ID A0A165EC73_9APHY Unreviewed; 566 AA.
AC A0A165EC73;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KZT06710.1};
GN ORFNames=LAESUDRAFT_759204 {ECO:0000313|EMBL:KZT06710.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT06710.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT06710.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT06710.1,
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}.
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DR EMBL; KV427623; KZT06710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165EC73; -.
DR STRING; 1314785.A0A165EC73; -.
DR InParanoid; A0A165EC73; -.
DR OrthoDB; 1507272at2759; -.
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:InterPro.
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; 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 Pfam; PF00026; Asp; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KZT06710.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KZT06710.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..474
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 566 AA; 59489 MW; 7B84D154B1CCD402 CRC64;
MPSFISARSY VFSLLQVLLI VIPFAVGIDL PLYRTVTRRL DKRDNGSTAI GLGDVLDVTY
NVVMSVGSTV TTLVVDTGSS DLWLVSDAYT GNGSEAEIPL YSHTAFQPTG LDAELFYGDS
RTGTYASGPI GGDMAGIAGL STNNQSFAAI NRTNTTVFQT GSAGILGLGF PPISMIWRQL
LQAALADEGS PLSKRELSPN ISSNVDTGTI GHPPFPSFEF LTPAITKRRK RLSDPSHTDF
AIASFAMFGP LLARLVLQQA LDQPLITTTL QRDTVQLGGN AGVLSLGGLP AGVREEQLVW
VPVRAYTADQ GGLPPPTDAP NEVYPLVWEV PVDDVYFDDV KLPQSALASP AISLSALIDT
GNSLIRGPRD ILSHIVARTG STFDCSVAHN LSFLIGGMLF PVDPRDFARP ISSESGDDAV
AKCSPALAAT DPPGVGGFLY SWSLGDPFLK SAMVAYYYGN LTHPSQDPPR VGLLSTVPAN
VTQDLQDAVE AAISNGGFPA TSNAAPSGTL APTLSGLDII PPPTHSSNVS VFWTSGAATC
TNNVALWIPL LVGMVSGLVL LGSLQI
//