ID A0A066X5D4_COLSU Unreviewed; 462 AA.
AC A0A066X5D4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative eukaryotic aspartyl protease {ECO:0000313|EMBL:KDN64358.1};
GN ORFNames=CSUB01_06239 {ECO:0000313|EMBL:KDN64358.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN64358.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN64358.1}.
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DR EMBL; JMSE01001140; KDN64358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066X5D4; -.
DR STRING; 1173701.A0A066X5D4; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_035052_0_0_1; -.
DR OMA; YFAPCDA; -.
DR OrthoDB; 4940213at2759; -.
DR Proteomes; UP000027238; 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 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:SF47; ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01220)-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
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 ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KDN64358.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..462
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001629884"
FT DOMAIN 104..448
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 120
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 339
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 462 AA; 49554 MW; CA0D493C08077D5D CRC64;
MKFVGLVSSL LGFGLLSASV ALAKDRHRVG VEIKSPLKGV NFQRIKAFRD VAPDEVSGLV
QALKPFRIII AGHNAATALG AAQPRGLSAA YQNITALSPY GTQYAVEVIW DGKPINMIFD
TGSSDTWATA SNFTCTNMAG TAAYSQEACG FGPSKIDSFK YGPAEDLHFT LSYGSGERVS
GPMGFSDIEV AGITVQQQQV GLANKTYWMG NNYTNGILGL AFPSLTSAFT GDMDEDRPAF
QVPYSPFFTS MVQQGMSADS FSVSLVRNSS GLIAWGGRTG LPVDGPTAYT SLIILTSGKT
TINPHRPEGS WQYSYYTVLV DGIRWGSTSD TRRFLYIVDT GTTLMYVPPP IAEAIARSFS
PSAVYLFQYG GYFAPCDAIA PKIAVVIEGA SFFINPVDLV YPGLVDPLTG YCQIGITTGG
TGPYVLGTVF LHNVEAYFDI GAGQMRFYGR DTYGPTPQLP EK
//
