ID C9SL07_VERA1 Unreviewed; 400 AA.
AC C9SL07;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Starch binding domain-containing protein {ECO:0000313|EMBL:EEY19375.1};
GN ORFNames=VDBG_05484 {ECO:0000313|EMBL:EEY19375.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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; DS985219; EEY19375.1; -; Genomic_DNA.
DR RefSeq; XP_003004371.1; XM_003004325.1.
DR AlphaFoldDB; C9SL07; -.
DR STRING; 526221.C9SL07; -.
DR GeneID; 9531357; -.
DR KEGG; val:VDBG_05484; -.
DR eggNOG; ENOG502QSJT; Eukaryota.
DR HOGENOM; CLU_055681_0_0_1; -.
DR OMA; GYNPDCT; -.
DR OrthoDB; 2782391at2759; -.
DR Proteomes; UP000008698; 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; 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:UP000008698};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..400
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003002134"
FT DOMAIN 294..400
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 400 AA; 42669 MW; C5FBF8C2888A73B6 CRC64;
MKTTTALTLL SLASSVLGHG YLTIPKSRTR LGAEFSRVDT NSFLVQAGLD SCPECNIREP
VEAWPNVTQA TVGRSGPCGY NARVSIDYNQ PKTNWGNSPV VTYTAGQTVD VEWCVDANGD
HGGMFSYRIC QDQALVNKFI TPGYLPTEAE KEAAEQCFQR GTLPCTDVTG QSCGFNPDCQ
PGQPCWRNDW FTCNAFQASN RRACQGVDGA ALGSCYTSIA GGYKVSKKIK IPNYNSAHTL
LSFRWNSFQT GQVYLTCADI AINGGSNNNP TTAVAPTTLR TTTTAAAATT TGACTPAANV
AVTFNTLATT VVGQTIKLAG SISQLGSWTP ASAPALSASG YTTSRPLWTY TVTLPAGTTF
QYKFINVQSD GSVRWESDPN RSYTVPTGCA SAVTVDSTWR
//
