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RBN_CROS8
ID   RBN_CROS8               Reviewed;         304 AA.
AC   A7MHT9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Ribonuclease BN {ECO:0000255|HAMAP-Rule:MF_01818};
DE            Short=RNase BN {ECO:0000255|HAMAP-Rule:MF_01818};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01818};
DE   AltName: Full=Ribonuclease Z homolog {ECO:0000255|HAMAP-Rule:MF_01818};
DE            Short=RNase Z homolog {ECO:0000255|HAMAP-Rule:MF_01818};
GN   Name=rbn {ECO:0000255|HAMAP-Rule:MF_01818}; Synonyms=rnz;
GN   OrderedLocusNames=ESA_00945;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
CC   -!- FUNCTION: Zinc phosphodiesterase, which has both exoribonuclease and
CC       endoribonuclease activities. {ECO:0000255|HAMAP-Rule:MF_01818}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01818};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000255|HAMAP-Rule:MF_01818};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01818}.
CC   -!- SIMILARITY: Belongs to the RNase Z family. RNase BN subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01818}.
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DR   EMBL; CP000783; ABU76215.1; -; Genomic_DNA.
DR   RefSeq; WP_004388264.1; NC_009778.1.
DR   AlphaFoldDB; A7MHT9; -.
DR   SMR; A7MHT9; -.
DR   EnsemblBacteria; ABU76215; ABU76215; ESA_00945.
DR   KEGG; esa:ESA_00945; -.
DR   PATRIC; fig|290339.8.peg.843; -.
DR   HOGENOM; CLU_031317_2_0_6; -.
DR   OMA; GTQRQMM; -.
DR   OrthoDB; 1712770at2; -.
DR   Proteomes; UP000000260; Chromosome.
DR   GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042779; P:tRNA 3'-trailer cleavage; IEA:InterPro.
DR   CDD; cd07717; RNaseZ_ZiPD-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   HAMAP; MF_01818; RNase_Z_BN; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR013471; RNase_Z/BN.
DR   Pfam; PF12706; Lactamase_B_2; 2.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   TIGRFAMs; TIGR02651; RNase_Z; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Exonuclease; Hydrolase; Metal-binding; Nuclease;
KW   tRNA processing; Zinc.
FT   CHAIN           1..304
FT                   /note="Ribonuclease BN"
FT                   /id="PRO_1000070281"
FT   ACT_SITE        67
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
SQ   SEQUENCE   304 AA;  32815 MW;  28EDEBCAEEB1E0C5 CRC64;
     MELTFLGTSA GLPSTTRNVT AIVLNPQNNR SGLWLFDCGE GTQHQMLRAT ATPGKIEKIF
     ITHLHGDHIF GLPGLLCSRS MAGCETPLEI YGPKGIAEFV ETTLRLSGSW TSYPLNVHEI
     TEGQLLDDGE LTVTAYPLTH PVECYGYRIE EQDKPGALDA ARLKAAGVMP GPLFQQLKRG
     ETVTLADGRT VCGADYLSAP RPGKKIAIFG DTGPTPQAVT LARDVDVMVH ETTLEAAMAE
     KANGRGHSTT QQAAEVARDA GAKRLLMTHF SSRYSAEECQ RLLAECQAIF PASELAEDFL
     TITV
 
 
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