TRM3_VZVD
ID TRM3_VZVD Reviewed; 747 AA.
AC P09294;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 84.
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};
DE Contains:
DE RecName: Full=Gene 42 protein;
GN Name=TRM3 {ECO:0000255|HAMAP-Rule:MF_04013}; OrderedLocusNames=45/42;
OS Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
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; X04370; CAB55553.1; -; Genomic_DNA.
DR PIR; A27344; WZBE45.
DR PIR; G27341; G27341.
DR SMR; P09294; -.
DR PRIDE; P09294; -.
DR Proteomes; UP000002602; 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..747
FT /note="Tripartite terminase subunit 3"
FT /id="PRO_0000038308"
FT CHAIN 353..747
FT /note="Gene 42 protein"
FT /id="PRO_0000038309"
FT MOTIF 194..198
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT MOTIF 267..274
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT MOTIF 361..366
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 366
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 521
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 593
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 722
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
SQ SEQUENCE 747 AA; 82757 MW; 1A056546B9BD5194 CRC64;
MSLIMFGRTL GEESVRYFER LKRRRDERFG TLESPTPCST RQGSLGNATQ IPFLNFAIDV
TRRHQAVIPG IGTLHNCCEY IPLFSATARR AMFGAFLSST GYNCTPNVVL KPWRYSVNAN
VSPELKKAVS SVQFYEYSPE EAAPHRNAYS GVMNTFRAFS LSDSFCQLST FTQRFSYLVE
TSFESIEECG SHGKRAKVDV PIYGRYKGTL ELFQKMILMH TTHFISSVLL GDHADRVDCF
LRTVFNTPSV SDSVLEHFKQ KSTVFLVPRR HGKTWFLVPL IALVMATFRG IKVGYTAHIR
KATEPVFEGI KSRLEQWFGA NYVDHVKGES ITFSFTDGSY STAVFASSHN TNGIRGQDFN
LLFVDEANFI RPDAVQTIVG FLNQTNCKII FVSSTNTGKA STSFLYNLRG SSDQLLNVVT
YVCDDHMPRV LAHSDVTACS CYVLNKPVFI TMDGAMRRTA DLFMADSFVQ EIVGGRKQNS
GGVGFDRPLF TKTARERFIL YRPSTVANCA ILSSVLYVYV DPAFTSNTRA SGTGVAIVGR
YKSDWIIFGL EHFFLRALTG TSSSEIGRCV TQCLGHILAL HPNTFTNVHV SIEGNSSQDS
AVAISLAIAQ QFAVLEKGNV LSSAPVLLFY HSIPPGCSVA YPFFLLQKQK TPAVDYFVKR
FNSGNIIASQ ELVSLTVKLG VDPVEYLCKQ LDNLTEVIKG GMGNLDTKTY TGKGTTGTMS
DDLMVALIMS VYIGSSCIPD SVFMPIK