TRM3_GAHVM
ID TRM3_GAHVM Reviewed; 737 AA.
AC Q9E6Q2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=MDV027;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
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; AF243438; AAG14207.1; -; Genomic_DNA.
DR RefSeq; YP_001033943.1; NC_002229.3.
DR SMR; Q9E6Q2; -.
DR PRIDE; Q9E6Q2; -.
DR GeneID; 4811488; -.
DR KEGG; vg:4811488; -.
DR Proteomes; UP000008072; 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..737
FT /note="Tripartite terminase subunit 3"
FT /id="PRO_0000406523"
FT MOTIF 188..194
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT MOTIF 263..270
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT MOTIF 357..362
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 362
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 517
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 589
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 712
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
SQ SEQUENCE 737 AA; 82648 MW; 1CBB5BB58E99BB46 CRC64;
MFGGLLGEET KRHFERLMKT KNDRLGASHR NERSIRDGDM VDAPFLNFAI PVPRRHQTVM
PAIGILHNCC DSLGIYSAIT TRMLYSSIAC SEFDELRRDS VPRCYPRITN AQAFLSPMMM
RVANSIIFQE YDEMECAAHR NAYYSTMNSF ISMRTSDAFK QLTVFISRFS KLLIASFRDV
NKLDDHTVKK RARIDAPSYD KLHGTLELFQ KMILMHATYF VTSVLLGDHA ERAERLLRVA
FDTPHFSDIV TRHFRQRATV FLVPRRHGKT WFLVPLIALA MSSFEGIRIG YTSHIRKAIE
PVFEDIGDRL RRWFGAHRVD HVKGETITFS FPSGLKSTVT FASSHNTNSI RGQDFNLLFV
DEANFIRPDA VQTIIGFLNQ ATCKIIFVSS TNSGKASTSF LYGLKGSADD LLNVVTYICD
EHMKHVTDYT NATSCSCYVL NKPVFITMDG AMRRTAEMFL PDSFMQEIIG GGVVDRTICQ
GDRSIFTASA IDRFLIYRPS TVNNQDPFSQ DLYVYVDPAF TANTKASGTG VAVIGKYGTD
YIVFGLEHYF LRALTGESSD SIGYCVAQCL IQICAIHRKR FGVIKIAIEG NSNQDSAVAI
ATRIAIEMIS YMKAAVAPTP HNVSFYHSKS NGTDVEYPYF LLQRQKTTAF DFFIAQFNSG
RVLASQDLVS TTVSLTTDPV EYLTKQLTNI SEVVTGPTCT RTFSGKKGGN DDTVVALTMA
VYISAHIPDM AFAPIRV
