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Database: UniProt
Entry: A0A0W8JAE3_9VIBR
LinkDB: A0A0W8JAE3_9VIBR
Original site: A0A0W8JAE3_9VIBR 
ID   A0A0W8JAE3_9VIBR        Unreviewed;       500 AA.
AC   A0A0W8JAE3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=VRK_36410 {ECO:0000313|EMBL:KUI97189.1};
OS   Vibrio sp. MEBiC08052.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUI97189.1, ECO:0000313|Proteomes:UP000054473};
RN   [1] {ECO:0000313|EMBL:KUI97189.1, ECO:0000313|Proteomes:UP000054473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUI97189.1,
RC   ECO:0000313|Proteomes:UP000054473};
RA   Kim Y.J., Lee J.-H., Kwon K.K.;
RT   "Genome sequence of Vibrio sp. MEBiC08052.";
RL   Submitted (DEC-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:KUI97189.1}.
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DR   EMBL; LQIY01000028; KUI97189.1; -; Genomic_DNA.
DR   RefSeq; WP_059122494.1; NZ_KQ947475.1.
DR   EnsemblBacteria; KUI97189; KUI97189; VRK_36410.
DR   PATRIC; fig|1761910.3.peg.3681; -.
DR   Proteomes; UP000054473; Unassembled WGS sequence.
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   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
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; 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:UP000054473};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054473};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     38       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        39    500       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5006944480.
FT   DOMAIN      226    497       GH10. {ECO:0000259|PROSITE:PS51760}.
FT   ACT_SITE    432    432       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU10061}.
SQ   SEQUENCE   500 AA;  55143 MW;  4C99316FCFA99901 CRC64;
     MKERTQRQWL GFNTKQFRTA PVLTALAALT MPFMSAVADT QVDVSAAAPS GFAAYYASES
     FAGLANNGGV ENGLTNWSSI GGYITRTNQA SHSGAASVLI LNRNATWNGI TFKPAPLVNG
     KKYNVSVWVR LAPGSQSTNI ILTGKRTDDA DSSTSNEYVR IASAQATDYQ WTELKGSYTQ
     SGTPFQHFII ESDNSKVSYY ADDMSVEDVG GGGSDNPTPG NGKKFVGNIT TSGQVRGDFT
     RYWNQITPEN EGKWGSVERT RDVYNWSGID ASYNYAKQHN IPFKQHTFVW GNQYPTWIDS
     LSPSEQAGEI EEWIRDFCHR YPDVAMIDVV NEATPGHAPA EYARRAFGND WIIKSFQLAR
     KYCPNATLIL NDYNVLSWNT DQFIAMAKPA VQAGVVDAIG LQSHGLEGFS NAALQANLNK
     VIALGLPIYI SEYDVAKTND QAQLDVMKRQ FPLFYNSDAV AGITLWGYVV GRTWVDGSGL
     IYDDGSPRPA MRWLMNYLGR
//
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