TRM1_HCMVA
ID TRM1_HCMVA Reviewed; 850 AA.
AC P16724; Q7M6M7;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [2]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [3]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
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 -!- 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; X17403; CAA35371.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00161.1; -; Genomic_DNA.
DR PIR; S09819; WMBE56.
DR SMR; P16724; -.
DR ChEMBL; CHEMBL3991482; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; 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_0000115890"
FT ZN_FING 191..219
FT /note="C3H1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT REGION 438..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..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 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"
SQ SEQUENCE 850 AA; 95868 MW; C32A91906D4FFE7D 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
PEGEAIHLRG REAMSGTGTT LMTASNSSNS STHSQRNNGG GGRARGGGKK VVGGGVNGQD
GDGSENGLRV RNCDEHEALD LVDARSRIHN VTREVNVRKR AYLQKVSEVG YGKVIRCIKT
QERLTSKLID VNLVGPLCLD FISKLMNGFL YRSQYHQDQD VVDVGDQFTY DEHLYVVNNL
IHKSLPVESL PLLGQQIYEL CNGPLFTHCT DRYPLSHNVD MAYACDNAGV LPHVKDDLVK
CAEGTVYPSE WMVVKYMGFF NFSDCQDLNV LQKEMWMHVR ELVLSVALYN ETFGKQLSIA
CLRDELHPDR DVILTYNKEW PLLLRHEGSL YKSKDLYLLL YRHLSRPDES GDVPTAPVAK
PSTLTAAAAV SGVFREPDRP WLPSPYPSSS TAGVSRRVRA TRKRPRRASS LLDLARDEHG
IQDLVPGSLR
