ID M9MCM2_PSEA3 Unreviewed; 606 AA.
AC M9MCM2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 08-NOV-2023, entry version 42.
DE SubName: Full=Aspartyl protease {ECO:0000313|EMBL:GAC71867.1};
DE Flags: Fragment;
GN ORFNames=PANT_5c00112 {ECO:0000313|EMBL:GAC71867.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC71867.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; DF196771; GAC71867.1; -; Genomic_DNA.
DR AlphaFoldDB; M9MCM2; -.
DR STRING; 1151754.M9MCM2; -.
DR OrthoDB; 4946at2759; -.
DR Proteomes; UP000011976; 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:SF75; ENDOPEPTIDASE (CTSD), PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07040)-RELATED; 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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:GAC71867.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011976};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..606
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004100912"
FT DOMAIN 275..588
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 85..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 293
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 478
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT NON_TER 606
FT /evidence="ECO:0000313|EMBL:GAC71867.1"
SQ SEQUENCE 606 AA; 64355 MW; EADB359B4C98481B CRC64;
MLKFSSRFLT LLLVLLSIGA FDLHSLVDQA ISGHDRVSSW PVAHAAPLYP NDQDAELHAR
ARKPRVGIVV KNGSGFKSGR TAINSLSASE SSSTTSAFES PDGRVGMKVQ LKRLEQDSAS
NPLMLYQRHI NRATSKLATI LGQTGPTPEE QRRALERRKV AILERRGVVS GPDGESSISA
REPQRHTNPR QGYTNHAESG GEMQRRFLEN IMDDLFGKTG SEGGVHAKST VKQVADEGYP
EIDLIASGSD NLTVAGAPTA VQSLGLDIES NDIGYVATIE IGSQNQTFRM LIDSGSADTW
VPSTACRACG SSHQKLGASN SDTFTALSTP FSIQYGTGDA SGNLARDNLE IANLELANYT
FAVTTQESSD FSDDTVPFDG LMGLARSELS NAGQPTPIDA LYKQGKVQAP VMGYHLGRIA
DGYNDGEVTF GGVDPAKYTG NITEIDNVST KGFWEAAMDK ITVGGKDLGL DGRTAILDTG
TTLIVAPEQD ADAVHAQIPG AKSDGQGGYT IPCTTTKQVA LTFGGVDFPI DTRDMLFLPV
DADNLLGDCI SAISAGNVGQ RNEWLVGATF LKNAYFATNT KANKIGLARL NTTDTSIAPS
AAKGKL
//