GenomeNet

Database: UniProt
Entry: A0A089X8W9_STRGA
LinkDB: A0A089X8W9_STRGA
Original site: A0A089X8W9_STRGA 
ID   A0A089X8W9_STRGA        Unreviewed;       301 AA.
AC   A0A089X8W9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
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   ECO:0000313|EMBL:AIR98321.1};
GN   ORFNames=SGLAU_11600 {ECO:0000313|EMBL:AIR98321.1};
OS   Streptomyces glaucescens.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1907 {ECO:0000313|EMBL:AIR98321.1, ECO:0000313|Proteomes:UP000029482};
RN   [1] {ECO:0000313|Proteomes:UP000029482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40922 / GLA O {ECO:0000313|Proteomes:UP000029482};
RX   PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA   Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA   Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT   GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT   plasmid.";
RL   J. Biotechnol. 194:81-83(2015).
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   ---------------------------------------------------------------------------
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; CP009438; AIR98321.1; -; Genomic_DNA.
DR   RefSeq; WP_043500765.1; NZ_CP009438.1.
DR   AlphaFoldDB; A0A089X8W9; -.
DR   STRING; 1907.SGLAU_11600; -.
DR   KEGG; sgu:SGLAU_11600; -.
DR   eggNOG; COG1234; Bacteria.
DR   HOGENOM; CLU_031317_2_1_11; -.
DR   OMA; GTQRQMM; -.
DR   OrthoDB; 9800940at2; -.
DR   Proteomes; UP000029482; 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; 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; PF00753; Lactamase_B; 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:UP000029482};
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          20..105
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF00753"
FT   DOMAIN          194..263
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         204
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         204
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         262
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   301 AA;  33723 MW;  FE850B9A1C38C912 CRC64;
     MSVRELVVLG TASQVPTRHR NHNGYLLRWD SEGILFDPGE GTQRQMVRAG VAAHDLNRIC
     VTHFHGDHSL GLPGVIQRIN LDQVPHPVTA HYPRSGQRFF ERLRYATAYR QTVRLAEAPV
     DADGVLARTR SYTLEAYRLS HPVESYGYRL VEPDGRRMLP ERLAAHGIEG PDVGRIQRDG
     VLGGVTLDEV SEARRGQRFA FVMDTRLCDG VYALADGCDM LVIESTFLDE DEHLAVEHGH
     LTAGQAARVA KASDVRHLVL THFSQRYSDP AEFERQARAA GFEGELTVAY DLLRVPLPKR
     R
//
DBGET integrated database retrieval system