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Database: UniProt
Entry: A0A0Q9MYC4_9BACL
LinkDB: A0A0Q9MYC4_9BACL
Original site: A0A0Q9MYC4_9BACL 
ID   A0A0Q9MYC4_9BACL        Unreviewed;      1308 AA.
AC   A0A0Q9MYC4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   22-NOV-2017, entry version 13.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=ASL11_11615 {ECO:0000313|EMBL:KRE70929.1};
OS   Paenibacillus sp. Soil750.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1736398 {ECO:0000313|EMBL:KRE70929.1, ECO:0000313|Proteomes:UP000051252};
RN   [1] {ECO:0000313|EMBL:KRE70929.1, ECO:0000313|Proteomes:UP000051252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil750 {ECO:0000313|EMBL:KRE70929.1,
RC   ECO:0000313|Proteomes:UP000051252};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE70929.1, ECO:0000313|Proteomes:UP000051252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil750 {ECO:0000313|EMBL:KRE70929.1,
RC   ECO:0000313|Proteomes:UP000051252};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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:KRE70929.1}.
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DR   EMBL; LMSD01000010; KRE70929.1; -; Genomic_DNA.
DR   EnsemblBacteria; KRE70929; KRE70929; ASL11_11615.
DR   Proteomes; UP000051252; 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: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; 2.
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:UP000051252};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:KRE70929.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:KRE70929.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051252};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:KRE70929.1}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31   1308       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5006379058.
FT   DOMAIN      355    688       GH10. {ECO:0000259|PROSITE:PS51760}.
FT   DOMAIN     1127   1187       SLH. {ECO:0000259|PROSITE:PS51272}.
FT   DOMAIN     1188   1251       SLH. {ECO:0000259|PROSITE:PS51272}.
FT   DOMAIN     1254   1308       SLH. {ECO:0000259|PROSITE:PS51272}.
FT   ACT_SITE    612    612       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU10061}.
SQ   SEQUENCE   1308 AA;  141616 MW;  2691E51C3F14B1F0 CRC64;
     MRKKFVRIAL ILLVAALVIP SSLLTKVTKA ATTETITLYH ETFASGQGKA TRAGSANLSQ
     VTGKTFTGND DGKALYVSNR VNNWDGADFK FSDIGLENGQ TYTVTATVYV DADVTVPSGA
     QAGFQTVNGY QNTIYVNYEA GKALTLTKEF TVDTSKDSAL RINSNTAGAG VPFYLGDILV
     TKNVAAGPVV ETPRLPAVDF PTITFEDQTN GGFAGRKGTE TLTVISDANH TEGGTSALKV
     EGRTETWHGP SLRVEKYVDK GFEYKITAWV KLISPGSSQL QLSTQVGNAS ASYNTVDKKT
     ISTEDGWVKF EGNYRYNTVP DEFLSIYVES SSSKDASFYI DDISFVESSA PISVQTNLTP
     IKDAYRNDFL IGNAVSAADL DGVRLQLLKL HNNVVTAENA MKPDQTYNAN KEFDFATEDA
     LVTKIQAAGL KLHGHVLVWH QQTPTWLTTT TDSLPLGRVE ALANLKTHIQ TVMEHYGNKV
     ISWDVVNEAM NDNPSNPSNW HGALRQSPWK AAIGDDYVEQ AFLAAKEVLD AHPTWDIKLY
     YNDYNEDNQN KAQAIYSMVK EINDRYALTH PGKLLIDGVG MQAHYNLNTK PDNVKLSLEK
     FISLGVQVSI SELDITAGSN SRLTEKEANA QGSLYAQIFQ IFKAHAAHIE RVTFWGLNDA
     TSWRASQNPQ LFNSDLQAKP AYFGVIDPAA FLAAHPPESV AQANQSTAKF ATPTIDGMAD
     DAAWSQAPDM AINRYQQAWQ GASGVAKALW DDQNLYVLIQ VSNAELDKSS ANAYEQDSVE
     IFLDENNAKT SSYEADDGQY RINFGNEQSF NPASKSAGVE SKTHVSGTNY TVEVKIPLKT
     ITPEDNTKLG FDVQINDAKN GARQSVAAWN DTTGTGFQDT SVYGVLNLTG KVSNPSDGGD
     PDPGSGTGSG SGTVPSTSTD TGSSGGTITP ELKTENGRTI AAISGDTLKK ALEQAAPTAN
     VQKQIVIEVP KQANATSYEV QLPTQSLRGQ DNFELSVKTA DATIQIPSNM LSGVTENAEQ
     VSLRVAKVSK DNMDTATREQ IGNRPVIELT LAAGDKVIAW NNPNAPVTVA IPYLPTEEEL
     SDTDHIIIWY IDGQGKATPV PNGRYNAASG TVVFQTTHFS TYAVASVFKT FGDLQYVPWA
     KQAIDTMASR DVIHGTDENS FSPEASIKRA DFIALLVRSL ELHTTSNDVA MFSDVPKTAY
     YYNELVIAKA LGITTGFEDN TFKPDSPISR QDMMVLTTRA MAAADKQVQV GGTLDAYPDA
     ASMSSYAKDS AAALVKSGIV NGKNDKLAPI DELTRAEGAV ILYRIWQK
//
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