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Database: UniProt
Entry: A0A0D2BHZ9_9EURO
LinkDB: A0A0D2BHZ9_9EURO
Original site: A0A0D2BHZ9_9EURO 
ID   A0A0D2BHZ9_9EURO        Unreviewed;       508 AA.
AC   A0A0D2BHZ9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=PV08_10283 {ECO:0000313|EMBL:KIW10984.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW10984.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW10984.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW10984.1,
RC   ECO:0000313|Proteomes:UP000053328};
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 Exophiala spinifera CBS89968.";
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; KN847499; KIW10984.1; -; Genomic_DNA.
DR   RefSeq; XP_016231200.1; XM_016384598.1.
DR   AlphaFoldDB; A0A0D2BHZ9; -.
DR   STRING; 91928.A0A0D2BHZ9; -.
DR   GeneID; 27337366; -.
DR   VEuPathDB; FungiDB:PV08_10283; -.
DR   HOGENOM; CLU_013253_9_3_1; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000053328; Unassembled WGS sequence.
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: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};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
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:UP000053328};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..508
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002249848"
FT   DOMAIN          55..392
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        309..355
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   508 AA;  53780 MW;  9C05EDC69B1C662C CRC64;
     MKHLILLSGI FTLVLAKSII FDFWKERPVH RPSLSRRSND DFSNPLYGDY EKVQYYVNVT
     IGTPGQRVAL QLDTGSSDTW VPSVDAESCA DDGCSDFGAF DKNTSSTYHL IEDQVGMFGI
     MYADGTYASG DYFTDVLSFG ENITLKDTTM ALANDTVLTE GLMGIGFRSN EASLENDEPF
     SFPTVPEQLK NQGYIDRVAY SLYLDSYEDN TGSILFGGID SSKHIGELLA LPLSKDDEGN
     YTEFLVALTQ ISIHDGKSTR SLTRPTFNTP ALLDSGTTDS YLPKKVFDAL SDGLGATEDQ
     GSGYAYVPCA YRKSNVSVIY TFGGKDGVNV SVPLSELISE QIDDDSAYEN GTPACALNFN
     PTDDQNGIIL GDSFLRSAYV VYDLENKVIA LGQAKLGGKS AANSAAITDI PKGTALPGVS
     RTATVTAAQA TSSLDDSPSS SSSSSLSLGA IGTPTFSLPG VSLTAVASPT GTAASAAKGA
     SKDNGAVLVG VSKSTCVMAV LAFVMCML
//
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