ID F9FQ74_FUSOF Unreviewed; 449 AA.
AC F9FQ74;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=CBM6 domain-containing protein {ECO:0000259|PROSITE:PS51175};
GN ORFNames=FOXB_08554 {ECO:0000313|EMBL:EGU80928.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU80928.1};
RN [1] {ECO:0000313|EMBL:EGU80928.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU80928.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU80928.1}.
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DR EMBL; AFQF01002506; EGU80928.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FQ74; -.
DR STRING; 660025.F9FQ74; -.
DR PaxDb; 5507-FOXG_10185P0; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd18618; GH43_Xsa43E-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR PANTHER; PTHR43772:SF2; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04480)-RELATED; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51175; CBM6; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..449
FT /note="CBM6 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003383208"
FT DOMAIN 324..449
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT ACT_SITE 34
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 148
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 449 AA; 49274 MW; A3B8822679862340 CRC64;
MWLTTPLLLV STLLGFSGVA VADNPIVQDI YTADPAPMVY NGRVYLFTGH DNDGSTDFNM
TDWRLFSSAD MVNWQHHGVP MSLKTFSWAN SRAWAGQVVA RNGKFYFYVP VRNAKTGGMA
IGVGVSTNIL GPYTDALGKP LVENNEIDPT VYIDTDGQAY LYWGNPGLYY VKLNQDMLSY
SGSINKVQLT TAGFGSRPNN AQRPTTFEEG PWLYKRGNLY YMIYAANCCS EDIRYSTGPS
ATGPWTYRGV VMNKEGRSFT NHPGIIDFEN NSYFFYHNGA LTGGSGYTRS VAVESFKYGS
DGLIPEIKMT TQGPAQVKSL NPYVKQEAET MAWSEGIETE VCSEGGLNVA FINNGDYIKV
KGVDFGSTGA KTFSARVASN SSGGKIELRL GSKTGKLVGT CTVTTTGNWQ TYKTVECPIS
GATGTSDLFF VFTGTTSDYL FNFNWWQFS
//