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Database: UniProt
Entry: A0A094CB89_9PEZI
LinkDB: A0A094CB89_9PEZI
Original site: A0A094CB89_9PEZI 
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
//
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