ID A0A094CB89_9PEZI Unreviewed; 395 AA.
AC A0A094CB89;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=V491_04179 {ECO:0000313|EMBL:KFY19837.1};
OS Pseudogymnoascus sp. VKM F-3775.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420901 {ECO:0000313|EMBL:KFY19837.1, ECO:0000313|Proteomes:UP000029338};
RN [1] {ECO:0000313|EMBL:KFY19837.1, ECO:0000313|Proteomes:UP000029338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY19837.1,
RC ECO:0000313|Proteomes:UP000029338};
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:KFY19837.1}.
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DR EMBL; JPJT01002463; KFY19837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094CB89; -.
DR HOGENOM; CLU_013253_0_1_1; -.
DR Proteomes; UP000029338; 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:SF1; ASPARTYL PROTEINASE; 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:UP000029338}.
FT DOMAIN 84..392
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 100
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 283
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 395 AA; 41842 MW; 0E433F17AB287C9E CRC64;
MSRLEDINDD LFAAESRSTN SFSVPAIHNE NYQRNGTLAL LKAYAKYGLT PAEPDNILNL
LLGNLVKRQD GTVPAKPDPQ NVEYVCEVTI GGQKLNLDFD TGSADLWVFS TSLPAASQKN
HNVFDPTKST TWKELSGATW EIQYADGSGS SGTVGTDTVT IGGTTVKAQA VEIADKASDQ
FVSGANDGLV GLSFGSINTV QPTQQKTFFD NAQAGLDSPL FAAFLPFQAT GAYDFGATDS
SRYTGEIAYT SVDDSNGWWE FPSTSYKVGD KAFTSTGYTA IADTGTTLIL MGDEQVANYY
KSVEGSKLDN TQGGYTFPCS ATLPSLTVAI GDGGDAVIPA KYLNFAPADD AGTTCFGSLQ
PSGNGKQNIY GDTFFNAYYG IFDASGPRFG FAATA
//