ID D4MYR1_ANAHA Unreviewed; 304 AA.
AC D4MYR1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
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:CUM74882.1};
GN ORFNames=CL2_07160 {ECO:0000313|EMBL:CBL37756.1}, DO83_09510
GN {ECO:0000313|EMBL:AQP39808.1}, ERS852425_00397
GN {ECO:0000313|EMBL:CUM74882.1}, ERS852475_02167
GN {ECO:0000313|EMBL:CUO47745.1}, ERS852520_03199
GN {ECO:0000313|EMBL:CUQ14809.1}, ERS852571_01795
GN {ECO:0000313|EMBL:CUM98480.1};
OS Anaerostipes hadrus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL37756.1, ECO:0000313|Proteomes:UP000008960};
RN [1] {ECO:0000313|EMBL:CBL37756.1, ECO:0000313|Proteomes:UP000008960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL37756.1,
RC ECO:0000313|Proteomes:UP000008960};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SSC/2.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL37756.1, ECO:0000313|Proteomes:UP000008960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL37756.1,
RC ECO:0000313|Proteomes:UP000008960};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000095553, ECO:0000313|Proteomes:UP000095564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608868 {ECO:0000313|EMBL:CUM74882.1,
RC ECO:0000313|Proteomes:UP000095598}, 2789STDY5834860
RC {ECO:0000313|EMBL:CUO47745.1, ECO:0000313|Proteomes:UP000095611},
RC 2789STDY5834908 {ECO:0000313|EMBL:CUQ14809.1,
RC ECO:0000313|Proteomes:UP000095564}, and 2789STDY5834959
RC {ECO:0000313|EMBL:CUM98480.1, ECO:0000313|Proteomes:UP000095553};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AQP39808.1, ECO:0000313|Proteomes:UP000188159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPB5 {ECO:0000313|EMBL:AQP39808.1,
RC ECO:0000313|Proteomes:UP000188159};
RX PubMed=27264309; DOI=10.1038/srep27572;
RA Zhang Q., Wu Y., Wang J., Wu G., Long W., Xue Z., Wang L., Zhang X.,
RA Pang X., Zhao Y., Zhao L., Zhang C.;
RT "Accelerated dysbiosis of gut microbiota during aggravation of DSS-induced
RT colitis by a butyrate-producing bacterium.";
RL Sci. Rep. 6:27572-27572(2016).
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; CP012098; AQP39808.1; -; Genomic_DNA.
DR EMBL; FP929061; CBL37756.1; -; Genomic_DNA.
DR EMBL; CYXT01000001; CUM74882.1; -; Genomic_DNA.
DR EMBL; CYXY01000010; CUM98480.1; -; Genomic_DNA.
DR EMBL; CYZM01000007; CUO47745.1; -; Genomic_DNA.
DR EMBL; CZAU01000045; CUQ14809.1; -; Genomic_DNA.
DR RefSeq; WP_008391736.1; NZ_WQRA01000041.1.
DR AlphaFoldDB; D4MYR1; -.
DR STRING; 649756.ERS852387_01569; -.
DR GeneID; 15230847; -.
DR KEGG; bprl:CL2_07160; -.
DR PATRIC; fig|245018.3.peg.909; -.
DR OrthoDB; 9800940at2; -.
DR Proteomes; UP000008960; Chromosome.
DR Proteomes; UP000095553; Unassembled WGS sequence.
DR Proteomes; UP000095564; Unassembled WGS sequence.
DR Proteomes; UP000095598; Unassembled WGS sequence.
DR Proteomes; UP000095611; Unassembled WGS sequence.
DR Proteomes; UP000188159; 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 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 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 28..128
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF00753"
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01818"
FT BINDING 61
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 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="2"
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 138
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 207
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 207
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 266
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 304 AA; 34304 MW; 2F4E056D5571FC06 CRC64;
MLDVCLLGTG GMMPLPYRKL TACMTRFNGH SLLIDCGEGT QVGIKERGWS VKPLDAICFT
HFHADHISGL PGLLLTLGNA ERTEPLLIIG PKGVERVVNS LRVIAPELPF PIEFYELNEK
EHVIEMDGYK IEAFYVKHNV PCYGYNMIIP RAGKFDPVKA KENDIPMKYW NRLQKGETVT
SEDGRVLTSD MILGSPRPGI KLTYCTDTRP VQTISEHAKN ADLFICEGMY GEEGKEKKAR
EYKHMTFYEA AHLAKEADVK QMWLTHYSPS LVRAEEFMGK VKSIFPRAKA GKDGKTITLD
FQEE
//
