ID A0A0F8BMR2_CERFI Unreviewed; 398 AA.
AC A0A0F8BMR2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Vacuolar protease A {ECO:0000313|EMBL:KKF93783.1};
DE EC=3.4.23.- {ECO:0000313|EMBL:KKF93783.1};
GN Name=pep-4 {ECO:0000313|EMBL:KKF93783.1};
GN ORFNames=CFO_g3854 {ECO:0000313|EMBL:KKF93783.1};
OS Ceratocystis fimbriata f. sp. platani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF93783.1, ECO:0000313|Proteomes:UP000034841};
RN [1] {ECO:0000313|EMBL:KKF93783.1, ECO:0000313|Proteomes:UP000034841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFO {ECO:0000313|EMBL:KKF93783.1,
RC ECO:0000313|Proteomes:UP000034841};
RA Belbahri L.;
RT "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT trees.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKF93783.1}.
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DR EMBL; LBBL01000207; KKF93783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8BMR2; -.
DR Proteomes; UP000034841; 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 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 PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF89; 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, ECO:0000313|EMBL:KKF93783.1};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KKF93783.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034841};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..398
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002527929"
FT DOMAIN 87..395
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 287
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 118..123
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 398 AA; 43162 MW; 5D9AAEE83531A46C CRC64;
MRGTNAFVVA MLGTASAAVH TMKLKKVPLT EQLATASIEE HVDALSQKYL GEHQFNLADA
MFNTKTSNFA MNSGHPVPVS NFMNAQYFSE ITIGTPPQTF KVVLDTGSSN LWVPSSKCGS
IACYLHEKYD SSQSNTYEKN GTKFEIHYGS GSMTGFVSQD TVTMGDIEIK KQLFAEATSE
PGLAFAFGRF DGILGLGYDT ISVNGIPPPF YNMVDQGLID EPVFAFYLSK EDKGESEAIF
GGVNKAHYTG DITYIPLRRK AYWEVDLDSI AFGEEVAELE NTGVILDTGT SLNVLPSSLA
ELLNKEIGAK KGYGGQWSVD CAKKSTLPDI TFNLAGHNYS LPAEDYILEV SGSCISTFQG
MDFPAPTGPL AILGDAFLRR YYSVYDLGKN AVGLAKAK
//
