ID A0A162PDB5_9PEZI Unreviewed; 461 AA.
AC A0A162PDB5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:KZL87018.1};
GN ORFNames=CI238_02174 {ECO:0000313|EMBL:KZL87018.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL87018.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL87018.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL87018.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-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:KZL87018.1}.
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DR EMBL; LFIW01000342; KZL87018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162PDB5; -.
DR STRING; 1573173.A0A162PDB5; -.
DR Proteomes; UP000076584; 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:SF81; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 2.
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, ECO:0000313|EMBL:KZL87018.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..461
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007838111"
FT DOMAIN 56..447
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 461 AA; 47234 MW; F2679264B76C3502 CRC64;
MAGFRRPLAL LASALLSSHC LSAPAGGGSA TTANGSAGVI QMPIIHFDSK ATGILPLVDV
GIGNPPQTVR MIIDTGSSDL IAAEAGSAVC KDPEQQCTKS KSGLILGSFD PNQSKGFEKV
AGQTLDTTFG TGESYQGPMV KDTLTLGSSQ VPAAQIGLME TGSIPPNTPS FSVFGVGPVG
NEGAAKQYVN VPARMKEAGV INKNAYGVYL NDFSKRHSTP AEPLQLMKRT YQKLTLPDLE
GSDGSITFGG MDTAKFDGKL QDVPLIPDDN GKFGQFVVSF SSMSVSGQAG AGAGVPNDGA
KKKRAQAAKG GAGADAAAAN FVSNPLPALL DTGNPALDLP LEAVTGMAKA LGINTQKDGD
ATLLGPMPCS MGASMNLVLG FNKDAVKMSV PFSLLMVPAT GKEGAAGQCV MPQIVGLKDV
GLTSLGAPFL QAMYAVFDVD QNQISLAQAK MNTTESKLVP F
//
