ID A0A067N6Q8_PLEOS Unreviewed; 622 AA.
AC A0A067N6Q8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 08-NOV-2023, entry version 35.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
DE Flags: Fragment;
GN ORFNames=PLEOSDRAFT_1049564 {ECO:0000313|EMBL:KDQ23529.1};
OS Pleurotus ostreatus PC15.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ23529.1, ECO:0000313|Proteomes:UP000027073};
RN [1] {ECO:0000313|Proteomes:UP000027073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; KL198013; KDQ23529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067N6Q8; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1049564; -.
DR HOGENOM; CLU_014988_0_0_1; -.
DR InParanoid; A0A067N6Q8; -.
DR OrthoDB; 1449676at2759; -.
DR Proteomes; UP000027073; 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:InterPro.
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 PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 2.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000027073};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 400..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..336
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 479..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KDQ23529.1"
SQ SEQUENCE 622 AA; 66474 MW; 9817F3CDAD0B0ABE CRC64;
WFASRSCSSQ ACSQTGGRLY DPSSSRPTGQ QFEIPYLRGR AAGPVVWDRF EIGGYSIENQ
AIAAVDDVSD EPLSPDFVGI LGLALPMNSI IARVLTPGTS DAPDGQSVPA NLFSITPRYA
APSYRFISIT LSRPGSDYPP SLLSIGRHPS AIRELHQDND TAKDLNATKV QYSTLVSERS
GILFWKVDVR GITVWVDGFA REVTLARGVS GTPWPTAVID SGVPLILTTS AIANGIYGAL
GIGPASDGQY YVPCNTPLNL TLTLDDRPPV ALHPLDLTGL PPKDTSSDFC IGLIQAADAA
LSSPTNGFGD MILGVPFMRS VYTVMAYDSP SEEGVFPNST VPTTGSANSI RPRLGLLSLV
DPHVAMDEFT RVRVAHQPLS TGGGTAGSNR APSSGDGKKI SVGIAVLIGL VGFFALCVAL
FALRWFITRR QWRNAGTSTL GGPNSTEGKD RGIEAKVMSE DELRALRYEA YMRKERVHSD
YTTSSAQTRV NEQDSDIDGE MGFRKEAPYE GTPALTTEDH HPTTQSVSPS PSPIPVAGRS
QPSASTSSHS SYDPHPPLSE HDARRSMHAD TTDELGVRLS MVGVGSGNRS SFMDTSSPHH
TRFTSFPSPE PPSGHSPRPV DS
//