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Database: UniProt
Entry: A0A135V3Z7_9PEZI
LinkDB: A0A135V3Z7_9PEZI
Original site: A0A135V3Z7_9PEZI 
ID   A0A135V3Z7_9PEZI        Unreviewed;       381 AA.
AC   A0A135V3Z7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Starch binding domain-containing protein {ECO:0000313|EMBL:KXH67368.1};
GN   ORFNames=CSAL01_04573 {ECO:0000313|EMBL:KXH67368.1};
OS   Colletotrichum salicis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH67368.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH67368.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH67368.1,
RC   ECO:0000313|Proteomes:UP000070121};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KXH67368.1}.
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DR   EMBL; JFFI01000487; KXH67368.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135V3Z7; -.
DR   STRING; 1209931.A0A135V3Z7; -.
DR   OrthoDB; 2782391at2759; -.
DR   Proteomes; UP000070121; 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; cd21137; AA13_LPMO-like; 1.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..381
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007805640"
FT   DOMAIN          275..381
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   381 AA;  40374 MW;  E2035531A1462188 CRC64;
     MKSSTILVVA TFVSSVYGHG YLTIPSSRTR LGAEAGIDSC PECTIREPVS AWPDLTAATV
     GRSGPCGYNA RVSVDYNQPG SSWGSNVVAT YTRGQTVDIQ WCVDNNGDHG GMFSYRICQD
     QSIVDKFITP GYLPTDDEKQ AAENCFQAGT LKCTDVSGQS CDYSPDCTSG QACWRNDWFT
     CNAFQASSRR GCQGVDNNAL GSCYTSIAGG YTVTKKIKIP DYVSNHTLLS LRWNSFQTGQ
     VYLTCADIAI SGGGSTSPSS TRTTSAAATA TSGTCAIASN VAVTFNEIVK TVPSQTIKVA
     GSIAALGNWN AASAPALSAA QYTSSNNLWT YTFSLPAGTS FEYKFINVAS DGTATWESDP
     NRSYTVPQSC STAVTVSTSW K
//
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