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-AUG-2020, entry version 21. 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 Turkey aviadenovirus 5. OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes; OC Rowavirales; Adenoviridae; Aviadenovirus; Turkey aviadenovirus D. OX NCBI_TaxID=1408258 {ECO:0000313|EMBL:AGX93379.1, ECO:0000313|Proteomes:UP000315075}; RN [1] {ECO:0000313|EMBL:AGX93379.1, ECO:0000313|Proteomes:UP000315075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., Hess M.; RT "Whole-genome sequences of two turkey adenovirus types reveal the existence RT of two unknown lineages that merit the establishment of novel species RT 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 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; KF477314; AGX93379.1; -; Genomic_DNA. DR Proteomes; UP000315075; Genome. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. 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; SSF54001; 1. PE 2: Evidence at transcript level; KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP- KW Rule:MF_04059, ECO:0000256|PIRNR:PIRNR001218}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04059}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_04059}; Host nucleus {ECO:0000256|HAMAP-Rule:MF_04059}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04059, ECO:0000256|PIRNR:PIRNR001218}; KW Late protein {ECO:0000256|HAMAP-Rule:MF_04059, KW ECO:0000256|PIRNR:PIRNR001218}; KW Protease {ECO:0000256|HAMAP-Rule:MF_04059, ECO:0000256|PIRNR:PIRNR001218, KW ECO:0000313|EMBL:AGX93379.1}; KW Thiol protease {ECO:0000256|HAMAP-Rule:MF_04059, KW ECO:0000256|PIRNR:PIRNR001218}; KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04059}. FT ACT_SITE 55 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04059, FT ECO:0000256|PIRSR:PIRSR001218-1" FT ACT_SITE 72 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04059, FT ECO:0000256|PIRSR:PIRSR001218-1" FT ACT_SITE 122 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04059, FT ECO:0000256|PIRSR:PIRSR001218-1" FT SITE 52..53 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04059" FT DISULFID 104 FT /note="Interchain (with C-10 in cleaved protease cofactor FT pVI-C)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04059" 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 //