ID   TRM3_HHV6Z              Reviewed;         666 AA.
AC   Q9QJ23;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Tripartite terminase subunit 3 {ECO:0000255|HAMAP-Rule:MF_04013};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04013};
DE   AltName: Full=Terminase large subunit {ECO:0000255|HAMAP-Rule:MF_04013};
GN   Name=TRM3 {ECO:0000255|HAMAP-Rule:MF_04013}; OrderedLocusNames=U66;
OS   Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=36351;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA   Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA   Pellett P.E.;
RT   "Human herpesvirus 6B genome sequence: coding content and comparison with
RT   human herpesvirus 6A.";
RL   J. Virol. 73:8040-8052(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 TRM1 and TRM2 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. TRM3 carries an RNase H-like nuclease
CC       activity that plays an important role for the cleavage of concatemeric
CC       viral DNA into unit length genomes. {ECO:0000255|HAMAP-Rule:MF_04013}.
CC   -!- SUBUNIT: Interacts with the terminase subunits TRM1 and TRM2. Interacts
CC       with portal protein. {ECO:0000255|HAMAP-Rule:MF_04013}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04013}.
CC       Note=Responsible for the nuclear localization of the two others
CC       subunits TRM1 and TRM2. {ECO:0000255|HAMAP-Rule:MF_04013}.
CC   -!- SIMILARITY: Belongs to the herpesviridae TRM3 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04013}.
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; AF157706; AAD49667.1; -; Genomic_DNA.
DR   RefSeq; NP_050241.1; NC_000898.1.
DR   SMR; Q9QJ23; -.
DR   PRIDE; Q9QJ23; -.
DR   DNASU; 1497066; -.
DR   GeneID; 1497066; -.
DR   KEGG; vg:1497066; -.
DR   Proteomes; UP000006930; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR   GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.320; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_04013; HSV_TRM3; 1.
DR   InterPro; IPR003498; DNA_pack_C.
DR   InterPro; IPR038435; DNA_pack_C_sf.
DR   InterPro; IPR003499; DNA_pack_N.
DR   InterPro; IPR033663; HSV_TRM3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF02499; DNA_pack_C; 1.
DR   Pfam; PF02500; DNA_pack_N; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Host nucleus; Hydrolase; Reference proteome;
KW   Viral genome packaging; Viral release from host cell.
FT   CHAIN           1..666
FT                   /note="Tripartite terminase subunit 3"
FT                   /id="PRO_0000408416"
FT   MOTIF           208..215
FT                   /note="Walker A motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   MOTIF           300..305
FT                   /note="Walker B motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        305
FT                   /note="For ATPase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        458
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        529
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        643
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
SQ   SEQUENCE   666 AA;  76264 MW;  2AAC8EBA9E00CB51 CRC64;
     MLRTCDITHI KNNYEAIIWK GERNCSTIST KYPNSAIFYK KRFIMLTPEL GFAHSYNQQV
     KPLYTFCEKQ RHLKNRKPLT ILPSLTRKLQ EMKFLPASDK SFESQYTEFL ESFKILYREP
     LFLQIDGFIK DFRKWIKGEF NDFGDTRKIQ LEPFQKNILI HVIFFIAVTK LPALANRVIN
     YLTHVFDIEF VNESTLNTLK QKTNVFLVPR RHGKTWFIVP IISFLLKNIE GISIGYVAHQ
     KHVSHFVMKE VEFKCRRMFP EKTITCLDNV ITIDHQNIKS TALFASCYNT HSIRGQSFNL
     LIVDESHFIK KDAFSTILGF LPQASTKILF ISSTNSGNHS TSFLMKLNNS PFEMLSVVSY
     VCEDHAHMLN ERGNATACSC YRLHKPKFIS INAEVKKTAN LFLEGAFIHE IMGGATCNVI
     NDVLITEQGQ TEFEFFRYST INKNLIPFLG KDLYVYLDPA YTGNRRASGT GIAAIGTYLD
     QYIVYGMEHY FLESLMTSSD TAIAECAAHM ILSILDLHPF FTEVKIIIEG NSNQASAVKI
     ACIIKENITA NKSIQVTFFH TPDQNQIAQP FYLLGKEKKL AVEFFISNFN SGNIKASQEL
     ISFTIKITYD PVEYALEQIR NIHQISVNNY ITYSAKKQAC SDDLIIAIIM AIYVCSGNSS
     ASFREI