TRM3_HCMVM
ID TRM3_HCMVM Reviewed; 674 AA.
AC F5HCU8;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
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=UL89;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
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; AY446894; AAR31641.1; -; Genomic_DNA.
DR RefSeq; YP_081537.1; NC_006273.2.
DR BMRB; F5HCU8; -.
DR SMR; F5HCU8; -.
DR DrugBank; DB12070; Letermovir.
DR DrugCentral; F5HCU8; -.
DR PRIDE; F5HCU8; -.
DR GeneID; 3077553; -.
DR KEGG; vg:3077553; -.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Proteomes; UP000000938; 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..674
FT /note="Tripartite terminase subunit 3"
FT /id="PRO_0000417832"
FT MOTIF 212..219
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT MOTIF 305..310
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 310
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 463
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 534
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 651
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
SQ SEQUENCE 674 AA; 77034 MW; EAE1087E3A907CAA CRC64;
MLRGDSAAKI QERYAELQKR KSHPTSCIST AFTNVAALCR KRYQMMHPEL GLAHSCNEAF
LPLMAFCGRH RDYNSPEESQ RELLFHERLK SALDELTFRP CSEEQRASYQ KLDALTELYR
DPQFQQINNF MTDFKKWLDG GFSTAVEGDA KAIRLEPFQK NLLIHVIFFI AVTKIPVLAN
RVLQYLIHAF QIDFLSQTSI DIFKQKATVF LVPRRHGKTW FIIPIISFLL KHMIGISIGY
VAHQKHVSQF VLKEVEFRCR HTFARDYVVE NKDNVISIDH RGAKSTALFA SCYNTNSIRG
QNFHLLLVDE AHFIKKEAFN TILGFLAQNT TKIIFISSTN TTSDATCFLT RLNNAPFDML
NVVSYVCEEH LHSFTEKGDA TACPCYRLHK PTFISLNSQV RKTANMFMPG AFMDEIIGGT
NKISQNTVLI TDQSREEFDI LRYSTLNTNA YDYFGKTLYV YLDPAFTTNR KASGTGVAAV
GAYRHQFLIY GLEHFFLRDL SESSEVAIAE CAAHMIISVL SLHPYLDELR IAVEGNTNQA
AAVRIACLIR QSVQSSTLIR VLFYHTPDQN HIEQPFYLMG RDKALAVEQF ISRFNSGYIK
ASQELVSYTI KLSHDPIEYL LEQIQNLHRV TLAEGTTARY SAKRQNRISD DLIIAVIMAT
YLCDDIHAIR FRVS
