ID A0A094CXR8_9PEZI Unreviewed; 443 AA.
AC A0A094CXR8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 34.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=V491_00950 {ECO:0000313|EMBL:KFY27312.1};
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:KFY27312.1, ECO:0000313|Proteomes:UP000029338};
RN [1] {ECO:0000313|EMBL:KFY27312.1, ECO:0000313|Proteomes:UP000029338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY27312.1,
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:KFY27312.1}.
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DR EMBL; JPJT01000479; KFY27312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094CXR8; -.
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: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; 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};
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_5001899074"
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; 47517 MW; C002922B4838C66C CRC64;
MQTFIKSFWA VLLVLSLTAW SVDASPRFKT KKFTKHYRTG PLVLGGSTFK VNQRYNPNYK
RTANSGTVEL AKTYKKYNVL FPDQLANAIA GIVGRLQGTG NGTTAVNASN VNFGTVETLP
EAYDREYLSP VQIGTPPQTV NLNFDTGSAD LWVNTNETPE NQQNGQVEYN PTLSSTASKM
EGATWDITYG DGSASSGIVY TDVVSIGGVT VQSQAVESAQ QVSASFQTDA ASSGLLGLGF
GTINTVQPEQ QKTFFENAIN DLASPLFTVN LMKQAAGSYD FGYINASEYT GEIQYTPVDN
SRGFWGFNPS GFQVGNSSFN ATSWFAIADT GTSLLLLPGD LVDNYWSAVS GAKFDALQGG
YTFPCNTTLP SWSFGVDEYR GVVPGHFMNY AAISASTCFG GIQSSDALGF SIFGDVVLKA
QFVVFDGGDN TLGWANKDLS SSI
//
