ID A0A1K1N033_9FIRM Unreviewed; 697 AA.
AC A0A1K1N033;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Carbohydrate binding domain-containing protein {ECO:0000313|EMBL:SFW28605.1};
GN ORFNames=SAMN02910447_01401 {ECO:0000313|EMBL:SFW28605.1};
OS Ruminococcus sp. YE71.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=244362 {ECO:0000313|EMBL:SFW28605.1, ECO:0000313|Proteomes:UP000182164};
RN [1] {ECO:0000313|EMBL:SFW28605.1, ECO:0000313|Proteomes:UP000182164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YE71 {ECO:0000313|EMBL:SFW28605.1,
RC ECO:0000313|Proteomes:UP000182164};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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DR EMBL; FPIR01000006; SFW28605.1; -; Genomic_DNA.
DR RefSeq; WP_072417504.1; NZ_FPIR01000006.1.
DR AlphaFoldDB; A0A1K1N033; -.
DR STRING; 244362.SAMN02910447_01401; -.
DR Proteomes; UP000182164; 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:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd14256; Dockerin_I; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF6; -; 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF02018; CBM_4_9; 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; 2.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000182164};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..697
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009665864"
FT DOMAIN 332..455
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 630..697
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT SITE 158
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 697 AA; 76109 MW; 7F6D7313D8B1E2CC CRC64;
MKKFFSAVTA AALTAVTLCT SAPIVTQADN PIVQTSFTPD PAPVVIGDEL YVFTGCDREG
DNDFYYMTGW QCFSTKDMKN WTDHGRILED TSFSWCNKND AWASQCIERN GKYYFYFTTT
NKGGGGRAIG VAVADSPAGP YRDPIGKPLC GPNWDYIDPT VILDDDGQAW LMFGNPKCYY
VKLKEDMVTL DGQIKQFDMN AQQFGSSQKG TTYGEGPWIY KHDSLYYLVW ASFVDGFGGE
SQCYATGPSV TGPWTYRGVI QEGSNCYTTH GGIIDYKDHS YFFYHKNGIP GGGAFNRSAS
CDEFTYNADG TIPVVKLTNS GPDQLEPLNP FERVEAETIC WSEGIKTEKD DNNSVNIGFI
QKGSYVKVAG VDFGEGADKF TASVASAGSG GTIELHLDSK TGKTIGTLKV GSTDGWHDWE
ELTCDVSGAS GEHDLYLVFN GGDGYLMNVD WWKFDGAGAS AAATDKTYIF KNTFEGKLDG
CTDRGGAKVA LTIDEAYEGS GSVYCSDRSA SWKGVGKSLN YKFKAGESYS FSTVVKYNEG
APTTKFHFTL QYKGSDGEIY YDKIDTKTVK KGEWTQLANT SYKIPAGAKE LLIYVETEGD
SDDDTPATNF YVDNFFAAVS GTVIEGPTVR TTNWGDANVD GVTDMSDVIL IMQSVAAPDK
YKLTEQGRYN ADVVGTDGSI TEDDALAIRK HLVSMPE
//
