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P21513 (RNE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease E

Short name=RNase E
EC=3.1.26.12
Gene names
Name:rne
Synonyms:ams, hmp1
Ordered Locus Names:b1084, JW1071
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1061 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.19 Ref.22

Catalytic activity

Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions. Ref.17 Ref.19 Ref.22

Cofactor

Binds 2 Zn2+ ions per homotetramer. Zinc ions are bound betweeen subunits and are essential for homotetramerization and catalytic activity, but not for RNA binding. In the absence of zinc, the protein dissociates into inactive dimers. Ref.17 Ref.22

Binds 1 Mg2+ ion per subunit. Ref.17 Ref.22

Enzyme regulation

Binding to the membrane stabilizes protein structure and increases affinity for the substrate. Ref.20

Subunit structure

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. Ref.11 Ref.13 Ref.16 Ref.17 Ref.18 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26

Subcellular location

Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note: Associated with the cytoplasmic membrane via the N- and C-terminal regions. Ref.13 Ref.20

Domain

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. Ref.11 Ref.21

Sequence similarities

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

Contains 1 S1 motif domain.

Sequence caution

The sequence AAA23443.1 differs from that shown. Reason: Frameshift at position 796.

The sequence CAA38206.1 differs from that shown. Reason: Frameshift at several positions.

The sequence CAA47818.1 differs from that shown. Reason: Frameshift at position 1003.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10611061Ribonuclease E HAMAP-Rule MF_00970
PRO_0000097373

Regions

Domain39 – 11981S1 motif
Region57 – 11256Interaction with RNA HAMAP-Rule MF_00970
Region169 – 1702Interaction with RNA 5'-terminal monophosphate HAMAP-Rule MF_00970
Region404 – 4074Required for zinc-mediated homotetramerization and catalytic activity HAMAP-Rule MF_00970
Region833 – 85018Interaction with enolase HAMAP-Rule MF_00970
Region1021 – 106141Interaction with PNPase HAMAP-Rule MF_00970

Sites

Metal binding3031Magnesium; catalytic
Metal binding3461Magnesium; catalytic
Metal binding4041Zinc; shared with dimeric partner
Metal binding4071Zinc; shared with dimeric partner

Experimental info

Mutagenesis571F → A: Reduces RNA cleavage by over 98%. Ref.22
Mutagenesis661G → S: Disrupts folding of the S1 motif. Ref.21
Mutagenesis671F → A: Reduces RNA cleavage by over 98%. Reduces affinity for RNA. Ref.22
Mutagenesis1121K → A: Reduces RNA cleavage by 98%. Loss of RNA-binding. Ref.22
Mutagenesis1701T → V: Abolishes enzyme activity toward RNA substrates with a 5' monophosphate (PubMed:16237448). Strongly reduces enzyme activity toward cspA mRNA (PubMed:19889093). Ref.19 Ref.22
Mutagenesis3031D → N: Reduces RNA cleavage by over 96%. Ref.22
Mutagenesis3051N → D or L: Reduces RNA cleavage by over 96%. Ref.22
Mutagenesis3461D → N: Reduces RNA cleavage by over 96%. Reduces affinity for RNA. Ref.22
Mutagenesis3731R → A or D: Reduces RNA cleavage by 89%. Ref.22
Mutagenesis4041C → A: Reduces zinc-binding. Abolishes homotetramerization and enzyme activity. Ref.17
Mutagenesis4071C → A: Reduces zinc-binding. Abolishes homotetramerization and enzyme activity. Ref.17
Sequence conflict3901Q → H in AAA23443. Ref.5
Sequence conflict4871L → V in CAA47818. Ref.4
Sequence conflict4871L → V in AAA23443. Ref.5
Sequence conflict5641A → R in CAA47818. Ref.4
Sequence conflict7841N → K in CAA47818. Ref.4
Sequence conflict8381A → R in AAA23443. Ref.5
Sequence conflict9051P → R in CAA47818. Ref.4
Sequence conflict10481H → R in AAA03347. Ref.7

Secondary structure

.......................................................................................................... 1061
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21513 [UniParc].

