ID G9B6K7_9ADEN Unreviewed; 202 AA. AC G9B6K7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 25-OCT-2017, entry version 21. 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 Skua adenovirus 1. OC Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Siadenovirus. OX NCBI_TaxID=1520004 {ECO:0000313|EMBL:ADP30823.1, ECO:0000313|Proteomes:UP000169712}; RN [1] {ECO:0000313|EMBL:ADP30823.1, ECO:0000313|Proteomes:UP000169712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T03 {ECO:0000313|EMBL:ADP30823.1}; RX PubMed=22078165; DOI=10.1016/j.virol.2011.10.008; RA Park Y.M., Kim J.H., Gu S.H., Lee S.Y., Lee M.G., Kang Y.K., RA Kang S.H., Kim H.J., Song J.W.; RT "Full genome analysis of a novel adenovirus from the South Polar skua RT (Catharacta maccormicki) in Antarctica."; RL Virology 422:144-150(2012). 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; HM585353; ADP30823.1; -; Genomic_DNA. DR RefSeq; YP_004935940.1; NC_016437.1. DR MEROPS; C05.001; -. DR GeneID; 11467757; -. DR KEGG; vg:11467757; -. DR Proteomes; UP000169712; Genome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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 Complete proteome {ECO:0000313|Proteomes:UP000169712}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR001218}; KW Late protein {ECO:0000256|PIRNR:PIRNR001218}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Protease {ECO:0000256|PIRNR:PIRNR001218, ECO:0000313|EMBL:ADP30823.1}; KW Thiol protease {ECO:0000256|PIRNR:PIRNR001218}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 114 134 Helical. {ECO:0000256|SAM:Phobius}. FT ACT_SITE 53 53 {ECO:0000256|PIRSR:PIRSR001218-1}. FT ACT_SITE 70 70 {ECO:0000256|PIRSR:PIRSR001218-1}. FT ACT_SITE 120 120 {ECO:0000256|PIRSR:PIRSR001218-1}. SQ SEQUENCE 202 AA; 23215 MW; 5F4D119752D35DE7 CRC64; MGTSDTELKH LCKSLGITNF IGVFDRNFPG FLDTSRVACA IVNTGDFSSG GVHYIAYAFD PNSFKFYMFD PFGWSKKDLL KIYQFQYDRM VKYTALNTPT RCVRLIKSIQ AVQCLCSGAC GLYCVLFLAS FTYYRHSPMG KNPIIDVVDG IPISMLNTPY GTCVTHCNQR KLYDWFYVHS MYFRKHVRRI THNTRINSIQ AH //