ID   TRM3_HHV6U              Reviewed;         667 AA.
AC   P24443;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 83.
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};
GN   OrderedLocusNames=12L/7L, U66/U60;
OS   Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS   lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=10370;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2152817; DOI=10.1128/jvi.64.1.287-299.1990;
RA   Lawrence G.L., Chee M., Craxton M.A., Gompels U.A., Honess R.W.,
RA   Barrell B.G.;
RT   "Human herpesvirus 6 is closely related to human cytomegalovirus.";
RL   J. Virol. 64:287-299(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA   Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA   Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT   "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT   genome evolution.";
RL   Virology 209:29-51(1995).
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}.
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DR   EMBL; M68963; AAA65570.1; -; Genomic_DNA.
DR   EMBL; X83413; CAA58358.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; X83413; CAA58352.1; ALT_FRAME; Genomic_DNA.
DR   PIR; A33560; QQBEH6.
DR   SMR; P24443; -.
DR   PRIDE; P24443; -.
DR   Proteomes; UP000009295; 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..667
FT                   /note="Tripartite terminase subunit 3"
FT                   /id="PRO_0000115941"
FT   MOTIF           208..215
FT                   /note="Walker A motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   MOTIF           301..306
FT                   /note="Walker B motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        306
FT                   /note="For ATPase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        459
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        530
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        644
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
SQ   SEQUENCE   667 AA;  76360 MW;  00F35C12C4039784 CRC64;
     MLRTCDITHI KNNYEAIIWK GERDCSTIST KYPNSAIFYK KRFIMLTPEL GFAHSYNQQV
     KPLYTFCEKQ RHLKNRKPLT ILPSLSHKLQ EMKFLPASDK SFESQYTEFL ESFKILYREP
     LFLQIDGFIK DFRKWIKGEF NDFGDTRKIQ LEPFQKNILI HVIFFIAVTK LPALANRVIN
     YLTHVFDIEF VNESTLNTLK QKTNVFLVPR RHGKTWFIVP IISFLLKNIE GISIGYVAHQ
     KHVSHFVMKE VEFKCRRMFP EKTITCLDNV ITIDHQNIKS TALFASCYNT HQSIRGQSFN
     LLIVDESHFI KKDAFSTILG FLPQASTKIL FISSTNSGNH STSFLMKLNN SPFEMLSVVS
     YVCEDHAHML NERGNATACS CYRLHKPKFI SINAEVKKTA NLFLEGAFIH EIMGGATCNV
     INDVLITEQG QTEFEFFRYS TINKNLIPFL GKDLYVYLDP AYTGNRRASG TGIAAIGTYL
     DQYIVYGMEH YFLESLMTSS DTAIAECAAH MILSILDLHP FFTEVKIIIE GNSNQASAVK
     IACIIKENIT ANKSIQVTFF HTPDQNQIAQ PFYLLGKEKK LAVEFFISNF NSGNIKASQE
     LISFTIKITY DPVEYALEQI RNIHQISVNN YITYSAKKQA CSDDLIIAII MAIYVCSGNS
     SASFREI