RNJ_SINM2
ID RNJ_SINM2 Reviewed; 564 AA.
AC M4MR97;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Ribonuclease J {ECO:0000255|HAMAP-Rule:MF_01491};
DE Short=RNase J {ECO:0000255|HAMAP-Rule:MF_01491};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01491};
GN Name=rnj {ECO:0000255|HAMAP-Rule:MF_01491};
GN OrderedLocusNames=SM2011_c01929;
OS Sinorhizobium meliloti (strain Sm2011 / Rm2011 / 2011).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1286640;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sm2011 / Rm2011 / 2011;
RX PubMed=23599422; DOI=10.1093/dnares/dst014;
RA Sallet E., Roux B., Sauviac L., Jardinaud M.F., Carrere S., Faraut T.,
RA de Carvalho-Niebel F., Gouzy J., Gamas P., Capela D., Bruand C., Schiex T.;
RT "Next-generation annotation of prokaryotic genomes with EuGene-P:
RT application to Sinorhizobium meliloti 2011.";
RL DNA Res. 20:339-354(2013).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Sm2011 / Rm2011 / 2011;
RX PubMed=19540834; DOI=10.1016/j.febslet.2009.06.026;
RA Madhugiri R., Evguenieva-Hackenberg E.;
RT "RNase J is involved in the 5'-end maturation of 16S rRNA and 23S rRNA in
RT Sinorhizobium meliloti.";
RL FEBS Lett. 583:2339-2342(2009).
CC -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly endonuclease
CC activity. Plays a role in 16S and 23S rRNA processing. Might have a
CC role in mRNA maturation and/or decay. {ECO:0000269|PubMed:19540834}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01491};
CC Note=Binds up to 2 Zn(2+) ions per subunit. It is not clear if Zn(2+)
CC or Mg(2+) is physiologically important. {ECO:0000255|HAMAP-
CC Rule:MF_01491};
CC -!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome.
CC {ECO:0000255|HAMAP-Rule:MF_01491}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491}.
CC -!- DISRUPTION PHENOTYPE: Not essential. Loss of 5'-processing of pre-5.8S
CC rRNA, and the 2.6 kb rRNA which form the two 23S rRNA fragments. No
CC removal of last 3 nucleotides at the 5' end during processing of 16S
CC rRNA. {ECO:0000269|PubMed:19540834}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. Bacterial RNase J
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01491}.
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DR EMBL; CP004140; AGG73861.1; -; Genomic_DNA.
DR AlphaFoldDB; M4MR97; -.
DR SMR; M4MR97; -.
DR KEGG; smel:SM2011_c01929; -.
DR PATRIC; fig|1286640.3.peg.4421; -.
DR HOGENOM; CLU_008727_3_3_5; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10710; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR HAMAP; MF_01491; RNase_J_bact; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR InterPro; IPR042173; RNase_J_2.
DR InterPro; IPR030854; RNase_J_bac.
DR InterPro; IPR041636; RNase_J_C.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR Pfam; PF07521; RMMBL; 1.
DR Pfam; PF17770; RNase_J_C; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Exonuclease; Hydrolase; Metal-binding; Nuclease;
KW RNA-binding; rRNA processing; Zinc.
FT CHAIN 1..564
FT /note="Ribonuclease J"
FT /id="PRO_0000429572"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 375..379
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
SQ SEQUENCE 564 AA; 61377 MW; BCA3664B8E03E3E0 CRC64;
MKKAKAHHDM AQDEELVFLP LGGVGEIGMN LGLYGYGRPG HRQWIMVDCG VTFPGPELPG
VDLVLPDIAF LAEQRRNLKA IIITHAHEDH YGALNDLWPG LNVPVYASPF TAGMLEAKRA
FEKSRSEIPI TIFKQGDRIN VGPFSVEAVG VNHSIPEPMA LVIRTQLGTV VHTGDWKIDL
EPSLGPLTDE SRFRQIGEEG VLALVCDSTN ALREGVSPSE RQVSESLAKI IADAEGRVGI
TTFSSNVGRI RSVAEAAEAA GREVLLLGSS MKRVVDVARD VGLMEGVKPF LAEDEFGYIP
RDKVVVILTG SQGEPRAALA KIARDEMRNV AFSAGDTIVF SSRTIPGNEK AINDIKNGLI
EQGIHIITDS EALVHVSGHP RRTELQQMYQ WVKPQILVPV HGEAAHLTAH AELGLQSGIP
SVPRLRNGEM LRLAPGPAEV IDEAPHGRIY KDGTLIGDFE EMGIGERRKL SFAGHVSVSV
VLDSRYDFLG DPDVVPIGLP EFDDEGEAME DTLYDAVLGA VESIPRAKRK DLAMLQEAVR
RAVRSTTNQV WGKKPVVTVF ITKV
