ID B9EAJ8_MACCJ Unreviewed; 438 AA.
AC B9EAJ8;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Bifunctional metallophosphatase/5'-nucleotidase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=MCCL_0552 {ECO:0000313|EMBL:BAH17259.1};
OS Macrococcus caseolyticus (strain JCSC5402).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX NCBI_TaxID=458233 {ECO:0000313|EMBL:BAH17259.1, ECO:0000313|Proteomes:UP000001383};
RN [1] {ECO:0000313|EMBL:BAH17259.1, ECO:0000313|Proteomes:UP000001383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC5402 {ECO:0000313|EMBL:BAH17259.1,
RC ECO:0000313|Proteomes:UP000001383};
RX PubMed=19074389; DOI=10.1128/JB.01058-08;
RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL J. Bacteriol. 191:1180-1190(2009).
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
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DR EMBL; AP009484; BAH17259.1; -; Genomic_DNA.
DR RefSeq; WP_012656460.1; NC_011999.1.
DR AlphaFoldDB; B9EAJ8; -.
DR STRING; 458233.MCCL_0552; -.
DR KEGG; mcl:MCCL_0552; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_8_1_9; -.
DR OrthoDB; 9793179at2; -.
DR Proteomes; UP000001383; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR CDD; cd00845; MPP_UshA_N_like; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR011240; Pesterase_YunD.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR PANTHER; PTHR11575:SF23; 5-NUCLEOTIDASE FAMILY PROTEIN; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF036361; YunD; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Reference proteome {ECO:0000313|Proteomes:UP000001383}.
FT DOMAIN 4..198
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 273..403
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 438 AA; 50408 MW; 7DAB62DB0C28BE8F CRC64;
MEVKLFHTND IHSYLSNYHK ISRYINDRRQ EHADMIYFDL GDHVDRSHPL TEATLGQANI
ELLNEAQVDV VTIGNNEGIT LDHDAFNQLY QDAEFEITCC NLFDEQGNLP ENIRTSVIME
RQGITYGIIG ATAEFTPFYK ALGWDVTDPM SAIIREVHRI HEHVDVVIIL SHLGKFFDRQ
LAEACPQIDI ILGAHTHHFF QQGEVVNDVL IGAAGRYGEY IGEITLTFEE RKLIRKSAKL
IDTNDLRSTG EDFFEVGAAL LSQKVSSKQL NLPRRLYSAS YTTDLLAQAL MDFTGGDCAL
INSGLIVKGF EGRDFSYFDL HTMLPHPINP VKITLSGREL KEIINMSMLH DYRDEIIKGF
GFRGDIFGMY VWKNIGYIQS QQRYFIGTEE IDNHKKYYLA TLDMYTFGRF FPQFTQNEKR
YYMPEFLRDI METAVKNL
//
