ID   TRM3_HHV7J              Reviewed;         663 AA.
AC   P52462;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
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/U60;
OS   Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=57278;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA   Nicholas J.;
RT   "Determination and analysis of the complete nucleotide sequence of human
RT   herpesvirus.";
RL   J. Virol. 70:5975-5989(1996).
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; U43400; AAC54723.1; -; Genomic_DNA.
DR   PIR; T41963; T41963.
DR   RefSeq; YP_073802.1; NC_001716.2.
DR   SMR; P52462; -.
DR   PRIDE; P52462; -.
DR   DNASU; 3289524; -.
DR   GeneID; 3289524; -.
DR   KEGG; vg:3289524; -.
DR   Proteomes; UP000009246; 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.
DR   SUPFAM; SSF52540; SSF52540; 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..663
FT                   /note="Tripartite terminase subunit 3"
FT                   /id="PRO_0000115942"
FT   MOTIF           205..212
FT                   /note="Walker A motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   MOTIF           297..302
FT                   /note="Walker B motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        302
FT                   /note="For ATPase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        455
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        526
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        640
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
SQ   SEQUENCE   663 AA;  76412 MW;  8002D6FA1D166DEC CRC64;
     MLRSCDIDAI QKAYQSIIWK HEQDVKISST FPNSAIFCQK RFIILTPELG FTHAYCRHVK
     PLYLFCDRQR HVKSKIAICD PLNCALSKLK FTAIIEKNTE VQYQKHLELQ TSFYRNPMFL
     QIEKFIQDFQ RWICGDFENT NKKERIKLEP FQKSILIHII FFISVTKLPT LANHVLDYLK
     YKFDIEFINE SSVNILKQKA SVFLVPRRHG KTWFMIPVIC FLLKNLEGIS IGYVAHQKHV
     SHFVMKDVEF KCRRFFPQKN ITCQDNVITI EHETIKSTAL FASCYNTHSI RGQSFNLLIV
     DESHFIKKDA FSTILGFLPQ SSTKIIFISS TNSGNHSTSF LTKLSNSPFE MLTVVSYVCE
     DHVHILNDRG NATTCACYRL HKPKFISINA DVKKTADLFL EGAFKHEIMG GSLCNVVNDT
     LITEQGLIEF DLFRYSTISK QIIPFLGKEL YIYIDPAYTI NRRASGTGVA AIGTYGDQYI
     IYGMEHYFLE SLLSNSDASI AECASHMILA VLELHPFFTE LKIIIEGNSN QSSAVKIACI
     LKQTISVIRY KHITFFHTLD QSQIAQPFYL LGREKRLAVE YFISNFNSGY IKASQELISF
     TIKITYDPIE YVIEQIKNLH QININEHVTY NAKKQTCSDD LLISIIMAIY MCHEGKQTSF
     KEI