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Database: UniProt
Entry: A6W6W7_KINRD
LinkDB: A6W6W7_KINRD
Original site: A6W6W7_KINRD 
ID   A6W6W7_KINRD            Unreviewed;       912 AA.
AC   A6W6W7;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   22-NOV-2017, entry version 65.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   OrderedLocusNames=Krad_1068 {ECO:0000313|EMBL:ABS02556.1};
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 /
OS   SRS30216).
OC   Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae;
OC   Kineococcus.
OX   NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS02556.1, ECO:0000313|Proteomes:UP000001116};
RN   [1] {ECO:0000313|Proteomes:UP000001116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC   {ECO:0000313|Proteomes:UP000001116};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E.,
RA   Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Lykidis A., Bagwell C.E.,
RA   Shimkets L., Berry C.J., Fliermans C., Richardson P.;
RT   "Complete sequence of chromosome of Kineococcus radiotolerans
RT   SRS30216.";
RL   Submitted (JUL-2007) 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}.
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DR   EMBL; CP000750; ABS02556.1; -; Genomic_DNA.
DR   ProteinModelPortal; A6W6W7; -.
DR   STRING; 266940.Krad_1068; -.
DR   CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   EnsemblBacteria; ABS02556; ABS02556; Krad_1068.
DR   KEGG; kra:Krad_1068; -.
DR   eggNOG; ENOG4105D9F; Bacteria.
DR   eggNOG; COG3693; LUCA.
DR   KO; K01181; -.
DR   OrthoDB; POG091H0Y2G; -.
DR   BioCyc; KRAD266940:GI4N-1159-MONOMER; -.
DR   Proteomes; UP000001116; Chromosome.
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; -; 2.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR003410; HYR_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF02018; CBM_4_9; 2.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   Pfam; PF02494; HYR; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51760; GH10_2; 1.
DR   PROSITE; PS50825; HYR; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001116};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:ABS02556.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:ABS02556.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001116};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:ABS02556.1}.
FT   SIGNAL        1     29       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        30    912       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002704030.
FT   DOMAIN      337    697       GH10. {ECO:0000259|PROSITE:PS51760}.
FT   DOMAIN      705    787       HYR. {ECO:0000259|PROSITE:PS50825}.
SQ   SEQUENCE   912 AA;  96786 MW;  BF2FFA5C1213EF0D CRC64;
     MRQRRLRAGA LATGLLAGLG TVVAPSATAA AVDYTAGFES GTSGWTGRGT TGVAVSTDQA
     HGGSSSLLAT GRTANWHGPA LDARTVMPAG RYTIEAWVRL VAGTGADTVS LTVARTPDGG
     AAAYDSVANG VAVTDSGWTR VSGTYEFATA NNSQLELYLE SPDATQAFYV DDVRITGETA
     APVQPGTTPP VTTAFDGGPD GWTARGDATV AHVTAGGRSG GALSVSGRTQ TWHGPALDVT
     PNLAVGRTVE ASVWARLAPG SAPAQLTLSI QRDRAGTQTA YENIAGAEVT ADAWTRIRGT
     YTLGSPVDRA QVYVEGTAGA AFLIDDFTLQ PFAETPVQDV PALKDVLGAQ GFEHVGVALD
     QRETTGRPAQ LVQKHFNAFT PENDGKPESV QPTEGTFTFG NLDRLLDFAD ATGTQVYGHV
     LVWHSQTPAW VFQRPDGTPL TNSPADRALL EQRMETHIKA IADHVNARYP DGNSPIWAWD
     VVNEVIADGD NANPHDMRDS RWFQVLGEGF VDHAFRLADQ YFPDAKLFIN DYNTEMPEKR
     ADYLGLVSSL IERGVPIDGV GHQAHVDFGR PVQWLDDSLT AVEELSAQEG HPLAQVITEL
     DVSTSTEMAS ADVNSTGAPE RATPDDAAAG VENGYYYRDL FAALREHSGS IESVTFWGIS
     NARTWLRTWP YPRPWERPLP FDDDLQVTPA YWGVVDPSKL PARPADFLIP RLAAKDPVRV
     SSTSPAGAEV TFTPPVAGDT RDGVLSPTCT PASGSQFPIG TTRVTCTLTD EAGNQATPGV
     FDVVVTPPPT TTKLYQRVNH GPVVRANVNQ TVQVVVQFGN EGTGTLLGRT FGHSCTQVNA
     GAAGSTPLAL ELAPGSAHTT QRNYPAGQNG NFTLRARPTR TGTAVLDCTL SLQDSFGAQV
     STTTRITVDV RK
//
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