ID A0A165PPC9_9APHY Unreviewed; 566 AA.
AC A0A165PPC9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KZT68462.1};
GN ORFNames=DAEQUDRAFT_327024 {ECO:0000313|EMBL:KZT68462.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT68462.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT68462.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT68462.1,
RC ECO:0000313|Proteomes:UP000076727};
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; KV429066; KZT68462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165PPC9; -.
DR STRING; 1314783.A0A165PPC9; -.
DR OrthoDB; 1665068at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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; 2.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KZT68462.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..566
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007864326"
FT TRANSMEM 426..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..415
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 510..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 59266 MW; F2E9E5D13C80EADC CRC64;
MSSSKKLACI AFCLAHVASA ISSLGITKRA TTQAPAPTTI DIPLHFDGSG RYIIPVGMSS
GANQQNFNFT LATSTGLTSV AGVGCSSCSD ISLYNQSASS TAQSLNGNDS VALVGGSFSG
SVIKEDCSMS TTGSAWVYNN QTIVVAHSQQ NGTVLGSGAS GLLGLGTNRL SSTQPNDSSS
GYMASFSDSI FSRWLQNNAD QESFQFGMDI LPPVVTPTNS SGLATAAPTS TDAGTLHWLA
PDTSKYNQSG LTYKDVQSNS SLVYSTGSQP DWTVLLDGWK VSSGGDSFES QDQIMVTVDP
YYTDIYFPAK EAEFFNAVIS GSSVQSGLST LGSQSQAWSV PCDTKVSLSI NINDQTFTLD
QSALVRQSSS GTCFSGVEGW TDSSIEQYIF GALFVSQVYL IFNVGRNGTD AVGFAPKVAS
RKGTKVGAIV GGTIGGVVGV LLVGIAAFFY LRSRQDRAIL KDTVAVIEEH KVANTIQPFT
LGAAAPRMGS PGVDVPLMTH HEDDVPPPAY EASEVGGSPT IASGGPMRMS KSEYVNPAPV
QAVGEGSSRL SQPPRVEPNR MYHIEE
//
