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Database: UniProt
Entry: A0A0J7HSU5_9BACT
LinkDB: A0A0J7HSU5_9BACT
Original site: A0A0J7HSU5_9BACT 
ID   A0A0J7HSU5_9BACT        Unreviewed;       590 AA.
AC   A0A0J7HSU5;
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:KMQ51836.1};
GN   ORFNames=CHISP_1332 {ECO:0000313|EMBL:KMQ51836.1};
OS   Chitinispirillum alkaliphilum.
OC   Bacteria; Fibrobacteres; Chitinispirillia; Chitinispirillales;
OC   Chitinispirillaceae; Chitinispirillum.
OX   NCBI_TaxID=1008392 {ECO:0000313|EMBL:KMQ51836.1, ECO:0000313|Proteomes:UP000036214};
RN   [1] {ECO:0000313|EMBL:KMQ51836.1, ECO:0000313|Proteomes:UP000036214}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACht6-1 {ECO:0000313|EMBL:KMQ51836.1,
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:KMQ51836.1}.
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DR   EMBL; LDWW01000007; KMQ51836.1; -; Genomic_DNA.
DR   EnsemblBacteria; KMQ51836; KMQ51836; CHISP_1332.
DR   PATRIC; fig|1008392.3.peg.1488; -.
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     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    590       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5005287910.
FT   DOMAIN       54    311       Cellulase. {ECO:0000259|Pfam:PF00150}.
FT   DOMAIN      350    480       CBM-cenC. {ECO:0000259|Pfam:PF02018}.
SQ   SEQUENCE   590 AA;  67594 MW;  67BAA2DE908011A4 CRC64;
     MLIKLIASAF FIFSVSTLRV SADPFVQNQK LGRGINMGNM FDAPSEGEWD VSFKDHYFDS
     IAQKGFQSVR VPIRWSAPQR TQLTEPYTIS DDFFARIDHV IEKALNSGLS IIINVHHYEE
     LFRDATGFHR DRFIAIWQQI SEHYSEYSDS LYFEVLNEPY GDLTPDRWNT LFAEVLQIIR
     SNNPTRTVLI GTAEWGGIEG LRHLEIPNDP NLILTVHYYS PFEFTHQNAF WLTGMEQYKG
     TTWDGTFIQK NDIINHMERI RSFAQKHNIP VNIGEFGAYG EADSTSRYLY SSFVSRLFER
     YDFSWHYWEF CAYFGAYDPY QEKWVDTIVN ALISSDTSIL YIDDFAPKGN NLITNGGFDS
     DLQDWTFGTW DQSGQASSEV INGELTINIE RKPQESWQVQ LIQNGIQLQQ NTEYIVMFDA
     RSKVPVSIHA DVSASGEPWT TFGSSDGLIL SEKMRTYAFE FTVTQSHSNA RLVFNLGTDP
     TTIHFDNIRI IELSDDRTNI QSRPKKTPSM FGSKIDKLPQ GLHLDFVSSK AQNATVALFN
     ANGRMIASKT IHTTAGQNSI QFPQHINPGP IFIRFQTEEG SHVERFMNVK
//
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