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Database: UniProt
Entry: A0A081CCU8_PSEA2
LinkDB: A0A081CCU8_PSEA2
Original site: A0A081CCU8_PSEA2 
ID   A0A081CCU8_PSEA2        Unreviewed;       609 AA.
AC   A0A081CCU8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   08-NOV-2023, entry version 43.
DE   SubName: Full=Acid protease {ECO:0000313|EMBL:GAK64494.1};
DE   SubName: Full=Related to extracellular aspartic proteinase {ECO:0000313|EMBL:SPO44997.1};
GN   ORFNames=PAN0_005d2708 {ECO:0000313|EMBL:GAK64494.1}, PSANT_02683
GN   {ECO:0000313|EMBL:SPO44997.1};
OS   Pseudozyma antarctica (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK64494.1, ECO:0000313|Proteomes:UP000053758};
RN   [1] {ECO:0000313|Proteomes:UP000053758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10317 {ECO:0000313|Proteomes:UP000053758};
RA   Saika A., Koike H., Hori T., Fukuoka T., Sato S., Habe H., Kitamoto D.,
RA   Morita T.;
RT   "Draft Genome Sequence of the Yeast Pseudozyma antarctica Type Strain
RT   JCM10317, a Producer of the Glycolipid Biosurfactants, Mannosylerythritol
RT   Lipids.";
RL   Genome Announc. 2:e00878-e00814(2014).
RN   [2] {ECO:0000313|EMBL:GAK64494.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK64494.1};
RA   Morita T., Saika A., Koike H.;
RT   "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT   as a producer of lipase B which used in a wide range of industrial
RT   applications.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SPO44997.1, ECO:0000313|Proteomes:UP000325008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34888 {ECO:0000313|Proteomes:UP000325008}, and ATCC34888
RC   {ECO:0000313|EMBL:SPO44997.1};
RA   Guldener U.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; DF830072; GAK64494.1; -; Genomic_DNA.
DR   EMBL; OOIQ01000005; SPO44997.1; -; Genomic_DNA.
DR   RefSeq; XP_014657434.1; XM_014801948.1.
DR   AlphaFoldDB; A0A081CCU8; -.
DR   GeneID; 26303589; -.
DR   HOGENOM; CLU_013253_1_1_1; -.
DR   OrthoDB; 4946at2759; -.
DR   Proteomes; UP000053758; Unassembled WGS sequence.
DR   Proteomes; UP000325008; 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:GAK64494.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053758};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..609
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035354825"
FT   DOMAIN          275..588
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          81..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..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"
SQ   SEQUENCE   609 AA;  64494 MW;  5CC4299173AE9466 CRC64;
     MLKFSSRFLT LLLVLLSIGA FDLHSLVDQA ISSHDRVSSW PVAHAAPLYP NGQGAELQAR
     AKKPRVGIVV KNGSGFKSGR TAINSLSTSE SSSTTSAFES PDGRVGMKVQ LKRLEPDSAS
     NPLMLYQRHL NRATSKLATI LGQTGPSPEE QCRALERRKV AILERRGMVS ALDGESLLSA
     RDPQRHTNPR QGYTNHAESG GEMQRRFFEN IMDDLFGKTG TEGGVHAKST VKQVADEGYP
     EIDLTASGSD NLTVSGAPTA VQSLGLDIES NDIGYVATIE IGSQNQTFRM LIDSGSADTW
     VPSTACRACG SSHQKLGASN SDTFTALSTP FSIQYGTGDA SGSLARDNLE IANLELANYT
     FAVTTQESSD FSDDTVPFDG LMGLARSELS NAGQPTPIDA LYKQGKVQAP VMGYHLGRIA
     DGYNDGEVTF GGVDPAKYTG NITEIDNVST KGFWEAAMDK ITVGGKDLGL DGRTAILDTG
     TTLIVAPEQD ADAVHAQIPG SKSDGQGGYT IPCTTTKQVA LTFGGVDFPI DTRDMLFLPV
     DADNLLGDCV SAISAGNVGQ RNEWLVGATF LKNAYFATNT KANKIGLARL NTTDTSIAPS
     AAKGKLASA
//
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