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Database: UniProt
Entry: A0A0D2IMY3_9EURO
LinkDB: A0A0D2IMY3_9EURO
Original site: A0A0D2IMY3_9EURO 
ID   A0A0D2IMY3_9EURO        Unreviewed;       504 AA.
AC   A0A0D2IMY3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=Z520_05677 {ECO:0000313|EMBL:KIX98376.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX98376.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIX98376.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX98376.1,
RC   ECO:0000313|Proteomes:UP000053411};
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 multimorphosa CBS 102226.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KN848071; KIX98376.1; -; Genomic_DNA.
DR   RefSeq; XP_016632499.1; XM_016776180.1.
DR   AlphaFoldDB; A0A0D2IMY3; -.
DR   STRING; 1442371.A0A0D2IMY3; -.
DR   GeneID; 27711423; -.
DR   VEuPathDB; FungiDB:Z520_05677; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000053411; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF81; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00022622};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..504
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002244148"
FT   DOMAIN          60..396
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   504 AA;  51217 MW;  E5D8BF19ED5DACBE CRC64;
     MYLLCATAIA ALATSCVAST GYLRLDLQRR TASEGRLVRR QNSDGSLDTV LTQNPDKLEY
     LVNVTVGTPP QHLGVTLDTG SSDLWVPASS AKLCQKGQCD LGDFNPSSSS TYKIIEQGGF
     NITYAQQGDS DAGDWSSDTI TVGGSPSIKN QQLGVATELF DQHGVMGIGF DTNEANNDSP
     NGVYPSVMDN LKSSGIINRK AFSLYLNDLE ANTGAVIFGG IDTTKYSGDL VALPLQPGPE
     GIVSEYYVAL TSVSFTDSTG QTTQLSPQGY AQATLLDSGT TNTLLTNDVF TGLALGFGAV
     FDPSQDAYLV PCSLASANGT INYSFGGDDG VTVQVPVSEV VGGLAYPSSL FDDPSGGCVL
     AFGTPSDSGG FSIMGDSFLR SAYAVFDIDN KVAALAQAVE NEASTSSIVV IPTGTTIPSA
     TATATATGTQ LSQVADETGV PTASVQGTTL LPGTPTFSLV TSSSAATSTA AGAGASSSSG
     AANNAAVPTA ALLGLGLAAG VMGL
//
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