TRM1_HCMVM
ID TRM1_HCMVM Reviewed; 850 AA.
AC F5HC79;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014}; OrderedLocusNames=UL56;
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).
RN [2]
RP FUNCTION, AND DOMAIN.
RX PubMed=12595550; DOI=10.1093/nar/gkg229;
RA Scholz B., Rechter S., Drach J.C., Townsend L.B., Bogner E.;
RT "Identification of the ATP-binding site in the terminase subunit pUL56 of
RT human cytomegalovirus.";
RL Nucleic Acids Res. 31:1426-1433(2003).
RN [3]
RP DOMAIN.
RX PubMed=18771048;
RA Champier G., Couvreux A., Hantz S., Rametti A., Mazeron M.C., Bouaziz S.,
RA Denis F., Alain S.;
RT "Putative functional domains of human cytomegalovirus pUL56 involved in
RT dimerization and benzimidazole D-ribonucleoside activity.";
RL Antivir. Ther. 13:643-654(2008).
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 TRM2 and TRM3 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. TRM1 carries an endonuclease activity
CC that plays an important role for the cleavage of concatemeric viral DNA
CC into unit length genomes. {ECO:0000255|HAMAP-Rule:MF_04014,
CC ECO:0000269|PubMed:12595550}.
CC -!- SUBUNIT: Associates with TRM2 and TRM3 to form the tripartite terminase
CC complex. Interacts with portal protein. {ECO:0000255|HAMAP-
CC Rule:MF_04014}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04014}.
CC Note=Found associated with the external surface of the viral capsid
CC during assembly and DNA packaging, but seems absent in extracellular
CC mature virions. {ECO:0000255|HAMAP-Rule:MF_04014}.
CC -!- SIMILARITY: Belongs to the herpesviridae TRM1 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04014}.
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DR EMBL; AY446894; AAR31621.1; -; Genomic_DNA.
DR RefSeq; YP_081515.1; NC_006273.2.
DR SMR; F5HC79; -.
DR DrugBank; DB12070; Letermovir.
DR DrugCentral; F5HC79; -.
DR PRIDE; F5HC79; -.
DR GeneID; 3077457; -.
DR KEGG; vg:3077457; -.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016485; P:protein processing; IEA:UniProtKB-UniRule.
DR GO; GO:0019069; P:viral capsid assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0019073; P:viral DNA genome packaging; IEA:InterPro.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04014; HSV_TRM1; 1.
DR InterPro; IPR000501; UL28/UL56.
DR Pfam; PF01366; PRTP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Host nucleus; Late protein; Metal-binding; Nucleotide-binding;
KW Reference proteome; Viral genome packaging; Viral release from host cell;
KW Zinc; Zinc-finger.
FT CHAIN 1..850
FT /note="Tripartite terminase subunit 1"
FT /id="PRO_0000436183"
FT ZN_FING 191..219
FT /note="C3H1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04014,
FT ECO:0000305|PubMed:18771048"
FT REGION 438..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 822..827
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04014,
FT ECO:0000305|PubMed:18771048"
FT COMPBIAS 438..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 709..716
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04014,
FT ECO:0000269|PubMed:12595550"
SQ SEQUENCE 850 AA; 95811 MW; DB388A772024D113 CRC64;
MEMNLLQKLC VVCSKCNEYA MELECLKYCD PNVLLAESTP FKRNAAAIVY LYRKIYPEVV
AQNRTQSSLL TLYLEMLLKA LHEDTALLDR ALMAYSRQPD RAAFYRTVLR LDRCDRHHTV
ELQFTDNVRF SVSLATLNDI ERFLCKMNYV YGILAPEAGL EVCAQLLELL RRLCGISPVA
RQEVYVEGTT CAQCYEELTI IPNQGRSLNK RLQGLLCNHI AVHRPSSQSD VNIQTVEQDL
LDLTTRIPHL AGVLSALKSL FSSSSAYHSY IQEAEEALRE YNLFTDIPER IYSLSDFTYW
SRTSEVIVKR VGITIQQLNV YHQLCRALMN GISRHLYGED VEDIFVLGEK ALDGEERMFV
GSVFAAPNRI IDLITSLSIQ AFEDNPVFNK LHESNEMYTK IKHILEEIRR PLPDGTGGDG
PEGEVIHLRG REAMSGTGTT LMTASNSSNS STHSQRNNGG GGRARGGGKK AVGGGANGQD
GDGSENGLRV RNCDEHEALD LVDARSRIHN VTREVNVRKR AYLQKVSEVG YGKVIRCIKT
QERLTSKLID VNLVGPLCLD FISKLMNGFL YRSQYHQDQD VVDVGNQFTY DEHLYVVNNL
IHKSLPVESL PLLGQQIYEL CNGPLFTHCT DRYPLSHNVD MAYACDNAGV LPHVKDDLVK
CAEGTVYPSE WMVVKYMGFF NFSDCQDLNV LQKEMWMHVR ELVLSVALYN ETFGKQLSIA
CLRDELHPDR DVILTYNKEW PLLLRHEGSL YKSKDLYLLL YRHLSRPDES GDVPTAPVAK
PSTLTAAAAV SGAFREPDRP WLPSPYPSSS TAGVSRRVRA TRKRPRRASS LLDLARDEHG
IQDLVPGSLR
