ID S8B8W8_DACHA Unreviewed; 417 AA.
AC S8B8W8;
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_11083 {ECO:0000313|EMBL:EPS35498.1};
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:EPS35498.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS35498.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS35498.1,
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:EPS35498.1}.
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DR EMBL; AQGS01001127; EPS35498.1; -; Genomic_DNA.
DR RefSeq; XP_011116453.1; XM_011118151.1.
DR AlphaFoldDB; S8B8W8; -.
DR STRING; 1284197.S8B8W8; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_1_1; -.
DR OMA; YAMAGVY; -.
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; 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|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..417
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004561052"
FT DOMAIN 106..414
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 122
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 307
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 343..378
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 417 AA; 44377 MW; 0A43C78BF7236229 CRC64;
MVAASSLIFA FSAIGALAVP IIPPLNVSPG IELKGGPGRF GQRKPGNSVG IRAIPNPTYK
PDGKRALKKV LSKYGLELPS ALRDIDLERR ADGTVEAKPG QYDIQYVCPV TVGSQKLNLN
FDTGSADLWV FSSIMPKSQQ GGHKIYTPGS GAKQVKGATW KIQYGDGSGA SGTVYKDTVS
IGNTVVKSQG VELAKTVSDS FSSDDFADGL VGLAFGSINT VQPKQEKTFF ENAMSGLSSA
VLTADLRHQE AGSYDFGTID NAKYQGEIQY APVDNSQGFW QFDAPSYSIG SNSTHLRHSS
GATAIADTGT TLLLVSNQIA KEYYAQVHGA KLDNEQGGYT FSCSASLPDI TISIGDKKAT
VPGSWMNYAP ITDGSSTCFG GLQGYDGDMF IYGDIFFKAF FSVFDYENQQ FGFAAKA
//