ID A0A0P1BGY4_9BASI Unreviewed; 765 AA.
AC A0A0P1BGY4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Aspartyl protease {ECO:0000313|EMBL:CEH15246.1};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH15246.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH15246.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; CCYA01000260; CEH15246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1BGY4; -.
DR STRING; 401625.A0A0P1BGY4; -.
DR OrthoDB; 2670782at2759; -.
DR Proteomes; UP000054845; 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 PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CEH15246.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:CEH15246.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054845};
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..765
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006059493"
FT TRANSMEM 642..663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..483
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 490..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 82467 MW; 4ABAD6ACEF191DA9 CRC64;
MRLSARMTLF LLVVCALAVS AAPSPPPIQW REVSTLLSPQ AVKRSEAIRP QSFRVPLRLS
KRAKSSTGVR DERLLSRKES DRATNATALE DLGMDTFYSA VWQVGTPAVD VHVLMDTGSS
APVIYAPEFM KGLNASYAQE ASESGDASTL PPAELLQGNA TYDWNNSTSS HAVTLQNGTT
NLQGSVAYGS GADVGYGVYL QDTVEIAGFK IEQQPFLYLT QGTITQAGKN LGGLFGLGWS
AMGATGDYPF INPLEYLWRS GALEEPLFTF ALLRNVGGED LSDGHEGAAS DNPGGLFTIG
SLDRTQYDGE IAWAPLVTSD AYPAPMPKEL VGKPNGWFAQ IDYLKVNGKI IETSRKLPAH
FDTGGIDMSM PPWITDDMFS KVKGARYQEE LGYTTFPCSL PGAGPATLNL TLAFGGQEFH
IDMEDLVSAR MHDSKGKVVC RRNSASNVDA SADGPVQPLL FGASVLKNVF AAFRFEPPSI
GLAHLSGSVK SREAPKDDDP NFSEAPPGAT PNADAPHVQP GPTIVKPEDY PWTIVTQTAS
KQVVDWPAAT LPNTAQQRLA AVPTGALPVA HGKLASSRLK AAKFGLYDSL TSAAAAAQTH
RPGQSWNMDF GKWGSPRQDW MDTHHFNDDD EPSRDISLAA RIGIIVGAAL LGAIVIGLCA
LICKRRRKVT RAPPMGHDGA LRGNAQATTP GVFQRSTYSV LSREKNDAES RYDAEEARQE
MASQHSEYAQ KYDQPNYAHV QQTSEPDFQK HGWTQHGGEP AAFHS
//