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Entry version 121 (10 Apr 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Ribonuclease J1

Gene

rnjA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

An RNase that has endonuclease and 5'-3' exonuclease activity, playing a role in both rRNA and mRNA stability and degradation. Endonuclease activity can cleave within 4 nucleotides of the 5'-end of a triphosphorylated RNA. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2 complex is highly processive on substrates longer than 5 nucleotides, on shorter substrates is distributive. Preferentially cleaves ssRNA, possibly in AU-rich regions. The 5'-exonuclease activity acts on 5'-hydroxyl and 5'-monophosphate but not 5'-triphosphate ends; it can digest through stem-loop structures if they are not too stable. Required for maturation of 16S rRNA. Acts preferentially on 16S rRNA precursors after association of the 30S and 50S ribosomal subunits. Plays a role in the secondary pathway of 23S rRNA 5' end maturation. Probably also participates in processing of pre-scRNA (the precursor of the signal recognition particle RNA).13 Publications

Miscellaneous

Present in about 2500 monomers per cell in mid-log phase.

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

30S ribosomal subunit binding to Shine-Dalgarno sequences blocks exonuclease activity.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.58 sec (-1) for J1, 0.13 sec (-1) for J1/J2 and <0.005 sec (-1) for J2.
  1. KM=0.47 µM for exonuclease on 30 nt RNA hybridized to 17 nt quenching DNA, J1 alone1 Publication
  2. KM=0.22 µM for exonuclease on 30 nt RNA hybridized to 17 nt quenching DNA, J1/J2 complex1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi49Calcium; via carbonyl oxygen1
    Metal bindingi51Calcium1
    Metal bindingi74Zinc 1; via pros nitrogen; catalytic1
    Metal bindingi76Zinc 1; via pros nitrogen; catalytic1
    Metal bindingi78Zinc 2; catalytic1
    Metal bindingi79Zinc 2; via tele nitrogen; catalytic1
    Metal bindingi142Zinc 1; via tele nitrogen; catalytic1
    Metal bindingi164Zinc 1; catalytic1
    Metal bindingi164Zinc 2; catalytic1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei195Proton donor1 Publication1
    Active sitei368Proton acceptor1 Publication1
    Metal bindingi390Zinc 2; via tele nitrogen; catalytic1
    Metal bindingi443Calcium1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionEndonuclease, Exonuclease, Hydrolase, Nuclease, RNA-binding
    Biological processmRNA processing, rRNA processing
    LigandCalcium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    BSUB:BSU14530-MONOMER

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Ribonuclease J1UniRule annotation (EC:3.1.-.-UniRule annotation)
    Short name:
    RNase J1UniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:rnjAUniRule annotation
    Synonyms:ykqC
    Ordered Locus Names:BSU14530
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBacillus subtilis (strain 168)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri224308 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000001570 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Essential. In depletion experiments there is decreased 5'-exonuclease processing of 16S rRNA (PubMed:17512403), decreased accumulation of correctly-sized scRNA (PubMed:17576666), decreased decay of trp mRNA leader (PubMed:18445592), while correct processing of the 5' end of 23S rRNA no longer occurs in the absence of mrnC (PubMed:19880604). While depletion/deletion of RNase J1 or J2 has no large impact on global gene expression, a double mutant alters the expression of hundreds of genes (PubMed:18713320). In a more severe depletion experiment alteration of about 30% of transcripts was seen (PubMed:22412379). Later shown not to be essential in 4 strains, with a tripled doubling time. 168 trpC2 cells able to grow on minimal medium. Loss of competence for plasmid transformation, nearly complete loss of sporulation, poor growth at 30 degrees Celsius and no growth under 25 degrees Celsius. Increased sensitivity to a wide range of antibiotics. Irregularly shaped cells form clumps of spiral cells connected by long chains, with few visible septa, cell walls are altered with looser, less dense peptidoglycan. Double pnp-rnjA or rnjA-rny mutants could not be isolated (PubMed:23504012).9 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi45D → A: Slight decrease in endonuclease and 10-fold decrease in 5'-exonuclease activity; when associated with A-337. 1 Publication1
    Mutagenesisi76H → A: Loss of endo- and 5'-exonuclease activity. 2 Publications1
    Mutagenesisi78 – 79DH → KA: Severe loss of endo- and 5'-exonuclease activity. 1 Publication2
    Mutagenesisi337N → A: Slight decrease in endonuclease and 10-fold decrease in 5'-exonuclease activity; when associated with A-45. 1 Publication1
    Mutagenesisi366S → L: 30% endonuclease and 10% 5'-exonuclease activity. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002152681 – 555Ribonuclease J1Add BLAST555

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q45493

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    Q45493

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q45493

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Unclear whether it forms homodimers or belongs to a larger complex. According to (PubMed:20025672) probably does not form homodimers, while (PubMed:21893285) shows homodimer formation. Both reports show RNase J1 and J2 interaction, probably as a heterotetramer (PubMed:19193632) shows it is a component of a possible RNA degradosome complex composed of rny, rnjA, rnjB, pnp, pfkA and eno, while (PubMed:20025672) finds no evidence of an RNA degradosome complex.6 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    Database of interacting proteins

    More...
    DIPi
    DIP-46392N

    Protein interaction database and analysis system

    More...
    IntActi
    Q45493, 3 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q45493

    STRING: functional protein association networks

    More...
    STRINGi
    224308.BSU14530

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1555
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3ZQ4X-ray3.00A/C/D/E1-555[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q45493

