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Database: UniProt
Entry: C1FQI0_CLOBJ
LinkDB: C1FQI0_CLOBJ
Original site: C1FQI0_CLOBJ 
ID   C1FQI0_CLOBJ            Unreviewed;       450 AA.
AC   C1FQI0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Amidohydrolase family protein {ECO:0000313|EMBL:ACO86938.1};
GN   OrderedLocusNames=CLM_2387 {ECO:0000313|EMBL:ACO86938.1};
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232 {ECO:0000313|EMBL:ACO86938.1, ECO:0000313|Proteomes:UP000001374};
RN   [1] {ECO:0000313|EMBL:ACO86938.1, ECO:0000313|Proteomes:UP000001374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2 {ECO:0000313|Proteomes:UP000001374};
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001581; ACO86938.1; -; Genomic_DNA.
DR   RefSeq; WP_012705596.1; NC_012563.1.
DR   AlphaFoldDB; C1FQI0; -.
DR   KEGG; cby:CLM_2387; -.
DR   eggNOG; COG0402; Bacteria.
DR   HOGENOM; CLU_012358_2_1_9; -.
DR   Proteomes; UP000001374; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01298; ATZ_TRZ_like; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR43794:SF11; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43794; AMINOHYDROLASE SSNA-RELATED; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACO86938.1}.
FT   DOMAIN          57..413
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   450 AA;  50245 MW;  F393C073D21F11DC CRC64;
     MNQILIKNGY IITMDSSKKI FEKSDILVED SKIITIGNVE SELIKSSVEI IDANGKIIMP
     GLVNTHVHLS QQLARGLADD VDLLTWLRKR IWPYESNMDL EDSYISSLAC CTELIRSGVT
     TFCEAGGQEV DGMGKAVEQA GLRGILCRST MDCGDGLPLK WQETTEESLE KQVELLEKWN
     GKGDGRIKYW FGLRTIFNTT DKLITKTKEL ADKYKVGIHM HVAEIEEEVR YAEATRGETT
     VQHLAKLGVL DKNFLAVHTV WLTEQEIDLF KLHNVKVSHN PGAAMKVVLG FARIPEMLEK
     GINVSIGTDG APSNNRMDMF DEMHLTSLIH KGRRLNPKVV PADEVLEMAT MNGAKCALWE
     DEIGSLEVGK KADLIIINPK SIGSLPMHDP IGNIVYSMHS SDVESSMCNG KWLMKNKVLL
     TINEEDIIRE VQERATALVK KAGIVLPKRF
//
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