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Database: UniProt
Entry: B0RCM6_CLAMS
LinkDB: B0RCM6_CLAMS
Original site: B0RCM6_CLAMS 
ID   B0RCM6_CLAMS            Unreviewed;       156 AA.
AC   B0RCM6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Nudix hydrolase domain-containing protein {ECO:0000259|PROSITE:PS51462};
GN   OrderedLocusNames=CMS1685 {ECO:0000313|EMBL:CAQ01794.1};
OS   Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS   / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Clavibacter.
OX   NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ01794.1, ECO:0000313|Proteomes:UP000001318};
RN   [1] {ECO:0000313|EMBL:CAQ01794.1, ECO:0000313|Proteomes:UP000001318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1
RC   {ECO:0000313|Proteomes:UP000001318};
RX   PubMed=18192393; DOI=10.1128/JB.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC       {ECO:0000256|ARBA:ARBA00005582, ECO:0000256|RuleBase:RU003476}.
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DR   EMBL; AM849034; CAQ01794.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RCM6; -.
DR   STRING; 31964.CMS1685; -.
DR   KEGG; cms:CMS1685; -.
DR   eggNOG; COG1051; Bacteria.
DR   HOGENOM; CLU_100874_2_0_11; -.
DR   OrthoDB; 9804442at2; -.
DR   Proteomes; UP000001318; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   PANTHER; PTHR43046:SF5; CONSERVED MEMBRANE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43046; GDP-MANNOSE MANNOSYL HYDROLASE; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003476}.
FT   DOMAIN          8..152
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   156 AA;  17770 MW;  35D46BF26E5C9AB3 CRC64;
     MSDGVVRHVR HTARILLVDE RDRLLLFLTN YSTNVDLPPR WLTPGGGIDP GESPAQAVRR
     ELFEETGLRV DSVGEPVWEH DYARQRIDGD LDTGHSTFYL VRADAFAPVS DNWMPDEFDD
     IHAHRWFTLD ELATTEDPIE PAEMVDVARE VLSRST
//
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