ID A0A010QTX4_9PEZI Unreviewed; 390 AA.
AC A0A010QTX4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=CFIO01_00789 {ECO:0000313|EMBL:EXF83647.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF83647.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF83647.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF83647.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) 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:EXF83647.1}.
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DR EMBL; JARH01000224; EXF83647.1; -; Genomic_DNA.
DR RefSeq; XP_007592777.1; XM_007592715.1.
DR AlphaFoldDB; A0A010QTX4; -.
DR KEGG; cfj:CFIO01_00789; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_062498_0_0_1; -.
DR OrthoDB; 398606at2759; -.
DR Proteomes; UP000020467; 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:SF68; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..390
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001455660"
FT DOMAIN 33..373
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 390 AA; 41838 MW; AF27223E2E70F0D9 CRC64;
MSPVTRFFSA SAVASVATAA VLDLGIIVDN GYKVVEFGIG TPAKTFRLLF DTGSSSSWAT
DSQCLAKGNC NNGSGYDRTG YSINASTSGH YTGESAVIPY LGGDVAGPTV AEKWTVGNFS
WDQSFIAANE SNWAALAADG FMGLGFSSII DGGANTVVET LMAENRLDAA KFGIYYGTEA
KNTSGVPGDG VLTIGGSRED EYVDGDLVTI PITRVDGTYD VWRSTILKVN GTRTTSNGSV
IETKTDFDQA RVVFDTGAGS ITLPTKQNLA VYESIGMNYT KILKGEHIPL CSEFNSSWSF
KFTFGDYRYP QTIEIPGDQL ARPGFAYRDD ACWPPFEDGA QSGFVLIGTP FLRNFYTVWD
YGSAANETVI GKFDPTLSFG YLKNKTTTAE
//