GenomeNet

Database: UniProt
Entry: A0A3D8L883_9BACT
LinkDB: A0A3D8L883_9BACT
Original site: A0A3D8L883_9BACT 
ID   A0A3D8L883_9BACT        Unreviewed;       305 AA.
AC   A0A3D8L883;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
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=DXT99_18970 {ECO:0000313|EMBL:RDV13619.1};
OS   Pontibacter diazotrophicus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=1400979 {ECO:0000313|EMBL:RDV13619.1, ECO:0000313|Proteomes:UP000256708};
RN   [1] {ECO:0000313|Proteomes:UP000256708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H4X {ECO:0000313|Proteomes:UP000256708};
RA   Liu Z.-W., Du Z.-J.;
RL   Submitted (AUG-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDV13619.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QRGR01000022; RDV13619.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8L883; -.
DR   OrthoDB; 9800940at2; -.
DR   Proteomes; UP000256708; 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   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:UP000256708};
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          34..155
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF12706"
FT   ACT_SITE        66
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|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:0000256|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:0000256|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: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         142
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   305 AA;  35166 MW;  A4584BEBBE761D9A CRC64;
     MDFELRILGS SSATPSANRH HTAQVLTIDN QYHLIDCGEG TQMQLMQYKI KHQRICNIYI
     SHLHGDHYFG LAGLLSSMHL QGRHTPLYLF GPPGLIEILS LQFKYSGTNL CYPLIFHELD
     TTSHKKIFEN KQITVHTIPM EHRVPCCGFL FREKQKARPL IKEKLPPFLT PPQLVSLKWG
     EDVTDEHGNV LVYNRDVTME PKRSRSYAYC SDSRFKPTLL PYLHYVDLLY HEATFTDELR
     ERAYYTFHST ARQAAELAAA AQVRRLLIGH FSVRYKDLTP LLTEAQEVFP QADLATEGSI
     FCIRE
//
DBGET integrated database retrieval system