ID A0A0D1Y8T0_9EURO Unreviewed; 504 AA.
AC A0A0D1Y8T0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=PV11_06883 {ECO:0000313|EMBL:KIV79317.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV79317.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV79317.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV79317.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KN846953; KIV79317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1Y8T0; -.
DR STRING; 1016849.A0A0D1Y8T0; -.
DR HOGENOM; CLU_013253_10_1_1; -.
DR OrthoDB; 3087283at2759; -.
DR Proteomes; UP000053599; 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; 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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..504
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002251761"
FT DOMAIN 88..392
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 393..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 106
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 288
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 119..124
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 504 AA; 52662 MW; CD96A3DAD52DB305 CRC64;
MYRQLLSLAL LFSHVSAFYP YGSDEGDDDR RWLSSDVEAR DRVTSGGITL DIKRMRTKRD
NTFTVVKSST PSAPNAMAIN SDGSDFTYFS VMEFGSSGQQ MYMLIDTGSA NSWVMGSSCQ
SNACLIHNTF GSAESTTLNT TSQSWSLSYG TGEVQGVVAQ DTVKVANYSV RVGFGLASSA
SDDFNNYPMD GILGLGRPSS DTLGTDTIMQ VLDQQGTLPK NVIGVHLQRA SDGTNDGEIT
FGGVDSSKYS GKLSYTKVAN TENWEIAASD AGVNGNGIGF KGKTAIIDTG TSYILMPEAD
AQAVHNLIPG SSQNGEIFVI PCSTTASVYF TFSGIKYAVP PKDFIGQTVG NGCQSKIIGH
QAFGPNEWIL GDVFLKNVYT VFDFDNNQIG FGTAGGSSSS SSSSSTSSSS TSSASSSAAA
DSTSTMKSST SSKTPSSSQT SSSKPSTTFS TTTFTGSSST TSTQATTSSG VTDSSPFASS
FGTPQINTNS VAAILLALLV ALIL
//
