ID A0A165F0Y7_EXIGL Unreviewed; 385 AA.
AC A0A165F0Y7;
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=Family A1 protease {ECO:0000313|EMBL:KZV88127.1};
GN ORFNames=EXIGLDRAFT_619812 {ECO:0000313|EMBL:KZV88127.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV88127.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV88127.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV88127.1,
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; KV426107; KZV88127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165F0Y7; -.
DR InParanoid; A0A165F0Y7; -.
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:KZV88127.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 56..378
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 74
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 255
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 385 AA; 39863 MW; ABF1BC856B32FED4 CRC64;
MKTPAQTISA RAPFKKLVNH DKLGDIPAAD KARAQSLLSR AFISTKNAAV NTVVSYVAEI
SVGTPATPRL LIVDTGSSNT WVGASTPFSS TGTTKQLNVS MGVNYGSGFV RGTQVVDAVS
FGSPLIIANQ SIGVAQQFSG FSGVDGIVGI GPARLTSGTV HGPSQGLVPT VTDNLFSSGV
IPAPIVGISF QATNDTFDVN GELVFGGVDS SKFTGELSVF SMSDVPAPAN QFFGINAQFT
PQGGDPLLNS VGIIDTGTTL IMLSKEAFAS YAAQTGAKLD NATGLLSVTE AQFTQMKTLN
LVVNGQVTLP ITRDAQRWPQ ALTTAIGGDP KAVYLIIGNL GTSRGSGIDF ILGQFFLERF
YSVFDSSGFV GLAQTAFTNA VVNGV
//