PRO_ADEF1
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 03-AUG-2022, entry version 67.
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}.
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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; SSF54001; 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
