ID W6ZHW7_COCMI Unreviewed; 399 AA.
AC W6ZHW7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=COCMIDRAFT_79427 {ECO:0000313|EMBL:EUC51427.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC51427.1};
RN [1] {ECO:0000313|EMBL:EUC51427.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC51427.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KI963918; EUC51427.1; -; Genomic_DNA.
DR RefSeq; XP_007682279.1; XM_007684089.1.
DR AlphaFoldDB; W6ZHW7; -.
DR STRING; 930090.W6ZHW7; -.
DR GeneID; 19125472; -.
DR KEGG; bor:COCMIDRAFT_79427; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_4_1; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000054032; Unassembled WGS sequence.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:InterPro.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05488; Proteinase_A_fungi; 1.
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 InterPro; IPR033819; Saccharopepsin.
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}.
FT DOMAIN 87..396
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 288
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 118..123
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 322..355
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 399 AA; 43348 MW; DCE6C631BE515C82 CRC64;
MKTAILLAAA SSASAAIYKT PLKKVSLSDQ LEHANIETQL AGLKHKYSHQ RMANFKSQSQ
MAAALKAPYI ADGSHPVPVS NFLNAQYFSE ISLGTPPQSF KVVLDTGSSN LWVPSTECSS
IACYLHTKYD SSASSTYKKN GTEFEIHYGS GSLSGFVSND VFQIGDLKVK NQDFAEATSE
PGLAFAFGRF DGIMGLGYDT ISVNRMVPPF YNMINQGLLD EPVFAFYLGD TKDSQESEAT
FGGIDESHYT GKLTKIPLRR KAYWEVDLDA ITFGKETAEM ENVGAILDTG TSLIALPSAM
AELLNKEIGA KKGFNGQYSV ECNKRDSLPD LTFTLTGHNF TIDAYDYILE VQGSCISAFM
GMDIPEPAGP LAILGDAFLR KWYSVYDLGN SAVALAKSK
//
