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Database: UniProt
Entry: R9P0A5_PSEHS
LinkDB: R9P0A5_PSEHS
Original site: R9P0A5_PSEHS 
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
//
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