ID   TRM3_SHV21              Reviewed;         683 AA.
AC   Q01020;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, 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=29;
OS   Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=10383;
OH   NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA   Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA   Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA   Honess R.W.;
RT   "Primary structure of the herpesvirus saimiri genome.";
RL   J. Virol. 66:5047-5058(1992).
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; X64346; CAA45657.1; -; Genomic_DNA.
DR   RefSeq; NP_040231.1; NC_001350.1.
DR   SMR; Q01020; -.
DR   GeneID; 1682488; -.
DR   KEGG; vg:1682488; -.
DR   Proteomes; UP000000587; 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..683
FT                   /note="Tripartite terminase subunit 3"
FT                   /id="PRO_0000115945"
FT   MOTIF           217..224
FT                   /note="Walker A motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   MOTIF           312..317
FT                   /note="Walker B motif"
FT   ACT_SITE        317
FT                   /note="For ATPase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        472
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        546
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        658
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
SQ   SEQUENCE   683 AA;  77050 MW;  1B66CC277156AFC4 CRC64;
     MLLLKAKKAI IENLSEVSST QAETDWDMST PTIITNTSKS ERTAYSKIGV IPSVNLYSST
     LTSFCKLYHP LTLNQTQPQT GTLRLLPHEK PLILQDLSNY VKLLTSQNVC HDTEANTEYN
     AAVQTQKTSM ECPTYLELRQ FVINLSSFLN GCYVKRSTHI EPFQLQLILH TFYFLISIKS
     PESTNRLFDI FKEYFGLREM DPDMLQIFKQ KASIFLIPRR HGKTWIVVAI ISMLLTSVEN
     IHVGYVAHQK HVANSVFTEI INTLQKWFPS RYIDIKKENG TIIYKSPDKK PSTLMCATCF
     NKNSIRGQTF NLLYIDEANF IKKDSLPAIL GFMLQKDAKL IFISSVNSGD RATSFLFNLK
     NASEKMLNIV NYICPDHKDD FSLQDSLISC PCYKLYIPTY ITIDETIKNT TNLFLDGAFT
     TELMGDMSGI SKSNMHKVIS EMAITQFDLC RADTTKPEIT QCLNSTMYIY IDPAYTNNSE
     ASGTGIGAIL TFKNNSSKCI IVGMEHYFLK DLTGTATYQI ASCACSLIRA SLVLYPHIQC
     VHVAVEGNSS QDSAVAISTL INECSPIKVY FIHYKDKTTT MQWPIYMLGA EKSIAFESFI
     YAINSGTISA SQSIISNTIK LSFDPISYLI EQIRSIRCYP LRDGSHTYCA KKRTVSDDVL
     VAVVMAYFFA TSNKHIFKPL NST