RBN_ECOSE
ID RBN_ECOSE Reviewed; 305 AA.
AC B6I7L2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=ECSE_2528;
OS Escherichia coli (strain SE11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=409438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SE11;
RX PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT "Complete genome sequence and comparative analysis of the wild-type
RT commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL DNA Res. 15:375-386(2008).
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; AP009240; BAG78052.1; -; Genomic_DNA.
DR RefSeq; WP_001300687.1; NC_011415.1.
DR AlphaFoldDB; B6I7L2; -.
DR SMR; B6I7L2; -.
DR EnsemblBacteria; BAG78052; BAG78052; ECSE_2528.
DR GeneID; 66673845; -.
DR KEGG; ecy:ECSE_2528; -.
DR HOGENOM; CLU_031317_2_0_6; -.
DR OMA; GTQRQMM; -.
DR Proteomes; UP000008199; 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 tRNA processing; Zinc.
FT CHAIN 1..305
FT /note="Ribonuclease BN"
FT /id="PRO_1000187959"
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; 32930 MW; 69A55EAE8BDDEF68 CRC64;
MELIFLGTSA GVPTRTRNVT AILLNLQHPT QSGLWLFDCG EGTQHQLLHT AFNPGKLDKI
FISHLHGDHL FGLPGLLCSR SMSGIIQPLT IYGPQGIREF VETALRISGS WTDYPLEIVE
IGAGEILDDG LRKVTAYPLE HPLECYGYRI EEHDKPGALN AQALKAAGVP PGPLFQELKA
GKTITLEDGR QINGADYLAA PVPGKALAIF GDTGPCDAAL DLAKGVDVMV HEATLDITME
AKANSRGHSS TRQAATLARE AGVGKLIITH VSSRYDDKGC QHLLRECRSI FPATELANDF
TVFNV
