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Database: UniProt
Entry: A0A0A0BTJ4_9CELL
LinkDB: A0A0A0BTJ4_9CELL
Original site: A0A0A0BTJ4_9CELL 
ID   A0A0A0BTJ4_9CELL        Unreviewed;      1653 AA.
AC   A0A0A0BTJ4;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-SEP-2017, entry version 16.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=N868_15200 {ECO:0000313|EMBL:KGM10504.1};
OS   Cellulomonas carbonis T26.
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=947969 {ECO:0000313|EMBL:KGM10504.1, ECO:0000313|Proteomes:UP000029839};
RN   [1] {ECO:0000313|EMBL:KGM10504.1, ECO:0000313|Proteomes:UP000029839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T26 {ECO:0000313|EMBL:KGM10504.1,
RC   ECO:0000313|Proteomes:UP000029839};
RA   Chen F., Li Y., Wang G.;
RT   "Genome sequencing of Cellulomonas carbonis T26.";
RL   Submitted (AUG-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:KGM10504.1}.
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DR   EMBL; AXCY01000048; KGM10504.1; -; Genomic_DNA.
DR   RefSeq; WP_043606956.1; NZ_AXCY01000048.1.
DR   EnsemblBacteria; KGM10504; KGM10504; N868_15200.
DR   Proteomes; UP000029839; 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   InterPro; IPR010502; Carb-bd_dom_fam9.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
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; PS00659; GLYCOSYL_HYDROL_F5; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029839};
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:UP000029839};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     31       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        32   1653       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5001967535.
FT   DOMAIN      363    708       GH10. {ECO:0000259|PROSITE:PS51760}.
FT   DOMAIN     1462   1646       NodB homology. {ECO:0000259|PROSITE:
FT                                PS51677}.
SQ   SEQUENCE   1653 AA;  173176 MW;  8D4721FF40BC496B CRC64;
     MMTPVRTAIS RWGTGLLALV LAGGAAPTAF AAPAPEGETA ASQEAAAAEV AAAAAVISTD
     FEDGTTAPWT ASGGPSLEVV DVDGGRALSV SDRTAGHDGI ETSLTGVLTP GEEYTFSFRA
     RLADGTEGAS SMHLTAVEQG TGDPAYVWIG GGADVTAAGW TDVTATYTLP AGLDSAKVYL
     EGAAIDGAFP GYLVDDLVVT GPADGGDGGD GGGSGTVVVG STFEGDLDGW TARGDGSATA
     ALVAGGHESD GALQVTGRTQ TWNGVQRTVA LEAGATYDLS VWVRMADGEP TSPVTLSAEL
     DVEENPWTNI ATASAVGPGA WTQISATYTV PAQGVRLLYL ESSNATASFL VDDVRVTAQE
     VAVEPLTPIK DTVDFPVGVA IDERETTGAP SELLLRHFDQ ITGENHMKPY AWYAEDRTFR
     PDPQATALME YAQANDLRVY GHTLVWHSQT PDWFFQRADG TPLTTSAADQ EVLRERMRTH
     IFAVAEHLAE TYGEFGSATN PLVAWDVVNE VVADQGGDDG LRRSEWYRVL GPQFIDLAFR
     YADEAFNTTY AADGTDRPVT LFINDYNTED AGKAQRLLAL VERLIADGVP VDGVGHQFHV
     SLSRSVGDLE AAIELFADLT TADGDPLLQV VSELDVTTGT PVTQRNLVEQ GYYYRDVFAM
     LREHAAELYS VTVWGLTDGR SWRVDSGAPL LFTDALAAKQ AYYGVAEPEN LQPRQQAANV
     FRGDVALDDA APDADVWGLL PQVRVGEDAG FGLRWAPDHL TVRVEVADAT DDATDAVELL
     LEGGSVTVTR DDASGDDRVV RSTDEGWVAV VRLPLAEPVA EGSTLSLDVR VTDGATTTAW
     NSEGAVGTLT LVEELSVTDV VAADAAPTVD GVVDDVWADA QTFSTHTQVQ GERGASAVVR
     TLWHGDRLYV LARVSDPVLD ASASDPWEDD SVEIFLDTGN VKNGSYRYED NQLRISFENV
     RSFGTGDEAY QDARLESATD VVTGGYVVEA AIELGDAGGL GSVHGLDVQV NDAADGSRTS
     VRTWADPTGL GYQSPSRWGV ARLVDEASAP YRPGVVTVTP SRVHADWRVA PLDPTCVPVA
     GTAGVPEDAT GVVLNVTTVR PTGPGHVVVY PGGPTTLTRV PNGSTVNFEP GKDVASSSFV
     GLADGEVCYV TRGSRAGVLL DVTGYVTADS GVVTQAPRRL LDTRPGPLRI GDLDGLAPRE
     EHTVQVVGEA RVPEGATGAL VTVTVVRPTS VGNLRVYPEG GDVPVASTIN YVPGQDKANA
     TLVALPESGR ITLWSDSSVE VDVVVDVVGW VQPGASLTPV PPVRVVDTRP GSQTGPLSGP
     LTGRTAHSVQ LADLGPLPVD ATTAVLNVTA VRPTTIGNLR VYPDAAGGGS TPPDASSVNY
     VPGRDIPNMV VVEIPASGVV TFWSDVPTGG QVHLVVDVVG YVAPEQPTVP EEEPVPTDPD
     VVPGGAVDPT ATPVSAARGD GDVAALTFDD GPNLGETEEV LDLLAEHDIQ AVFCVIGQNI
     EAAGGAEILR RIVDEGHTLC NHTTSYADMG SWTPAQVQAD LVENLRIIRE ALGDPEAPVP
     YFRAPNGSWG RTPEVAVALG MQPLAVTNTI SDWETQDEAT LTAALRAAMV PGELVLVHDG
     GGDRAGTVAA VRTVVTERLA DGWTFTLPVG GAE
//
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