ID S8BBE9_DACHA Unreviewed; 419 AA.
AC S8BBE9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 03-MAY-2023, entry version 46.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=H072_10035 {ECO:0000313|EMBL:EPS36483.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS36483.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS36483.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS36483.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-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:EPS36483.1}.
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DR EMBL; AQGS01000906; EPS36483.1; -; Genomic_DNA.
DR RefSeq; XP_011115541.1; XM_011117239.1.
DR AlphaFoldDB; S8BBE9; -.
DR STRING; 1284197.S8BBE9; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_1_1; -.
DR OMA; WFANAMS; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000015100; 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; 1.
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|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..419
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004548416"
FT DOMAIN 99..415
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 115
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 304
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 340..375
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 419 AA; 45026 MW; 152378826CEFF85D CRC64;
MHSTFLLAAA WASYTLAVPV TLPEAQNEGF TVPVVHTPNT KRDPLSAMYQ AYQRYGDGIE
MPAALLEFAN NLQSDGKTHQ KRQDSASVAA TPTSKDVEYW CPVQVGVNTL NLNFDTGSNA
LWVFSSVTPA DQRGSHNLYT PNGRSLKKLG YTWSIGYADG SKAAGVVYMD KVQIGSATVT
SQAVQAATSV SSKFVSKSGI DGLLGLGYSA FNNVSPQRSG TWFANAMSSL RSGVFTADLR
PGAVGAYTFG FIDPERYTGS ITYQALHSSA LSKGWWLIDA SKGYKVGTQQ FTDTAGSSNG
AVLDTGTTLL LMSDQVVKTY YSKVPSSQYV ASRGGWVFPC SATLPDIQVP FGSSFATIPG
KYMNYVALDS QNVSCFGSLQ SLGSQNTALP YIYGDIFFKA NYVVFDMKND KVGFATKKN
//