RNZ_CLOB8
ID RNZ_CLOB8 Reviewed; 308 AA.
AC A6LU82;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Ribonuclease Z {ECO:0000255|HAMAP-Rule:MF_01818};
DE Short=RNase Z {ECO:0000255|HAMAP-Rule:MF_01818};
DE EC=3.1.26.11 {ECO:0000255|HAMAP-Rule:MF_01818};
DE AltName: Full=tRNA 3 endonuclease {ECO:0000255|HAMAP-Rule:MF_01818};
DE AltName: Full=tRNase Z {ECO:0000255|HAMAP-Rule:MF_01818};
GN Name=rnz {ECO:0000255|HAMAP-Rule:MF_01818}; OrderedLocusNames=Cbei_1740;
OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS acetobutylicum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=290402;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA Blaschek H., Richardson P.;
RT "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'-
CC processing endonuclease activity. Probably involved in tRNA maturation,
CC by removing a 3'-trailer from precursor tRNA. {ECO:0000255|HAMAP-
CC Rule:MF_01818}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing extra 3' nucleotides
CC from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy
CC group is left at the tRNA terminus and a 5'-phosphoryl group is left
CC at the trailer molecule.; EC=3.1.26.11; Evidence={ECO:0000255|HAMAP-
CC 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. {ECO:0000255|HAMAP-
CC Rule:MF_01818}.
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DR EMBL; CP000721; ABR33912.1; -; Genomic_DNA.
DR RefSeq; WP_011969064.1; NC_009617.1.
DR AlphaFoldDB; A6LU82; -.
DR SMR; A6LU82; -.
DR STRING; 290402.Cbei_1740; -.
DR EnsemblBacteria; ABR33912; ABR33912; Cbei_1740.
DR KEGG; cbe:Cbei_1740; -.
DR eggNOG; COG1234; Bacteria.
DR HOGENOM; CLU_031317_2_1_9; -.
DR OMA; GTQRQMM; -.
DR OrthoDB; 1712770at2; -.
DR Proteomes; UP000000565; Chromosome.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR02651; RNase_Z; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Metal-binding; Nuclease; tRNA processing; Zinc.
FT CHAIN 1..308
FT /note="Ribonuclease Z"
FT /id="PRO_1000088332"
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT BINDING 61
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 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="2"
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="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT BINDING 142
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 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 308 AA; 34790 MW; 7A0D37291AB27450 CRC64;
MIDILLLGCG GGMPMPNRFL SATLINYRGR KILVDCGEGT QVSMRISNTG FKSIDIICIT
HIHGDHIVGL PGLLGTIGNS GRTEPITIIG PEGIRETVEK LRVIANWLPY EINIIENPKD
TFKLFDGNIN LDVDISVLEL DHSSPCIGYC FYFKRQPKFD VEKAEKNKVP KILWNRLQRN
EENIVLDGAL YTNDMVTGEE RKGIKVSIIT DTRPIKNIIE FINDSDYFIC EGTYGEDKDL
PKAIKNKHMT FREAADLALK GNVKKLLLTH FGTAMNEPEE YLNNANEVFD KTIIGFDRYK
TTLNFNED
