ID A0A094EVV2_9PEZI Unreviewed; 475 AA.
AC A0A094EVV2;
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=V499_00585 {ECO:0000313|EMBL:KFY80583.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY80583.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY80583.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY80583.1,
RC ECO:0000313|Proteomes:UP000029295};
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:KFY80583.1}.
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DR EMBL; JPKB01000060; KFY80583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EVV2; -.
DR HOGENOM; CLU_013253_9_3_1; -.
DR Proteomes; UP000029295; 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 Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 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};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..475
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001895122"
FT DOMAIN 53..395
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 421..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 71
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 265
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 303..352
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 475 AA; 49970 MW; D23AA32B3AF03164 CRC64;
MRLVELSLLL ASADALTLRP ARANPKVVGY GINRRDTSPY STPIYNYFAG FDYTINITIG
SPPQSVMVVV DTGSSNLIVN SPQSDFCQGG NCTQYGSYDP TTSDTSKWYN NLMYTQYEIE
TQKGAWVTDD VTFGGKTLTQ IPIGSGNESS NSDINIWGFG GNGQLGAALP GIPSNDTTLK
SIHKSGVINS ASVSIYLNQT GSETGSMLFG GVDTSLYTGT LQTLPVIPRD GFYDRLTVNL
TTISYNDGKT TKSIETHLPT RVMLDTGNFD IKLPLEIATA IQKSFGITQQ FHLKEYDFAL
TACSMADSPA VVSFGFGGEL INVPMSSLVV NPPESILASY GLPPGTLPEG VCLFLINGFK
DELVESGQLV YILGGAFLAN AYFVSDEDSQ EIGLAQANFN PGPSNILEIA PANGGIAGIN
NSTAGSGASK PGGTPTPTGG AVPSATQTGD AMKAWHSPTG WIVAAAGAFG LLLSF
//