ID A0A060SXF8_PYCCI Unreviewed; 426 AA.
AC A0A060SXF8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 22-FEB-2023, entry version 39.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=BN946_scf184747.g26 {ECO:0000313|EMBL:CDO77213.1};
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:CDO77213.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO77213.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO77213.1,
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:CDO77213.1}.
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; CCBP010000446; CDO77213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060SXF8; -.
DR STRING; 5643.A0A060SXF8; -.
DR MEROPS; A01.080; -.
DR HOGENOM; CLU_013253_0_2_1; -.
DR OrthoDB; 4946at2759; -.
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; cd06097; Aspergillopepsin_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; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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}.
FT DOMAIN 92..422
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 110
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 316
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 426 AA; 46522 MW; A416B39D43E0AD01 CRC64;
MTLHQLVRPE KYQGGKRPSF AAAYARAARR YGIQAGRNVG FVKRNNVVVK VKGRDDKNTE
HEVPAESIQN VSMLMHSDVR EPCAHLVASL EYVVPVKIGT PGVTLHLDFD TGSSDLWVWS
TELARASTLK GHTVYNPSKS HTAKKAPGTW SISYEDGSSA SGNVYTDNVT VADITIKNQA
VELAEKLSAS FLQDNGKDGL LGLAWPQINT VQPEPVATPV ENMIKQKLIN PPVFTVKLDR
GDDAGFYSFG YIDTSVTHHP IKYTSVDKCV FIESFGAYIL TEPRVDSSQG FWQVASTSWT
LNGQIRARYG NTAVLDTGTT LLLVDDEIVD AIYDSIDGAV YDDQQGGYKY PSNATIPDIC
FAVGDTLYKV NPKDFAFGDA GNGFTFGGIQ SRGDLGFDIF GDIFLKSVYV VFNQGNSTVG
LAQRDE
//