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Database: UniProt
Entry: A5I6A1_CLOBH
LinkDB: A5I6A1_CLOBH
Original site: A5I6A1_CLOBH 
ID   A5I6A1_CLOBH            Unreviewed;       585 AA.
AC   A5I6A1; A7G7I4;
DT   26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=F5/8 type C domain-containing protein {ECO:0000259|Pfam:PF00754};
GN   OrderedLocusNames=CBO3022 {ECO:0000313|EMBL:CAL84583.1};
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL84583.1, ECO:0000313|Proteomes:UP000001986};
RN   [1] {ECO:0000313|EMBL:CAL84583.1, ECO:0000313|Proteomes:UP000001986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC   {ECO:0000313|Proteomes:UP000001986};
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA   Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA   Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT   Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
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DR   EMBL; AM412317; CAL84583.1; -; Genomic_DNA.
DR   RefSeq; WP_012048044.1; NC_009698.1.
DR   RefSeq; YP_001255512.1; NC_009495.1.
DR   RefSeq; YP_001388749.1; NC_009698.1.
DR   AlphaFoldDB; A5I6A1; -.
DR   GeneID; 5186998; -.
DR   KEGG; cbh:CLC_2919; -.
DR   KEGG; cbo:CBO3022; -.
DR   PATRIC; fig|413999.7.peg.2998; -.
DR   HOGENOM; CLU_465976_0_0_9; -.
DR   Proteomes; UP000001986; Chromosome.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT   DOMAIN          353..470
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|Pfam:PF00754"
SQ   SEQUENCE   585 AA;  68222 MW;  CBBF7318517639CA CRC64;
     MDNSIFCYLD NSNGNDLNIG TTKDKAFKTI GKAKDFIKNN GGIGDVYIIG YYNIPSFELV
     NNDIFLNIIG ISKQSEIYYV HPFGDNVNCL KNVNFYKLKV SCGDSRFNYH PYTENVNFYN
     CIITFSGCPF YGYKSNFYNC IFENALTSID YRFSDGNVYR IGGKFSNCIF NKNIFNEKTN
     FISAIKQSYN LSVDNIYFYI NEKNKNDISI RNNGDINILN EDGTRSDIGI YGGMTPYIFN
     FYKFLLKQNQ NYYTIKSEFY KNNNYKPITE LEGKEVLTQN NFETYGIDDL NLLTKTIDTR
     VINGIDKGRL GSGKYFEVGL YNCCKRVKSQ PVLDYTDNIM PQMNASTVNG ITVTASSTEG
     NYYPYQAFDR NPSNAYAWSS NRYDSPEIRQ SANLYINFNT LTRKVSKYKI LSYYCYPYDI
     KLYGSNDNTD WKLLDERNNV VSEYKWYDFK FKNTINYQYY KFNFKTNEEK VFINEMELME
     LIIPFKYLIE YNSQLYTFNN TEIILSSSQV LDENNFINNG FVDATAITEE QWNTAFSDKS
     NLKLLIWTDD MSKTDVNIET ETIPFRPIDK LKKNSDICNI LFKEV
//
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