ID Q2H5A6_CHAGB Unreviewed; 628 AA.
AC Q2H5A6;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=CBM6 domain-containing protein {ECO:0000259|PROSITE:PS51175};
GN ORFNames=CHGG_06159 {ECO:0000313|EMBL:EAQ89540.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ89540.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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DR EMBL; CH408031; EAQ89540.1; -; Genomic_DNA.
DR RefSeq; XP_001222254.1; XM_001222253.1.
DR AlphaFoldDB; Q2H5A6; -.
DR GeneID; 4391340; -.
DR VEuPathDB; FungiDB:CHGG_06159; -.
DR eggNOG; ENOG502SI39; Eukaryota.
DR HOGENOM; CLU_009397_11_2_1; -.
DR InParanoid; Q2H5A6; -.
DR OMA; FNFNWWQ; -.
DR OrthoDB; 5470935at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
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:UniProtKB-KW.
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; IPR002575; Aminoglycoside_PTrfase.
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 InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR43772:SF6; -; 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF01636; APH; 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 SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51175; CBM6; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001056};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..628
FT /note="CBM6 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004208969"
FT DOMAIN 289..426
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT ACT_SITE 33
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 146
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 628 AA; 68062 MW; 280B9B4A7FE3AEB3 CRC64;
MKSSSLSLTA ALATLATRAT ADNPIIQTLY TTDPAPLVYD DRIYLYTGHD EPNAQTFQMN
DWRVYSSSDM VNWQDHGSPL SLKTFSWATA QAWAGQTIPR NGKFYWYVPM RHTSGSMAIG
VAVGDTPTGP FKDAIGKPLV MNNGIDPTVW IDDDGQAYLY WGNPGLWYIK LNPDMVSYTG
NINTVTLTAA GFGGRSGNAQ RPTTFEEGPW LYKRSGKYYM VFAASCCSEH LGWSTGPSPT
GPWTYGGVMM PAQGSSFTNH AGVVDFRGGS YLFYHNGALP GGGGYDRSVC VEKFAYGTNG
SIPVINMSKE GAPQVGTLDP YVRQEAETMA WSSGVQTEVK GVAFGGGAKT FTARVSSGSS
GGKIELRLGS ASGTVVGTCN VSGTGGWQNW ASVGCNVSGA TGTQDVFFRF TGGGGELFRF
NWWQFKQRPG LSVPDAVTLK DEELENEGAW AYSLERLPGK MWVLGVAGKG AEGRIAINRS
LGCVLSKGCL ANDSDEAVAA KVRPHLEAVL ASPLDEIATY RPLLQGFLDK LDDISELPLW
VSHYDLNGVN VLIDESCEVT GLIDWELSTP KPFAFWMPDE FEVAERAFWE ELFAGMPQET
RAMLEKNIDL VQDAVILGTL LDTFSGRM
//