ID A0A165I9N6_9APHY Unreviewed; 566 AA.
AC A0A165I9N6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 27.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KZT12774.1};
GN ORFNames=LAESUDRAFT_640006 {ECO:0000313|EMBL:KZT12774.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT12774.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT12774.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT12774.1,
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; KZT12774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165I9N6; -.
DR STRING; 1314785.A0A165I9N6; -.
DR InParanoid; A0A165I9N6; -.
DR OrthoDB; 1656645at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KZT12774.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..566
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007859173"
FT TRANSMEM 455..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..392
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 86
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 282
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 318..351
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 566 AA; 60633 MW; 1219D0EC08A28525 CRC64;
MRLHALRLTL WLAFSISLSH AARISFSRHQ RGSGESALQR RGGKTSYSYA TTSSSSGESV
DLSTVRDLLY IANITIADTA YPVQIDTGSS DLWVKGSSFP LSGATTTSLA DNMTYGIGWA
YGNVSYAEVE FAGIEVKSQA FMDVSSASNP ALAYGAVGII GLGFDSLSNV DALVNRSGSD
TGRTFLYNAF AQDKSEPNFI SFSLQDIDDT YDDVEGYFSI GEYEPEYSAV ANSTTISTWP
ESYPKRWSVL LDYLLLGADS TAVPVTTSIS GAPSNRAVVV LDSGTSYTYV TTDIANTIFG
NISNAKYDDS LGQWALPCDS EVDIALQFGE DIYPIDPLDI TVKTSSDSSQ CLATILPDDD
IGGGEFDWLI GDNMLRSVYA VYDFGDYDSS GDLGDPYIKL LSLVNADTAS VNFHKIRGGT
AQNITYNAAN VTAATSTTVS LSSELADTLT KLGTYLPAVL ALMAFNAFIL LALVIAGIVY
VCRRNGGGLA RPRRVAGRTS PMPMNSISTY GLMNPDRESH VYQPVSMALT DDAFTPPSPA
FSKPGFEVDK RRASAITIAD RPMSVA
//