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Entry version 197 (17 Jun 2020)
Sequence version 6 (29 Aug 2003)
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Protein

Ribonuclease E

Gene

rne

Organism
Escherichia coli (strain K12)
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

Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs. Can also process other RNA species, such as RNAI, a molecule that controls the replication of ColE1 plasmid, and the cell division inhibitor DicF-RNA. It initiates the decay of RNAs by cutting them internally near their 5'-end. It is able to remove poly(A) tails by an endonucleolytic process. Required to initiate rRNA degradation during both starvation and quality control; acts after RNase PH (rph) exonucleolytically digests the 3'-end of the 16S rRNA (PubMed:27298395). Degradation of 16S rRNA leads to 23S rRNA degradation (PubMed:27298395).UniRule annotation10 Publications

Miscellaneous

In K12 strains that are derived from W1485 (including MG1655 and W3110) the rph gene has a frameshift that leads to loss of its ribonuclease PH activity. In strain K12 / MG1655(Seq)* the wild-type Rph protein has been restored (PubMed:27298395).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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

Binding to the membrane stabilizes protein structure and increases affinity for the substrate.1 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 bindingi303Magnesium; catalytic1 Publication1
Metal bindingi346Magnesium; catalytic1 Publication1
Metal bindingi404Zinc; shared with dimeric partner2 Publications1
Metal bindingi407Zinc; shared with dimeric partner2 Publications1

<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, Hydrolase, Nuclease, RNA-binding
Biological processrRNA processing, tRNA processing
LigandMagnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10859-MONOMER
ECOL316407:JW1071-MONOMER
MetaCyc:EG10859-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.26.12 2026

<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 EUniRule annotation (EC:3.1.26.12UniRule annotation)
Short name:
RNase EUniRule 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:rneUniRule annotation
Synonyms:ams, hmp1
Ordered Locus Names:b1084, JW1071
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 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

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

<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

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>Mutagenesisi57F → A: Reduces RNA cleavage by over 98%. 1 Publication1
Mutagenesisi66G → S: Disrupts folding of the S1 motif. 1 Publication1
Mutagenesisi67F → A: Reduces RNA cleavage by over 98%. 1 Publication1
Mutagenesisi112K → A: Reduces RNA cleavage by 98%. 1 Publication1
Mutagenesisi170T → V: Abolishes enzyme activity toward RNA substrates with a 5' monophosphate (PubMed:16237448). Strongly reduces enzyme activity toward cspA mRNA (PubMed:19889093). 2 Publications1
Mutagenesisi303D → N: Reduces RNA cleavage by over 96%. 1 Publication1
Mutagenesisi305N → D or L: Reduces RNA cleavage by over 96%. 1 Publication1
Mutagenesisi346D → N: Reduces RNA cleavage by over 96%. 1 Publication1
Mutagenesisi373R → A or D: Reduces RNA cleavage by 89%. 1 Publication1
Mutagenesisi404C → A: Reduces zinc-binding. Abolishes homotetramerization and enzyme activity. 1 Publication1
Mutagenesisi407C → A: Reduces zinc-binding. Abolishes homotetramerization and enzyme 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_00000973731 – 1061Ribonuclease EAdd BLAST1061

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P21513

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

More...
PaxDbi
P21513

PRoteomics IDEntifications database

More...
PRIDEi
P21513

<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

Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Within the RNA degradosome, Rnase E assembles into a homotetramer formed by a dimer of dimers. Tetramerization is essential for catalytic activity, but not for RNA-binding.

Interacts with RhlB, PNPase (pnp) and enolase (eno).

Interacts with DeaD at reduced temperature.

UniRule annotation11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="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

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4261023, 251 interactors
850013, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-403 Degradosome

Database of interacting proteins

More...
DIPi
DIP-10727N

Protein interaction database and analysis system

More...
IntActi
P21513, 63 interactors

Molecular INTeraction database

More...
MINTi
P21513

STRING: functional protein association networks

More...
STRINGi
511145.b1084

<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

11061
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

More...
SMRi
P21513

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P21513

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini39 – 119S1 motifUniRule annotationAdd BLAST81

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>Regioni57 – 112Interaction with RNAAdd BLAST56
Regioni169 – 170Interaction with RNA 5'-terminal monophosphate2
Regioni404 – 407Required for zinc-mediated homotetramerization and catalytic activity4
Regioni833 – 850Interaction with enolaseAdd BLAST18
Regioni1021 – 1061Interaction with PNPaseAdd BLAST41

<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 N-terminal S1 motif binds RNA, and can also bind single-stranded DNA (in vitro). The C-terminal region interacts with the other degradosomal components.2 Publications

