ID A0A094FR12_9PEZI Unreviewed; 443 AA.
AC A0A094FR12;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=V497_02637 {ECO:0000313|EMBL:KFY62042.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY62042.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY62042.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
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:KFY62042.1}.
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DR EMBL; JPJZ01000660; KFY62042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094FR12; -.
DR STRING; 1420910.A0A094FR12; -.
DR HOGENOM; CLU_013253_0_1_1; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000029268; 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; 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:UP000029268};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..443
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001897020"
FT DOMAIN 127..435
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 145
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 329
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 443 AA; 47775 MW; 40715CCEC3243DFB CRC64;
MHTFIKLISA VLLVLSLTAW GVDASPRRHK GKFTKHYRTG PSVLGGSTFK VNQHHNPNYK
RTANSGPVEL AKTYKKFNVL FPDQLSNAIA GIVGRLQGTD GVPAKVDPSN VNFGTVETIP
EAFDREYLSP VQIGTPAQTV NLNFDTGSAD LWVNTNETPE NQQNGQKEYN PTLSSTASRM
DGATWDITYG DGSASSGIVY LDTVTIGGVT VQKQAVESAQ KVSSSFQSDA ASSGLLGLGF
GSINTVQPQQ QKTFFENAMN DLASPLFTVN LMKQAAGSYD FGYINESEHT GEIKYTPVDN
TRGFWGFNPT GFQVGNSSFN STNWFAIADT GTSLLLLPSD IVDNYWSNVQ GAFFDALQGG
YTFPCKNPLP SFSFGIEEYR GVVPGHFMNY ASISNLTCFG GIQSSDALGF SIFGDVVLKA
QFVVFDGGDN TLGWANKDLS SSV
//