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Database: UniProt
Entry: R7SY97_DICSQ
LinkDB: R7SY97_DICSQ
Original site: R7SY97_DICSQ 
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
//
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