TRM3_HHV8P
ID TRM3_HHV8P Reviewed; 687 AA.
AC F5HGB6;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 33.
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=ORF29;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF148805; ABD28880.1; -; Genomic_DNA.
DR RefSeq; YP_001129382.1; NC_009333.1.
DR SMR; F5HGB6; -.
DR PRIDE; F5HGB6; -.
DR DNASU; 4961443; -.
DR GeneID; 4961443; -.
DR KEGG; vg:4961443; -.
DR Proteomes; UP000000942; 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..687
FT /note="Tripartite terminase subunit 3"
FT /id="PRO_0000423805"
FT REGION 67..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 221..228
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT MOTIF 316..321
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT COMPBIAS 67..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 321
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 476
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 550
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 662
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
SQ SEQUENCE 687 AA; 76529 MW; 545C88220B48616C CRC64;
MLLSRHRERL AANLQETAKD AGERWELSAP TFTRHCPKTA RMAHPFIGVV HRINSYSSVL
ETYCTRHHPA TPTSANPDVG TPRPSEDNVP AKPRLLESLS TYLQMRCVRE DAHVSTADQL
VEYQAARKTH DSLHACSVYR ELQAFLVNLS SFLNGCYVPG VHWLEPFQQQ LVMHTFFFLV
SIKAPQKTHQ LFGLFKQYFG LFETPNSVLQ TFKQKASVFL IPRRHGKTWI VVAIISMLLA
SVENINIGYV AHQKHVANSV FAEIIKTLCR WFPPKNLNIK KENGTIIYTR PGGRSSSLMC
ATCFNKNSIR GQTFNLLYVD EANFIKKDAL PAILGFMLQK DAKLIFISSV NSSDRSTSFL
LNLRNAQEKM LNVVSYVCAD HREDFHLQDA LVSCPCYRLH IPTYITIDES IKTTTNLFME
GAFDTELMGE GAASSNATLY RVVGDAALTQ FDMCRVDTTA QQVQKCLGKQ LFVYIDPAYT
NNTEASGTGV GAVVTSTQTP TRSLILGMEH FFLRDLTGAA AYEIASCACT MIKAIAVLHP
TIERVNAAVE GNSSQDSGVA IATVLNEICP LPIHFLHYTD KSSALQWPIY MLGGEKSSAF
ETFIYALNSG TLSASQTVVS NTIKISFDPV TYLVEQVRAI KCVPLRDGGQ SYSAKQKHMS
DDLLVAVVMA HFMATDDRHM YKPISPQ
