ID A0A066XBH7_COLSU Unreviewed; 328 AA.
AC A0A066XBH7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Putative glycosyl hydrolase family 43 {ECO:0000313|EMBL:KDN63365.1};
GN ORFNames=CSUB01_06584 {ECO:0000313|EMBL:KDN63365.1};
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:KDN63365.1, 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 glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:KDN63365.1}.
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DR EMBL; JMSE01001236; KDN63365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XBH7; -.
DR STRING; 1173701.A0A066XBH7; -.
DR eggNOG; ENOG502QTYK; Eukaryota.
DR HOGENOM; CLU_009397_4_1_1; -.
DR OMA; SFEGHEF; -.
DR OrthoDB; 5470935at2759; -.
DR Proteomes; UP000027238; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd18619; GH43_CoXyl43_like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238}.
FT SITE 134
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 328 AA; 37001 MW; 885B48A373E259A0 CRC64;
MAVLLTSAIF TADPSAHVFN NRVYVYPSHD RISNTTGTGD SKYDMADYHI FSTSSLNPYD
PAIDHGVALS TADIPWASKQ LWAPDAAFKN DKYYLYFPAR NKENIFQIGV AVSEKPEGPF
KPDPEPIPGS FSIDPASFID DDGQGYMYFG GLWGGQLQCY QKDNKYDAAW EGELAPNGTG
IYALGPRVAK ISSDMHQFDG EPKELQILDP ETNKPLLADD QDRRFFEAPW MHKKGDTYYL
SYSTGTTHYL VYATSKSPLG PFTYAGRILE PVLGWTTHHS IVEYKNQWWL FFHDASLSNG
TDYLRSVKFE PIFYDKDGKL TIVKPETE
//
