ID A0A165L4D3_EXIGL Unreviewed; 415 AA.
AC A0A165L4D3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 28.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KZV97330.1};
GN ORFNames=EXIGLDRAFT_608140 {ECO:0000313|EMBL:KZV97330.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV97330.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV97330.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV97330.1,
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}.
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DR EMBL; KV425931; KZV97330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165L4D3; -.
DR InParanoid; A0A165L4D3; -.
DR OrthoDB; 656651at2759; -.
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; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
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:KZV97330.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..415
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007861535"
FT DOMAIN 91..404
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 109
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 287
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 415 AA; 43152 MW; F88DCB299C0B6F3C CRC64;
MLSTSFLSLV LFAALGLGVA GLSIHELANS TETSSIRAPI RKLVRHEKLK DLVVHDQAHA
KALVHRGTGG KSLSEDAQVA GAAIANLVTT YIASMNVGSP ATTYDVIVDT GSSNTWVGSG
TPFRFTRTTR NLSESMFVQY GSGFVVGFEV IDQVSFGGPL TIPNQEIGVA TASQGFAGVD
GIVGLGPTDL TEGTVQGQDT IPTVTDNLFA LGIIPAPVIS VSFAPTNLTF DVNGELVFGG
VDTSKFIGTL SVFRITSSSP ANAFFGIDAS FSFGGTTILP LSPGIVDTGT TLILLATQAF
SAYTKRSGAV PDGATGLLRL TPAQFAALPS LNVIVGGVTF TLTPDAQRWP QQLNTAIGGS
TSFVYLIVNT LGSPEGQGLD FILGQFFLER FYSVFDSTGF VGLAPTVFTN ATVNN
//