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Database: UniProt
Entry: D4LFB0_RUMC1
LinkDB: D4LFB0_RUMC1
Original site: D4LFB0_RUMC1 
ID   D4LFB0_RUMC1            Unreviewed;       883 AA.
AC   D4LFB0;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   22-NOV-2017, entry version 47.
DE   RecName: Full=Endo-1,4-beta-xylanase {ECO:0000256|PROSITE-ProRule:PRU01097};
DE            EC=3.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU01097};
GN   OrderedLocusNames=RUM_23130 {ECO:0000313|EMBL:CBL18305.1};
OS   Ruminococcus champanellensis (strain DSM 18848 / JCM 17042 /
OS   KCTC 15320 / 18P13).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus.
OX   NCBI_TaxID=213810 {ECO:0000313|EMBL:CBL18305.1, ECO:0000313|Proteomes:UP000007054};
RN   [1] {ECO:0000313|Proteomes:UP000007054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18848 / JCM 17042 / 18P13
RC   {ECO:0000313|Proteomes:UP000007054};
RA   Pajon A., Turner K., Parkhill J., Bernalier A.;
RT   "The genome sequence of Ruminococcus sp. 18P13.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|PROSITE-ProRule:PRU01097}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000256|PROSITE-ProRule:PRU01097}.
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DR   EMBL; FP929052; CBL18305.1; -; Genomic_DNA.
DR   RefSeq; WP_015559211.1; NC_021039.1.
DR   ProteinModelPortal; D4LFB0; -.
DR   STRING; 213810.RUM_23130; -.
DR   CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   EnsemblBacteria; CBL18305; CBL18305; RUM_23130.
DR   KEGG; rch:RUM_23130; -.
DR   PATRIC; fig|213810.4.peg.2201; -.
DR   eggNOG; ENOG4108ZJ4; Bacteria.
DR   eggNOG; COG0726; LUCA.
DR   OMA; ALNIEGY; -.
DR   BioCyc; RCHA213810:G13CZ-2047-MONOMER; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000007054; Chromosome.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.180; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR013320; ConA-like_dom_sf.
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; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   InterPro; IPR002509; NODB_dom.
DR   Pfam; PF02018; CBM_4_9; 2.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF63446; SSF63446; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
DR   PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 1.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007054};
KW   Glycosidase {ECO:0000256|PROSITE-ProRule:PRU01097,
KW   ECO:0000313|EMBL:CBL18305.1};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01097,
KW   ECO:0000313|EMBL:CBL18305.1};
KW   Polysaccharide degradation {ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007054};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|PROSITE-ProRule:PRU01097,
KW   ECO:0000313|EMBL:CBL18305.1}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31    883       Endo-1,4-beta-xylanase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003061259.
FT   DOMAIN       33    234       GH11. {ECO:0000259|PROSITE:PS51761}.
FT   DOMAIN      419    487       Dockerin. {ECO:0000259|PROSITE:PS51766}.
FT   DOMAIN      675    860       NodB homology. {ECO:0000259|PROSITE:
FT                                PS51677}.
FT   ACT_SITE    124    124       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    221    221       Proton donor. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01097}.
SQ   SEQUENCE   883 AA;  94529 MW;  8DEE32814AA92046 CRC64;
     MRKHTISRFF HGLLAAAVCL TFTPLPTASA ATVITENKTG TEDGYAYELW KDNGNTSMTL
     TGGGTFSCEW SNINNCLFRK GKKYDCTQTY EELGNITIEY GVDYQPNGNS YMCVYGWTRN
     PLVEYYIVET WGSWRPPGAT SALGTVYADG GTYDIYKTVR ENQPSIDGNT TFDQYWSVRQ
     SKPSANGTKI EGTISVSQHF KAWEQVGLKM GKMYEVALNI EGYQSSGKAT VYKNNLSVGG
     EIPDPVEPDP VEPDENGYYF HSTFEKNTDN WSSRGDSTVT DSSSAAAAGS KSLAVTGRTD
     TWNGAGYTLD TATFQPGSAY SFSVLAMQDA VASDDFKLSL QYDLDGETNY DTIATATGAK
     GEWVQLANTA YTIPAGATGL LLYVETADST NSFYMDEAIG AVKGTKIDAG LPDQPDQPDT
     PTMGDVDGSG TVDAKDVKAL QNYLTRKAST LANAEAADLD GNGVINAMDL ALLKRSLLGN
     QGGTTPVTPS ESGYFKSTFE TGKDGWVSRG DTTLSTDSES YYSGSKSLRI SGRTDTWQGA
     AYTLDTKTFL PGSSYSFSAA VMQASGSSEE LRLTLQYTDA DGETAYDTVA SATAASKTWT
     KLENKSYKIP AGASDLLLYV ESVDSTTDLY LDEAVAAASG TASSVVTGGG KVGNITTPTP
     AAGTVDISWI DKSKPMVAIA FDDGAVGTAS TDYSIRIQDA IANSGFHATF FYVGNWINGS
     NQGEIKRAYE LGMEIANHFT SHTDLTKLSA AEIRKEYDTT SDKIKAITGQ GTSPVMRPPY
     LSVNDTVKSA LSDVALVNCS IDTGDWNGAT SDQIISKIKT AMSNGTLDNA IVLCHETYDS
     TATAMEYLAP YLKSQGWQIV TVSELFAANG KELKGGTLYN ACN
//
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