RNZ_THEVO
ID RNZ_THEVO Reviewed; 304 AA.
AC Q979A8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 109.
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=TV1254;
GN ORFNames=TVG1292892;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB60396.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000011; BAB60396.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_010917488.1; NC_002689.2.
DR AlphaFoldDB; Q979A8; -.
DR SMR; Q979A8; -.
DR STRING; 273116.14325492; -.
DR EnsemblBacteria; BAB60396; BAB60396; BAB60396.
DR GeneID; 1441370; -.
DR KEGG; tvo:TVG1292892; -.
DR eggNOG; arCOG00501; Archaea.
DR HOGENOM; CLU_031317_2_1_2; -.
DR OMA; GTQRQMM; -.
DR OrthoDB; 111803at2157; -.
DR PhylomeDB; Q979A8; -.
DR Proteomes; UP000001017; 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; PF12706; Lactamase_B_2; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR02651; RNase_Z; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Metal-binding; Nuclease; tRNA processing; Zinc.
FT CHAIN 1..304
FT /note="Ribonuclease Z"
FT /id="PRO_0000155940"
FT ACT_SITE 68
FT /note="Proton acceptor"
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="1"
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 69
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 141
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 267
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 304 AA; 34316 MW; A331167B7F2C44E5 CRC64;
MASNIKIVFF GTGGSWPTPI RAMPGVGIQI DDVFNLFDCG EGTQKQIMKS KWSFMSIDNI
FITHFHGDHF LGLIGLVQSM SFNNRTKDLN IFGPRGAIGI ISNAINIGYY TLRFRINVYE
LEPDKTYDLG KFLLKTTLND HPVPALSYTI EEKDIIRVDP QKAKELGIPS KIIEKIRDNG
TYEYRGRKYS IDEISGGIRK GRKIVYTGDT KPMQKMADFA KHADVLIHDT TTDSSFEPAV
NQFGHSSAKQ AARIARDAGV SRLFLYHYSP RITDVSPLVD DARAEFQESY ASEDLMEYEV
KVKH
