ID   RNZ_MYCTO               Reviewed;         224 AA.
AC   P9WGZ4; L0TB48; P71736; Q8VJJ4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Putative ribonuclease Z;
DE            Short=RNase Z;
DE            EC=3.1.26.11;
DE   AltName: Full=tRNA 3 endonuclease;
DE   AltName: Full=tRNase Z;
GN   Name=rnz; OrderedLocusNames=MT2479;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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 (By similarity).
CC       {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
CC   -!- CAUTION: The N-terminus is shorter than in related proteins.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK46775.1; Type=Miscellaneous discrepancy; Note=Sequence is shorter in its N-terminus and cannot be extended.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46775.1; ALT_SEQ; Genomic_DNA.
DR   PIR; B70684; B70684.
DR   AlphaFoldDB; P9WGZ4; -.
DR   SMR; P9WGZ4; -.
DR   EnsemblBacteria; AAK46775; AAK46775; MT2479.
DR   KEGG; mtc:MT2479; -.
DR   PATRIC; fig|83331.31.peg.2670; -.
DR   HOGENOM; CLU_031317_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd07719; arylsulfatase_AtsA-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR044094; AtsA-like_MBL-fold.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   Pfam; PF12706; Lactamase_B_2; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Metal-binding; Nuclease; tRNA processing; Zinc.
FT   CHAIN           1..224
FT                   /note="Putative ribonuclease Z"
FT                   /id="PRO_0000428276"
FT   BINDING         120
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   224 AA;  24076 MW;  5800FCB544A31175 CRC64;
     MLLTHLHSDH IAELGDVLIT SWVTNFAADP APLPIIGPPG TAEVVEATLK AFGHDIGYRI
     AHHADLTTPP PIEVHEYTAG PAWDRDGVTI RVAPTDHRPV TPTIGFRIES DGASVVLAGD
     TVPCDSLDQL AAGADALVHT VIRKDIVTQI PQQRVKDICD YHSSVQEAAA TANRAGVGTL
     VMTHYVPAIG PGQEEQWRAL AATEFSGRIE VGNDLHRVEV HPRR