ID A0A1I0SI03_9SPHI Unreviewed; 301 AA.
AC A0A1I0SI03;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-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=SAMN04488511_101356 {ECO:0000313|EMBL:SFA39063.1};
OS Pedobacter suwonensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=332999 {ECO:0000313|EMBL:SFA39063.1, ECO:0000313|Proteomes:UP000198836};
RN [1] {ECO:0000313|Proteomes:UP000198836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18130 {ECO:0000313|Proteomes:UP000198836};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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|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; FOJM01000001; SFA39063.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0SI03; -.
DR STRING; 332999.SAMN04488511_101356; -.
DR OrthoDB; 9800940at2; -.
DR Proteomes; UP000198836; 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 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 33..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 210
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 210
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 268
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; 34475 MW; CE13612216065529 CRC64;
MKFEVTILGS SSATPVFNRN PSAQLLNCNE KYYLIDCGEG TQQQLAKYNL KAARIDYIFI
SHLHGDHYFG LIGLLSSLHL NGRIKPIKIF GPKPLLEILE IQFKYSDTVL RYPIEFFPIE
ADQSIQIFEN SDLTVKTIVL NHRIPTTGFI FQQKKRQRKL IKEKSDQVPM AYYTALKKGM
DVELPNGDIL RSEDYTTEAD APRCYAYCSD TLFDESYFAT IKDCDTLYHE ATFMHDLLER
AKETHHTTAL QAGEVAKITG AKKLLIGHFS SRYKTLQMLF EEAQSVFENT ELAVEGRTFQ
L
//