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Database: UniProt
Entry: A0A165I5C7_9APHY
LinkDB: A0A165I5C7_9APHY
Original site: A0A165I5C7_9APHY 
ID   A0A165I5C7_9APHY        Unreviewed;       399 AA.
AC   A0A165I5C7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Acid protease {ECO:0000313|EMBL:KZT12610.1};
GN   ORFNames=LAESUDRAFT_718890 {ECO:0000313|EMBL:KZT12610.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT12610.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT12610.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT12610.1,
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; KV427605; KZT12610.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165I5C7; -.
DR   STRING; 1314785.A0A165I5C7; -.
DR   InParanoid; A0A165I5C7; -.
DR   OrthoDB; 656651at2759; -.
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; cd05471; pepsin_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; IPR018222; Nuclear_transport_factor_2_euk.
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; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50177; NTF2_DOMAIN; 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:KZT12610.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..399
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007859095"
FT   DOMAIN          73..392
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DOMAIN          370..399
FT                   /note="NTF2"
FT                   /evidence="ECO:0000259|PROSITE:PS50177"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   399 AA;  42668 MW;  266CF67FCCD8621E CRC64;
     MFKSLAASVV LAVVSASFVG AFTKVSLEPV KNRTGAYMHG APDAERARAA LMKSRAKGEA
     ATIPATNLAY VQYTALIGVG SPPTYYNLVV DTGSSNTFVG TGKTYVRTST SIPTGQEVNV
     TYGSGFFSGY EYLDQVTIAL GFVIKNQSIG DALEYADFEG VDGIIGVGPV DLTLDTLYPD
     VNAEILTVMN NAYEQGLISK QILGVSFAPA DSYSDTNGAL TFGGIDSSLY TGKITYTPVT
     TTYPSNYYWG INVTRATYGD AAVIPYSDAG IVDTGTTLIY IADDFYSTYQ NAIPGAYYDD
     NTGLIVIPES SVASMQDFDF EIGGTTFTLD AEAQLLPRDQ NVAWGAEPGL QYGYIGPIGS
     PSGEGLDFII GQKFMERYYA IFDTDNEVVG FAYTDHTYS
//
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