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Database: UniProt
Entry: A0A1Y2M8E7_EPING
LinkDB: A0A1Y2M8E7_EPING
Original site: A0A1Y2M8E7_EPING 
ID   A0A1Y2M8E7_EPING        Unreviewed;       395 AA.
AC   A0A1Y2M8E7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=CBM20 domain-containing protein {ECO:0000259|PROSITE:PS51166};
GN   ORFNames=B5807_02758 {ECO:0000313|EMBL:OSS52386.1};
OS   Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX   NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS52386.1, ECO:0000313|Proteomes:UP000193240};
RN   [1] {ECO:0000313|EMBL:OSS52386.1, ECO:0000313|Proteomes:UP000193240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS52386.1,
RC   ECO:0000313|Proteomes:UP000193240};
RA   Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT   "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT   strain isolated from New Zealand.";
RL   Genome Announc. 0:0-0(2017).
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; KZ107839; OSS52386.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2M8E7; -.
DR   SMR; A0A1Y2M8E7; -.
DR   STRING; 105696.A0A1Y2M8E7; -.
DR   InParanoid; A0A1Y2M8E7; -.
DR   OMA; GYNPDCT; -.
DR   OrthoDB; 2782391at2759; -.
DR   Proteomes; UP000193240; 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; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR034836; CBM20_glucoamylase.
DR   InterPro; IPR002044; CBM_fam20.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000193240}.
FT   DOMAIN          289..395
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   395 AA;  41489 MW;  C78AFAB34A3E9C56 CRC64;
     MKWAITQALA FAAGVKAHGY LSQPMSRTGL NAQSGADTCP ECTILEPVTA WPDLESAQVG
     RSGPCGYNAR VSVDYNQPGP RWGSAPVITY KGGDVADVQW CVDANGDHGG MFSYRICQDQ
     ALVDKFLTPG YLPTEAEKQA AEDCFEKGTL PCTDVTGQTC GYNADCTQGQ ACWRNDWFTC
     KGFDDTKCRG VDNAPLNSCY TSIAGGYTVS SRIKIPNYVS DHTLLSFKWN SFQTPQIYLT
     CADIKITGAS GSTPPTTTSK VSSAAPSATS ATKSSSAASS STSAAAGCAT PVATVAVTFN
     SKTTTVVGQT VKVAGSIAQL GSWNTANAPA LSASKYTSSN PLWTTTLNVP AGTSFEYKFI
     KVESNGAVTY ESGANRVYTV PKSCASTATL EAAWK
//
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