901;
OH   NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9261371; DOI=10.1128/jvi.71.9.6517-6525.1997;
RA   Ensser A., Pflanz R., Fleckenstein B.;
RT   "Primary structure of the alcelaphine herpesvirus 1 genome.";
RL   J. Virol. 71:6517-6525(1997).
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; AF005370; AAC58058.1; -; Genomic_DNA.
DR   PIR; T03106; T03106.
DR   RefSeq; NP_065510.1; NC_002531.1.
DR   SMR; O36361; -.
DR   GeneID; 911746; -.
DR   KEGG; vg:911746; -.
DR   Proteomes; UP000000941; 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..680
FT                   /note="Tripartite terminase subunit 1"
FT                   /id="PRO_0000405759"
FT   ZN_FING         180..208
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT   BINDING         610..617
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ   SEQUENCE   680 AA;  77179 MW;  9EF3823A17F3E455 CRC64;
     MGQYLAALYS QIYGLCLDVS LVEFCKPTSL CLTKIADACN KVHKIHEYVS ASLLQQNSLE
     ACALSLELSH LLENLKTRLF FIYHALLDNP TYFSKLHSSV GLCDLHKKLN VQFYNECGIE
     VNLTLINDIE RFLSRLNCVF YCLSSSSALL ALKEALTFLG QLRGISPVPR TDIYITSSSC
     LECVLETSVV PNQGETLNEL LLNHNCHHLV ERVPPEPIKG LFESELQNLG LKVHIATDTI
     EQSVGKHEAV LQESLAYLKA HTIFNNTPKQ VLELSNLLYW NSGQNQPSDS GVKCSELSKI
     WSRENELQKY RPKLNNGEPP GHFFDLHSPQ GTELLFCGGI FSSTHDTITA LKQDCSNTFM
     KQTRLTGVAK RQNELFMRLS NILYGEEVPT KPKQTESALK TCDQSDASKN QVLQEAELRK
     EAYLNKLSKE GFRKLQACLS THEEMLNSQL SLKIWGSVVY KQSATLLNHF LFRQSWVTQA
     SLPPSVNGSP EQFENSKFIK SSLYVKSLSR EYLSTLRLHF FALITGPLTT QEGLFPSPPN
     VQLAHCLEAA HFMPHQKMLL NEMIKPTMEP QDWICSNFNE FYTIHETDLN GVQYECWKYL
     RELVLSVALY NITWEKNLCI YRTDHSCPTA CSSGIKEGLY VTYESHAPLI LVYSNKKWIF
     KDLYALLYAH MQLANNGAHR