ID W9YT40_9EURO Unreviewed; 397 AA.
AC W9YT40;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 22-FEB-2023, entry version 35.
DE SubName: Full=Aspergillopepsin I {ECO:0000313|EMBL:EXJ96072.1};
GN ORFNames=A1O1_01198 {ECO:0000313|EMBL:EXJ96072.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ96072.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ96072.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ96072.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ96072.1}.
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DR EMBL; AMWN01000001; EXJ96072.1; -; Genomic_DNA.
DR RefSeq; XP_007720301.1; XM_007722111.1.
DR AlphaFoldDB; W9YT40; -.
DR STRING; 1182541.W9YT40; -.
DR GeneID; 19156100; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_1_1; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000019484; 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; cd06097; Aspergillopepsin_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; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF2; ASPERGILLOPEPSIN-1-RELATED; 1.
DR PANTHER; PTHR47966; 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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000019484};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..397
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004934668"
FT DOMAIN 85..393
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 101
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 287
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 397 AA; 41664 MW; 504BE948EA12B081 CRC64;
MPSFSVLLAI SALASFTHAK PIPAPQVTTK KGFTIVQAVA KPFQAGPVVL QKAYNKFNKA
IPADVKAAAA DGSVTATPEE YDAEYLCPVT VGGQTLNLDF DTGSADLWVF SSELPASQRS
GHSYYDASKS NTSRMLSGAT WNISYGDGSG ASGNVYTDTV NVGGTTVTGQ AVELASQISA
EFQQDEDNDG LLGLAFSSIN TVQPTQQTTF FDTAINEGAL DQNVFTADLK KGAPGTYNFG
FIDGSKHTGA ITYTPVNTAN GFWEFTGTGY GVGDGSFQQI SIDAIADTGT TLLLLDDSIV
SDYYSQVSSA RYDNTQGGYI FPCSASLPDF VVGIEDYHAV VPGSFINFAP ATGSTCYGGI
QSNQGLGFSI YGDVFLKAVF AVFDSDNTQV GFAPKAL
//