ID A0A1M5BGC2_9BACT Unreviewed; 410 AA.
AC A0A1M5BGC2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN05443144_108111 {ECO:0000313|EMBL:SHF41357.1};
OS Fodinibius roseus.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Fodinibius.
OX NCBI_TaxID=1194090 {ECO:0000313|EMBL:SHF41357.1, ECO:0000313|Proteomes:UP000184041};
RN [1] {ECO:0000313|EMBL:SHF41357.1, ECO:0000313|Proteomes:UP000184041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21986 {ECO:0000313|EMBL:SHF41357.1,
RC ECO:0000313|Proteomes:UP000184041};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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|ARBA:ARBA00001947};
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01818}.
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DR EMBL; FQUS01000008; SHF41357.1; -; Genomic_DNA.
DR RefSeq; WP_073062720.1; NZ_FQUS01000008.1.
DR AlphaFoldDB; A0A1M5BGC2; -.
DR STRING; 1194090.SAMN05443144_108111; -.
DR OrthoDB; 9800940at2; -.
DR Proteomes; UP000184041; Unassembled WGS sequence.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01818};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01818}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 20..80
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF00753"
FT DOMAIN 202..271
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT REGION 322..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..373
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
SQ SEQUENCE 410 AA; 46789 MW; 9C87B3B7FDA24DDD CRC64;
MIIVPLGVAS ATPTATRHLS SIAVWREGSV FLFDCGENAQ MRMLQGGLKR SQIDYIFISH
FDTDHYSGLI GLLSTLQLQR RDRPITLVGP TGIKDFVEWN FEFSNINLNY EIEYVEVEED
FEEERVVDTD DYYVEARPLN HTKFCIGYRL QEKDLPGKVD AEKAQKQGIS EDWQYKDLKA
GIDVELEDGT VVKSADIVGH PRPGDSFAYI TDTKYCPNSV RLAKNTNVLI HEATFSDSLS
DKAEETGHST AKDAARVANE AKTKLLVITH FSARYTNEYV LLREARDDFF PTWVATELRP
IFTDPAHEKG IIKPKVYIKE INRDNNNSNK NKGSKRKKRS SGKKKRRMRK RKNSPGKKRR
SRKSSKKRSG KSRSSNNKNN GGNGGNKNNN NERKPKQITP RTPFDDFDRF
//
