ID   TRM3_HHV2H              Reviewed;         734 AA.
AC   P89438;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=UL15;
OS   Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HG52;
RX   PubMed=1662697; DOI=10.1099/0022-1317-72-12-3057;
RA   McGeoch D.J., Cunningham C., McIntyre G., Dolan A.;
RT   "Comparative sequence analysis of the long repeat regions and adjoining
RT   parts of the long unique regions in the genomes of herpes simplex viruses
RT   types 1 and 2.";
RL   J. Gen. Virol. 72:3057-3075(1991).
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; Z86099; CAB06775.1; -; Genomic_DNA.
DR   RefSeq; YP_009137166.1; NC_001798.2.
DR   SMR; P89438; -.
DR   PRIDE; P89438; -.
DR   DNASU; 1487298; -.
DR   GeneID; 1487298; -.
DR   KEGG; vg:1487298; -.
DR   Proteomes; UP000001874; 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..734
FT                   /note="Tripartite terminase subunit 3"
FT                   /id="PRO_0000406186"
FT   MOTIF           183..189
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   MOTIF           258..265
FT                   /note="Walker A motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   MOTIF           352..357
FT                   /note="Walker B motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        357
FT                   /note="For ATPase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        509
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        581
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        706
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
SQ   SEQUENCE   734 AA;  80973 MW;  793F7A8874D0EC9F CRC64;
     MFGQQLASDV QQYLERLEKQ RQQKVGVDEA SAGLTLGGDA LRVPFLDFAT ATPKRHQTVV
     PGVGTLHDCC EHSPLFSAVA RRLLFNSLVP AQLRGRDFGG DHTAKLEFLA PELVRAVARL
     RFRECAPEDA VPQRNAYYSV LNTFQALHRS EAFRQLVHFV RDFAQLLKTS FRASSLAETT
     GPPKKRAKVD VATHGQTYGT LELFQKMILM HATYFLAAVL LGDHAEQVNT FLRLVFEIPL
     FSDTAVRHFR QRATVFLVPR RHGKTWFLVP LIALSLASFR GIKIGYTAHI RKATEPVFDE
     IDACLRGWFG SSRVDHVKGE TISFSFPDGS RSTIVFASSH NTNGIRGQDF NLLFVDEANF
     IRPDAVQTIM GFLNQANCKI IFVSSTNTGK ASTSFLYNLR GAADELLNVV TYICDDHMPR
     VVTHTNATAC SCYILNKPVF ITMDGAVRRT ADLFLPDSFM QEIIGGQARE TGDDRPVLTK
     SAGERFLLYR PSTTTNSGLM APELYVYVDP AFTANTRASG TGIAVVGRYR DDFIIFALEH
     FFLRALTGSA PADIARCVVH SLAQVLALHP GAFRSVRVAV EGNSSQDSAV AIATHVHTEM
     HRILASAGAN GPGPELLFYH CEPPGGAVLY PFFLLNKQKT PAFEYFIKKF NSGGVMASQE
     LVSVTVRLQT DPVEYLSEQL NNLIETVSPN TDVRMYSGKR NGAADDLMVA VIMAIYLAAP
     TGIPPAFFPI TRTS