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Database: UniProt
Entry: E6UB84_RUMA7
LinkDB: E6UB84_RUMA7
Original site: E6UB84_RUMA7 
ID   E6UB84_RUMA7            Unreviewed;       780 AA.
AC   E6UB84;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-SEP-2017, entry version 46.
DE   RecName: Full=Endo-1,4-beta-xylanase {ECO:0000256|PROSITE-ProRule:PRU01097};
DE            EC=3.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU01097};
DE   Flags: Precursor;
GN   OrderedLocusNames=Rumal_0908 {ECO:0000313|EMBL:ADU21434.1};
OS   Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO
OS   2250 / 7).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus.
OX   NCBI_TaxID=697329 {ECO:0000313|EMBL:ADU21434.1, ECO:0000313|Proteomes:UP000006919};
RN   [1] {ECO:0000313|EMBL:ADU21434.1, 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.,
RA   Cheng J.F., Detter C., Detter J.C., Goodwin L.A., Han C.S.,
RA   Hauser L.J., Ivanova N.N., Kyrpides N.C., Land M.L., Lapidus A.,
RA   Lucas S., Ovchinnikova G., Pitluck S., Tapia R., Woyke T., Boyum J.,
RA   Mead D., Weimer P.J.;
RT   "Complete genome of the cellulolytic ruminal bacterium Ruminococcus
RT   albus 7.";
RL   J. Bacteriol. 193:5574-5575(2011).
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; CP002403; ADU21434.1; -; Genomic_DNA.
DR   RefSeq; WP_013497612.1; NC_014833.1.
DR   STRING; 697329.Rumal_0908; -.
DR   EnsemblBacteria; ADU21434; ADU21434; Rumal_0908.
DR   KEGG; ral:Rumal_0908; -.
DR   eggNOG; ENOG4108ZJ4; Bacteria.
DR   eggNOG; COG0726; LUCA.
DR   HOGENOM; HOG000167165; -.
DR   OMA; MEIANHT; -.
DR   OrthoDB; POG091H02KS; -.
DR   BioCyc; RALB697329:GIWQ-897-MONOMER; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000006919; 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; -; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR013320; ConA-like_dom.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002509; NODB_dom.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
DR   PROSITE; PS00776; GH11_1; 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:UP000006919};
KW   Glycosidase {ECO:0000256|PROSITE-ProRule:PRU01097,
KW   ECO:0000313|EMBL:ADU21434.1};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01097,
KW   ECO:0000313|EMBL:ADU21434.1};
KW   Polysaccharide degradation {ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006919};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|PROSITE-ProRule:PRU01097,
KW   ECO:0000313|EMBL:ADU21434.1}.
FT   SIGNAL        1     31       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        32    780       Endo-1,4-beta-xylanase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003209844.
FT   DOMAIN       39    247       GH11. {ECO:0000259|PROSITE:PS51761}.
FT   DOMAIN      577    757       NodB homology. {ECO:0000259|PROSITE:
FT                                PS51677}.
FT   ACT_SITE    142    142       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    234    234       Proton donor. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01097}.
SQ   SEQUENCE   780 AA;  86280 MW;  9532DD278B050943 CRC64;
     MKTTVSKRII SALVSGVLMA TPIMSAVTAS AAKTLTTSPS HTQEVGWYND YHHEIWQADT
     PNSSTMTLHD NDGGFSTQWK CGPNNSRGNF LARRGLYWGL NNPKTYKDYK PFYCDYDCSW
     YAGSSGNSRI CIYGWAQNPL VEYYIIEDWK NWSPAQDGSA QYKGQTTIDG SVYKVYTTSR
     NSYTIEGNKN FTQYISIRQN LRTKGTISVS EHFKVWESMG MKMGNLYEVA FNVEGWESDG
     QADVTLNMYE GESGYHPDPE PEESEIEGTL YSATFENGTN YWSGRGSASV ASSSSKAYEG
     SKSLYVSGRT ANWNGGEVEV NTSTFKPGNS YSFSAMVNPA ESTTVQLSMQ YDQNGTTKYT
     QIAEGSCTAG KWTKLENTNF TIPSGASNVK MYVEAPDSLC DIYVDRAIIA DKGYVASGDT
     PVYNNANVPS NVKMEYNSQY KQMKFTWDAV NGADKYGIAV YLAGKWRVQD SNISGTSYTT
     PKGLTPGMSY KVAIAARVNG KWDTTAAIDN YVVVTTRSYN NIQYHTPSNT NTNTNTNTNT
     NTNTNTNTNT NTNTNTNTNT NTNTNTNNGY YVDPNKPMVA ISFDDGTAQG YSGQKIIDAL
     YKNGFRATFF YVGNWIGKPD QVRDAYSKGM EIANHTTSHP NLTEIQSYQI RSEYDNCASK
     LKSIIGAEPS KLMRLPYLAS NWQVQQTLND VPLISCAIDT QDWNGASAYQ IENTIKNAAN
     NGSLNGAIVL CHETYDNTAT AMENVLPWLK SQGYQVVTIS DMFKAKGKTL NGGQVYTRVS
//
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