ID   TRM3_EBVB9              Reviewed;         690 AA.
AC   P03219; Q777C9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 2.
DT   03-AUG-2022, entry version 93.
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}; ORFNames=BGRF1/BDRF1;
OS   Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=10377;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6087149; DOI=10.1038/310207a0;
RA   Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA   Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA   Tuffnell P.S., Barrell B.G.;
RT   "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL   Nature 310:207-211(1984).
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   -!- INTERACTION:
CC       P03219; Q1HVD3: BTRF1; Xeno; NbExp=3; IntAct=EBI-9644804, EBI-9644838;
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; V01555; CAA24829.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; V01555; CAA24834.1; -; Genomic_DNA.
DR   EMBL; AJ507799; CAD53440.1; -; Genomic_DNA.
DR   PIR; A43044; QQBE38.
DR   RefSeq; YP_401690.1; NC_007605.1.
DR   SMR; P03219; -.
DR   BioGRID; 3509104; 3.
DR   IntAct; P03219; 26.
DR   MINT; P03219; -.
DR   DNASU; 3783767; -.
DR   GeneID; 3783767; -.
DR   KEGG; vg:3783767; -.
DR   Proteomes; UP000153037; 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   1: Evidence at protein level;
KW   DNA-binding; Host nucleus; Hydrolase; Reference proteome;
KW   Viral genome packaging; Viral release from host cell.
FT   CHAIN           1..690
FT                   /note="Tripartite terminase subunit 3"
FT                   /id="PRO_0000115946"
FT   MOTIF           226..233
FT                   /note="Walker A motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   MOTIF           321..326
FT                   /note="Walker B motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        326
FT                   /note="For ATPase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        481
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        555
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        667
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
SQ   SEQUENCE   690 AA;  76694 MW;  849EBABCEFF1977C CRC64;
     MLYASQRGRL TENLRNALQQ DSTTQGCLGA ETPSIMYTGA KSDRWAHPLV GTIHASNLYC
     PMLRAYCRHY GPRPVFVASD ESLPMFGASP ALHTPVQVQM CLLPELRDTL QRLLPPPNLE
     DSEALTEFKT SVSSARAILE DPNFLEMREF VTSLASFLSG QYKHKPARLE AFQKQVVLHS
     FYFLISIKSL EITDTMFDIF QSAFGLEEMT LEKLHIFKQK ASVFLIPRRH GKTWIVVAII
     SLILSNLSNV QIGYVAHQKH VASAVFTEII DTLTKSFDSK RVEVNKETST ITFRHSGKIS
     STVMCATCFN KNSIRGQTFH LLFVDEANFI KKEALPAILG FMLQKDAKII FISSVNSADQ
     ATSFLYKLKD AQERLLNVVS YVCQEHRQDF DMQDSMVSCP CFRLHIPSYI TMDSNIRATT
     NLFLDGAFST ELMGDTSSLS QGSLSRTVRD DAINQLELCR VDTLNPRVAG RLASSLYVYV
     DPAYTNNTSA SGTGIAAVTH DRADPNRVIV LGLEHFFLKD LTGDAALQIA TCVVALVSSI
     VTLHPHLEEV KVAVEGNSSQ DSAVAIASII GESCPLPCAF VHTKDKTSSL QWPMYLLTNE
     KSKAFERLIY AVNTASLSAS QVTVSNTIQL SFDPVLYLIS QIRAIKPIPL RDGTYTYTGK
     QRNLSDDVLV ALVMAHFLAT TQKHTFKKVH