<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

Belongs to the RNase E/G family. RNase E subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4107QQB Bacteria
COG1530 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_003468_1_2_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P21513

KEGG Orthology (KO)

More...
KOi
K08300

Family and domain databases

Database of protein disorder

More...
DisProti
DP00207

HAMAP database of protein families

More...
HAMAPi
MF_00970 RNase_E, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR012340 NA-bd_OB-fold
IPR021968 PNPase_C
IPR019307 RNA-bd_AU-1/RNase_E/G
IPR028878 RNase_E
IPR004659 RNase_E/G
IPR022967 S1_dom
IPR003029 S1_domain

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12111 PNPase_C, 1 hit
PF10150 RNase_E_G, 1 hit
PF00575 S1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00316 S1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50249 SSF50249, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00757 RNaseEG, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50126 S1, 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.

P21513-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKRMLINATQ QEELRVALVD GQRLYDLDIE SPGHEQKKAN IYKGKITRIE
60 70 80 90 100
PSLEAAFVDY GAERHGFLPL KEIAREYFPA NYSAHGRPNI KDVLREGQEV
110 120 130 140 150
IVQIDKEERG NKGAALTTFI SLAGSYLVLM PNNPRAGGIS RRIEGDDRTE
160 170 180 190 200
LKEALASLEL PEGMGLIVRT AGVGKSAEAL QWDLSFRLKH WEAIKKAAES
210 220 230 240 250
RPAPFLIHQE SNVIVRAFRD YLRQDIGEIL IDNPKVLELA RQHIAALGRP
260 270 280 290 300
DFSSKIKLYT GEIPLFSHYQ IESQIESAFQ REVRLPSGGS IVIDSTEALT
310 320 330 340 350
AIDINSARAT RGGDIEETAF NTNLEAADEI ARQLRLRDLG GLIVIDFIDM
360 370 380 390 400
TPVRHQRAVE NRLREAVRQD RARIQISHIS RFGLLEMSRQ RLSPSLGESS
410 420 430 440 450
HHVCPRCSGT GTVRDNESLS LSILRLIEEE ALKENTQEVH AIVPVPIASY
460 470 480 490 500
LLNEKRSAVN AIETRQDGVR CVIVPNDQME TPHYHVLRVR KGEETPTLSY
510 520 530 540 550
MLPKLHEEAM ALPSEEEFAE RKRPEQPALA TFAMPDVPPA PTPAEPAAPV
560 570 580 590 600
VAPAPKAAPA TPAAPAQPGL LSRFFGALKA LFSGGEETKP TEQPAPKAEA
610 620 630 640 650
KPERQQDRRK PRQNNRRDRN ERRDTRSERT EGSDNREENR RNRRQAQQQT
660 670 680 690 700
AETRESRQQA EVTEKARTAD EQQAPRRERS RRRNDDKRQA QQEAKALNVE
710 720 730 740 750
EQSVQETEQE ERVRPVQPRR KQRQLNQKVR YEQSVAEEAV VAPVVEETVA
760 770 780 790 800
AEPIVQEAPA PRTELVKVPL PVVAQTAPEQ QEENNADNRD NGGMPRRSRR
810 820 830 840 850
SPRHLRVSGQ RRRRYRDERY PTQSPMPLTV ACASPELASG KVWIRYPIVR
860 870 880 890 900
PQDVQVEEQR EQEEVHVQPM VTEVPVAAAI EPVVSAPVVE EVAGVVEAPV
910 920 930 940 950
QVAEPQPEVV ETTHPEVIAA AVTEQPQVIT ESDVAVAQEV AEQAEPVVEP
960 970 980 990 1000
QEETADIEEV VETAEVVVAE PEVVAQPAAP VVAEVAAEVE TVAAVEPEVT
1010 1020 1030 1040 1050
VEHNHATAPM TRAPAPEYVP EAPRHSDWQR PTFAFEGKGA AGGHTATHHA
1060
SAAPARPQPV E
Length:1,061
Mass (Da):118,197
Last modified:August 29, 2003 - v6
<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:iD4066D80E1DE7D37
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA23443 differs from that shown. Reason: Frameshift.Curated
The sequence CAA38206 differs from that shown. Reason: Frameshift.Curated
The sequence CAA47818 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti390Q → H in AAA23443 (PubMed:1704367).Curated1
Sequence conflicti487L → V in CAA47818 (PubMed:1447789).Curated1
Sequence conflicti487L → V in AAA23443 (PubMed:1704367).Curated1
Sequence conflicti564A → R in CAA47818 (PubMed:1447789).Curated1
Sequence conflicti784N → K in CAA47818 (PubMed:1447789).Curated1
Sequence conflicti838A → R in AAA23443 (PubMed:1704367).Curated1
Sequence conflicti905P → R in CAA47818 (PubMed:1447789).Curated1
Sequence conflicti1048H → R in AAA03347 (PubMed:8415644).Curated1

