RNZ_THEVB
ID RNZ_THEVB Reviewed; 407 AA.
AC Q8DKE4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=tll0915;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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}.
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DR EMBL; BA000039; BAC08467.1; -; Genomic_DNA.
DR RefSeq; NP_681705.1; NC_004113.1.
DR RefSeq; WP_011056759.1; NC_004113.1.
DR AlphaFoldDB; Q8DKE4; -.
DR SMR; Q8DKE4; -.
DR STRING; 197221.22294638; -.
DR EnsemblBacteria; BAC08467; BAC08467; BAC08467.
DR KEGG; tel:tll0915; -.
DR PATRIC; fig|197221.4.peg.960; -.
DR eggNOG; COG1234; Bacteria.
DR eggNOG; COG1555; Bacteria.
DR OMA; GTQRQMM; -.
DR OrthoDB; 1712770at2; -.
DR Proteomes; UP000000440; 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 InterPro; IPR010994; RuvA_2-like.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR02651; RNase_Z; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Metal-binding; Nuclease; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..407
FT /note="Ribonuclease Z"
FT /id="PRO_0000155914"
FT REGION 1..308
FT /note="Ribonuclease Z"
FT REGION 309..407
FT /note="Unknown"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 407 AA; 45213 MW; C65FD56BA88A1601 CRC64;
MEITFLGTSS GVPTRTRNVS SVALRLPQRK EIWLFDCGEA TQHQLLRSDL RTSQIRRIFI
THMHGDHIFG LMGLLASCGL AGTVSQIDVY GPPTLDRYIA SCLRWSVMRL PYKLQVHTVE
PGEVFSDGEF TVTCRLLHHR VPAFGYRVTE GDRPGRFHVE KAQALGIPFG PLYGQLKQGK
TITLEDGRTF DGRDFCDPPQ RGRSMVYCTD TVFCDSAVEL AQQADVLIHE ATFSHQEANL
AFARLHSTST MAAQVAAFAQ VKLLFLTHFS ARYAPGNPVQ VEDLLAEAQA IFPNTRLAQD
FLHYAIPRDG QICAEMPPSD SPAAANIDTL EATLEPLEAQ TVAADAKNAP AIAINRATRQ
QMQQKLGIDA TTANAILERR RQQKFTCLGE LERLYPQVDW SALNVLF
