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RBN_CITK8
ID   RBN_CITK8               Reviewed;         305 AA.
AC   A8ADW5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=CKO_00522;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000822; ABV11678.1; -; Genomic_DNA.
DR   RefSeq; WP_012131503.1; NC_009792.1.
DR   AlphaFoldDB; A8ADW5; -.
DR   SMR; A8ADW5; -.
DR   STRING; 290338.CKO_00522; -.
DR   EnsemblBacteria; ABV11678; ABV11678; CKO_00522.
DR   GeneID; 45134764; -.
DR   KEGG; cko:CKO_00522; -.
DR   HOGENOM; CLU_031317_2_0_6; -.
DR   OMA; GTQRQMM; -.
DR   OrthoDB; 1712770at2; -.
DR   Proteomes; UP000008148; 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; IPR013469; Rnase_BN.
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.
DR   TIGRFAMs; TIGR02649; true_RNase_BN; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Exonuclease; Hydrolase; Metal-binding; Nuclease;
KW   Reference proteome; tRNA processing; Zinc.
FT   CHAIN           1..305
FT                   /note="Ribonuclease BN"
FT                   /id="PRO_1000070269"
FT   ACT_SITE        68
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         64
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         66
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         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         69
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         141
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         212
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         212
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         270
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   305 AA;  32698 MW;  CA7972033AC264A5 CRC64;
     MELIFLGTSA GVPTRTRNVT AILLNLQHPT QAGLWLFDCG EGTQHQMLNT AFNPGKLDRI
     FISHLHGDHL FGLPGLLCSR SMAGNAQPLT IYGPKGIREF TETALRLSGS WTDYPLEIVE
     ITAGEILNDG LRKVTAFALE HPLECYGYRI EEHDKPGALD ASALKAAGVK PGPLFQDLKA
     GKTVTLNDGR VINGADFLAP ATPGKSVAIF GDTAPCASAI TLAKGVDVMV HEATLDTSME
     EKANSRGHSS TRQAAQLAHN AEVGQLIITH VSSRYDDRGC QRLLAECQAI FPATALAHDF
     AVFTV
 
 
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