ID R9P0A5_PSEHS Unreviewed; 432 AA.
AC R9P0A5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Aspartic peptidase {ECO:0000313|EMBL:GAC94514.1};
GN ORFNames=PHSY_002086 {ECO:0000313|EMBL:GAC94514.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC94514.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; DF238784; GAC94514.1; -; Genomic_DNA.
DR RefSeq; XP_012188101.1; XM_012332711.1.
DR AlphaFoldDB; R9P0A5; -.
DR STRING; 1305764.R9P0A5; -.
DR MEROPS; A01.078; -.
DR GeneID; 24107380; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_1_2_1; -.
DR OrthoDB; 1203010at2759; -.
DR Proteomes; UP000014071; 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; cd05471; pepsin_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; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF57; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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:UP000014071}.
FT DOMAIN 74..378
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 92
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 264
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 432 AA; 44689 MW; 453214B862387371 CRC64;
MAAPAPASSS ASSSTPIHVP ISKRNVVKRS GNDLLNWAYD QKTILQSKYN LPASANQRRA
GATSLTNVQY DSSWVASLSG GTPSKSYEVV LDTGSADLWI SSQYYQPSSS STFQNQSTAF
DIQYGSGAVD GYQATDTFTL AGTTVQNLHF AVATSVSSGL TSASMEGIMG MGFQKLASSG
QPPLWVAAGV DTFSFYLERA SLTSSDSTQP GGTFTLGGTN TSLYQGDISY NSLIEELYWM
VRLGGLGARG SAVNLNSLTR AAIDTGTTLI GGPDSVVQQF YSQIPNSQSQ GNGYYSFPCS
SSVDATLTFG TQQYTIPNSD FVAGTLDQSG TQCLGAIFGL GSSAQTDLQW IIGDAFLKNV
YSIFTTNGNN GNAGVGFASL ANGLNSGTNS KSVGSSSNGA SSSSPAAATV KRWNSVAAVL
AAVALPVAVL VA
//