ID M2QLC4_CERS8 Unreviewed; 426 AA.
AC M2QLC4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=CERSUDRAFT_50799 {ECO:0000313|EMBL:EMD37833.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD37833.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD37833.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD37833.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; KB445796; EMD37833.1; -; Genomic_DNA.
DR AlphaFoldDB; M2QLC4; -.
DR STRING; 914234.M2QLC4; -.
DR HOGENOM; CLU_013253_1_4_1; -.
DR OrthoDB; 4946at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..426
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004023524"
FT DOMAIN 115..423
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 312
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 146..151
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 426 AA; 45746 MW; ED65BA9695733DED CRC64;
MFPKATLTIT VALAVLSSAT PVVLDSGVRV PYQKREFLTN DDGTFNHEEA IRQTARTHNK
HRQNMINLKN NMGYEAFPEK GAEIKPVMSY NTTSWRHYEK RQKEPTIDES NDLEWAGTIS
IGTPAQSFLI DFDTGSSDLW VPNIACTSST CKSKHRYNPA SSSTKANQTG TFSIQYGDGS
TVSGPVYTDK VTVAGITAAN QYFSPVTTVS TFFAGEPADG ILGMAYPGIS NLGKSPYFNT
AFTQKTAAAN VFAMKLAKSG SELYLGGTDT ALYKGTIEYQ PLSTSNRFWQ LGNAKALVGT
NVTNSGFQTI IDSGTTIMYG PPAAVQALYA AIPGSKLYDS TNGYYTFPCA TPPTVSFNWG
GKNWVVSTAN FNLGTTARGA KTCIGALAGK DLGLGSGVWL LGDSFMKNQY NVFSFAQNAV
GFATLA
//