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Database: UniProt
Entry: A0A089M4C6_9BACL
LinkDB: A0A089M4C6_9BACL
Original site: A0A089M4C6_9BACL 
ID   A0A089M4C6_9BACL        Unreviewed;      1340 AA.
AC   A0A089M4C6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-NOV-2017, entry version 23.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=R70331_08830 {ECO:0000313|EMBL:AIQ51609.1};
OS   Paenibacillus sp. FSL R7-0331.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ51609.1, ECO:0000313|Proteomes:UP000029487};
RN   [1] {ECO:0000313|EMBL:AIQ51609.1, ECO:0000313|Proteomes:UP000029487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ51609.1,
RC   ECO:0000313|Proteomes:UP000029487};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) 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; CP009284; AIQ51609.1; -; Genomic_DNA.
DR   RefSeq; WP_042174544.1; NZ_CP009284.1.
DR   EnsemblBacteria; AIQ51609; AIQ51609; R70331_08830.
DR   KEGG; paee:R70331_08830; -.
DR   KO; K01181; -.
DR   Proteomes; UP000029487; 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   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   InterPro; IPR001119; SLH_dom.
DR   Pfam; PF06452; CBM9_1; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   Pfam; PF00395; SLH; 3.
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.
DR   PROSITE; PS51272; SLH; 3.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029487};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:AIQ51609.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:AIQ51609.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029487};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:AIQ51609.1}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31   1340       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5001846999.
FT   DOMAIN      366    703       GH10. {ECO:0000259|PROSITE:PS51760}.
FT   DOMAIN     1158   1218       SLH. {ECO:0000259|PROSITE:PS51272}.
FT   DOMAIN     1219   1282       SLH. {ECO:0000259|PROSITE:PS51272}.
FT   DOMAIN     1286   1340       SLH. {ECO:0000259|PROSITE:PS51272}.
FT   ACT_SITE    627    627       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU10061}.
SQ   SEQUENCE   1340 AA;  141999 MW;  D152D7E9D1526F49 CRC64;
     MSRMFKRVFP AILAASLLLP LGWAAPAAQA SQVSRATETG QAEVTTVYHE TFAGGAGKAG
     QSGGASLAAV NGIPFDGNTD GAALYVSNRV NNWDAADFKF SDLGLVNGET YTVTAVVYVD
     AAVILPEGAK AALQTVNSYG NYAEAAYEAG KAVTLTKEFI ADTSKDQALR INSNEAGKAV
     SFYIGDVLIT GKAASGGGEE PDRDPALPFS TITFEDQTAG GFTGRSGNET LTVTDEANHT
     AEGSYALKVE GRTSTWHGPA LRVEKYVDKG SEYKISAWVK LIDPASSQLQ LSTQVGNGSS
     ANYVALSPKT ISAADGWVKF EGSYRYNSVG DEFLTIYVES SNNAAASFYI DDISFEHTGT
     GPVAIQKDLV PVKDAYRDDF LIGNAITAED LEGVRLELLK MHHNVATAGN VMKPDGLQNV
     KGEFTFSEAD TMVDKVLAEG MQMHGHVLVW HQQSPVWMNT GKDVEGNSVP LGREEALVNL
     RTHIRTVMEH FGDKVISWDV VNEAMNDNPG NPADWESSLR QAPWKTAIGA DYVEQAFLAA
     REVLDEHPEW NIKLYYNDYN EDNQNKAQAI YNMVKALNDK YALSHPGKQL IDGIGMQAHY
     NVNTNPENVR LSLEKFISLG VEVSVTELDI QAGSNYELSA KLADAQGYLY AQLMGLYKEH
     AANIARVTFW GMDDNTSWRA SANPLLFDKS LQAKPAYYGV IDPVKYIAEH QPDTTDANVS
     NAVYGTPVID GTVDALWTGV PEMQVNRYQL AWQGASGIAK ALWDDQNLYV LVQVSDAQLD
     KASANVWEQD SVEIFVDQNN GKTSFYQDDD GQFRINFNNE TTFNPDRIAA GFTSAAKVSG
     TNYTVEVKIP LTGVTPANAK KLGFDVQIND AKDGARQSVA AWNDTTGNGY QDTSVYGVLT
     LTGKPDAPEV TPTPTPTPTP TPTPTPEVTP SPVAIPGGTN TMATPKPVTA ENKDGVVTLK
     PEVKITGGEV KADVSADNLT KALEQALLGI DGLKHIGIEL PEQRDAAAYE LQLPAQSLKG
     QANFVLLVKT AAASIEIPGD VLSGAAADTE YVSVHVKQAV KDSLASVART LIGEGPVIDL
     SLTAGAKEIA LGAPDAPVKV AIPYTPASAQ LGNPAALIAG QLGSTGGLTP IPNSRYDAAS
     GSLVFHITGS GTYAVAYNPV SFTELEKLTW AKEAITALAA RGVVQGSAEG SFTPAAPVKR
     ADFVVMLVKA LELKGTGSAA SGFSDVPAGI DYSNGLAIAH QLGIISGYAD GTVRPDNPIS
     RQEMMVIAAR ALAAAGKAAA TSNGSLNAYP DAAQVAGYAA DSASLLVKAG VITGKNGLLA
     PGDTLTRAEA AVIVYRIWGL
//
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