ID M5CH05_THACB Unreviewed; 411 AA.
AC M5CH05;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN Name=ctsD {ECO:0000313|EMBL:CCO37027.1};
GN Synonyms=CTSE {ECO:0000313|EMBL:CEL56330.1};
GN ORFNames=BN14_11177 {ECO:0000313|EMBL:CCO37027.1}, RSOLAG1IB_11901
GN {ECO:0000313|EMBL:CEL56330.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO37027.1, ECO:0000313|Proteomes:UP000012065};
RN [1] {ECO:0000313|EMBL:CCO37027.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Isolate 7/3/14 {ECO:0000313|EMBL:CCO37027.1};
RA Jelonek L.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCO37027.1, ECO:0000313|Proteomes:UP000012065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065},
RC and Isolate 7/3/14 {ECO:0000313|EMBL:CCO37027.1};
RX PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA Schlueter A.S.;
RT "Establishment and interpretation of the genome sequence of the
RT phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL J. Biotechnol. 0:0-0(2013).
RN [3] {ECO:0000313|EMBL:CEL56330.1, ECO:0000313|Proteomes:UP000059188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL56330.1};
RA Wibberg Daniel;
RL Submitted (NOV-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAOJ01016677; CCO37027.1; -; Genomic_DNA.
DR EMBL; LN679312; CEL56330.1; -; Genomic_DNA.
DR AlphaFoldDB; M5CH05; -.
DR STRING; 1108050.M5CH05; -.
DR HOGENOM; CLU_013253_1_0_1; -.
DR Proteomes; UP000012065; Unassembled WGS sequence.
DR Proteomes; UP000059188; 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: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:UP000059188};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..411
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010503103"
FT DOMAIN 100..408
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 118
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 131..136
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 411 AA; 42644 MW; 3E511FDDF5B2D698 CRC64;
MLTSVIIATA AIAATTVLTS PISEDRIISI PLHKRGSPLN KDGRIIPSAL ARQVTRVQNK
YSHGHAAYKK NTGLELFKEA GGKVKRQAEA LIDEEDDLLW AGTVTIGTPG QSFLIDFDTG
SADLWVPSSS CKTSGCSPHK KYSASASSTS ASKSGTFSIQ YGDGSTASGP IYSDTVTVGG
LSATGQYFSP VTSESSSFAS DPEDGIMGLA FKSISSIGQP TIIDNLYSQG KISAPTFSFR
LATTGSELYL GGANTAKYTG SITYAALTSK TYWLTTGSSS VGSTVGYSGA MIIDSGTTII
VGPTASISSW WSKVSGAAAC STSVCGTTGY YTYLCASPPT VSFTFNGAKF TIPSSDFNLG
TIDNAGTRCV GAIVGTSGVP DNAWIVGDTL MKQTYTVFDQ ANSRVGFATP R
//
