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Database: UniProt
Entry: A0A165E8X8_9APHY
LinkDB: A0A165E8X8_9APHY
Original site: A0A165E8X8_9APHY 
ID   A0A165E8X8_9APHY        Unreviewed;       422 AA.
AC   A0A165E8X8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 27.
DE   SubName: Full=Acid protease {ECO:0000313|EMBL:KZT06492.1};
GN   ORFNames=LAESUDRAFT_653338 {ECO:0000313|EMBL:KZT06492.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT06492.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT06492.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT06492.1,
RC   ECO:0000313|Proteomes:UP000076871};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KV427624; KZT06492.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165E8X8; -.
DR   STRING; 1314785.A0A165E8X8; -.
DR   InParanoid; A0A165E8X8; -.
DR   OrthoDB; 4946at2759; -.
DR   Proteomes; UP000076871; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06097; Aspergillopepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 1.
DR   PANTHER; PTHR47966; 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; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KZT06492.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT   DOMAIN          101..418
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        119
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        312
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   422 AA;  47387 MW;  F311921E0AEA63BE CRC64;
     MAEQRLHHLS RPDRYRQGFR PSFYAAYARA AKRYGFEAGK YGGFAFRNNV VVKVRGMLDR
     STDHEVPAES IQNGAIYLSV KTRLHTTVPE YLIGWSDSTE YVVPVSIGMP PITLMLDFDT
     GSSDMWVWSS EIAGALKYRQ QHRVYHPHRS ATARKADGTW EISYGDGSSA SGDVYTDHVR
     VAGVHIHGQA LEVAKELSSS FLSDGGNDGL LGLAWPTINT VKPRRVATPM ENMIQNKLID
     LASPQPVFTV KLGHGSEQSF YSFGFIDETV TRHPIVYHHI TTQLGFWQVA SAAWMLNGRS
     HNRHQDNSAI LDTGTTLCLV HDDVVERIYH SIDGAQYSNH RGGWIYPNHA RLPEIYFAIG
     HTMYRLNEVD FGYSDAGQGY TFGGIQSRGD LRYDIFGDVF LKSLYIVFDQ GNKRVGVAQR
     DD
//
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