RNZ_LIGS1
ID RNZ_LIGS1 Reviewed; 317 AA.
AC Q1WT50;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=LSL_1093;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000233; ABD99901.1; -; Genomic_DNA.
DR RefSeq; WP_011476161.1; NC_007929.1.
DR RefSeq; YP_535984.1; NC_007929.1.
DR AlphaFoldDB; Q1WT50; -.
DR SMR; Q1WT50; -.
DR STRING; 362948.LSL_1093; -.
DR EnsemblBacteria; ABD99901; ABD99901; LSL_1093.
DR KEGG; lsl:LSL_1093; -.
DR PATRIC; fig|362948.14.peg.1165; -.
DR HOGENOM; CLU_031317_2_0_9; -.
DR OMA; GTQRQMM; -.
DR Proteomes; UP000006559; 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 SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR02651; RNase_Z; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Metal-binding; Nuclease; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..317
FT /note="Ribonuclease Z"
FT /id="PRO_1000070292"
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 143
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 214
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 214
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 272
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 317 AA; 35603 MW; 7948FA28E596435D CRC64;
MELEFLGTGA GSPSKSRNVS AVALKLLDEI KKIWLFDVGE GTQHQILNTT IRPRKIDKIF
ITHMHGDHIF GLPGFLSSRS FQGGEKMGPL TIYGPKGISD FVNISLKVSQ TKLSYELNFV
ELEEEGLLLE NDRFKVYAYK LDHRIECWGY RIEEKDYPGE LQVEKLREAK APSGPIYGRL
KAGEVVTLED GRTIDGKDFI GKAKKGRIVT ILGDTRQTPN LKLLAKDADV LVHESTFGKG
EGKLARNYHH STCVQAATLA KEVGVKQLLL THISARYVGK MVKVLEKEAK KVFPNTKVVK
DFDTFNIPFP ERKDDEQ
