ID G9B6K7_9ADEN Unreviewed; 202 AA. AC G9B6K7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 20-DEC-2017, entry version 23. DE RecName: Full=Protease {ECO:0000256|HAMAP-Rule:MF_04059}; DE EC=3.4.22.39 {ECO:0000256|HAMAP-Rule:MF_04059}; DE AltName: Full=Adenain {ECO:0000256|HAMAP-Rule:MF_04059}; DE AltName: Full=Adenovirus protease {ECO:0000256|HAMAP-Rule:MF_04059}; DE Short=AVP {ECO:0000256|HAMAP-Rule:MF_04059}; DE AltName: Full=Adenovirus proteinase {ECO:0000256|HAMAP-Rule:MF_04059}; DE AltName: Full=Endoprotease {ECO:0000256|HAMAP-Rule:MF_04059}; GN Name=L3 {ECO:0000256|HAMAP-Rule:MF_04059}; 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. Late in adenovirus infection, in the CC cytoplasm, may participate in the cytoskeleton destruction. CC Cleaves host cell cytoskeletal keratins K7 and K18. CC {ECO:0000256|HAMAP-Rule:MF_04059}. CC -!- CATALYTIC ACTIVITY: Cleaves adenovirus and host cell proteins at CC two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly- CC Xaa-|-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino CC acid). {ECO:0000256|HAMAP-Rule:MF_04059}. 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 -!- ENZYME REGULATION: Requires DNA and protease cofactor for maximal CC activation. Inside nascent virions, becomes partially activated by CC binding to the viral DNA, allowing it to cleave the cofactor that CC binds to the protease and fully activates it. Actin, like the CC viral protease cofactor, seems to act as a cofactor in the CC cleavage of cytokeratin 18 and of actin itself. CC {ECO:0000256|HAMAP-Rule:MF_04059}. CC -!- SUBUNIT: Interacts with protease cofactor pVI-C; this interaction CC is necessary for protease activation. {ECO:0000256|HAMAP- CC Rule:MF_04059}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|HAMAP-Rule:MF_04059}. CC Host nucleus {ECO:0000256|HAMAP-Rule:MF_04059}. Note=Present in CC about 10 copies per virion. {ECO:0000256|HAMAP-Rule:MF_04059}. CC -!- INDUCTION: Expressed in the late phase of the viral replicative CC cycle. {ECO:0000256|HAMAP-Rule:MF_04059}. CC -!- MISCELLANEOUS: All late proteins expressed from the major late CC promoter are produced by alternative splicing and alternative CC polyadenylation of the same gene giving rise to non-overlapping CC ORFs. A leader sequence is present in the N-terminus of all these CC mRNAs and is recognized by the viral shutoff protein to provide CC expression although conventional translation via ribosome scanning CC from the cap has been shut off in the host cell. CC {ECO:0000256|HAMAP-Rule:MF_04059}. CC -!- SIMILARITY: Belongs to the peptidase C5 family. CC {ECO:0000256|HAMAP-Rule:MF_04059, 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 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 HAMAP; MF_04059; ADV_PRO; 1. 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 2: Evidence at transcript level; KW Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_04059, KW ECO:0000256|PIRNR:PIRNR001218}; KW Complete proteome {ECO:0000313|Proteomes:UP000169712}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04059}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_04059}; KW Host nucleus {ECO:0000256|HAMAP-Rule:MF_04059}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04059, KW ECO:0000256|PIRNR:PIRNR001218}; KW Late protein {ECO:0000256|HAMAP-Rule:MF_04059, KW ECO:0000256|PIRNR:PIRNR001218}; Membrane {ECO:0000256|SAM:Phobius}; KW Protease {ECO:0000256|HAMAP-Rule:MF_04059, KW ECO:0000256|PIRNR:PIRNR001218, ECO:0000313|EMBL:ADP30823.1}; KW Thiol protease {ECO:0000256|HAMAP-Rule:MF_04059, KW ECO:0000256|PIRNR:PIRNR001218}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04059}. FT TRANSMEM 114 134 Helical. {ECO:0000256|SAM:Phobius}. FT ACT_SITE 53 53 {ECO:0000256|HAMAP-Rule:MF_04059, FT ECO:0000256|PIRSR:PIRSR001218-1}. FT ACT_SITE 70 70 {ECO:0000256|HAMAP-Rule:MF_04059, FT ECO:0000256|PIRSR:PIRSR001218-1}. FT ACT_SITE 120 120 {ECO:0000256|HAMAP-Rule:MF_04059, FT ECO:0000256|PIRSR:PIRSR001218-1}. FT SITE 50 51 Cleavage; by autolysis. FT {ECO:0000256|HAMAP-Rule:MF_04059}. FT DISULFID 102 102 Interchain (with C-10 in cleaved protease FT cofactor pVI-C). {ECO:0000256|HAMAP-Rule: FT MF_04059}. 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 //