ID R6CDJ9_9FIRM Unreviewed; 901 AA.
AC R6CDJ9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Beta-glucosidase A {ECO:0000313|EMBL:CDA63367.1};
GN ORFNames=BN708_00738 {ECO:0000313|EMBL:CDA63367.1};
OS Firmicutes bacterium CAG:56.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263031 {ECO:0000313|EMBL:CDA63367.1, ECO:0000313|Proteomes:UP000018123};
RN [1] {ECO:0000313|EMBL:CDA63367.1, ECO:0000313|Proteomes:UP000018123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:56 {ECO:0000313|Proteomes:UP000018123};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:CDA63367.1}.
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DR EMBL; CBCG010000129; CDA63367.1; -; Genomic_DNA.
DR AlphaFoldDB; R6CDJ9; -.
DR Proteomes; UP000018123; 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; cd04080; CBM6_cellulase-like; 1.
DR CDD; cd14256; Dockerin_I; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 2.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR Pfam; PF03422; CBM_6; 2.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF07554; FIVAR; 4.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM00606; CBD_IV; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51175; CBM6; 2.
DR PROSITE; PS51766; DOCKERIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000018123}.
FT DOMAIN 1..102
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 442..563
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 835..901
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
SQ SEQUENCE 901 AA; 97318 MW; 551B0543D49EB534 CRC64;
MNYAGNYVSY YLNVEEAGDY NVILNVANGR AAFDFDPGME VDGTKFPATI NAKQTGDGEK
NEWYNFENLE PVTVTLPKGH SILTLRASEK DKYPNIDYIL VEKKQTATQS LKSAAAKKAR
TAEDTPASEP ADSGKIMLVD VYNNPELMDD FLAQLSDDQL CGLMGGQTNT GVANTGGMGN
LMEYGIPNAM TADGPQGIRI GTTCTAWPIS TLLASTWDVD LVKQVGKAAA VEAHNNGIDI
WLAPGMNIHR DPLCGRNFEY YSEDPLITGK MAAAITEGCQ SKGVSITLKH FTTNNKETNR
NSSDSRVSER ALREIYLKGF EIAVKEAQPW SIMTSYNFLN GIETSENKDL LTNITRGEWG
YEGIFMTDWG NNSNHAREVL AGNDVKMPSG SPATLKAALK KGILKRSDLE DCAERLVKMI
MKVNIFKEKI LNPVTVAIGD DTYFKAAENI LWSQTARGEN TSDEDGGKDL GYCDAGAWTQ
YQINVAKSGT YSLSARSASN AGGGAFDILA DGTKIASFKA VNTGGWQKWT TLEAQQIKLE
AGVHTLRIEF TESGSNLNWL HFVRQSEYIE NLEKLYQAWA SQDLSEYTAE SAETMRTALA
AAKAVLDKEN ATDSEIQTAI IQMTQAINAM EYGTNKVHLE AIIEVAEKTL ANPGDYADVS
ALEAAVKAGK EILAKADATQ EEANAAANAI ADSMQALMER ADIRSLRELT DAANELLEKN
SGKYTDDTAK ALQDAVAHAE EILGKDGKSD AEIKEAYNQI MDAIVGLKMK GNKAALEAMI
KKAESILAEN SRYVAATIEG LDEELAAAKA VYENNQALQS EVNEAVKSLT FKIAEARLLG
DVDGDGQITT NDTVEILRAA AEIATLSAED AASADVNGDG VADTADAVLV LQYASEAVSG
F
//
