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Database: UniProt
Entry: A0A0J7KJ45_9BACT
LinkDB: A0A0J7KJ45_9BACT
Original site: A0A0J7KJ45_9BACT 
ID   A0A0J7KJ45_9BACT        Unreviewed;       590 AA.
AC   A0A0J7KJ45;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-SEP-2017, entry version 11.
DE   SubName: Full=Endo-1,4-beta-glucanase {ECO:0000313|EMBL:KMQ52113.1};
GN   ORFNames=CHISP_1102 {ECO:0000313|EMBL:KMQ52113.1};
OS   Chitinispirillum alkaliphilum.
OC   Bacteria; Fibrobacteres; Chitinispirillia; Chitinispirillales;
OC   Chitinispirillaceae; Chitinispirillum.
OX   NCBI_TaxID=1008392 {ECO:0000313|EMBL:KMQ52113.1, ECO:0000313|Proteomes:UP000036214};
RN   [1] {ECO:0000313|EMBL:KMQ52113.1, ECO:0000313|Proteomes:UP000036214}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACht6-1 {ECO:0000313|EMBL:KMQ52113.1,
RC   ECO:0000313|Proteomes:UP000036214};
RA   Sorokin D.Y., Rakitin A.L., Gumerov V.M., Beletsky A.V.,
RA   Sinninghe Damste J.S., Mardanov A.V., Ravin N.V.;
RT   "Phenotypic and genomic properties of Chitinispirillum alkaliphilum
RT   gen. nov., sp. nov., a haloalkaliphilic anaerobic chitinolytic
RT   bacterium from the candidate phylum TG3.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A)
CC       family. {ECO:0000256|RuleBase:RU361153}.
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:KMQ52113.1}.
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DR   EMBL; LDWW01000005; KMQ52113.1; -; Genomic_DNA.
DR   EnsemblBacteria; KMQ52113; KMQ52113; CHISP_1102.
DR   PATRIC; fig|1008392.3.peg.1213; -.
DR   Proteomes; UP000036214; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 1.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000036214};
KW   Glycosidase {ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036214};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    590       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5005290118.
FT   DOMAIN       49    311       Cellulase. {ECO:0000259|Pfam:PF00150}.
FT   DOMAIN      351    478       CBM-cenC. {ECO:0000259|Pfam:PF02018}.
SQ   SEQUENCE   590 AA;  67143 MW;  B5F4F6D2E418CFE8 CRC64;
     MFLRTFIFTL MVTAVYTLSA ASDPFVQNQK LGRGINLGNI FEAPGEGQWG ISFHDHYLDS
     ISQKGFQSIR VPIRWSAPQR TQLSEPYTIS EDFFSRIDHV IERAFDTGLS VIINVHHYEE
     LFEDATGFHR DRFVAIWEQI SKHYSQYGDS LYFEVLNEPH DDLTPQRWNL LFSEVLQIIR
     EKNPTRTVLL GTAEWGGIEG LSSLEIPEDP NLILTVHYYS PFQFTHQGAS WVENTDRFLG
     TTWSGTYIQK NEILNHIETI HAFGEKHNIP VNIGEFGAYS RADIESRHLW TKYCARLFER
     YGFSWHYWEF GSGFGAYDPS REEWIDTLVN ALISSDTSIL NIEEDVVDGV DLVTNGDFSS
     GMRPWVFGVW DQSGSASSKI QDEELVITVT KKPQATWQIQ LTQGEIDLEK NSEYIVLFDA
     RSSAPVSISA SVGMSEEPYT NFASTEGVML SDRMSTFGFQ FTATEDHSGA RLAFNLGTEP
     ADITFDNIRL IKITNSSSIR SSTRSANYAF NNNVSYKLSR DLQIFFHDSD RQKTTVSLFD
     AQGRIFGTKI YDPFSGANSI TFPRPFSRGP LFARFSNEAG SYVKRIIHVK
//
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