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Database: UniProt
Entry: R7SWN9_DICSQ
LinkDB: R7SWN9_DICSQ
Original site: R7SWN9_DICSQ 
ID   R7SWN9_DICSQ            Unreviewed;       545 AA.
AC   R7SWN9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   08-NOV-2023, entry version 42.
DE   SubName: Full=Acid protease {ECO:0000313|EMBL:EJF60496.1};
GN   ORFNames=DICSQDRAFT_87642 {ECO:0000313|EMBL:EJF60496.1};
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:EJF60496.1, ECO:0000313|Proteomes:UP000053319};
RN   [1] {ECO:0000313|EMBL:EJF60496.1, ECO:0000313|Proteomes:UP000053319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF60496.1,
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).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; JH719415; EJF60496.1; -; Genomic_DNA.
DR   RefSeq; XP_007366635.1; XM_007366573.1.
DR   AlphaFoldDB; R7SWN9; -.
DR   GeneID; 18844726; -.
DR   KEGG; dsq:DICSQDRAFT_87642; -.
DR   HOGENOM; CLU_021426_0_0_1; -.
DR   OMA; WIRTSAC; -.
DR   OrthoDB; 1507272at2759; -.
DR   Proteomes; UP000053319; 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; 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   Hydrolase {ECO:0000313|EMBL:EJF60496.1};
KW   Protease {ECO:0000313|EMBL:EJF60496.1};
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..545
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004445061"
FT   DOMAIN          68..438
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        84
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        325
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        361..395
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   545 AA;  56091 MW;  9172E8EE70060C2C CRC64;
     MCHTPLWRTL VLLSLLTLSS ATTLVQLNSG LKTAAVSFAR RNSSAIRALH GDAVGGTVGL
     GDVSDLTYLV AATVGNSTVS LNIDTGSTDL WVVSSACQTQ TCQSFAGEPY ALTQAFQQSQ
     QGSVDLLFGD STTGTHAAGP LGRDVVVLAG LTATNQTLAA INDTDNSAVA NGGAGILGLG
     FPSQSFIGES IVASVFKDIR GSDTFVEQWV NYGPIIPRLI LAGVLDQPLF TITLQRDELD
     VSGTGQLTIG QLPSGIDNSS LTWVPVRLYS ESEGGMTPPS FASNEVYPLR WEIPLDGVFL
     DGVKLADSAQ NASGISKPSL SALIDTGNSL IRGPADVVSA ILANVSSTFA ANASNAPLLP
     CVPGHNLTFQ IGGKLFPVDP RDFVSQNSPG DAATCVANAV VGTDPPSSGA LFSWSLGDPF
     LKSNLVAFYY GNLTNPSADP PRIGLLSLVP SDAEEELEQA VNEAQENGGV FETTSQAAPT
     DSRVIVGTAS KTHTPGLNGL PGSLSTATPD EENAAFAVRG LAVGAVSRAC VLVVLSSLSL
     SLGVL
//
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