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Database: UniProt
Entry: A0A0J5QY43_9BACI
LinkDB: A0A0J5QY43_9BACI
Original site: A0A0J5QY43_9BACI 
ID   A0A0J5QY43_9BACI        Unreviewed;       984 AA.
AC   A0A0J5QY43;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   20-DEC-2017, entry version 15.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=AB990_16675 {ECO:0000313|EMBL:KMK75361.1};
OS   Bacillus pseudalcaliphilus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=79884 {ECO:0000313|EMBL:KMK75361.1, ECO:0000313|Proteomes:UP000035915};
RN   [1] {ECO:0000313|EMBL:KMK75361.1, ECO:0000313|Proteomes:UP000035915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8725 {ECO:0000313|EMBL:KMK75361.1,
RC   ECO:0000313|Proteomes:UP000035915};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Zheng C., Lan J., Che J.,
RA   Ge C., Shi H., Pan Z., Liu X.;
RL   Submitted (JUN-2015) 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:KMK75361.1}.
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DR   EMBL; LFJO01000006; KMK75361.1; -; Genomic_DNA.
DR   EnsemblBacteria; KMK75361; KMK75361; AB990_16675.
DR   PATRIC; fig|79884.3.peg.870; -.
DR   Proteomes; UP000035915; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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_sf.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF06452; CBM9_1; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000035915};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:KMK75361.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035915};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    984       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5005264039.
FT   TRANSMEM    958    979       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      346    678       GH10. {ECO:0000259|PROSITE:PS51760}.
FT   COILED      335    355       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    602    602       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU10061}.
SQ   SEQUENCE   984 AA;  108995 MW;  36B6C9E23D690D82 CRC64;
     MNLLFLIILL TTSSNWSAIV VKAETLTRIV YHQKFEDGVG VAKSAGNSTL DWVTSSEEGH
     AIYVTDRTND YDGVDIFFSD VGMEQDKKYS IEVSGYIGND ENIPSDARAL LQNVDSYQGL
     YVSSELATGE PFTLKGSYIV DINKDKAFRI QTNGAGKELS FYIEEILITE EEQEDEEVPT
     EPSEPIEEFS AINFENGELN GFEGRAGTEI LTVTNEANAT EDGSYSLKVE NREQPWHGPT
     LDVDPFIELG AEYKISAMVK LISPETAQLQ LSTQIGSGDG ASYNHIHGET LDVEDGWVKL
     EGTYRYTSLG NGNVSIYIES SNQATASFYV DDVTFEKLNS EAIEIEDELE AIKDVYQDYF
     LIGNAGAMNE FDGVRGQLLM KHHNLITAEN AMKPGYAYNE QREFDFTAED DFVSAALENE
     LRIHGHVLVW HQQSAEWLHT DDEGNYLDRE EALANLRTHV QTTVEHFGED VISWDVVNEA
     MNDNPPTPTD WRSSLRQSGW YHAIGEDYVE QAFLAAKEVI VANGWDIKLY YNDYNDDNRN
     KAEAIYQMVK EINDNYAAEN NGELLIDGIG MQGHYNLNTN PENVRMSLEK FISLGVEVGV
     TELDITAGSN GVQTEEEANT QGYLYAQLFQ LYKEHAEHIS RVTFWGLNDA TSWRAAQSPL
     LFDRDLKAKP AYYAVIDPER FIENHEVDSQ EANQATAVYG TPLVDGEYDE IWDNADELLI
     NRYQTAWNGA DGVGRVLWDE ENLYVFIEVN DSELDKTSDN PWEHDSIEVF IDENNTKTSY
     YEEDDGQYRV NFDNETSFNP PNKSEGFESV TKVTETGYTV ELKIPFTEVT PESAMKLGFD
     LQINDAQNGS RQSVATWNDL TGQGFQDPSV FGVLTLVADG EPGEPGEPGE PGGPGEPGGP
     GGPGEPGEPG EPGEPGGPGE PGEPGEPGGP GEPGEPGGSG GKGTEQNGNT LPHTASNFYQ
     YLLIGFVFLL IGGTVYVVAK RRLA
//
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