ID A0A061HG24_9BASI Unreviewed; 418 AA.
AC A0A061HG24;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=PFL1_02785 {ECO:0000313|EMBL:EPQ29566.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ29566.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ29566.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ29566.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KE361630; EPQ29566.1; -; Genomic_DNA.
DR RefSeq; XP_007878491.1; XM_007880300.1.
DR AlphaFoldDB; A0A061HG24; -.
DR MEROPS; A01.018; -.
DR GeneID; 19316900; -.
DR KEGG; pfp:PFL1_02785; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_4_1; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:InterPro.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05488; Proteinase_A_fungi; 1.
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 InterPro; IPR033819; Saccharopepsin.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF87; 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|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000053664};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..418
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001604175"
FT DOMAIN 106..414
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 124
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 306
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 137..142
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 418 AA; 44622 MW; AD270029D3382549 CRC64;
MKLNLSLTFV AGLAAAAIGV DAGVHKAKLQ KLPSAAKLTP ELLAAQAEIL QLKYGGAKQA
PFKSGNNAEH DFSIQPVEQA SDASAWYAEA KKGHGVPLTD FLNAQYFCDI SLGTPPQEFK
VILDTGSANL WVPSTHCSSI ACFLHKKYDS SASSSYKKNG TEFKIQYGSG SMEGIVSQDT
LKIGDLTVKG QDFAEATSEP GLAFAFGKFD GILGLAYDTI SVNGIVPPLY QMINQGLLDE
PVVSFYLGSS ESDGGVATFG GIDENHYDGK IHWAPVKRKG YWEVGLDKLA LGDEELELDN
GSAAIDTGTS LIALAQDTAD ILNAEIGAKK GWNGQYSIEC EKVPSLPKLT FYIDGKPFEL
EGKDYILEVQ GSCISSFQGL NLPGPLADLI IVGDVFLRKY YSAYHLGKNA VGLAPSRA
//
