ID L8WU24_THACA Unreviewed; 554 AA.
AC L8WU24;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Asp domain-containing protein {ECO:0000313|EMBL:ELU39834.1};
GN ORFNames=AG1IA_06115 {ECO:0000313|EMBL:ELU39834.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU39834.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU39834.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(2013).
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:ELU39834.1}.
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DR EMBL; AFRT01001600; ELU39834.1; -; Genomic_DNA.
DR AlphaFoldDB; L8WU24; -.
DR STRING; 983506.L8WU24; -.
DR HOGENOM; CLU_491901_0_0_1; -.
DR Proteomes; UP000011668; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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:SF6; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022750};
KW Protease {ECO:0000256|ARBA:ARBA00022750};
KW Reference proteome {ECO:0000313|Proteomes:UP000011668};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..554
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005358062"
FT DOMAIN 111..447
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 554 AA; 59784 MW; 42ED54C3D5F17844 CRC64;
MWHLSVSALS LGLALTVAAA PTPAQPKILR RLTPGANVIS LSRTNSITDL ETGQFNETFC
MKGSNMQMRW HHPDLNVSVE QLQTTHARLF RRQAAQNTTI TLTDIGPDLL WSGPVTVGSK
TFNVDFDTGE LPMICVLPDL DSQHLINVSA QAISIPKLFT DIGCTGPAAQ CAGKNIYTPS
QVSHIFLILN ADLRHAYSVQ SSTSAKTPNT FQISFGDGSA VRANVFTDTV SIGGLAITNS
GVGAVTQLSQ SFTNAGGDTS DGLMGMAFPV LAESKQTPYF SNLAKLSPTQ GMMSFKFVGK
NAPGSELTVG GMNTAAFTGH HHRSGPLTWG RRALAENRAS QFATIDTGTS VVIAPQADAQ
AIYAAIPGSK LGQNGLFTYP CNANPDVALN FAGQNFNIKA ADISHMYRTC RYLTFCYQVP
QERVYCRICQ TRARMDFGDG GARLTPLEEF TRLDDAVIAG IGTGTACPIE GWNYAAPPES
GLYKAPWWAL ELFRNTTTPI LISNTYHYDY RTSRLLTTAA YVDVPSRCTA CSYVLTPPRS
HGIVRKTASG EYLF
//