ID R7SY97_DICSQ Unreviewed; 354 AA.
AC R7SY97;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 08-NOV-2023, entry version 43.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:EJF60938.1};
GN ORFNames=DICSQDRAFT_170483 {ECO:0000313|EMBL:EJF60938.1};
OS Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF60938.1, ECO:0000313|Proteomes:UP000053319};
RN [1] {ECO:0000313|EMBL:EJF60938.1, ECO:0000313|Proteomes:UP000053319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF60938.1,
RC ECO:0000313|Proteomes:UP000053319};
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).
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DR EMBL; JH719412; EJF60938.1; -; Genomic_DNA.
DR RefSeq; XP_007366158.1; XM_007366096.1.
DR AlphaFoldDB; R7SY97; -.
DR GeneID; 18839158; -.
DR KEGG; dsq:DICSQDRAFT_170483; -.
DR HOGENOM; CLU_037868_1_0_1; -.
DR OrthoDB; 4946at2759; -.
DR Proteomes; UP000053319; Unassembled WGS sequence.
DR GO; GO:0008233; F:peptidase 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; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EJF60938.1};
KW Protease {ECO:0000313|EMBL:EJF60938.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053319};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..354
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004455888"
FT DOMAIN 36..351
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 354 AA; 37893 MW; D4AE1DD6E2489252 CRC64;
MKLFSTASLL YALGAVGLVA AALPKDVPLR LSQGFWHARF SVGPQNFSLT VDTGSFAVLI
SEGLYKPNPT SVQTNQGEFI QFNGANEDGT LFASETFTFV KDNVTFDDVA LAGFLVGNIT
DGDPLDEDGI IGFSPPASEI TDPNDPTFLA GQSLAQAICD QENISPCEFG LALKTDGTGS
LIFGPIDESK IKGNLTTQKT LAFDAWWVVN NTEADSPFFV VGDQVVTHIQ PIFDNGTPNV
IGPLDTVRAA LESVGYAIIE TTDDNNVTNI FGTYDCSCEP ARFGFSFPPS AEVHYIDLGA
NVLNRTADGK TCTANILGSS MVDAPTWQIG QTWFQGRYVQ HNLNTSTIAF AELA
//