ID M1VYR0_CLAP2 Unreviewed; 395 AA.
AC M1VYR0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Probable aspartic proteinase,pepstatin-sensitive {ECO:0000313|EMBL:CCE27446.1};
GN ORFNames=CPUR_00920 {ECO:0000313|EMBL:CCE27446.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE27446.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE27446.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE27446.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(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:CCE27446.1}.
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DR EMBL; CAGA01000004; CCE27446.1; -; Genomic_DNA.
DR AlphaFoldDB; M1VYR0; -.
DR STRING; 1111077.M1VYR0; -.
DR MEROPS; A01.018; -.
DR VEuPathDB; FungiDB:CPUR_00920; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_4_1; -.
DR OrthoDB; 615305at2759; -.
DR PhylomeDB; M1VYR0; -.
DR Proteomes; UP000016801; 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:SF89; 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:UP000016801}.
FT DOMAIN 85..392
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 103
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 284
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 116..121
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 395 AA; 42661 MW; F436DD50AE49911E CRC64;
MKSVLIAAAA LAGSAQAGVH KMKLQKISLE EQLAGASIEQ HVQHLGQKYL GSRPLSRVDV
MFNAAAPQPQ GGHPVPVTNF MNAQYFSEIT IGTPPQTFKV VLDTGSSNLW VPSQSCSSIA
CYLHNKYDSS SSSTYEKNGT QFEIRYGSGS LSGFVSNDVM SIGDLKIKKQ DFAEATAEPG
LAFAFGKFDG ILGLGYDSIS VNNIVPPFYN MVKQKLLDEP VFAFYLGSSE EGSMATFGGL
DKSHYTGKLE YIPLRRKAYW EVDINSIAFG DEVADLENTG AILDTGTSLN VLPSSLADML
NKEIGAKKGW NGQYTIECDK KKSLPDIVFN LAGSNYSLPA SDYILELQGS CISTFQGMDI
PEPAGPLIIL GDAFLRRYYS VYDLGKNAVG LALAK
//
