ID M5G2Q1_DACPD Unreviewed; 374 AA.
AC M5G2Q1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:EJU04501.1};
GN ORFNames=DACRYDRAFT_105560 {ECO:0000313|EMBL:EJU04501.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU04501.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJU04501.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU04501.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; JH795858; EJU04501.1; -; Genomic_DNA.
DR AlphaFoldDB; M5G2Q1; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR OrthoDB; 1696312at2759; -.
DR Proteomes; UP000030653; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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; 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; 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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:EJU04501.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030653}.
FT DOMAIN 38..358
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DISULFID 69..74
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 374 AA; 40420 MW; 9139593360264E86 CRC64;
MTVDRFIVDV SNHSAGRPTA PIFPANTVLS TVPLQLSYIA PITLGGNEPA LEVLLDAGAP
DVWVDSVFCT GTNCNGHNKY HPGPKFVNLS IKDTEIYGGG GPDETFITWR VNDSVTFGDI
TIPTTTLGAA VRIGPDQSYD GNFGIAKAYY AQCSYSNIYP NFVENMYLQG IIKNPVIAFY
QLDGSESVPS GVVSQASIGG LDANKFTGQV DWIPMGPQFM WTNPTSTRWV QASPSATVQD
ATEEFNHPAI TFDTGDPGLL GLPHDDWVTL MSLLGAEGPD SNGNYLIPWE STMTWNFYGS
QMRNYTFNLA DTTTDNGSGF CNPSANDAGD TTNWITGAPF LHQYYIAFHY AANLMGFATR
NLGASAAHSS PYFS
//
