ID   TRM3_EHV1V              Reviewed;         734 AA.
AC   P84396; Q6S6S7;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
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=44;
OS   Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=310273;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1] {ECO:0000312|EMBL:AAS45929.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Davis-Poynter N., Nugent J., Birch-Machin I., Allen G.P.;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; AY464052; AAS45929.1; -; Genomic_DNA.
DR   RefSeq; YP_053090.1; NC_001491.2.
DR   SMR; P84396; -.
DR   GeneID; 1487536; -.
DR   KEGG; vg:1487536; -.
DR   Proteomes; UP000008296; 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; Viral genome packaging;
KW   Viral release from host cell.
FT   CHAIN           1..734
FT                   /note="Tripartite terminase subunit 3"
FT                   /id="PRO_0000115944"
FT   MOTIF           184..190
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   MOTIF           259..266
FT                   /note="Walker A motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   MOTIF           353..358
FT                   /note="Walker B motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        358
FT                   /note="For ATPase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        511
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        583
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        707
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
SQ   SEQUENCE   734 AA;  81078 MW;  3FF360DD02DEF9CC CRC64;
     MFGRVLGRET VQYFEALRRE VQARRGAKNR AAEAQNGGED DAKTAFLNFA IPTPQRHQTV
     VPGVGTLHDC CETAQIFASV ARRLLFRSLS KWQSGEARER LDPASVEAYV DPKVRQALKT
     ISFVEYSDDE ARSCRNAYYS IMNTFDALRS SDAFHQVASF VARFSRLVDT SFNGADLDGD
     GQQASKRARV DVPTYGKQRG TLELFQKMIL MHATYFIAAV ILGDHADRIG AFLKMVFNTP
     EFSDATIRHF RQRATVFLVP RRHGKTWFLV PLIALALATF KGIKIGYTAH IRKATEPVFD
     EIGARLRQWF GNSPVDHVKG ENISFSFPDG SKSTIVFASS HNTNGIRGQD FNLLFVDEAN
     FIRPEAVQTI IGFLNQTNCK IIFVSSTNTG KASTSFLYNL KGAADDLLNV VTYICDEHME
     RVKAHTNATA CSCYILNKPV FITMDGAMRN TAELFLPDSF MQEIIGGGNV SGAHRDEPVF
     TKTAQDRFLL YRPSTVANQD IMSSDLYVYV DPAFTTNAMA SGTGVAVVGR YRSNWVVFGM
     EHFFLSALTG SSAELIARCV AQCLAQVFAI HKRPFDSVRV AVEGNSSQDA AVAIATNIQL
     ELNTLRRADV VPMPGAVLFY HCTPHGSSVA YPFFLLQKQK TGAFDHFIKA FNSGSVLASQ
     ELVSNTVRLQ TDPVEYLLTQ MKNLTEVVTG TSETRVFTGK RNGASDDMLV ALVMAVYLSS
     LPPTSDAFSS LPAQ