ID E6UC21_RUMA7 Unreviewed; 744 AA.
AC E6UC21;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Carbohydrate-binding CenC domain protein {ECO:0000313|EMBL:ADU21572.1};
DE Flags: Precursor;
GN OrderedLocusNames=Rumal_1046 {ECO:0000313|EMBL:ADU21572.1};
OS Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 /
OS 7).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=697329 {ECO:0000313|EMBL:ADU21572.1, ECO:0000313|Proteomes:UP000006919};
RN [1] {ECO:0000313|EMBL:ADU21572.1, ECO:0000313|Proteomes:UP000006919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7
RC {ECO:0000313|Proteomes:UP000006919};
RX PubMed=21914885; DOI=10.1128/JB.05621-11;
RA Suen G., Stevenson D.M., Bruce D.C., Chertkov O., Copeland A., Cheng J.F.,
RA Detter C., Detter J.C., Goodwin L.A., Han C.S., Hauser L.J., Ivanova N.N.,
RA Kyrpides N.C., Land M.L., Lapidus A., Lucas S., Ovchinnikova G.,
RA Pitluck S., Tapia R., Woyke T., Boyum J., Mead D., Weimer P.J.;
RT "Complete genome of the cellulolytic ruminal bacterium Ruminococcus albus
RT 7.";
RL J. Bacteriol. 193:5574-5575(2011).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002403; ADU21572.1; -; Genomic_DNA.
DR RefSeq; WP_013497750.1; NZ_JHYT01000025.1.
DR AlphaFoldDB; E6UC21; -.
DR STRING; 697329.Rumal_1046; -.
DR KEGG; ral:Rumal_1046; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_016001_0_0_9; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000006919; Chromosome.
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 CDD; cd09003; GH43_XynD-like; 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; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 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; PF00404; Dockerin_1; 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.
DR PROSITE; PS00018; EF_HAND_1; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..744
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003212370"
FT DOMAIN 206..273
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT DOMAIN 630..744
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT SITE 444
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 744 AA; 80744 MW; 435C2A7591255D4C CRC64;
MKLKKTITRL CTATLSSAVL LSTTSALPVS AAMSPDSNGF YYHDTFEDSS GNWEIRGSGE
ILLSGRHPFK GTNALLIKDR TSAWQGAQMA LDTSTFIPGK SYSFNVFVDY EEGESTQNFL
LSMQYTDSTG TVKYLHLAEG STSRGQYLQL SNPSFQIPSD ASDVYLYVET TDVYGNFYID
EAIVAADGVT IDSSGASQGY TAPKTPGDIR GDVNQDGRIN LADLILAKRG MYSGFPNKQS
QKAADIDKSG TVDNDDINYL QDFILKKINS FPKINKIDFN EMAGKFGNVS LATGYKKSNE
NNPLISQYFG ADPGVMEYNG RVYVFMTDDH LLYSNGQLKD IEYGTINCIR CISSDDLVNW
TDHGLINAAG SNGLCRWGGN SWAPTACHKK INGKEKFFLY FANGGNGIAV LEADSPTGPW
KDPIGKALIS RSTPNCGNVE WLFDPAVLVD DDGTGYLYFG GGVPSGQNAH PKTARCVKLG
SDMTSIVGTP QTIDPPYLFE DSGIHKFNGK YYYSYCSNFS TGGNQYGLSG GAIQYMVSDY
PLGPFTYVGE AFKGIGTFFG TGGNNHHTIF KFNNQWYLFY HAQYLQDNMG LKGGYRSTHI
DKVTINSNGT IQAITGTKKG VSQIKSFDPF RTQRAATFSH QGGITISGSG DYSTVQAKKG
SWYRVSGVDC GSGAETMTFK ASSNTGCIVK VCTGSANGTV VSYVEIPAGS SMQEITVPVQ
GLSGKNDLYF VFNNNASVDS WKLD
//
