PRO_ADES1
ID PRO_ADES1 Reviewed; 201 AA.
AC Q8JN66;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 66.
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 Snake adenovirus serotype 1 (SnAdV-1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Atadenovirus.
OX NCBI_TaxID=189830;
OH NCBI_TaxID=94885; Pantherophis guttatus (Corn snake) (Elaphe guttata).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12237421; DOI=10.1099/0022-1317-83-10-2403;
RA Farkas S.L., Benko M., Elo P.T., Ursu K., Dan A., Ahne W., Harrach B.;
RT "Genetic analysis of an adenovirus isolated from corn snake (Elaphe
RT guttata) implies common origin with the members of the proposed new genus
RT Atadenovirus.";
RL J. Gen. Virol. 83:2403-2410(2002).
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; DQ106414; AAL92453.1; -; Genomic_DNA.
DR RefSeq; YP_001552256.1; NC_009989.1.
DR SMR; Q8JN66; -.
DR MEROPS; C05.001; -.
DR PRIDE; Q8JN66; -.
DR GeneID; 10973870; -.
DR KEGG; vg:10973870; -.
DR Proteomes; UP000136605; 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..201
FT /note="Protease"
FT /id="PRO_0000218048"
FT ACT_SITE 55
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
FT ACT_SITE 72
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
FT ACT_SITE 122
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
FT SITE 52..53
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
FT DISULFID 104
FT /note="Interchain (with C-10 in cleaved protease cofactor
FT pVI-C)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04059"
SQ SEQUENCE 201 AA; 22713 MW; 3A724D70E6D4F645 CRC64;
MSGSSEQELK MMVRSLNLES GFLGTFDCRF PGFISKDRRQ TAIVNTGPRE QGGVHWIALA
WDPTSRKMFL FDPLGWTNAE LKKYYGFSYQ NMVQRSALSS ADRCVTLERN TQAVQCTCAG
SCGLFCILFL YCAHLSPSNP FGTSLFQSLD GQKSGMVPRS PEALHKNQQI LYNFLSSKCA
YFRKNARNIV MNTRLHLIKT H
