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Database: UniProt
Entry: L8WU24_THACA
LinkDB: L8WU24_THACA
Original site: L8WU24_THACA 
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
//
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