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-APR-2017, entry version 8.
DE   RecName: Full=Protease {ECO:0000256|PIRNR:PIRNR001218};
DE            EC=3.4.22.39 {ECO:0000256|PIRNR:PIRNR001218};
DE   AltName: Full=Adenain {ECO:0000256|PIRNR:PIRNR001218};
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. {ECO:0000256|PIRNR:PIRNR001218}.
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   -!- SIMILARITY: Belongs to the peptidase C5 family.
CC       {ECO:0000256|PIRNR:PIRNR001218}.
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DR   EMBL; KF477314; AGX93379.1; -; Genomic_DNA.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Autocatalytic cleavage {ECO:0000256|PIRNR:PIRNR001218};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001218};
KW   Late protein {ECO:0000256|PIRNR:PIRNR001218};
KW   Protease {ECO:0000256|PIRNR:PIRNR001218, ECO:0000313|EMBL:AGX93379.1};
KW   Thiol protease {ECO:0000256|PIRNR:PIRNR001218}.
FT   ACT_SITE     55     55       {ECO:0000256|PIRSR:PIRSR001218-1}.
FT   ACT_SITE     72     72       {ECO:0000256|PIRSR:PIRSR001218-1}.
FT   ACT_SITE    122    122       {ECO:0000256|PIRSR:PIRSR001218-1}.
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
//