ID A0A093Y7R8_9PEZI Unreviewed; 451 AA.
AC A0A093Y7R8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 36.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=O988_06033 {ECO:0000313|EMBL:KFX95014.1};
OS Pseudogymnoascus sp. VKM F-3808.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX95014.1, ECO:0000313|Proteomes:UP000029329};
RN [1] {ECO:0000313|EMBL:KFX95014.1, ECO:0000313|Proteomes:UP000029329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX95014.1,
RC ECO:0000313|Proteomes:UP000029329};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFX95014.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPJR01001255; KFX95014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093Y7R8; -.
DR STRING; 1391699.A0A093Y7R8; -.
DR HOGENOM; CLU_013253_0_0_1; -.
DR Proteomes; UP000029329; 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:SF23; ASPARTIC ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15950)-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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000029329};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..451
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001894691"
FT DOMAIN 141..448
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 157
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 342
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 451 AA; 46946 MW; 738039953F2EDA9B CRC64;
MHSHLYSLIL VTVFAAFVFA IPTPSTSRIQ KRSFKVHRRR NPDFKGYDGP TQLMRAYQKF
GMTVPEGLHL SVGGHRHRKG KNNGAGAGAA AGAGAGVGAG AGTAAGNGTA TGNGTTQAAA
PQTSGVGSVT ATPVEPNDLE YIAPVTIGGQ TIDMNFDTGS SDLWVFNTQL NAQSGQGHTL
YDPTKSPDFK LLKGASFDIS YGDGSGAAGN VGTDTVDIGG ATVTGQAIEM ATDVSDSFVQ
DINSNGLVGL AFSKINTVKP QKQKTFFDNA MPTLAEPVFT ADLRQDEVGA YEFGKIDTAR
FTGDLTWAPI DPSNGFWEFT STKFSVGNGK ALNAIGGTAI ADTGTTLMLV NAAVVNAYYS
QVEGAVNNEQ VGGITFPCDS VLPDLNVDVG GTYTATIQGK FINFAQVNAN TCFGGVQPTT
GNLQIYGDIF FKSQFIVFNG GNNTLGLAPH A
//