RBN_SALTY
ID RBN_SALTY Reviewed; 305 AA.
AC P60195; Q8XFF2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=elaC, rnz;
GN OrderedLocusNames=STM2313;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE006468; AAL21214.1; -; Genomic_DNA.
DR RefSeq; NP_461255.1; NC_003197.2.
DR RefSeq; WP_000419093.1; NC_003197.2.
DR AlphaFoldDB; P60195; -.
DR SMR; P60195; -.
DR STRING; 99287.STM2313; -.
DR PaxDb; P60195; -.
DR EnsemblBacteria; AAL21214; AAL21214; STM2313.
DR GeneID; 1253835; -.
DR KEGG; stm:STM2313; -.
DR PATRIC; fig|99287.12.peg.2449; -.
DR HOGENOM; CLU_031317_2_0_6; -.
DR OMA; GTQRQMM; -.
DR PhylomeDB; P60195; -.
DR BioCyc; SENT99287:STM2313-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central.
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; IBA:GO_Central.
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 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_0000155891"
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; 32877 MW; ADFF10EF73051FE6 CRC64;
MELIFLGTSA GVPTRSRNVT AILLHLQHPT QPGVWLFDCG EGTQHQMLNT AFHPGKLERI
FISHLHGDHL FGLPGLLCSR SMAGNPHPLT VYGPQGVREF IATTLRLSGS WTDFPLQIEE
ISAGDILDDG LRKVTAFRLE HPLECYGYRV VEHDKPGALN ARALKAAGVT PGPLFQALKA
GKTVTLADGR QINGADYLAP AVAGKSVAIF GDTAPCEAAL ALAQGVDVMV HETTLDASME
EKANARGHSS TRQTATLARE AAVGRLIMTH ISSRYDDKGC QRLLAECRAI FPATELAYDF
SVFPV
