TRM1_HHV7J
ID TRM1_HHV7J Reviewed; 721 AA.
AC P52385;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Tripartite terminase subunit 1 {ECO:0000255|HAMAP-Rule:MF_04014};
GN Name=TRM1 {ECO:0000255|HAMAP-Rule:MF_04014}; OrderedLocusNames=U40;
OS Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=57278;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA Nicholas J.;
RT "Determination and analysis of the complete nucleotide sequence of human
RT herpesvirus.";
RL J. Virol. 70:5975-5989(1996).
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; U43400; AAC54702.1; -; Genomic_DNA.
DR PIR; T41942; T41942.
DR SMR; P52385; -.
DR PRIDE; P52385; -.
DR Proteomes; UP000009246; 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..721
FT /note="Tripartite terminase subunit 1"
FT /id="PRO_0000115884"
FT ZN_FING 189..217
FT /note="C3H1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
FT BINDING 625..632
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04014"
SQ SEQUENCE 721 AA; 83167 MW; BE5BED64E46EC9CC CRC64;
MNSLQSLCVL CSRLSECALE LECLRFCDPV TLIPDMTNFR KNGVVIIHLF KTLFAELCHQ
NFNCASPVTI YLQILLKAMY NQVLLLDASI HQFLLDNDKQ KYFENIFQLN ECKQHLKLDL
ALNNYLTFSV DISTINDIEK LLCKMNCIFG LISPLDGINA CSQIIEFLTI LCGVCVVMKP
EVFSETTTCL KCYEELSLVP NQGKSIRKRL AGKFCNHLTE THMVSNLEKN VDIIEKDLDF
STKQYGLVKE YMAKITNIFQ QQLYSKPPHL QEAENTLINF DLFSKIPDTI YSLSEFTYWS
KISESVIQKA SITLNQLNLC HSLYADLQNE ISKFLYGETI QDVFNFNEEN VTNDDKLYIG
SRFISPCRLV DIITNVSIKN LEEDPVFTKL AEEDEIQTKI KTLLNELENS AHETVPKKYV
THSMTQDHNL QQEIHIRKKA YYQKISESGY SKVMLCIKEQ EALINKLMNI NILGNHIFES
LSKMMNAFAN RQLQSLENFS ADPFTYDDHL YIKNNLLSKK LPQELLPNLS QEMYRLLTGP
LSNYHTASFP LSSNISMAYA CDVADFLPHM KEDLAKCVEG TIYPENWMLC TYNKFFNFDG
LHNINDMQRQ MWNFIRELVL SVALYNDVFG KQLSIVKFGE ETETVEKILL TFDSGSPLLF
KRGTTTTKFN DLYSLLYFDL KTQCDPVQIS QTKQVSHIPA PNLLDLCRQN ENSIPECFYN
F