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RNZ_MYCLE
ID   RNZ_MYCLE               Reviewed;         220 AA.
AC   Q49744; O33130;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Putative ribonuclease Z;
DE            Short=RNase Z;
DE            Short=tRNase Z;
DE            EC=3.1.26.11;
DE   AltName: Full=tRNA 3 endonuclease;
GN   Name=rnz; OrderedLocusNames=ML0608; ORFNames=B1937_C1_163, MLCL536.01;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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 2 Zn(2+) ions. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. This sequence is much
CC       shorter in its N-terminus than orthologs. {ECO:0000305}.
CC   -!- CAUTION: Lacks two conserved zinc binding sites. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17148.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U00016; AAA17148.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z99125; CAB16144.1; -; Genomic_DNA.
DR   EMBL; AL583919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; T10042; T10042.
DR   AlphaFoldDB; Q49744; -.
DR   SMR; Q49744; -.
DR   Leproma; ML0608; -.
DR   Proteomes; UP000000806; 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   Gene3D; 3.60.15.10; -; 1.
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   5: Uncertain;
KW   Endonuclease; Hydrolase; Metal-binding; Nuclease; Reference proteome;
KW   tRNA processing; Zinc.
FT   CHAIN           1..220
FT                   /note="Putative ribonuclease Z"
FT                   /id="PRO_0000155877"
FT   REGION          193..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        42
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   220 AA;  23634 MW;  C3F0F9B5B2F3F92A CRC64;
     MQAGRQLFLV DCWLGVLQRA SAGPTHTPAV CQRCCSTHLH GDRISDLGDL LITHWVTTFA
     LDPPPLPIIG SPDTAETVEA KLKASGHDIE YQITHHTYLN TPPLIEVYEY TKGFVGAPPD
     GVSIRGSTNH GPVTPTIGFR IESGPTSVVL TGGTVPCASL DELAAEADAL VHTIIRKNIV
     IRVHQQADQG HLQPPLVNRA SDSNRGARGH RHPGHNVLCP
 
 
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