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Database: UniProt
Entry: A0A074XRP7_9PEZI
LinkDB: A0A074XRP7_9PEZI
Original site: A0A074XRP7_9PEZI 
ID   A0A074XRP7_9PEZI        Unreviewed;       470 AA.
AC   A0A074XRP7;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   28-JUN-2023, entry version 38.
DE   SubName: Full=Candidapepsin-4 {ECO:0000313|EMBL:KEQ77246.1};
GN   ORFNames=M436DRAFT_78972 {ECO:0000313|EMBL:KEQ77246.1};
OS   Aureobasidium namibiae CBS 147.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ77246.1, ECO:0000313|Proteomes:UP000027730};
RN   [1] {ECO:0000313|EMBL:KEQ77246.1, ECO:0000313|Proteomes:UP000027730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ77246.1,
RC   ECO:0000313|Proteomes:UP000027730};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KL584703; KEQ77246.1; -; Genomic_DNA.
DR   RefSeq; XP_013431466.1; XM_013576012.1.
DR   AlphaFoldDB; A0A074XRP7; -.
DR   STRING; 1043004.A0A074XRP7; -.
DR   GeneID; 25416351; -.
DR   HOGENOM; CLU_013253_9_3_1; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000027730; 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; 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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027730};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..470
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001702527"
FT   DOMAIN          69..391
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        87
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   470 AA;  49922 MW;  F6B48C48FD7422B0 CRC64;
     MKHISTLALA ASTIIGAEAI NLQKRSNGAP KVVEYEIERK TVVNPLKRDR LRRRQNTISE
     DLDNEQTLYF ANASIGTPAQ SFRLHIDTGS SDLWVNVATS SQCENTQQND CSISGTYAPN
     SSSTYEYVNS LFNISYVDGS GSSGDYATDV FRIGGAELQN QQLGIGYVSS SEEGILGIGY
     PTNEAILQYS RESYVNVPQH MMQAGLINTN AYSLWLNDLD ASKGSILFGG VNTEKYTGSL
     QTLPIIQEQG IYAEFIIALT GVGYNGNDNS IASNLNTAAL LDSGSSLMYL PNDVTESIYR
     MTGAKYSQEY GAAFIDCNMR YNDTTIDFTF SSPTIRVSMS ELVLVMGYQG RTPLCILGIA
     PADGTTPVLG DTFLRSAYVV YDITNNEISL AQTNFNSTGS NIMEITNTSI PDATGVASAV
     TSVSEQTGGA RLGGVPSGSV TSSGIGAVIT PGPKGVAALA AVGAAALFAL
//
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