ID U5NE79_9ADEN Unreviewed; 206 AA. AC U5NE79; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=Protease {ECO:0000256|PIRNR:PIRNR001218}; DE EC=3.4.22.39 {ECO:0000256|PIRNR:PIRNR001218}; DE AltName: Full=Adenain {ECO:0000256|PIRNR:PIRNR001218}; OS Turkey aviadenovirus 5. OC Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Aviadenovirus; OC Turkey aviadenovirus D. OX NCBI_TaxID=1408258 {ECO:0000313|EMBL:AGX93379.1}; RN [1] {ECO:0000313|EMBL:AGX93379.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D1648 {ECO:0000313|EMBL:AGX93379.1}; RX PubMed=24077297; DOI=10.1099/vir.0.057711-0; RA Marek A., Ballmann M.Z., Kosiol C., Harrach B., Schlotterer C., RA Hess M.; RT "Whole-genome sequences of two turkey adenovirus types reveal the RT existence of two unknown lineages that merit the establishment of RT novel species within the genus Aviadenovirus."; RL J. Gen. Virol. 95:156-170(2014). CC -!- FUNCTION: Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, CC pVIII, and pX) inside newly assembled particles giving rise to CC mature virions. Protease complexed to its cofactor slides along CC the viral DNA to specifically locate and cleave the viral CC precursors. Mature virions have a weakened organization compared CC to the unmature virions, thereby facilitating subsequent CC uncoating. Without maturation, the particle lacks infectivity and CC is unable to uncoat. {ECO:0000256|PIRNR:PIRNR001218}. CC -!- CATALYTIC ACTIVITY: Cleaves proteins of the adenovirus and its CC host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and - CC Yaa-Xaa-Gly-Xaa-|-Gly- (in which Yaa is Met, Ile or Leu, and Xaa CC is any amino acid). {ECO:0000256|PIRNR:PIRNR001218}. CC -!- SIMILARITY: Belongs to the peptidase C5 family. CC {ECO:0000256|PIRNR:PIRNR001218}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KF477314; AGX93379.1; -; Genomic_DNA. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR InterPro; IPR000855; Peptidase_C5. DR Pfam; PF00770; Peptidase_C5; 1. DR PIRSF; PIRSF001218; Protease_ADV; 1. DR PRINTS; PR00703; ADVENDOPTASE. DR ProDom; PD003705; Peptidase_C5; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage {ECO:0000256|PIRNR:PIRNR001218}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR001218}; KW Late protein {ECO:0000256|PIRNR:PIRNR001218}; KW Protease {ECO:0000256|PIRNR:PIRNR001218, ECO:0000313|EMBL:AGX93379.1}; KW Thiol protease {ECO:0000256|PIRNR:PIRNR001218}. FT ACT_SITE 55 55 {ECO:0000256|PIRSR:PIRSR001218-1}. FT ACT_SITE 72 72 {ECO:0000256|PIRSR:PIRSR001218-1}. FT ACT_SITE 122 122 {ECO:0000256|PIRSR:PIRSR001218-1}. SQ SEQUENCE 206 AA; 23839 MW; 86EECA321927910A CRC64; MAGTTETQLR DLLASMHLRH RFLGVFDKDF PGFLNPKMPA SAIVNTGSRA SGGMHWIGFA FDPAAGRCYM FDPFGWSDRE LWELYRVKYD AFMKRTGLRQ PDRCFDLVRS TEAVQCPCSA ACGLFSALFI VSFDRYRTRP MSGNPVIDTV VGVKHSKMEE PLYRDILHRN QERLYFWWIK HSAYFRAHQE RFKRETALDS VPEGHA //