ID A0A165I046_EXIGL Unreviewed; 422 AA.
AC A0A165I046;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KZV92706.1};
GN ORFNames=EXIGLDRAFT_646916 {ECO:0000313|EMBL:KZV92706.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV92706.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV92706.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV92706.1,
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; KV426003; KZV92706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165I046; -.
DR STRING; 1314781.A0A165I046; -.
DR InParanoid; A0A165I046; -.
DR OrthoDB; 3087283at2759; -.
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:SF92; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KZV92706.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..422
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007859010"
FT DOMAIN 108..418
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 126
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 306
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 422 AA; 45267 MW; 7FCB0C24EFFB3F3C CRC64;
MLAPLVLAAM SAQVADALIS RAEIKIAVAN NTWEVPAGYE WGLFRESVLD QDRDRIVTKY
KNAGNWITGV GLGPMPNITV ADTPDDLGFL RDDHGAQPLT NYNRDSFYYG AVSIGTPGQV
LNVDIDTGSA DLWVQSGCTS SGCSSSQFRP TKSKSFKGTG KPFHVQYGSG SVTGSLVHDT
VTIAGLTVKD QYFGAVNKPS EDFKGTPSSG LIGMAFSSIA TSRKPTWFEN IIMTSPKTSP
LFSVFLTRGT ARGSEACFGC YDKTKARSPI TWLPVVSKTY WAVAMTGAIV NKNIVPVHRN
IFAAIDTGTT LIYVPDALAK SIYSQVPGAK HMSAGYYTAP CDTFSRLSVA LVFNGSPFNI
NMVDFNLGRI APGSSTCVAG LLGLGNSFPD NLAIIGDEFL KSWYSTYDYS KGSRVGFSRS
IL
//
