GenomeNet

Database: UniProt
Entry: M9MCM2_PSEA3
LinkDB: M9MCM2_PSEA3
Original site: M9MCM2_PSEA3 
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
//
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