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
//