TRM3_EHV1B
ID TRM3_EHV1B Reviewed; 734 AA.
AC P28969; Q6S6S7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 Ab4p) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31520;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT "The DNA sequence of equine herpesvirus-1.";
RL Virology 189:304-316(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; AY665713; AAT67302.1; -; Genomic_DNA.
DR PIR; A36795; WZBEA1.
DR RefSeq; YP_053090.1; NC_001491.2.
DR SMR; P28969; -.
DR GeneID; 1487536; -.
DR KEGG; vg:1487536; -.
DR Proteomes; UP000001189; 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..734
FT /note="Tripartite terminase subunit 3"
FT /id="PRO_0000115943"
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
