RNZ_HALVD
ID RNZ_HALVD Reviewed; 315 AA.
AC D4GZ88;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=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=HVO_0144;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=DS2 / DS70;
RX PubMed=18437358; DOI=10.1007/s00203-008-0368-4;
RA Spath B., Schubert S., Lieberoth A., Settele F., Schutz S., Fischer S.,
RA Marchfelder A.;
RT "Two archaeal tRNase Z enzymes: similar but different.";
RL Arch. Microbiol. 190:301-308(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=DS2 / DS70;
RX PubMed=18369184; DOI=10.1261/rna.933208;
RA Holzle A., Fischer S., Heyer R., Schutz S., Zacharias M., Walther P.,
RA Allers T., Marchfelder A.;
RT "Maturation of the 5S rRNA 5' end is catalyzed in vitro by the endonuclease
RT tRNase Z in the archaeon H. volcanii.";
RL RNA 14:928-937(2008).
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. Can also catalyze the 5'
CC end cleavage of the 5S rRNA. {ECO:0000269|PubMed:18369184,
CC ECO:0000269|PubMed:18437358}.
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 Evidence={ECO:0000269|PubMed:18369184, ECO:0000269|PubMed:18437358};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by high salt concentrations.
CC {ECO:0000269|PubMed:18369184, ECO:0000269|PubMed:18437358}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:18437358};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:18437358};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18437358}.
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
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DR EMBL; CP001956; ADE02929.1; -; Genomic_DNA.
DR AlphaFoldDB; D4GZ88; -.
DR SMR; D4GZ88; -.
DR STRING; 309800.C498_18963; -.
DR EnsemblBacteria; ADE02929; ADE02929; HVO_0144.
DR KEGG; hvo:HVO_0144; -.
DR eggNOG; arCOG00501; Archaea.
DR HOGENOM; CLU_031317_2_1_2; -.
DR OMA; GTQRQMM; -.
DR Proteomes; UP000008243; 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 SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR02651; RNase_Z; 1.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Metal-binding; Nuclease; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..315
FT /note="Ribonuclease Z"
FT /id="PRO_0000411053"
FT ACT_SITE 63
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 315 AA; 34088 MW; 688AE3967CC52D60 CRC64;
MRATFLGTGG AVPTTARAPS AFLVNRDGER LLFDCGEGTQ RQMMRYGTGF GVSHLFVTHL
HGDHILGIPG LIQTLDFNDR DDSLAIHGPP GSKGHLEQLV HAGGYQPGFH VSVHEVRPGN
VAYRADDYEV RAFDTEHRTA SVGYALVEDD RPGRFDREKA EELGVPVGPA FGRLHAGEDV
ELEDGTVVRS EQVVGDPRPG RTVVYTGDTR PLNSTVEVAC DADLLVHDAT FTDEEAERAK
QTAHSTAREA ARVARDADVR RFALTHISAR YAADPSPLLE QAREVYDGEA FVAEDGQKLE
VPYADSDGGG AETGE
