ID A0A165QHA2_EXIGL Unreviewed; 505 AA.
AC A0A165QHA2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KZW03614.1};
GN ORFNames=EXIGLDRAFT_721804 {ECO:0000313|EMBL:KZW03614.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW03614.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW03614.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW03614.1,
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}.
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DR EMBL; KV425883; KZW03614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165QHA2; -.
DR InParanoid; A0A165QHA2; -.
DR OrthoDB; 1705132at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:KZW03614.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 161..487
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 505 AA; 53324 MW; 4A9D9467CF0A241B CRC64;
MDIGVGSSDA AVSYQPSDGW AGIGAPGAFG GGDAQFLLSN ADQGVVTFTF PAASSSFEFW
GYKRSDGGMY SLTVDGGDAV QVDYYDPNST GDDPPAKLYS RDDLSNDMHT VVITNVNDDR
VSKFGQMNID HFEIVGVPAP PKAPSFPDGS WIAEAPLEFS YHVKISLGAD SPLNGGNGDT
VNVLFDTGAT GDWVIWNGCE QEQCQNHGQY KSSTSNFQNT SQTDIAVYGS GGPANTLGSW
RITDTVTLGN ATIQSTTFGA CYQVPEGGEG LDGNFGMAKA YCNGNLCGNY PSFVENMYEQ
GIISAPVLAF YQLAPNDKPA DGVQSVAQIG GIDANKFKGS MDWVPLTSES QWQIPNAQRF
ISDGSGNTVD GTSQFTHTTM ALDTGDPGLL GLPSNDWQTL LNLAGARDDG KFPCSSTMTW
NFHGTTNRNY TFALADTGSD DGSGFCNALA NDAGDTTNWI TGAPFLDQYY VAWYFGEKGV
GSTIGFAEKN LDANAATVSP VVGTA
//
