ID A0A094DEW3_9PEZI Unreviewed; 480 AA.
AC A0A094DEW3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 28-JUN-2023, entry version 36.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=V497_01536 {ECO:0000313|EMBL:KFY64986.1};
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:KFY64986.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY64986.1, 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:KFY64986.1}.
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DR EMBL; JPJZ01000264; KFY64986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DEW3; -.
DR STRING; 1420910.A0A094DEW3; -.
DR HOGENOM; CLU_013253_9_3_1; -.
DR OrthoDB; 615305at2759; -.
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; cd05474; SAP_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; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 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|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..480
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001894746"
FT DOMAIN 71..402
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 89
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 285
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 480 AA; 50510 MW; FC76F8E5029E7AE4 CRC64;
MKCAFALGVT AAFLSPLIDA AALEKRNDRQ PRAVGLPIKR EPVADPIEAD RTRMRKRDTL
EATLDNQQSL YFANITIGTP AQRLRVHIDT GSSDLWVNSD SSTICTGTDK MPGQCAESGT
YSANSSSTYK YVRSNFNITY MDLSGASGDY VTDNMMIAGA EIKDLQFGVG YRSSSAEAVM
GIGYVTNEVQ VANLGLKAYN NVPAALASQE IISSNAYSLW LNDLDSNSGS ILFGGADTER
FTGALQTLPV QKTNTGYTDF LITLTGLSLG GKTLVEKQAQ AVLLDSGSSL TYLPNAMANA
IYEAIGAQYD SAQSAAFVPC SMRSINSTLD FTFTSPTISV PLDELILDIP ERNGQASTFP
GGAPACLFGI APSGVTVPVL GDTFLRSAYV IYDLDNNEIS LAQTKFNATG SNIVDFGGGK
YASGIATAVA NPVFATAGVG KSGPNKGSDD EEGSAWRSGI AVSPLAVALC GVAAFFTGYM
//
