ID A0A093ZZ82_9PEZI Unreviewed; 403 AA.
AC A0A093ZZ82;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=V490_06099 {ECO:0000313|EMBL:KFX91066.1};
OS Pseudogymnoascus sp. VKM F-3557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX91066.1, ECO:0000313|Proteomes:UP000029320};
RN [1] {ECO:0000313|EMBL:KFX91066.1, ECO:0000313|Proteomes:UP000029320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX91066.1,
RC ECO:0000313|Proteomes:UP000029320};
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:KFX91066.1}.
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DR EMBL; JPJS01001783; KFX91066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093ZZ82; -.
DR STRING; 1437433.A0A093ZZ82; -.
DR HOGENOM; CLU_013253_0_1_1; -.
DR Proteomes; UP000029320; 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; 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:UP000029320};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..403
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001895703"
FT DOMAIN 92..400
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 108
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 291
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 403 AA; 42003 MW; 03C0E30CB6B24C98 CRC64;
MVAASKLALF ASAAASVAAA PAAEANAKTS FSIPAIHSGA TRNGTTALLK AYAKYGLTPS
HPDNILNTLL GNIVKRQDGT VPAKPDADNV EYICEVDIGG QTLNLDFDTG SADLWVFSTS
LPAASQKNHN VFDPSKSSTW KELSGESWSI QYADGSGSSG TVGTDTVTIG GTTVKTQAVE
IASKASDQFL SGANDGLVGL SFGSINTVQP TQQKTFFDNA KASLDSPLFA AYLPFQASGA
YDFGAIDSSR YTGEVAYTDV DNSNGWWEFP STSYKVGDKS FTSSGYTAIA DTGTTLILMG
DDQVANYYKS VEGSQLDNQQ GGYTFPCSAT LPSLTVAIGD GNEAVIPAKY LNFAPVDQSG
SSCFGSLQPS GNGQQNIYGD TFFNANYGIF DATGPRFGFA ATA
//