ID A0A0D2B6P3_9EURO Unreviewed; 419 AA.
AC A0A0D2B6P3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 37.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=PV07_00142 {ECO:0000313|EMBL:KIW33282.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW33282.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW33282.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW33282.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KN847040; KIW33282.1; -; Genomic_DNA.
DR RefSeq; XP_016253498.1; XM_016386570.1.
DR AlphaFoldDB; A0A0D2B6P3; -.
DR STRING; 569365.A0A0D2B6P3; -.
DR MEROPS; A01.080; -.
DR GeneID; 27339336; -.
DR VEuPathDB; FungiDB:PV07_00142; -.
DR HOGENOM; CLU_013253_0_2_1; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000054466; 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:UP000054466}.
FT DOMAIN 72..397
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 400..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 287
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 419 AA; 44756 MW; AFC2EC2B51F3A4E3 CRC64;
MASLIRVPIR RNPHYKRNGL KSYVYLLNKY RISPTIQGPY SAAKGKKLLV KQNADGSQGE
VTASDQQNDS LYTCPVKIGT PAQTLNLDFD SGSSDLWCWS TELPQSTLSA GKGHTIFDPS
KSSTFQTSQG STWQIQYGDQ SSASGSVGTD NIEIGNITVK NQAIELATKL SSQFTQDASS
DGLLGLAFGS INTVKPSAVQ TPVANMIAQD DIPQNAELFT CYLGSIKDAN EESFYTFGQI
DQSVVPSGSS IGYTPVDNSQ GFWMFDSTSA QVNGKTIQLS GNKAIADTGT TLLLTSDEVC
QAIYSAIPGA QQDSSQQGWV YPANTAESDL PTVTFMVGDT PITIEKQHLA FAGGSDGNMV
YGGIQSRGDQ NFDIFGDTFL QNVYAVFDVG NTRFGVVQRA APTSTSTTTS ASTQPKAEL
//
