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Protease (EC 3.4.22.39) (Adenain) (Adenovirus protease) (AVP) (Adenovirus proteinase) (Endoprotease)

 PRO_ADECR               Reviewed;         206 AA.
P68985; P35990;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 1.
10-MAY-2017, entry version 44.
RecName: Full=Protease {ECO:0000255|HAMAP-Rule:MF_04059};
EC=3.4.22.39 {ECO:0000255|HAMAP-Rule:MF_04059};
AltName: Full=Adenain {ECO:0000255|HAMAP-Rule:MF_04059};
AltName: Full=Adenovirus protease {ECO:0000255|HAMAP-Rule:MF_04059};
Short=AVP {ECO:0000255|HAMAP-Rule:MF_04059};
AltName: Full=Adenovirus proteinase {ECO:0000255|HAMAP-Rule:MF_04059};
AltName: Full=Endoprotease {ECO:0000255|HAMAP-Rule:MF_04059};
Name=L3 {ECO:0000255|HAMAP-Rule:MF_04059};
Canine adenovirus serotype 1 (strain RI261) (CAdV-1) (Canine
adenovirus 1 (strain RI261)).
Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus;
Canine mastadenovirus A.
NCBI_TaxID=69151;
NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=9129661;
Morrison M.D., Onions D.E., Nicolson L.;
"Complete DNA sequence of canine adenovirus type 1.";
J. Gen. Virol. 78:873-878(1997).
-!- FUNCTION: Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII,
pVIII, and pX) inside newly assembled particles giving rise to
mature virions. Protease complexed to its cofactor slides along
the viral DNA to specifically locate and cleave the viral
precursors. Mature virions have a weakened organization compared
to the unmature virions, thereby facilitating subsequent
uncoating. Without maturation, the particle lacks infectivity and
is unable to uncoat. Late in adenovirus infection, in the
cytoplasm, may participate in the cytoskeleton destruction.
Cleaves host cell cytoskeletal keratins K7 and K18.
{ECO:0000255|HAMAP-Rule:MF_04059}.
-!- CATALYTIC ACTIVITY: Cleaves proteins of the adenovirus and its
host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and
-Yaa-Xaa-Gly-Xaa-|-Gly- (in which Yaa is Met, Ile or Leu, and Xaa
is any amino acid).
-!- CATALYTIC ACTIVITY: Cleaves adenovirus and host cell proteins at
two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly-
Xaa-|-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino
acid). {ECO:0000255|HAMAP-Rule:MF_04059}.
-!- ENZYME REGULATION: Requires DNA and protease cofactor for maximal
activation. Inside nascent virions, becomes partially activated by
binding to the viral DNA, allowing it to cleave the cofactor that
binds to the protease and fully activates it. Actin, like the
viral protease cofactor, seems to act as a cofactor in the
cleavage of cytokeratin 18 and of actin itself.
{ECO:0000255|HAMAP-Rule:MF_04059}.
-!- SUBUNIT: Interacts with protease cofactor pVI-C; this interaction
is necessary for protease activation. {ECO:0000255|HAMAP-
Rule:MF_04059}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04059}.
Host nucleus {ECO:0000255|HAMAP-Rule:MF_04059}. Note=Present in
about 10 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04059}.
-!- INDUCTION: Expressed in the late phase of the viral replicative
cycle. {ECO:0000255|HAMAP-Rule:MF_04059}.
-!- MISCELLANEOUS: All late proteins expressed from the major late
promoter are produced by alternative splicing and alternative
polyadenylation of the same gene giving rise to non-overlapping
ORFs. A leader sequence is present in the N-terminus of all these
mRNAs and is recognized by the viral shutoff protein to provide
expression although conventional translation via ribosome scanning
from the cap has been shut off in the host cell.
{ECO:0000255|HAMAP-Rule:MF_04059}.
-!- SIMILARITY: Belongs to the peptidase C5 family.
{ECO:0000255|HAMAP-Rule:MF_04059}.
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EMBL; Y07760; CAA69037.1; -; Genomic_DNA.
RefSeq; AP_000060.1; AC_000003.1.
RefSeq; NP_044199.1; NC_001734.1.
ProteinModelPortal; P68985; -.
SMR; P68985; -.
MEROPS; C05.001; -.
GeneID; 1488932; -.
KEGG; vg:1488932; -.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
HAMAP; MF_04059; ADV_PRO; 1.
InterPro; IPR000855; Peptidase_C5.
Pfam; PF00770; Peptidase_C5; 1.
PIRSF; PIRSF001218; Protease_ADV; 1.
PRINTS; PR00703; ADVENDOPTASE.
ProDom; PD003705; Peptidase_C5; 1.
3: Inferred from homology;
Autocatalytic cleavage; Disulfide bond; DNA-binding; Host nucleus;
Hydrolase; Late protein; Protease; Thiol protease; Virion.
CHAIN 1 206 Protease.
/FTId=PRO_0000218039.
ACT_SITE 57 57 {ECO:0000255|HAMAP-Rule:MF_04059}.
ACT_SITE 74 74 {ECO:0000255|HAMAP-Rule:MF_04059}.
ACT_SITE 125 125 {ECO:0000255|HAMAP-Rule:MF_04059}.
SITE 54 55 Cleavage; by autolysis.
{ECO:0000255|HAMAP-Rule:MF_04059}.
DISULFID 107 107 Interchain (with C-10 in cleaved protease
cofactor pVI-C). {ECO:0000255|HAMAP-
Rule:MF_04059}.
SEQUENCE 206 AA; 23327 MW; 34DFC112FBE2892D CRC64;
MAEGGSSEEE LRAIVRDLAV TPFFLGTFDK RFPGFISSQR ITCAVVNTAG RETGGVHWLA
MAWNPRSKTF YMFDPFGFSD SKLKQVYSFE YEGLLRRSAI ASTPDRCVTL AKSNETIQGP
NSAACGLFCC MFLHAFVNWP DNPFNHNPTM GPLKSVPNYK LYDPTVQHVL WENQEKLYKF
LEKNSAYFRA HAAAIKTRTA FNKLKQ


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