ID A0A165KZN6_EXIGL Unreviewed; 387 AA.
AC A0A165KZN6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KZV97131.1};
GN ORFNames=EXIGLDRAFT_764725 {ECO:0000313|EMBL:KZV97131.1},
GN EXIGLDRAFT_769513 {ECO:0000313|EMBL:KZV91924.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV97131.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV97131.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV97131.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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; KV426018; KZV91924.1; -; Genomic_DNA.
DR EMBL; KV425934; KZV97131.1; -; Genomic_DNA.
DR OrthoDB; 2670782at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KZV97131.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 62..383
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 80
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 266
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 93..97
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 387 AA; 40513 MW; 2891308BF2A52083 CRC64;
MRTTTTVTAL AALAGVNAVR HSDNKVSLAA RKIAPVSRRA RLAVSASEVP LLDYFNGTDL
QWFGDITVGT PPQTFSVVFD TGSTTLEIPG TACGKACSNQ RQFNSSRSST FVDGGRTSTI
TFGTGVGVDP VIGNNWQLSL RSATDTVAVG GISIPRISFF QITNQTPTFL PDPFDGIMGM
GATAQGWFAG AIAQGLPSMF GMFFTHQNEG GAELTLGGAD TTKFTQPLKF SPQASTGSTW
QLTSPGIFVN GKTSSTLNVR RTIIFDSGTS NILFPQATAN AMHALISPNI TANAAEPGTF
GLPCSQIASL PAVIDITFAG AAGQPAFNLT IPSSELSVGP FKSNPSQCQT LINVSEGFTL
VGASLLKHYY SVWDVGGRRL GFSPTAF
//
