ID PRO_ADEF1 Reviewed; 204 AA. AC Q9IIH4; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 14-DEC-2022, entry version 68. DE RecName: Full=Protease {ECO:0000255|HAMAP-Rule:MF_04059}; DE EC=3.4.22.39 {ECO:0000255|HAMAP-Rule:MF_04059}; DE AltName: Full=Adenain {ECO:0000255|HAMAP-Rule:MF_04059}; DE AltName: Full=Adenovirus protease {ECO:0000255|HAMAP-Rule:MF_04059}; DE Short=AVP {ECO:0000255|HAMAP-Rule:MF_04059}; DE AltName: Full=Adenovirus proteinase {ECO:0000255|HAMAP-Rule:MF_04059}; DE AltName: Full=Endoprotease {ECO:0000255|HAMAP-Rule:MF_04059}; GN Name=L3 {ECO:0000255|HAMAP-Rule:MF_04059}; OS Frog adenovirus 1 (strain ATCC VR-896) (FrAdV-1). OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes; OC Rowavirales; Adenoviridae; Siadenovirus. OX NCBI_TaxID=114102; OH NCBI_TaxID=8404; Lithobates pipiens (Northern leopard frog) (Rana pipiens). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Isolate ATCC VR-896; RA Davison A.J., Wright K.M., Harrach B.; RT "Phylogenetic position of an amphibian adenovirus."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. 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:0000255|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:0000255|HAMAP-Rule:MF_04059}; 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:0000255|HAMAP-Rule:MF_04059}. CC -!- SUBUNIT: Interacts with protease cofactor pVI-C; this interaction is CC necessary for protease activation. {ECO:0000255|HAMAP-Rule:MF_04059}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04059}. Host CC nucleus {ECO:0000255|HAMAP-Rule:MF_04059}. Note=Present in about 10 CC copies per virion. {ECO:0000255|HAMAP-Rule:MF_04059}. CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle. CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_04059}. CC -!- SIMILARITY: Belongs to the peptidase C5 family. {ECO:0000255|HAMAP- CC Rule:MF_04059}. 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; AF224336; AAF86933.1; -; Genomic_DNA. DR RefSeq; NP_062444.1; NC_002501.1. DR SMR; Q9IIH4; -. DR MEROPS; C05.001; -. DR GeneID; 1732705; -. DR KEGG; vg:1732705; -. DR Proteomes; UP000009247; Genome. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. 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 3: Inferred from homology; KW Autocatalytic cleavage; Disulfide bond; DNA-binding; Host nucleus; KW Hydrolase; Late protein; Protease; Reference proteome; Thiol protease; KW Virion. FT CHAIN 1..204 FT /note="Protease" FT /id="PRO_0000218042" FT ACT_SITE 54 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059" FT ACT_SITE 71 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059" FT ACT_SITE 121 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059" FT SITE 51..52 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059" FT DISULFID 103 FT /note="Interchain (with C-10 in cleaved protease cofactor FT pVI-C)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059" SQ SEQUENCE 204 AA; 23222 MW; 91DC0B01544577A5 CRC64; MGTSGADLEN IVLSLGLHSG FLGIFDKHFP GFLNVNKPSF AIVNTGDIIQ GGLHWIAFAF DNVTSTFFMF DPFGWSDMEL YRKYEFQYHR ILKSTALTKP SRCIKLVKSK EAVQCTCSAA CGLFCCLFLA SFYHYPTFPM RGNPIIDLVD GIPPTKLHSS YGIYLTHCNQ KKLIAWLLSN SAYFRKNAML MIHNTRLYYL YTHL //