ID G9B6K7_9ADEN Unreviewed; 202 AA. AC G9B6K7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 02-OCT-2024, entry version 57. 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; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes; OC Rowavirales; Adenoviridae; Siadenovirus; Skua siadenovirus A. 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., Kang S.H., RA 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 mature CC virions. Protease complexed to its cofactor slides along the viral DNA CC to specifically locate and cleave the viral precursors. Mature virions CC have a weakened organization compared to the unmature virions, thereby CC facilitating subsequent uncoating. Without maturation, the particle CC lacks infectivity and is unable to uncoat. Late in adenovirus CC infection, in the cytoplasm, may participate in the cytoskeleton CC destruction. Cleaves host cell cytoskeletal keratins K7 and K18. CC {ECO:0000256|HAMAP-Rule:MF_04059}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Cleaves proteins of the adenovirus and its host cell at two CC consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly-Xaa-|- CC Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid).; CC EC=3.4.22.39; Evidence={ECO:0000256|HAMAP-Rule:MF_04059, CC ECO:0000256|PIRNR:PIRNR001218}; CC -!- ACTIVITY 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 binds CC to the protease and fully activates it. Actin, like the viral protease CC cofactor, seems to act as a cofactor in the cleavage of cytokeratin 18 CC and of actin itself. {ECO:0000256|HAMAP-Rule:MF_04059}. CC -!- SUBUNIT: Interacts with protease cofactor pVI-C; this interaction is CC necessary for protease activation. {ECO:0000256|HAMAP-Rule:MF_04059}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|HAMAP-Rule:MF_04059}. Host CC nucleus {ECO:0000256|HAMAP-Rule:MF_04059}. Note=Present in about 10 CC copies per virion. {ECO:0000256|HAMAP-Rule:MF_04059}. CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle. CC {ECO:0000256|HAMAP-Rule:MF_04059}. CC -!- MISCELLANEOUS: All late proteins expressed from the major late promoter CC are produced by alternative splicing and alternative polyadenylation of CC the same gene giving rise to non-overlapping ORFs. A leader sequence is CC present in the N-terminus of all these mRNAs and is recognized by the CC viral shutoff protein to provide expression although conventional CC translation via ribosome scanning from the cap has been shut off in the CC host cell. {ECO:0000256|HAMAP-Rule:MF_04059}. CC -!- SIMILARITY: Belongs to the peptidase C5 family. {ECO:0000256|HAMAP- CC 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 KEGG; vg:11467757; -. DR OrthoDB; 9248at10239; -. DR Proteomes; UP000169712; Genome. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR HAMAP; MF_04059; ADV_PRO; 1. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR InterPro; IPR000855; Peptidase_C5. DR Pfam; PF00770; Peptidase_C5; 1. DR PIRSF; PIRSF001218; Protease_ADV; 1. DR PRINTS; PR00703; ADVENDOPTASE. DR SUPFAM; SSF54001; Cysteine proteinases; 1. PE 2: Evidence at transcript level; KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP- KW Rule:MF_04059}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP- KW Rule:MF_04059}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_04059}; KW Host nucleus {ECO:0000256|ARBA:ARBA00022562, ECO:0000256|HAMAP- KW Rule:MF_04059}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04059, ECO:0000256|PIRNR:PIRNR001218}; KW Late protein {ECO:0000256|ARBA:ARBA00022921, ECO:0000256|HAMAP- KW Rule:MF_04059}; Membrane {ECO:0000256|SAM:Phobius}; KW Protease {ECO:0000256|HAMAP-Rule:MF_04059, ECO:0000256|PIRNR:PIRNR001218}; KW Thiol protease {ECO:0000256|HAMAP-Rule:MF_04059, KW ECO:0000256|PIRNR:PIRNR001218}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04059}. FT TRANSMEM 114..134 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT ACT_SITE 53 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04059, FT ECO:0000256|PIRSR:PIRSR001218-1" FT ACT_SITE 70 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04059, FT ECO:0000256|PIRSR:PIRSR001218-1" FT ACT_SITE 120 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04059, FT ECO:0000256|PIRSR:PIRSR001218-1" FT SITE 50..51 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04059" FT DISULFID 102 FT /note="Interchain (with C-10 in cleaved protease cofactor FT pVI-C)" FT /evidence="ECO:0000256|HAMAP-Rule: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 //