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Database: UniProt
Entry: S0FMR7_9FIRM
LinkDB: S0FMR7_9FIRM
Original site: S0FMR7_9FIRM 
ID   S0FMR7_9FIRM            Unreviewed;      1496 AA.
AC   S0FMR7;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-SEP-2017, entry version 24.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=CTER_2434 {ECO:0000313|EMBL:EMS71646.1};
OS   [Clostridium] termitidis CT1112.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=1195236 {ECO:0000313|EMBL:EMS71646.1, ECO:0000313|Proteomes:UP000014155};
RN   [1] {ECO:0000313|EMBL:EMS71646.1, ECO:0000313|Proteomes:UP000014155}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT1112 {ECO:0000313|EMBL:EMS71646.1,
RC   ECO:0000313|Proteomes:UP000014155};
RX   PubMed=23704187;
RA   Lal S., Ramachandran U., Zhang X., Munir R., Sparling R., Levin D.B.;
RT   "Draft Genome Sequence of the Cellulolytic, Mesophilic, Anaerobic
RT   Bacterium Clostridium termitidis Strain CT1112 (DSM 5398).";
RL   Genome Announc. 1:E00281-13(2013).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans. {ECO:0000256|RuleBase:RU361174}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family. {ECO:0000256|RuleBase:RU361174}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EMS71646.1}.
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DR   EMBL; AORV01000035; EMS71646.1; -; Genomic_DNA.
DR   RefSeq; WP_004625996.1; NZ_AORV01000035.1.
DR   EnsemblBacteria; EMS71646; EMS71646; CTER_2434.
DR   PATRIC; fig|1195236.3.peg.2748; -.
DR   OrthoDB; POG091H0Y2G; -.
DR   Proteomes; UP000014155; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.260; -; 3.
DR   InterPro; IPR010502; Carb-bd_dom_fam9.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR001119; SLH_dom.
DR   Pfam; PF06452; CBM9_1; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   Pfam; PF00395; SLH; 2.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF49785; SSF49785; 3.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
DR   PROSITE; PS51272; SLH; 2.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW   Complete proteome {ECO:0000313|Proteomes:UP000014155};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:EMS71646.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:EMS71646.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014155};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:EMS71646.1}.
FT   SIGNAL        1     34       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        35   1496       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004497249.
FT   DOMAIN      515    853       GH10. {ECO:0000259|PROSITE:PS51760}.
FT   DOMAIN     1312   1372       SLH. {ECO:0000259|PROSITE:PS51272}.
FT   DOMAIN     1437   1496       SLH. {ECO:0000259|PROSITE:PS51272}.
FT   ACT_SITE    777    777       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU10061}.
SQ   SEQUENCE   1496 AA;  161814 MW;  95444814E405F68E CRC64;
     MSSTIFRNWR KAAAVFLVLC LVISLMPVNS IVYADSTAVY HETFAGGVGK AVQSGGAKLT
     QVTDKVFEGN DDGAALYVSN RANGWDAADF KFADLHLENG KTYNITINGY VDPNVEVSPG
     GLIVAQAVNP SPEAYDNYMG QAVITTGAAF TITSNYTVNN TYDRIRIQSN DAGAAVPFYI
     GDILITAENT PPVTTEKEIY HEDFLNSAGK AVQSGGANLT QVTNKVFEGN DDGAALYVSN
     RINNYDAADF KFADVGMQNG KTYTVTVKGY VDAGEAVPAG AQAYLQTVDS YDWLAGADMI
     AGEAFTLTKK FTADTTKDSA VRVQSNDAGA TVPFYIGDIL ITETVSGGDT EEPPRDPALP
     FTTITFEDQT TGGFVGRGGV EILTPTNEAS HTGEYSLKVE GRTKTWNGPT LRVEKYVDKG
     SEYKVTAWVK LIEPESSQIQ LSTQVGSSTP GYSTFQAKTI STNDGWVKYE GKYRYNSVPD
     EYLTIYIESS NNATASFYID DISFEKTQAG PIEIQKDLVP VKDAYKDEFL IGNAISGEDL
     SGVRLELLKM HNNSATAGND MKPGSLQPTK GNYTFAAADT MVDKVLSEGI KMHGHVLVWH
     QQTGEWMNTA TDGSGNKVPL PREEALQNMT THIKTVVEHF GNKVISWDVV NEAMGDNPSN
     PSDWRSSLRN DSMWGKAIGP DYVELAFLAA REVLDAHPDW NIKLYYNDYN EDNQKKSQAI
     YNMVKEINEK YAETHPGKLL IDGIGMQGHY NIQTNPLNVE LSLERFISLG VEVSITELDI
     TAGENSQLSE KLAEAQGYLY AQLFKIFKAH AANIERVTIW GMDDGTSWRS SQNPLLFDRN
     LQAKLAYYGA IDPDKYMSEH QPTTPVGAKQ STANFGTPVI DGTIDQIWSN APALAINEYQ
     MAWQGATGTA RTLWDDSNLY VLVQVSDEQL DKSSINAYEQ DSVEVFVDEN NGKTPFYQED
     DGQYRVNFDN ETSFNPASIS EGFESAARVS GTNYTVEMKI PFKTLTPANG IRIGFDTQVN
     DAQNSARQSV AAWNDQSGSG YQDTSVFGVL TLTGKGDSGE PGEPGNPDNP SNPGNSGSSN
     TGSGGGSNSG SSDNSTPAAG TKAESNVTVK LTAAVNADGS ANVKVTDKTV EDILKDLSKI
     KDGVKPTVLL AVNVPSNADA VTLELPADTL GKILEADGNA SIKVSAGIGE LLFDSRAMKT
     ISETGTGTIE IKISKVAAAD LSAIPSDAAD RIADRPVFEF TVSRGGTKIS DFNGSTVSVS
     IPYTLKQDED PNAVLVYYID SSNSLIPVRG YYHNGTIEFI TAHFSKFAVG YNKISFSDVK
     STDSYYDAVT YLGAREIATG TGFDPKHTVT RGEAIVMLMK AYDIKPLAEP EDNFSDAAGE
     FAGYYAKARE IGLTGGVGYN RIDADAPLTR EMLYTLVYNL KKYLGELPAT GTAVTEYKGF
     GDENKLSDWS VNAVKQLVEA GIIKDGTSTQ LNPKFNCSRG KFAIVLHSLL SNNTIN
//
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