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Database: UniProt
Entry: U2LY59_9FIRM
LinkDB: U2LY59_9FIRM
Original site: U2LY59_9FIRM 
ID   U2LY59_9FIRM            Unreviewed;      1158 AA.
AC   U2LY59;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   22-NOV-2017, entry version 25.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=RUMCAL_02087 {ECO:0000313|EMBL:ERJ94429.1};
OS   Ruminococcus callidus ATCC 27760.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus.
OX   NCBI_TaxID=411473 {ECO:0000313|EMBL:ERJ94429.1, ECO:0000313|Proteomes:UP000016662};
RN   [1] {ECO:0000313|EMBL:ERJ94429.1, ECO:0000313|Proteomes:UP000016662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27760 {ECO:0000313|EMBL:ERJ94429.1,
RC   ECO:0000313|Proteomes:UP000016662};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R.,
RA   Fronick C., O'Laughlin M., Godfrey J., Miner T., Herter B.,
RA   Appelbaum E., Cordes M., Lek S., Wollam A., Pepin K.H., Palsikar V.B.,
RA   Mitreva M., Wilson R.K.;
RL   Submitted (JUL-2013) 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:ERJ94429.1}.
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DR   EMBL; AWVF01000254; ERJ94429.1; -; Genomic_DNA.
DR   RefSeq; WP_021683601.1; NZ_KI260494.1.
DR   EnsemblBacteria; ERJ94429; ERJ94429; RUMCAL_02087.
DR   PATRIC; fig|411473.3.peg.1723; -.
DR   OrthoDB; POG091H0Y2G; -.
DR   Proteomes; UP000016662; Unassembled WGS sequence.
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; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
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; 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; SSF63446; SSF63446; 1.
DR   PROSITE; PS51766; DOCKERIN; 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   Complete proteome {ECO:0000313|Proteomes:UP000016662};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:ERJ94429.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016662};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     31       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        32   1158       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004630486.
FT   DOMAIN      346    694       GH10. {ECO:0000259|PROSITE:PS51760}.
FT   DOMAIN     1088   1156       Dockerin. {ECO:0000259|PROSITE:PS51766}.
FT   ACT_SITE    619    619       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU10061}.
SQ   SEQUENCE   1158 AA;  126895 MW;  15970241C63C3BAB CRC64;
     MKFKKLMAAV TTGVLAVTSL SLSGLIGSAE VQELMNDTFE SGYGAWKGVG SSLSLSTEQA
     HNGGTSLYCY DRTANWGAPR CSLTGIVAAG QSYEISASAM YEGSGQQNMA IKMIYTDANG
     TDHYDQVAAA QATAGQWVEI KGNYTVPSGA TDMILYVEMP DANTDQTYYI DDVVIKGEKT
     EIQLDDKFES DFDNNSTQKW NGRGSAKVEL STKYAHSGTT SLYVSGRTQL WNGATRSASD
     IMEAGGYYKV GTYVLYDGDQ YTDTQKFSIN LQYDLNGKEN YYTIATETAN KGEWKYVGSE
     FTVPEGATNF YIYVQTGYTS APKEQDLMNF YMDDAVGEHL PDPAIQDDIA SLKDAYSDYF
     KIGCACAGSE FAQGATKDLI KKHYNSLTLG NELKPDSVLD QALSQKYVAE TGDDTMPQIS
     LNEADEILKF AGENKIPVRG HVLVWHSQTP DWFFKENFDP NGAWVSKDKM TKRLENYIKT
     VMETLKKDYP DVEFYAWDVV NEAASDAGTI RDAGSNNEVN GQSAWVKVYG DQSYIPLAFE
     FAKKYAPAGC KLFYNDYNEY SPNKQAYIIS DILKPLVEKN LIDGVGMQSH ISMSYPTIDL
     YKSAMQQYAD LGLEIQVTEL DVSEKSNEYA DQLALAQRYQ DVFKMYKEMK DSGVNLSAVV
     LWGITDSTSW IGGYPLLFDK DYQAKPSYYA VIDTDSEVEK LQTMTAYRYD GTDADLERAL
     EIGTAQYLST KTGSTGTYFK AAWSDENMIV RVYNPAVSAD AKNSYVEIFG NQLDSMGGFP
     IDDQTITSAM EYVDLKWESN SNDWNPKSGS TVHLDVFNNN AAWNCVDVAD YVFNNSDVPT
     GALPTCGIVT LAEQPKYAEA TKTETPITID GDIDAAWADA NTIDVNTYSM GNGATAVSKM
     LWDENCLYVL TEVTDPVLSV ASANAYEQDT VEVFFDENNH KTSSYESDDI QCRINYENDK
     TVTDGRSTDA FLSGTKKTDK GYIVEVAIPY TIGSFHADQI VGFDVQVNDD GTGDGKRTSM
     ANWNDLTGQG YINTSGFGVL KLVGDGTVTT DTTVTTTTTG TTSTTTETVT SATTSDSSTN
     TSESGESGLT LYGDVNMDSR VDITDAVLLN KAVANVVTLG STQKKNADCD ADSEISGNDA
     VVLLKFLVSI IHTLPSAE
//
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