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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
 
 
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