ID G8YP67_PICSO Unreviewed; 414 AA.
AC G8YP67;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Piso0_001822 protein {ECO:0000313|EMBL:CCE79735.1};
GN Name=Piso0_001822 {ECO:0000313|EMBL:CCE79735.1};
GN ORFNames=GNLVRS01_PISO0E13424g {ECO:0000313|EMBL:CCE79735.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE79735.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; FO082055; CCE79735.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YP67; -.
DR STRING; 559304.G8YP67; -.
DR MEROPS; A01.018; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_4_1; -.
DR InParanoid; G8YP67; -.
DR OMA; EGDAAQC; -.
DR Proteomes; UP000005222; Chromosome E.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF89; SACCHAROPEPSIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000005222};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..414
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003518943"
FT DOMAIN 100..411
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 118
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 303
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 131..136
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 337..370
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 414 AA; 44533 MW; E9656E91C54740BC CRC64;
MRVSGTLINS VVLASILQAG VDAKKVSTSI SKVPLEETLN DKSFNKYTEA LANKYLNLFN
NAGGKGAGAP VQSSQEGAQI PFVAQGGHDA PLVDYLNAQY YTTIGLGSPA QEFKVILDTG
SSNLWVPSTD CSSLACFLHS KYYHDESSSY KQNGSDFSIQ YGTGSLEGYV SQDTLNLAGL
TIEKQDFAEA TSEPGLTFAF AKFDGILGLA YDSISVDNIV PPIYNAIDQG LLDEPKFAFY
LGDKDKDENE GGVATFGGVD TKHYKGDIIE LPVRRKAYWE VSFDGIGLGD EYAELTSTGA
AIDTGTSLIT LPSSLAEIIN AKIGAKKSWS GQYSVDCDSR DSLPELTMTF HGHNFTLSPY
EYTLEVGGSC ISAFTPMDFP KPIGDLAIVG DSFLRKYYSV YDIGKNVVGL AESR
//
