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
//