ID U5NE79_9ADEN Unreviewed; 206 AA. AC U5NE79; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 05-DEC-2018, entry version 15. 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; dsDNA viruses, no RNA stage; Adenoviridae; Aviadenovirus; OC Turkey aviadenovirus D. OX NCBI_TaxID=1408258 {ECO:0000313|EMBL:AGX93379.1}; RN [1] {ECO:0000313|EMBL:AGX93379.1} RP NUCLEOTIDE SEQUENCE. 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., RA Hess M.; RT "Whole-genome sequences of two turkey adenovirus types reveal the RT existence of two unknown lineages that merit the establishment of RT novel species 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 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: CC Reaction=Cleaves proteins of the adenovirus and its host cell 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 CC amino acid).; EC=3.4.22.39; Evidence={ECO:0000256|HAMAP- CC Rule:MF_04059, ECO:0000256|PIRNR:PIRNR001218}; CC -!- ACTIVITY REGULATION: Requires DNA and protease cofactor for CC maximal activation. Inside nascent virions, becomes partially CC activated by binding to the viral DNA, allowing it to cleave the CC cofactor that binds to the protease and fully activates it. Actin, CC like the viral protease cofactor, seems to act as a cofactor in CC the 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; KF477314; AGX93379.1; -; Genomic_DNA. 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 ProDom; PD003705; Peptidase_C5; 1. DR SUPFAM; SSF54001; SSF54001; 1. PE 2: Evidence at transcript level; KW Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_04059, KW ECO:0000256|PIRNR:PIRNR001218}; 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}; KW Protease {ECO:0000256|HAMAP-Rule:MF_04059, KW ECO:0000256|PIRNR:PIRNR001218, ECO:0000313|EMBL:AGX93379.1}; KW Thiol protease {ECO:0000256|HAMAP-Rule:MF_04059, KW ECO:0000256|PIRNR:PIRNR001218}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04059}. FT ACT_SITE 55 55 {ECO:0000256|HAMAP-Rule:MF_04059, FT ECO:0000256|PIRSR:PIRSR001218-1}. FT ACT_SITE 72 72 {ECO:0000256|HAMAP-Rule:MF_04059, FT ECO:0000256|PIRSR:PIRSR001218-1}. FT ACT_SITE 122 122 {ECO:0000256|HAMAP-Rule:MF_04059, FT ECO:0000256|PIRSR:PIRSR001218-1}. FT SITE 52 53 Cleavage; by autolysis. FT {ECO:0000256|HAMAP-Rule:MF_04059}. FT DISULFID 104 104 Interchain (with C-10 in cleaved protease FT cofactor pVI-C). {ECO:0000256|HAMAP-Rule: FT 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 //