ID W6Z8F0_COCMI Unreviewed; 391 AA.
AC W6Z8F0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Carbohydrate-binding module family 20 protein {ECO:0000313|EMBL:EUC46068.1};
GN ORFNames=COCMIDRAFT_4809 {ECO:0000313|EMBL:EUC46068.1};
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:EUC46068.1};
RN [1] {ECO:0000313|EMBL:EUC46068.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC46068.1};
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 -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
CC -!- SIMILARITY: Belongs to the polysaccharide monooxygenase AA13 family.
CC {ECO:0000256|ARBA:ARBA00034311}.
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DR EMBL; KI963972; EUC46068.1; -; Genomic_DNA.
DR RefSeq; XP_007687387.1; XM_007689197.1.
DR AlphaFoldDB; W6Z8F0; -.
DR SMR; W6Z8F0; -.
DR STRING; 930090.W6Z8F0; -.
DR GeneID; 19124387; -.
DR KEGG; bor:COCMIDRAFT_4809; -.
DR eggNOG; ENOG502QSJT; Eukaryota.
DR HOGENOM; CLU_055681_0_0_1; -.
DR OrthoDB; 2782391at2759; -.
DR Proteomes; UP000054032; Unassembled WGS sequence.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd05811; CBM20_glucoamylase; 1.
DR Gene3D; 2.70.50.70; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR034836; CBM20_glucoamylase.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR004302; Cellulose/chitin-bd_N.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR36575; BINDING PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G14430)-RELATED; 1.
DR PANTHER; PTHR36575:SF2; CHITIN-BINDING TYPE-4 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF03067; LPMO_10; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..391
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004889799"
FT DOMAIN 285..391
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 251..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 41127 MW; 209B25E10D0D376A CRC64;
MLSKILLPVL TLAASANAHG YLTSPMSRTG LNAQSGADTC PECTILEPVT AWPDLDAAAV
GRSGPCGYNA RVSVDYNQPG PRWGSEPVIT YKAGDVVDVQ WCVDANGDHG GMFTYRICQN
QALVDKLLTP GYLPTEAEKQ AAEDCFEAGE LKCTDVPGQT CGFNSDCQQG QACWRNDWFT
CGGFNDNTKC RSVDNAPLNS CYTSIAGGYT VSSKIKIPNY TSNHTLLSFK WNSFQTPQVY
LTCADIKITG SGSGTSPPPT SSKPPTSSSK PTSTSTSAAT ATACATPLST VAVTFNSKTS
TTFGQTVKIA GSISQLGSWN TANAPALSAA QYTSANPLWT TTINLPAGTS FEYKYIKVES
GGAVTYESGA NRQFTVPKGC AAGVSVEGSW K
//
