Tripartite terminase subunit 1

Details

Name
Tripartite terminase subunit 1
Synonyms
Not Available
Gene Name
TRM1
Organism
Human Cytomegalovirus
Amino acid sequence
>lcl|BSEQ0051322|Tripartite terminase subunit 1
MEMNLLQKLCVVCSKCNEYAMELECLKYCDPNVLLAESTPFKRNAAAIVYLYRKIYPEVV
AQNRTQSSLLTLYLEMLLKALHEDTALLDRALMAYSRQPDRAAFYRTVLRLDRCDRHHTV
ELQFTDNVRFSVSLATLNDIERFLCKMNYVYGILAPEAGLEVCAQLLELLRRLCGISPVA
RQEVYVEGTTCAQCYEELTIIPNQGRSLNKRLQGLLCNHIAVHRPSSQSDVNIQTVEQDL
LDLTTRIPHLAGVLSALKSLFSSSSAYHSYIQEAEEALREYNLFTDIPERIYSLSDFTYW
SRTSEVIVKRVGITIQQLNVYHQLCRALMNGISRHLYGEDVEDIFVLGEKALDGEERMFV
GSVFAAPNRIIDLITSLSIQAFEDNPVFNKLHESNEMYTKIKHILEEIRRPLPDGTGGDG
PEGEVIHLRGREAMSGTGTTLMTASNSSNSSTHSQRNNGGGGRARGGGKKAVGGGANGQD
GDGSENGLRVRNCDEHEALDLVDARSRIHNVTREVNVRKRAYLQKVSEVGYGKVIRCIKT
QERLTSKLIDVNLVGPLCLDFISKLMNGFLYRSQYHQDQDVVDVGNQFTYDEHLYVVNNL
IHKSLPVESLPLLGQQIYELCNGPLFTHCTDRYPLSHNVDMAYACDNAGVLPHVKDDLVK
CAEGTVYPSEWMVVKYMGFFNFSDCQDLNVLQKEMWMHVRELVLSVALYNETFGKQLSIA
CLRDELHPDRDVILTYNKEWPLLLRHEGSLYKSKDLYLLLYRHLSRPDESGDVPTAPVAK
PSTLTAAAAVSGAFREPDRPWLPSPYPSSSTAGVSRRVRATRKRPRRASSLLDLARDEHG
IQDLVPGSLR
Number of residues
850
Molecular Weight
95810.305
Theoretical pI
Not Available
GO Classification
Functions
ATP binding / metal ion binding
Processes
viral DNA genome packaging / viral release from host cell
Components
host cell nucleus
General Function
Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.
Specific Function
Atp binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Host nucleus
Gene sequence
>lcl|BSEQ0051323|Tripartite terminase subunit 1 (TRM1)
ATGGAGATGAATTTGTTACAGAAACTATGCGTAGTGTGTTCGAAATGCAACGAATACGCC
ATGGAGCTGGAGTGTCTAAAGTACTGCGATCCGAACGTGTTACTGGCGGAGTCCACGCCG
TTCAAGAGAAACGCGGCGGCTATAGTGTATCTGTACCGGAAGATCTACCCGGAGGTGGTG
GCGCAGAATCGTACGCAGAGTTCGCTGCTGACTCTCTATCTGGAGATGCTGCTGAAGGCG
CTGCACGAGGATACGGCTTTGCTGGATCGGGCGCTGATGGCCTACTCGCGCCAGCCGGAC
CGGGCGGCCTTCTACCGTACCGTCCTCCGTTTGGATCGCTGCGATCGCCATCACACCGTG
GAGCTCCAGTTTACGGACAACGTCCGTTTCAGCGTCAGTCTGGCCACACTCAACGACATC
GAGCGCTTCCTGTGCAAAATGAACTACGTGTACGGGATCCTGGCGCCGGAGGCCGGCCTG
GAGGTCTGCGCGCAGCTGCTGGAGCTCCTCCGTCGCCTATGCGGCATCTCGCCGGTGGCG
CGTCAGGAAGTGTACGTCGAAGGGACGACATGCGCCCAATGCTACGAGGAGCTGACCATC
ATCCCGAATCAGGGCCGCTCGCTGAACAAGCGGCTGCAGGGCTTGCTGTGCAACCATATA
GCGGTCCACCGTCCGTCAAGCCAGTCCGATGTGAATATCCAGACGGTGGAGCAGGACCTG
CTGGACCTGACAACGCGCATCCCCCACTTGGCTGGAGTCCTTTCGGCCCTCAAAAGCCTA
TTCTCTTCTTCATCGGCCTACCACAGCTACATCCAGGAGGCGGAGGAGGCGCTGAGGGAG
TACAACCTGTTTACGGATATACCGGAACGAATATATTCCTTGTCGGATTTTACCTACTGG
TCCCGTACCTCGGAGGTTATCGTCAAGCGGGTGGGCATCACCATCCAGCAGCTAAATGTG
TATCACCAGCTGTGCCGGGCGCTCATGAACGGCATCAGTCGCCATCTGTACGGGGAGGAC
