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Database: UniProt
Entry: A0A060SYQ9_PYCCI
LinkDB: A0A060SYQ9_PYCCI
Original site: A0A060SYQ9_PYCCI 
ID   A0A060SYQ9_PYCCI        Unreviewed;       415 AA.
AC   A0A060SYQ9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   08-NOV-2023, entry version 39.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=BN946_scf184787.g18 {ECO:0000313|EMBL:CDO77369.1};
OS   Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO77369.1, ECO:0000313|Proteomes:UP000029665};
RN   [1] {ECO:0000313|EMBL:CDO77369.1, ECO:0000313|Proteomes:UP000029665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRFM137 {ECO:0000313|EMBL:CDO77369.1,
RC   ECO:0000313|Proteomes:UP000029665};
RA   Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA   Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA   Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA   Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA   Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA   Pontarotti P., Henrissat B., Record E.;
RT   "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT   basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT   breakdown.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDO77369.1}.
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DR   EMBL; CCBP010000451; CDO77369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A060SYQ9; -.
DR   STRING; 5643.A0A060SYQ9; -.
DR   HOGENOM; CLU_038846_0_0_1; -.
DR   OrthoDB; 656651at2759; -.
DR   Proteomes; UP000029665; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029665};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..415
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001587844"
FT   DOMAIN          90..405
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   415 AA;  43102 MW;  634E835249FA2C58 CRC64;
     MLTSLLPLVV LSVAAAAAAK PVVVRKSPVT LPIARRLNVT SAPELLKIDQ ARAKVLKEQG
     LARGKGAGSL RKAAQDAIFN LPVTNGAVDY TASVGIGTPP TQYDLIVDTG SSNTWVGAGT
     AYVQTSSSED TGQEFLVEYG SGLVFGELYT DTVTLGDLKQ TNQGIGDGLL AFGFDGVDGI
     LGIGPVDLTD GTTSGGGLVP TVLDTARSEG LISSEVIGIS FEPTTELSVT NGELTFGGTD
     SSKHTGNIAY VPVTSTSPAS SYVGIDQSIT YGSAGTTILS STAGITDTGT TLTLIASDAL
     AKYQKATGAV SDSATGLLKI TQAQFENLES LFFHIGDNTY EFTPNAQIWP RSLNTAIGGD
     ADSIYLVVAD LGSDSGEGLD FIDGFTFLER FYYVWDVENT RVGFATTEFT DATTN
//
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