ID A0A1Q2D4W1_9ENTE Unreviewed; 312 AA.
AC A0A1Q2D4W1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ribonuclease Z {ECO:0000256|HAMAP-Rule:MF_01818};
DE Short=RNase Z {ECO:0000256|HAMAP-Rule:MF_01818};
DE EC=3.1.26.11 {ECO:0000256|HAMAP-Rule:MF_01818};
DE AltName: Full=tRNA 3 endonuclease {ECO:0000256|HAMAP-Rule:MF_01818};
DE AltName: Full=tRNase Z {ECO:0000256|HAMAP-Rule:MF_01818};
GN Name=rnz {ECO:0000256|HAMAP-Rule:MF_01818};
GN ORFNames=BW732_03800 {ECO:0000313|EMBL:AQP53446.1}, CBF34_08065
GN {ECO:0000313|EMBL:RSU00836.1};
OS Vagococcus penaei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=633807 {ECO:0000313|EMBL:AQP53446.1, ECO:0000313|Proteomes:UP000188246};
RN [1] {ECO:0000313|EMBL:AQP53446.1, ECO:0000313|Proteomes:UP000188246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD276 {ECO:0000313|EMBL:AQP53446.1,
RC ECO:0000313|Proteomes:UP000188246};
RX PubMed=19897618; DOI=10.1099/ijs.0.012872-0;
RA Jaffres E., Prevost H., Rossero A., Joffraud J.J., Dousset X.;
RT "Vagococcus penaei sp. nov., isolated from spoilage microbiota of cooked
RT shrimp (Penaeus vannamei).";
RL Int. J. Syst. Evol. Microbiol. 60:2159-2164(2010).
RN [2] {ECO:0000313|EMBL:AQP53446.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CD276 {ECO:0000313|EMBL:AQP53446.1};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RSU00836.1, ECO:0000313|Proteomes:UP000286995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24833 {ECO:0000313|EMBL:RSU00836.1,
RC ECO:0000313|Proteomes:UP000286995};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-2017) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_01818};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01818};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000256|HAMAP-Rule:MF_01818};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01818}.
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000256|HAMAP-
CC Rule:MF_01818}.
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DR EMBL; CP019609; AQP53446.1; -; Genomic_DNA.
DR EMBL; NGJV01000015; RSU00836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2D4W1; -.
DR STRING; 633807.BW732_03800; -.
DR KEGG; vpi:BW732_03800; -.
DR OrthoDB; 9800940at2; -.
DR Proteomes; UP000188246; Chromosome.
DR Proteomes; UP000286995; Unassembled WGS sequence.
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; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 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 NCBIfam; TIGR02651; RNase_Z; 1.
DR PANTHER; PTHR46018; ZINC PHOSPHODIESTERASE ELAC PROTEIN 1; 1.
DR PANTHER; PTHR46018:SF2; ZINC PHOSPHODIESTERASE ELAC PROTEIN 1; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_01818};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01818};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01818};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01818};
KW Reference proteome {ECO:0000313|Proteomes:UP000188246};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01818};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01818}.
FT DOMAIN 35..152
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01818"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
SQ SEQUENCE 312 AA; 35114 MW; 8DD25607550975D8 CRC64;
MELEFLGTGA GVPSKQRNVT SIALKMLDER NEVWLFDCGE GTQQQILNTA IRPRKIEKIF
ITHLHGDHIF GLPGLISSRS FQGGDTPLEI YGPKGIKQYV LTSLKLSDTH LKYPIKFIEI
ETTGVIFTDK KIKVTCEELD HRIKCFGYRI EEADFQGELQ VEKLKALNIP SGPIYKRIKD
GEIVTLADGR IIDGRDFIGE AKKGRTVTIL GDTRLTKNCY KLAQNADVLV HESTFNQNEA
KLAKSYYHST TAQAAQVAKE SGVQMLLLTH ISSRYLGKAV YELQQEAQQI FKQTKVVKDF
DIITIPIPTN KK
//
