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Database: UniProt
Entry: A0A135TTW7_9PEZI
LinkDB: A0A135TTW7_9PEZI
Original site: A0A135TTW7_9PEZI 
ID   A0A135TTW7_9PEZI        Unreviewed;       449 AA.
AC   A0A135TTW7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:KXH51569.1};
GN   ORFNames=CSAL01_03385 {ECO:0000313|EMBL:KXH51569.1};
OS   Colletotrichum salicis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH51569.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH51569.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH51569.1,
RC   ECO:0000313|Proteomes:UP000070121};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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:KXH51569.1}.
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DR   EMBL; JFFI01001879; KXH51569.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135TTW7; -.
DR   STRING; 1209931.A0A135TTW7; -.
DR   OrthoDB; 2900143at2759; -.
DR   Proteomes; UP000070121; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KXH51569.1};
KW   Protease {ECO:0000313|EMBL:KXH51569.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..449
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007804223"
FT   DOMAIN          106..433
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   449 AA;  48167 MW;  CD794AAC837EFF21 CRC64;
     MIPSLAFPLL WSALAHAIPT DIQQQPELPE LQRRSTLTVP VRSNPDFILD GPAALATAYE
     RWNMPVPASL AYHNRSRKPQ PQSTPKADRP CPAAVVAAKS SNDFYWLTDI FVGSATQKMP
     VIIDTASSDF WLMSTDTELG EVAVNGLPAL YDPAKSASSQ EPTKISQLTS AVIADSSTSS
     GKVYFDTVGF GLVTDNNHFT IANATIQSAV NVAPRWAIEP KISGVMGLAK SKPSSVKPGM
     PSMLDRLKPS LHYEWIGIDL RPNSDKGFFS FGYAMGTANN KEPPVDDDEH WSFELQGTRP
     SSMNGRLWNK FKKRTIATID TGSSFVLLPG DMVANYYAGI PDSAHDPKLK AWVFPCASAP
     SIPDLQFLTA GGYVGTILKE SINLGPAPGS SEMCFGGIQG SESGGRSIFG GVALKSMYVQ
     LNYGASGTFV SFGEKSSLDV CSTTTACQS
//
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