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q45493

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q45493

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni364 – 368Substrate bindingUniRule annotation5
    Regioni450 – 555Required for endo- and 5'-exonuclease activity and dimerizationAdd BLAST106

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The C-terminal domain (residues 450-555) are required for nuclease activity and dimerization.1 Publication

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CN5 Bacteria
    COG0595 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000280201

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q45493

    KEGG Orthology (KO)

    More...
    KOi
    K12574

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    KNTCVFE

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q45493

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.60.15.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01491 RNase_J_bact, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001279 Metallo-B-lactamas
    IPR036866 RibonucZ/Hydroxyglut_hydro
    IPR011108 RMMBL
    IPR004613 RNase_J
    IPR030854 RNase_J_bac
    IPR001587 RNase_J_CS

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00753 Lactamase_B, 1 hit
    PF07521 RMMBL, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF004803 RnjA, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00849 Lactamase_B, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF56281 SSF56281, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00649 MG423, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS01292 UPF0036, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    Q45493-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKFVKNDQTA VFALGGLGEI GKNTYAVQFQ DEIVLIDAGI KFPEDELLGI
    60 70 80 90 100
    DYVIPDYTYL VKNEDKIKGL FITHGHEDHI GGIPYLLRQV NIPVYGGKLA
    110 120 130 140 150
    IGLLRNKLEE HGLLRQTKLN IIGEDDIVKF RKTAVSFFRT THSIPDSYGI
    160 170 180 190 200
    VVKTPPGNIV HTGDFKFDFT PVGEPANLTK MAEIGKEGVL CLLSDSTNSE
    210 220 230 240 250
    NPEFTMSERR VGESIHDIFR KVDGRIIFAT FASNIHRLQQ VIEAAVQNGR
    260 270 280 290 300
    KVAVFGRSME SAIEIGQTLG YINCPKNTFI EHNEINRMPA NKVTILCTGS
    310 320 330 340 350
    QGEPMAALSR IANGTHRQIS INPGDTVVFS SSPIPGNTIS VSRTINQLYR
    360 370 380 390 400
    AGAEVIHGPL NDIHTSGHGG QEEQKLMLRL IKPKFFMPIH GEYRMQKMHV
    410 420 430 440 450
    KLATDCGIPE ENCFIMDNGE VLALKGDEAS VAGKIPSGSV YIDGSGIGDI
    460 470 480 490 500
    GNIVLRDRRI LSEEGLVIVV VSIDMDDFKI SAGPDLISRG FVYMRESGDL
    510 520 530 540 550
    INDAQELISN HLQKVMERKT TQWSEIKNEI TDTLAPFLYE KTKRRPMILP

    IIMEV
    Length:555
    Mass (Da):61,517
    Last modified:November 1, 1996 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i48091B448B8431C9
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AF012285 Genomic DNA Translation: AAC24928.1
    AL009126 Genomic DNA Translation: CAB13326.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    B69862

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_389336.1, NC_000964.3
    WP_003245660.1, NZ_JNCM01000035.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CAB13326; CAB13326; BSU14530

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    939483

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    bsu:BSU14530

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|224308.179.peg.1583

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF012285 Genomic DNA Translation: AAC24928.1
    AL009126 Genomic DNA Translation: CAB13326.1
    PIRiB69862
    RefSeqiNP_389336.1, NC_000964.3
    WP_003245660.1, NZ_JNCM01000035.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3ZQ4X-ray3.00A/C/D/E1-555[»]
    ProteinModelPortaliQ45493
    SMRiQ45493
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-46392N
    IntActiQ45493, 3 interactors
    MINTiQ45493
    STRINGi224308.BSU14530

    Proteomic databases

    jPOSTiQ45493
    PaxDbiQ45493
    PRIDEiQ45493

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB13326; CAB13326; BSU14530
    GeneIDi939483
    KEGGibsu:BSU14530
    PATRICifig|224308.179.peg.1583

    Phylogenomic databases

    eggNOGiENOG4105CN5 Bacteria
    COG0595 LUCA
    HOGENOMiHOG000280201
    InParanoidiQ45493
    KOiK12574
    OMAiKNTCVFE
    PhylomeDBiQ45493

    Enzyme and pathway databases

    BioCyciBSUB:BSU14530-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiQ45493

    Family and domain databases

    Gene3Di3.60.15.10, 1 hit
    HAMAPiMF_01491 RNase_J_bact, 1 hit
    InterProiView protein in InterPro
    IPR001279 Metallo-B-lactamas
    IPR036866 RibonucZ/Hydroxyglut_hydro
    IPR011108 RMMBL
    IPR004613 RNase_J
    IPR030854 RNase_J_bac
    IPR001587 RNase_J_CS
    PfamiView protein in Pfam
    PF00753 Lactamase_B, 1 hit
    PF07521 RMMBL, 1 hit
    PIRSFiPIRSF004803 RnjA, 1 hit
    SMARTiView protein in SMART
    SM00849 Lactamase_B, 1 hit
    SUPFAMiSSF56281 SSF56281, 1 hit
    TIGRFAMsiTIGR00649 MG423, 1 hit
    PROSITEiView protein in PROSITE
    PS01292 UPF0036, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRNJ1_BACSU
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q45493
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: April 10, 2019
    This is version 121 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Uncharacterized protein families (UPF)
      List of uncharacterized protein family (UPF) entries
    4. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
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