ID L8WJZ1_THACA Unreviewed; 800 AA.
AC L8WJZ1;
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=Aspergillopepsin A {ECO:0000313|EMBL:ELU37057.1};
GN ORFNames=AG1IA_08912 {ECO:0000313|EMBL:ELU37057.1};
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:ELU37057.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU37057.1, 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, 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:ELU37057.1}.
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DR EMBL; AFRT01002884; ELU37057.1; -; Genomic_DNA.
DR AlphaFoldDB; L8WJZ1; -.
DR STRING; 983506.L8WJZ1; -.
DR HOGENOM; CLU_351666_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:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 4.
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:SF1; ASPARTYL PROTEINASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 3.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 2.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011668}.
FT DOMAIN 106..398
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 491..797
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 800 AA; 89284 MW; 34F273C978E46124 CRC64;
MIPPDYNYPT HGIIHYGPGG FSVHADRNVK YRPNGPSDYA KCIRKYRIGA TQYTPFYFDT
NRACVCHCKQ PEKVNIMGNI PGNIRVAAFD RDPVNLDHDD GMTIVQANDI QNGRYRVRMS
GDNWDTCTGS SDFWVWSSEF RATRAQLEGH KVYDPHRSKT AESLPGATWK ISYGDGSHAS
GDVVMDTIII GDITIKQQAV EVARQLSDEF LRGGSDGLLG LAFPKLNTVQ PHQQKTPMQN
MVEQGLVKDL DKHDSRGFYT FGYINEHVHA SKLYWQGVIT KNGWWEGDTG TTLILLDDDT
IERLYSQIPG ARLDRHIVHT GGYVFPTHAR IPELAFCVGR WLFTIPGRDL AFSDAGNGMS
YGAIQSRGQN KQDILGDVFL KHVYVVFDQG KTPRVGVPIS LAPHKLQIIL PEIHSDYGTV
HYKPAGFSIH AHRNTLHRRH GPNAYAKSVR KYKIGPTNHT PFFFDEIAAC VFHHKHWREI
LGNNAVGLDV KGPDNRMAIV QAEDIHNGDN GLLLSWISTN RAQIESHRVY TPHKSRTSER
VPGATWSISY GDGSHASGDV VLDTVAIGDI TIRSQAVGVS QHLSDEFLKD GSDGLLGLAC
NAVPKLNTVK PYQQKTPMQN MVEQGLIKDL DKHDSHGFYT FGYISEHIHA SKLYWQDVIS
DNGWWEVVSP YVKIGHNIYD RGHLNTAIID TGTTLILMDD RTVENLYSQI PGAKLDRTLG
GYIFPTDACV PKLAFSIGKW LFTIPSEDLA FSDAGDGMSY GAIQSRGQNK QDILGDVFLK
HVYVVFDQGM NPKVGVAQRD
//
