RNZ_MYCBP
ID RNZ_MYCBP Reviewed; 280 AA.
AC A1KL99;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=BCG_2423;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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; AM408590; CAL72411.1; -; Genomic_DNA.
DR RefSeq; WP_011799262.1; NC_008769.1.
DR AlphaFoldDB; A1KL99; -.
DR SMR; A1KL99; -.
DR KEGG; mbb:BCG_2423; -.
DR HOGENOM; CLU_031317_0_0_11; -.
DR OMA; DHNADYG; -.
DR Proteomes; UP000001472; Chromosome.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01818; RNase_Z_BN; 1.
DR InterPro; IPR044094; AtsA-like_MBL-fold.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR013471; RNase_Z/BN.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Metal-binding; Nuclease; tRNA processing; Zinc.
FT CHAIN 1..280
FT /note="Ribonuclease Z"
FT /id="PRO_1000070302"
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 153
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 176
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 176
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 240
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 280 AA; 29500 MW; FEBF540F94E78E08 CRC64;
MLEITLLGTG SPIPDPDRAG PSTLVRAGAQ AFLVDCGRGV LQRAAAVGVG AAGLSAVLLT
HLHSDHIAEL GDVLITSWVT NFAADPAPLP IIGPPGTAEV VEATLKAFGH DIGYRIAHHA
DLTTPPPIEV HEYTAGPAWD RDGVTIRVAP TDHRPVTPTI GFRIESDGAS VVLAGDTVPC
DSLDQLAAGA DALVHTVIRK DIVTQIPQQR VKDICDYHSS VREAAATANR AGVGTLVMTH
YVPAIGPGQE EQWRALAATE FSGRIEVGND LHRVEVHPRR
