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Database: UniProt
Entry: A0A0A0B669_9CELL
LinkDB: A0A0A0B669_9CELL
Original site: A0A0A0B669_9CELL 
ID   A0A0A0B669_9CELL        Unreviewed;      1334 AA.
AC   A0A0A0B669;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   22-NOV-2017, entry version 18.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=Q760_06120 {ECO:0000313|EMBL:KGM00771.1};
OS   Cellulomonas cellasea DSM 20118.
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1408250 {ECO:0000313|EMBL:KGM00771.1, ECO:0000313|Proteomes:UP000029833};
RN   [1] {ECO:0000313|EMBL:KGM00771.1, ECO:0000313|Proteomes:UP000029833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20118 {ECO:0000313|EMBL:KGM00771.1,
RC   ECO:0000313|Proteomes:UP000029833};
RA   Wang G., Zhuang W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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:KGM00771.1}.
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DR   EMBL; AXNT01000167; KGM00771.1; -; Genomic_DNA.
DR   EnsemblBacteria; KGM00771; KGM00771; Q760_06120.
DR   Proteomes; UP000029833; 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:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.40.230; -; 1.
DR   InterPro; IPR010502; Carb-bd_dom_fam9.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR027273; Neocarzinostatin-like.
DR   InterPro; IPR002509; NODB_dom.
DR   Pfam; PF06452; CBM9_1; 1.
DR   Pfam; PF02018; CBM_4_9; 2.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
DR   PROSITE; PS51760; GH10_2; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029833};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029833}.
FT   DOMAIN      195    381       NodB homology. {ECO:0000259|PROSITE:
FT                                PS51677}.
FT   DOMAIN      548    889       GH10. {ECO:0000259|PROSITE:PS51760}.
SQ   SEQUENCE   1334 AA;  141745 MW;  7EE8C5F98416C47F CRC64;
     MAPGAAAAST TTDLAAAADE PVVVLGTDFE DGTWAPWTQS GAAPLSVVDV DGGKALLVSG
     RAADYEGIQS PTGLLEPGAS YTFSMRARLA EGTEGSAGIR FVVKPDYTWV GNTTMTADAW
     TTVTGSFTAP AAADPATLQV YLGTGDLAAP YDYLVDDLVL TAAGGGGGEP DPDVVPGGAV
     NPVPTPVTTA RGTGNVAALT FDDGPNPGET DDLLDLLAEN DLTATFCVIG QNVQAEGGAA
     LLRRIVDEGH TVCNHTTTYA DMGSWTPEQI RADLARNLAI IREAAGDPEL EVPYFRAPNG
     SWGATPAVAV ELGMQPLGLG NVISDWDGND LSEETLTANL RAAVTPGAVV LVHDGGGDRA
     NGIAAVRTVL GERLAEGWTF TLPTGGAAPT VTSLSSDFED GLDGWVPRGD ADGDPTVEVT
     TTQAHGGTQA ALVTGRTTQG DGIGRDVTGL LTAGTTYDIS AWVRFGEGAP TDDVWLSLQR
     TSEGATTYDT VAQLTGVTSG AWHEIRATYQ MPEAESAFLY LETSYPDGSA ADLLVDDVVI
     SAKQPSEVQD LTPLQDTVDF PVGVAIDSRE TTGPAAELLL RHFDQITGEN HMKPEAWYTD
     AREFRTHPEA TTLMEFAQEN DVRVYGHTLV WHSQTPAWFF THEDGTPLTT SEADKQELRM
     RMRTHIFDVA EALSTGGGYG LFGSETNPVV AFDVVNEVVS DGRSEEDGLR RSEWYRVLGE
     EFIDLAFRYA DEAFNGEFAV EGERPVTLTI NDYNTEQVGK QQRLHALVER LLARDVPVDA
     VGHQFHVSLA MPVQALEDAI VAFDDLGLTQ VVSELDVTTG TPVTQASLIE QGYYYRDAFR
     IFREHAEDLF SVTVWGLTDG RSWRVDSGAP LLFDDALQAK PAYYGAVDGE LSARQRAANA
     FRGDVAVAAG ATGAVEWRQL PLQTVEDVAG FSVRWEADHL SVYARVTDAT VDASDAVTFV
     VGEESYTVGR NGEAEVEAVV EAVDGGYAVV AHLPRTSAEG DQVSFDVRVT DGESSAAWNQ
     PGVLGTLTLV EALSTTQVVE AAGAPVIDGQ VDAAWASANA VTTDKQIEGE GGATANVRTL
     WRENTLYVLA EVTDPTLDAT GSDPWVQDSL EIFLDAGNVK NGPYRYDDTQ IRISYLNEAS
     FGTGDEAFQQ NRLVSQTSTV AGGYVVEASI SLLEAGGVGT FHGLDFQVND ATAGARTAVR
     AWADPTGRGY QSTARWGVAE LVPAVVVPEP DPSVTADRKV RAGDQLEVTL EGYLPSSTVD
     LVLERRIGRW VVARVDLGDV TVGADGSATT EVRVPRGVLP GKYTLRGTSG EVTADTTVTV
     QLAKPSWWWG WWPF
//
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