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Entry version 135 (23 Feb 2022)
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). Major RNase that degrades both RNAs of the type I toxin-antitoxin system BsrE/SR5 (PubMed:26940229).

14 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q45493

<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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

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). Increased half-life of both RNAs of the type I toxin-antitoxin system BsrE/SR5 (PubMed:26940229).10 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002152681 – 555Ribonuclease J1Add BLAST555

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q45493

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

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PaxDbi
Q45493

PRoteomics IDEntifications database

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PRIDEi
Q45493

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Part of the rpoY-rnjA operon, transcribed constitutively.1 Publication

<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%5Fsection">'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%5Fsection">'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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-46392N

Protein interaction database and analysis system

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IntActi
Q45493, 3 interactors

Molecular INTeraction database

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MINTi
Q45493

STRING: functional protein association networks

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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

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

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SMRi
Q45493

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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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

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eggNOGi
COG0595, Bacteria

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q45493

Identification of Orthologs from Complete Genome Data

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OMAi
KNTCVFE

Database for complete collections of gene phylogenies

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PhylomeDBi
Q45493

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.50.10710, 1 hit
3.60.15.10, 1 hit

HAMAP database of protein families

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HAMAPi
MF_01491, RNase_J_bact, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001279, Metallo-B-lactamas
IPR036866, RibonucZ/Hydroxyglut_hydro
IPR011108, RMMBL
IPR004613, RNase_J
IPR042173, RNase_J_2
IPR030854, RNase_J_bac
IPR041636, RNase_J_C
IPR001587, RNase_J_CS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00753, Lactamase_B, 1 hit
PF07521, RMMBL, 1 hit
PF17770, RNase_J_C, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF004803, RnjA, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00849, Lactamase_B, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56281, SSF56281, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00649, MG423, 1 hit

PROSITE; a protein domain and family database

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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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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

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EMBLi

GenBank nucleotide sequence database

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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

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PIRi
B69862

NCBI Reference Sequences

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

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

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EnsemblBacteriai
CAB13326; CAB13326; BSU_14530

Database of genes from NCBI RefSeq genomes

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GeneIDi
939483

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
bsu:BSU14530

Pathosystems Resource Integration Center (PATRIC)

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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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZQ4X-ray3.00A/C/D/E1-555[»]
SMRiQ45493
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

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

Proteomic databases

jPOSTiQ45493
PaxDbiQ45493
PRIDEiQ45493

Genome annotation databases

EnsemblBacteriaiCAB13326; CAB13326; BSU_14530
GeneIDi939483
KEGGibsu:BSU14530
PATRICifig|224308.179.peg.1583

Phylogenomic databases

eggNOGiCOG0595, Bacteria
InParanoidiQ45493
OMAiKNTCVFE
PhylomeDBiQ45493

Enzyme and pathway databases

BioCyciBSUB:BSU14530-MONOMER
SABIO-RKiQ45493

Miscellaneous databases

EvolutionaryTraceiQ45493

Family and domain databases

Gene3Di3.40.50.10710, 1 hit
3.60.15.10, 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
IPR042173, RNase_J_2
IPR030854, RNase_J_bac
IPR041636, RNase_J_C
IPR001587, RNase_J_CS
PfamiView protein in Pfam
PF00753, Lactamase_B, 1 hit
PF07521, RMMBL, 1 hit
PF17770, RNase_J_C, 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

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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%5Fand%5Fisoforms">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: February 23, 2022
This is version 135 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, Reference proteome

Documents

  1. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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