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
//