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RNZ_PSEPW
ID   RNZ_PSEPW               Reviewed;         321 AA.
AC   B1J6H3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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};
GN   OrderedLocusNames=PputW619_1839;
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W619;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas putida W619.";
RL   Submitted (FEB-2008) 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; CP000949; ACA72342.1; -; Genomic_DNA.
DR   RefSeq; WP_012313739.1; NC_010501.1.
DR   AlphaFoldDB; B1J6H3; -.
DR   SMR; B1J6H3; -.
DR   STRING; 390235.PputW619_1839; -.
DR   EnsemblBacteria; ACA72342; ACA72342; PputW619_1839.
DR   KEGG; ppw:PputW619_1839; -.
DR   eggNOG; COG1234; Bacteria.
DR   HOGENOM; CLU_031317_2_0_6; -.
DR   OMA; GTQRQMM; -.
DR   OrthoDB; 1712770at2; -.
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.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Metal-binding; Nuclease; tRNA processing; Zinc.
FT   CHAIN           1..321
FT                   /note="Ribonuclease Z"
FT                   /id="PRO_1000187978"
FT   ACT_SITE        66
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         62
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         64
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         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         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         139
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         209
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         209
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         268
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   321 AA;  34931 MW;  DB2F093D797DD428 CRC64;
     MDLLFLGTSA GVPTKARNVS ATAVIEASGS HWYLVDCGEG TQHQLLHTPL SVRDLRAIFI
     THVHGDHCFG LPGLLASAGM SGRTAPLDLV LPAALHDWVR LSLAASDSFL PFELRLLAVE
     QLGEWRSDTL AVSTVQLSHR VPSVAFVFTE LNPEPRLDVQ RLDAEGIPRG PLWGELAKGL
     TVEHAGRMLH GRDYLRASRP ARRVIVCGDN DNPELLAEAA KDVDVLVHEA TFTQPIIART
     GVSFGHSSAA AVARFAETAG VRNLVLTHFS ARYQPDPRRS PCIDEVREEA QVHYSGNLTL
     AQDLQRYHIG RDGCLGRVTG I
 
 
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