ID A0A074XPH3_9PEZI Unreviewed; 429 AA.
AC A0A074XPH3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 30.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KEQ76486.1};
GN ORFNames=M436DRAFT_37338 {ECO:0000313|EMBL:KEQ76486.1};
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:KEQ76486.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ76486.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ76486.1,
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}.
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DR EMBL; KL584703; KEQ76486.1; -; Genomic_DNA.
DR RefSeq; XP_013430613.1; XM_013575159.1.
DR AlphaFoldDB; A0A074XPH3; -.
DR STRING; 1043004.A0A074XPH3; -.
DR MEROPS; A01.080; -.
DR GeneID; 25408817; -.
DR HOGENOM; CLU_013253_0_2_1; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000027730; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KEQ76486.1};
KW Protease {ECO:0000313|EMBL:KEQ76486.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027730}.
FT DOMAIN 98..421
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 116
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 312
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 429 AA; 46406 MW; 025E0A5E4EE4398B CRC64;
MKHNLHRVKL IHNPKYQHSG LKSYVYLLRK YNFAPTLEGP YFVSNIVEQL GKPSLMNKFA
THIGGHAKVK KHQLMKKDAT SGQEGQVSAA DQQNDSEYLC QVSIGTPAQV LTLDFDTGSS
DLWVWSTNLS QDIQTQGKQA GHTIFDPSKS STWKDSQGST WQISYGDSSS ASGTVGTDVV
NVGGLAIQNQ AVEVANQISD QFVQSTGDGL LGLAWGSINT VQPTPVETPV ENMISQDDIP
KDSELFTAYL SSEKSGEESF YTFGFIDTSV TNGQTINYTP VDNSQGFWSV PSASAHVNGK
QIKRNNNTAI MDTGTTLCLV DDNLVKAVYA AIPGAKYDSS QQGYTFPTNT ATSDLPVVTV
AIGNHQYTIG KETLGFADAG NGMTYGGIQS RGDMTFDILG DVVLRSIYAV FDQGNQRFGA
VQRTSPSTQ
//
