ID A0A0D2G6U2_9EURO Unreviewed; 416 AA.
AC A0A0D2G6U2;
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=Z517_11104 {ECO:0000313|EMBL:KIW76358.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW76358.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW76358.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW76358.1,
RC ECO:0000313|Proteomes:UP000053029};
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 Fonsecaea pedrosoi CBS 271.37.";
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; KN846975; KIW76358.1; -; Genomic_DNA.
DR RefSeq; XP_013280166.1; XM_013424712.1.
DR AlphaFoldDB; A0A0D2G6U2; -.
DR STRING; 1442368.A0A0D2G6U2; -.
DR GeneID; 25310594; -.
DR VEuPathDB; FungiDB:Z517_11104; -.
DR HOGENOM; CLU_013253_0_2_1; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000053029; 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; 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:UP000053029}.
FT DOMAIN 73..405
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 111..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 295
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 416 AA; 45119 MW; 7F61B12130FE6FCB CRC64;
MALSKVTRVP VLRNADYKAN GTKSLVWLYN KYNITPTRPG PYHRDEKNRL MKRQDDGSST
EVTAQDQQND VYYTCPVTIG TPGQRLQVTF DSGSADFWVW SSHLPESTKK SGTASGAAIY
DPNKSSTQKP MAGSTWQIRY GDGSSASGTV VTDVVKVGDI TIEGQAVEIA SHISSSLTTQ
TASQGILGLA FGNINTVTPV PVKTPLDNMI AQEDIPNDQE IFTCYMGSYK DAKDPDHGES
FFTFGNIDSE VVHATGGEIS YTPVNDSNGF WEFASEYVVI NGKKTPLPGN TAIADTGTTL
MIIDDDLVEE IYSSIPGAAY DQSQQGWLIP SDTPLEQIPD VAFAVGGVDI AIQKEHIAFA
PLKNTGMVFG GIQGRGRLPY NIYGDTFLKC VYAVFDAGKK QFGVVQRVDP TQKIAF
//
