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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//