Entry: Q9CBW5 Genes: rnj ML1512 Length: 558 aa

Ribonuclease J (RNase J)

Q9CBW5_MYCLE • Mycobacterium leprae (strain TN)
Navigate Overview Model Scores RCSB 1D Mol* Pockets B-Cell Epitopes Function and interactions Ontology and localisation Sequence features and PTMs Evidence and cross-references

Summary

Download FASTA UniProt: Q9CBW5 ML Locus: ML1512
Entry Q9CBW5
Reviewed unreviewed
Entry Name Q9CBW5_MYCLE
Gene Names rnj ML1512
ML locus tag ML1512
Organism Mycobacterium leprae (strain TN)
Length 558 aa
Mass 59347 Da
Annotation 3.0
Annotation Summary

Evidence and cross-references

PubMed ID 11234002
DOI ID 10.1038/35059006
STRING 272631.gene:17575353;
KEGG mle:ML1512;
eggNOG COG0595;
OrthoDB 9770211at2;
InterPro IPR001279;IPR036866;IPR011108;IPR004613;IPR042173;IPR055132;IPR030854;IPR041636;

Oligomer Models

Best Boltz2 oligomer and local AlphaFold‑3 homooligomer structure models matched to ML1512, with the same model switching, Mol*, Nightingale, pLDDT, PAE, and download functionality as monomers.
Count: 2
Assembly Method Template / Source Overall Rank Download
Homo 2-mer Boltz2 7WNU 0.895205 Download Model
homo 2-mer AlphaFold‑3 — — Download Model

Ligands

Curated ligands imported from the selected oligomer template/YAML rows. The displayed ligand code is the original template CCD code; predicted-model placeholders such as LIG1/LIG2 are not shown. Click a ligand code to focus the ligand in Mol*.
Ligands: 0
Ligand Code Ligand Name PubChem ID
No curated ligand rows were found for this oligomer in the database.

Monomer Models

Monomer structure models for ML1512, retaining all existing model selection, Mol*, Nightingale, pLDDT, PAE, and download functionality.
Count: 4
Assembly Method Model Overall Rank Download
Monomer Boltz2 0 0.857630 Download Model
Monomer AlphaFold‑3 3 0.930151 Download Model
Monomer Boltz 0 0.862437 Download Model
Monomer CHAI 1 0.183990 Download Model

Sequence & Feature Viewer

Residue-level feature tracks for the loaded model — pLDDT confidence colouring, mapped annotations, and interactive PAE selection ranges. Drag a region on the heatmap to highlight it here and in Mol*.
RCSB 1D
Sequence viewer will initialise once a structure model is loaded.
Mol* — ML1512

Mol* Structure Viewer

Local mmCIF model display for ML1512 with Mol* controls hidden.
Default: Homo 2-mer • Boltz2
Preparing Homo 2-mer • Boltz2 model 0 for ML1512…
Residue focus: none
Heterooligomer ML IDs / chain selection

PAE Map Panel

Predicted aligned error heatmap for the currently loaded model, when pairwise confidence data are available in the local mmCIF.
PAE • Waiting for Model
PAE Heatmap
Loading pairwise confidence data for the selected model…
Scored residue
Aligned residue
Hover over the heatmap to inspect residue-pair PAE values.
Click a cell or drag across the heatmap to select residue blocks and mirror them in the sequence viewer.

B-cell Epitope Propensity

Per-residue conformational B-cell epitope predictions from DiscoTope-3.0.
Epitope · Loading
Low
Epitope
Residue number Residue type DiscoTope-3.0 score Focus
Loading epitope predictions…
Click a residue to focus it in Mol*.
Annotation Summary

Function and interactions

EC number 3.1.-.-
Binding site BINDING 56; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000256|PIRSR:PIRSR004803-3"; BINDING 58; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000256|PIRSR:PIRSR004803-3"; BINDING 81; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR004803-3"; BINDING 83; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR004803-3"; BINDING 85; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR004803-3"; BINDING 86; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR004803-3"; BINDING 148; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR004803-3"; BINDING 170; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR004803-3"; BINDING 239..241; /ligand="substrate"; /evidence="ECO:0000256|PIRSR:PIRSR004803-2"; BINDING 371..375; /ligand="substrate"; /evidence="ECO:0000256|HAMAP-Rule:MF_01491, ECO:0000256|PIRSR:PIRSR004803-2"; BINDING 397; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR004803-3"; BINDING 450; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /evidence="ECO:0000256|PIRSR:PIRSR004803-3"
Cofactor COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PIRSR:PIRSR004803-3}; Note=Binds 1 Ca(2+) cation per subunit. Seen in 1 crystal structure, it is not clear if it is physiologically important. {ECO:0000256|PIRSR:PIRSR004803-3}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRSR:PIRSR004803-3}; Note=Binds 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or Mg(2+) is physiologically important. {ECO:0000256|PIRSR:PIRSR004803-3};
Active site ACT_SITE 202; /note="Proton donor"; /evidence="ECO:0000256|PIRSR:PIRSR004803-1"; ACT_SITE 375; /note="Proton acceptor"; /evidence="ECO:0000256|PIRSR:PIRSR004803-1"
Subunit structure SUBUNIT: Homodimer, may be a subunit of the RNA degradosome. {ECO:0000256|HAMAP-Rule:MF_01491}.
Annotation Summary

Ontology and localisation

Gene Ontology (biological process) rRNA processing [GO:0006364]
Gene Ontology (cellular component) cytoplasm [GO:0005737]
Gene Ontology (GO) cytoplasm [GO:0005737]; 5'-3' RNA exonuclease activity [GO:0004534]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521]; zinc ion binding [GO:0008270]; rRNA processing [GO:0006364]
Gene Ontology (molecular function) 5'-3' RNA exonuclease activity [GO:0004534]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521]; zinc ion binding [GO:0008270]
Gene Ontology IDs GO:0003723; GO:0004521; GO:0004534; GO:0005737; GO:0006364; GO:0008270
Subcellular location [CC] SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01491}.
Protein families Metallo-beta-lactamase superfamily, RNA-metabolizing metallo-beta-lactamase-like family, Bacterial RNase J subfamily
Sequence similarities SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. Bacterial RNase J subfamily. {ECO:0000256|HAMAP-Rule:MF_01491}.
Annotation Summary

Sequence features and PTMs

Domain [FT] DOMAIN 28..222; /note="Metallo-beta-lactamase"; /evidence="ECO:0000259|SMART:SM00849"