GTGGAGGACATCTTCGTGCTCGGGGAAAAGGCGTTGGACGGGGAGGAGCGCATGTTCGTG
GGGTCGGTCTTTGCCGCCCCCAACAGGATCATCGACCTCATCACATCCCTCAGCATTCAA
GCTTTCGAGGACAACCCGGTGTTCAACAAGCTCCACGAAAGCAACGAGATGTACACCAAA
ATCAAGCATATTCTCGAGGAGATTCGACGTCCGCTGCCCGATGGCACGGGGGGCGACGGC
CCCGAGGGCGAGGTTATTCACCTGCGTGGACGGGAGGCGATGTCGGGGACGGGTACGACT
TTGATGACGGCCAGCAACAGCAGCAACAGCAGTACTCACAGTCAGAGGAATAACGGTGGC
GGCGGCCGGGCCCGTGGAGGAGGCAAGAAAGCTGTAGGGGGAGGGGCGAATGGGCAGGAC
GGCGACGGCAGCGAAAACGGCTTACGGGTGCGCAACTGCGACGAACACGAAGCTCTCGAC
TTGGTGGACGCGCGTTCCCGCATCCACAACGTCACCCGCGAGGTGAACGTGCGCAAACGC
GCCTACCTGCAGAAGGTCTCGGAGGTGGGCTATGGCAAGGTGATCCGTTGCATCAAAACG
CAGGAGCGTCTGACTAGCAAACTCATCGATGTCAACCTAGTGGGGCCCTTGTGTCTGGAC
TTTATCTCTAAGCTCATGAATGGGTTTCTATACCGCAGCCAATACCACCAGGACCAAGAC
GTGGTGGACGTGGGGAATCAGTTCACGTACGATGAGCACCTGTATGTGGTCAATAACCTG
ATCCACAAGAGTCTGCCTGTGGAATCCCTCCCGCTACTGGGTCAGCAGATCTACGAGTTG
TGTAACGGGCCCCTCTTCACACACTGTACCGATCGCTATCCCCTCTCTCACAATGTGGAC
ATGGCCTATGCCTGCGACAACGCGGGCGTACTACCCCACGTCAAGGACGATTTGGTCAAA
TGCGCGGAAGGTACCGTGTATCCCAGTGAGTGGATGGTGGTGAAGTACATGGGTTTTTTC
AATTTTTCGGACTGTCAGGACCTAAACGTGCTGCAGAAGGAGATGTGGATGCACGTGCGG
GAGCTCGTGCTCTCCGTCGCACTATATAATGAAACTTTCGGGAAACAACTCTCGATCGCG
TGCCTGCGCGACGAACTGCACCCGGACAGAGATGTGATTCTCACGTATAACAAAGAGTGG
CCGCTGCTGCTTCGTCACGAAGGAAGTCTTTATAAGTCCAAAGATCTATATCTCCTCCTC
TACAGGCATCTGTCCAGACCGGATGAGAGTGGCGACGTGCCAACAGCTCCCGTGGCCAAG
CCCTCCACCCTGACGGCCGCCGCGGCCGTCTCGGGTGCCTTCAGGGAGCCGGACCGACCT
TGGCTGCCAAGTCCGTACCCCTCCTCCTCGACCGCGGGCGTTTCCCGGAGGGTCCGCGCA
ACACGCAAGAGACCACGACGCGCCTCATCGCTGCTGGATTTGGCCCGCGACGAACATGGA
ATCCAGGATCTGGTGCCTGGTAGTCTGCGTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDF5HC79
UniProtKB Entry NameTRM1_HCMVM
General References
  1. Dolan A, Cunningham C, Hector RD, Hassan-Walker AF, Lee L, Addison C, Dargan DJ, McGeoch DJ, Gatherer D, Emery VC, Griffiths PD, Sinzger C, McSharry BP, Wilkinson GW, Davison AJ: Genetic content of wild-type human cytomegalovirus. J Gen Virol. 2004 May;85(Pt 5):1301-12. [PubMed:15105547]
  2. Scholz B, Rechter S, Drach JC, Townsend LB, Bogner E: Identification of the ATP-binding site in the terminase subunit pUL56 of human cytomegalovirus. Nucleic Acids Res. 2003 Mar 1;31(5):1426-33. [PubMed:12595550]
  3. Champier G, Couvreux A, Hantz S, Rametti A, Mazeron MC, Bouaziz S, Denis F, Alain S: Putative functional domains of human cytomegalovirus pUL56 involved in dimerization and benzimidazole D-ribonucleoside activity. Antivir Ther. 2008;13(5):643-54. [PubMed:18771048]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB12070Letermovirapproved, investigationalyesinhibitorDetails