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Database: UniProt
Entry: A0A0V8ST89_9CELL
LinkDB: A0A0V8ST89_9CELL
Original site: A0A0V8ST89_9CELL 
ID   A0A0V8ST89_9CELL        Unreviewed;      1088 AA.
AC   A0A0V8ST89;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   25-OCT-2017, entry version 12.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=ATM99_12815 {ECO:0000313|EMBL:KSW23552.1};
OS   Cellulomonas sp. B6.
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1295626 {ECO:0000313|EMBL:KSW23552.1, ECO:0000313|Proteomes:UP000054319};
RN   [1] {ECO:0000313|EMBL:KSW23552.1, ECO:0000313|Proteomes:UP000054319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B6 {ECO:0000313|EMBL:KSW23552.1,
RC   ECO:0000313|Proteomes:UP000054319};
RA   Piccinni F.E., Campos E.;
RT   "Draft Genome Sequence of Cellulolytic and Xylanolytic Cellulomonas
RT   strain Isolated from Decaying Forest Soil.";
RL   Submitted (NOV-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:KSW23552.1}.
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DR   EMBL; LNTD01000099; KSW23552.1; -; Genomic_DNA.
DR   EnsemblBacteria; KSW23552; KSW23552; ATM99_12815.
DR   Proteomes; UP000054319; 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; -; 1.
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.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR027273; Neocarzinostatin-like.
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; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054319};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054319};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     36       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        37   1088       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5006895791.
FT   TRANSMEM   1060   1078       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      210    561       GH10. {ECO:0000259|PROSITE:PS51760}.
SQ   SEQUENCE   1088 AA;  112417 MW;  90EA60104C1E37F4 CRC64;
     MHAPAQRRRH RHAIGGAAAA TALVLTGLVA PPGAAADTGT VPYTVMFNNF ESSVGSRAPA
     WSALDVAGPS GTPAATSFST TDVRTRVSHA RSLQVAARDH VGDGAQMPIP ATLLTAGQTY
     TISVWVHVAE GSAPVTAGTP LTARVAVGGT ALPAAAGTDL VLEPGVWKRV AVTYTHTAGA
     TPLTVTVDNT TGTFYLDDAM VSGERVGEPV PATGTLKNTL GYPVGVAVER RSTLVGTEAE
     QVLSTQFDQV TPENAMKPES WYGADGKFAG TPGAEMTSNE GADALMDWAK RNDGRVYGHV
     LVWHGQNPGW FFQDENGAPL DAAGASERMR THIFDVAKYL SDRYGAFGSP GNPLAAFDVV
     NEVIADNAAT ASNGMRTSTW FNTLGEEFVD QAFRDADEAF NDVYAQPGSD RPVKLFINDY
     GTEGGDAAGS KLNRYYDLVQ RLIARDVPID GVGHQYHVNL NTPTANLRTG LEKFTATGLQ
     LAVTEFDVTT GYPQTERLAI RQGQYYKTAF DIFNAYDRTH PDRLFSVTVW GLNDAGSWLY
     YDGAPLMFDD YLNPKWSLVG ALGGDVPAEP KAMTVFGGDV DLDAPRVTTD PQWSLVAPSA
     VGDHARFTLR WAPDALTAYV DVDDATVDAT DGVTFRVGAQ RYGITRAGEG DLPVVVSERD
     GGWTAVVQLP LTGATEGGTV PFDVAVTDGA TTAGWNAPGI LGELTLREPL SHVDVLQVDA
     PPAVDAEVDD LWAAAPVVRT DKVTQGTAAA AYADVRTVWS GDGSSLFVLA EVTDPQVSLT
     PNNAWEKDSL EIFVDPGNAK NGAYRAGEDV QIRIAADNAV SSGGGRVVAS ATRQTATGYV
     VEAEISLLDA GGPGTLHGLD FQVNDATGNA RTGVKAWADP TGQGYQNTSR WGVARLAERG
     TPALTLGAAE VTAGGDVTVT ATGFPARATV ELQLVAATSG AARAAADPVA LGTVEVAADG
     VAQTTVTVPA SVAAGDYRIA AVGADETLAT ADLRVVAAAV EPTPGPTPGP TSQPTPGATP
     TPGATATPGA DPTPGGTGGT TGSGTTGASS GRLATTGSAI ALWSVLAAAL LTGGGVLVRA
     RRAAGADD
//
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