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
U00096 Genomic DNA Translation: AAC74168.1
AP009048 Genomic DNA Translation: BAA35893.1
X67470 Genomic DNA Translation: CAA47818.1 Frameshift.
M62747 Genomic DNA Translation: AAA23443.1 Frameshift.
X54309 Genomic DNA Translation: CAA38206.1 Frameshift.
L23942 Genomic DNA Translation: AAA03347.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A64852 S27311

NCBI Reference Sequences

More...
RefSeqi
NP_415602.1, NC_000913.3
WP_000827360.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74168; AAC74168; b1084
BAA35893; BAA35893; BAA35893

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945641

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1071
eco:b1084

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1184

<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
U00096 Genomic DNA Translation: AAC74168.1
AP009048 Genomic DNA Translation: BAA35893.1
X67470 Genomic DNA Translation: CAA47818.1 Frameshift.
M62747 Genomic DNA Translation: AAA23443.1 Frameshift.
X54309 Genomic DNA Translation: CAA38206.1 Frameshift.
L23942 Genomic DNA Translation: AAA03347.1
PIRiA64852 S27311
RefSeqiNP_415602.1, NC_000913.3
WP_000827360.1, NZ_LN832404.1

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
1SLJNMR-A35-125[»]
1SMXX-ray1.80A/B35-125[»]
1SN8X-ray2.00A/B35-125[»]
2BX2X-ray2.85L1-510[»]
2C0BX-ray3.18L1-510[»]
2C4RX-ray3.60L1-510[»]
2FYMX-ray1.60B/E833-850[»]
2VMKX-ray3.30A/B/C/D1-515[»]
2VRTX-ray3.50A/B/C/D1-509[»]
3GCMX-ray2.50D/E/F1021-1061[»]
3GMEX-ray2.40D1021-1061[»]
3H1CX-ray3.57D/E/F/H/J/L/N/P/S/U/W/Y1021-1061[»]
3H8AX-ray1.90E/F823-850[»]
5F6CX-ray3.00A1-510[»]
B1-511[»]
6G63X-ray3.95A/G/L/N1-510[»]
SMRiP21513
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261023, 251 interactors
850013, 1 interactor
ComplexPortaliCPX-403 Degradosome
DIPiDIP-10727N
IntActiP21513, 63 interactors
MINTiP21513
STRINGi511145.b1084

Proteomic databases

jPOSTiP21513
PaxDbiP21513
PRIDEiP21513

Genome annotation databases

EnsemblBacteriaiAAC74168; AAC74168; b1084
BAA35893; BAA35893; BAA35893
GeneIDi945641
KEGGiecj:JW1071
eco:b1084
PATRICifig|1411691.4.peg.1184

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

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EchoBASEi
EB0852

Phylogenomic databases

eggNOGiENOG4107QQB Bacteria
COG1530 LUCA
HOGENOMiCLU_003468_1_2_6
InParanoidiP21513
KOiK08300

Enzyme and pathway databases

BioCyciEcoCyc:EG10859-MONOMER
ECOL316407:JW1071-MONOMER
MetaCyc:EG10859-MONOMER
BRENDAi3.1.26.12 2026

Miscellaneous databases

EvolutionaryTraceiP21513

Protein Ontology

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PROi
PR:P21513

Family and domain databases

DisProtiDP00207
HAMAPiMF_00970 RNase_E, 1 hit
InterProiView protein in InterPro
IPR012340 NA-bd_OB-fold
IPR021968 PNPase_C
IPR019307 RNA-bd_AU-1/RNase_E/G
IPR028878 RNase_E
IPR004659 RNase_E/G
IPR022967 S1_dom
IPR003029 S1_domain
PfamiView protein in Pfam
PF12111 PNPase_C, 1 hit
PF10150 RNase_E_G, 1 hit
PF00575 S1, 1 hit
SMARTiView protein in SMART
SM00316 S1, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit
TIGRFAMsiTIGR00757 RNaseEG, 1 hit
PROSITEiView protein in PROSITE
PS50126 S1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiRNE_ECOLI
<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: P21513
Secondary accession number(s): P77591
<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: May 1, 1991
Last sequence update: August 29, 2003
Last modified: June 17, 2020
This is version 197 of the entry and version 6 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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