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
//