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Database: UniProt
Entry: F2JLG8_CELLD
LinkDB: F2JLG8_CELLD
Original site: F2JLG8_CELLD 
ID   F2JLG8_CELLD            Unreviewed;      1383 AA.
AC   F2JLG8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   25-OCT-2017, entry version 40.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   OrderedLocusNames=Clole_0518 {ECO:0000313|EMBL:ADZ82256.1};
OS   Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB
OS   11756 / RHM5) (Clostridium lentocellum).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Cellulosilyticum.
OX   NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ82256.1, ECO:0000313|Proteomes:UP000008467};
RN   [1] {ECO:0000313|EMBL:ADZ82256.1, ECO:0000313|Proteomes:UP000008467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC   {ECO:0000313|Proteomes:UP000008467};
RX   PubMed=21398547; DOI=10.1128/JB.00239-11;
RG   US DOE Joint Genome Institute;
RA   Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA   Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA   Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA   Angert E.R., Currie C.R.;
RT   "Complete genome sequence of the cellulose-degrading bacterium
RT   Cellulosilyticum lentocellum.";
RL   J. Bacteriol. 193:2357-2358(2011).
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; CP002582; ADZ82256.1; -; Genomic_DNA.
DR   ProteinModelPortal; F2JLG8; -.
DR   STRING; 642492.Clole_0518; -.
DR   EnsemblBacteria; ADZ82256; ADZ82256; Clole_0518.
DR   KEGG; cle:Clole_0518; -.
DR   eggNOG; ENOG4105D9F; Bacteria.
DR   eggNOG; COG3693; LUCA.
DR   KO; K01181; -.
DR   OMA; IGMQMHI; -.
DR   OrthoDB; POG091H0Y2G; -.
DR   Proteomes; UP000008467; Chromosome.
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:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 3.30.457.10; -; 3.
DR   InterPro; IPR010502; Carb-bd_dom_fam9.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR036582; Mao_N_sf.
DR   Pfam; PF06452; CBM9_1; 1.
DR   Pfam; PF02018; CBM_4_9; 2.
DR   Pfam; PF07833; Cu_amine_oxidN1; 2.
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   SUPFAM; SSF55383; SSF55383; 2.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008467};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:ADZ82256.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:ADZ82256.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008467};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:ADZ82256.1}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31   1383       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003284245.
FT   DOMAIN      350    716       GH10. {ECO:0000259|PROSITE:PS51760}.
SQ   SEQUENCE   1383 AA;  150345 MW;  B079B69B74D2C779 CRC64;
     MSLLKKRIAY LTTSTLLASS VLGITPCLFA SSTPSTITYN FDGGTEGWIA RGDAQVTTTS
     SSLTIDSTNH CLYVTNRTSN WHGVSKELKD TLKAGETYTF SVYVKYDEGA DTESLSLTLE
     TGLEENGYIT IASNSAVSKG EWTQLTGEVT VPEAATKANV YMEAANADLS FYVDELKITG
     SFATDSPEVP NAPLTTWDFE SGLGDWSVRG SGEATAEVST TAPHGGNQCA FVSGRTQDWN
     GIQVNLTNSA KKGGKYTFEA WVKYDAADEG TEQFVLALQY DAESESSTQY KWITNADVKN
     GEWTKLQGEY TLPKDFTDIS LYIQVNGSTI DFYADDITMQ GEPELDVEIQ KDIPSLKEVY
     SDYFKFGTAI ASNNLNDLEQ ELVLKHFNSI THENALKPES ILDHAATIAY MNANGDQTHP
     QVTLSSDAKA TLDFARDNHI PVRAHVLVWH SQTPNWLFTE NYSTEKDAPV VSKEVMKQRL
     ENYTNAYFKL LSEEYPDVDF YAIDVVNEAV NPDRPDGLRA PATVATTSGD DDNDENANNS
     MWMTTIGAEF IEDAFTYARA AADQYMPNVK LAYNDYNECD PKKTEIIYSI CKDLYDKGLL
     DVVGMQGHYN MSSPSTSQFE NALLKYASIG DNIEIQITEL DITQDDTSEE GLIKQAYRYK
     GFLDIMKKLD SEGAANITSC VVWGVKDDES WRSERLPLLF DADYQAKPSF WAITDSSKLP
     VLAQEVKAYS LGSKDYTHAF LIQKGTALET TSGTQIASYK VAWDANNIYV NVIPTEKGKS
     GTVKVFLNDN SISANLTDNT VIQIPLSEAI SEGGTLSFDL FVQVGDEKAT WNNLAYDGTS
     APNQSTFGKL LLSKAPHSSS AIKGTPIIDG KMDGLWNKAE TINVNTFSIG TSGATATAKA
     LWDENYVYVL VEVKDSLLSK ASTNTYEQDS VEIFIDEDNA KSTSYELGDI QYRVNFDNER
     SINGASDADS FITATQIIDG GYIVEAALPS RIAAFTKNQV VGFDFQINDD ADGNGKRDNV
     SNWNDLTGNG WSSTAGYGVL QLVKPTTSDD SGSGSGSGSG AGSGTGSSST STSTTSVNKT
     PDQIIASALS DNTALELSIG TTPITISQNS IEQLSTQEKA LVLKSGKVTA TITPAFINTN
     LSNANKILSS LEVSMLPVSD TLFTSLKNQL AKDDNLSIVG TSANTSVINI KGHSSLSTFT
     EPLLLSVDLV NATITDSSHL TLARVSKNTD GTFTFTQLGG DYQLNNHTLT GYVTEPGTYI
     VIEKKNLIKL NLIIGKTTIN SNQSTSITSD TAPKIVNGTT MVPLRFVAEQ LGADVKWNAV
     NKEITLLFDN QKVILNMGKG QTSSNPETIL ENGRTLVPLR YVSENLGANV LWIPSSKTIE
     IVK
//
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