Last modified August 29, 2003. Version 6.
Checksum: D4066D80E1DE7D37

FASTA1,061118,197
        10         20         30         40         50         60 
MKRMLINATQ QEELRVALVD GQRLYDLDIE SPGHEQKKAN IYKGKITRIE PSLEAAFVDY 

        70         80         90        100        110        120 
GAERHGFLPL KEIAREYFPA NYSAHGRPNI KDVLREGQEV IVQIDKEERG NKGAALTTFI 

       130        140        150        160        170        180 
SLAGSYLVLM PNNPRAGGIS RRIEGDDRTE LKEALASLEL PEGMGLIVRT AGVGKSAEAL 

       190        200        210        220        230        240 
QWDLSFRLKH WEAIKKAAES RPAPFLIHQE SNVIVRAFRD YLRQDIGEIL IDNPKVLELA 

       250        260        270        280        290        300 
RQHIAALGRP DFSSKIKLYT GEIPLFSHYQ IESQIESAFQ REVRLPSGGS IVIDSTEALT 

       310        320        330        340        350        360 
AIDINSARAT RGGDIEETAF NTNLEAADEI ARQLRLRDLG GLIVIDFIDM TPVRHQRAVE 

       370        380        390        400        410        420 
NRLREAVRQD RARIQISHIS RFGLLEMSRQ RLSPSLGESS HHVCPRCSGT GTVRDNESLS 

       430        440        450        460        470        480 
LSILRLIEEE ALKENTQEVH AIVPVPIASY LLNEKRSAVN AIETRQDGVR CVIVPNDQME 

       490        500        510        520        530        540 
TPHYHVLRVR KGEETPTLSY MLPKLHEEAM ALPSEEEFAE RKRPEQPALA TFAMPDVPPA 

       550        560        570        580        590        600 
PTPAEPAAPV VAPAPKAAPA TPAAPAQPGL LSRFFGALKA LFSGGEETKP TEQPAPKAEA 

       610        620        630        640        650        660 
KPERQQDRRK PRQNNRRDRN ERRDTRSERT EGSDNREENR RNRRQAQQQT AETRESRQQA 

       670        680        690        700        710        720 
EVTEKARTAD EQQAPRRERS RRRNDDKRQA QQEAKALNVE EQSVQETEQE ERVRPVQPRR 

       730        740        750        760        770        780 
KQRQLNQKVR YEQSVAEEAV VAPVVEETVA AEPIVQEAPA PRTELVKVPL PVVAQTAPEQ 

       790        800        810        820        830        840 
QEENNADNRD NGGMPRRSRR SPRHLRVSGQ RRRRYRDERY PTQSPMPLTV ACASPELASG 

       850        860        870        880        890        900 
KVWIRYPIVR PQDVQVEEQR EQEEVHVQPM VTEVPVAAAI EPVVSAPVVE EVAGVVEAPV 

       910        920        930        940        950        960 
QVAEPQPEVV ETTHPEVIAA AVTEQPQVIT ESDVAVAQEV AEQAEPVVEP QEETADIEEV 

       970        980        990       1000       1010       1020 
VETAEVVVAE PEVVAQPAAP VVAEVAAEVE TVAAVEPEVT VEHNHATAPM TRAPAPEYVP 

      1030       1040       1050       1060 
EAPRHSDWQR PTFAFEGKGA AGGHTATHHA SAAPARPQPV E 

« Hide

References

« Hide 'large scale' references
[1]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Cloning and analysis of the entire Escherichia coli ams gene. ams is identical to hmp1 and encodes a 114 kDa protein that migrates as a 180 kDa protein."
Casaregola S., Jacq A., Laoudj D., McGurk G., Margarson S., Tempete M., Norris V., Holland I.B.
J. Mol. Biol. 228:30-40(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1025.
Strain: K12.
[5]"Analysis of the altered mRNA stability (ams) gene from Escherichia coli. Nucleotide sequence, transcriptional analysis, and homology of its product to MRP3, a mitochondrial ribosomal protein from Neurospora crassa."
Claverie-Martin F., Diaz-Torres M., Yancey S.D., Kushner S.R.
J. Biol. Chem. 266:2843-2851(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-844.
Strain: K12.
[6]"Sequencing and expression of the rne gene of Escherichia coli."
Chauhan A.K., Miczak A., Taraseviciene L., Apirion D.
Nucleic Acids Res. 19:125-129(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-27.
Strain: K12.
[7]"RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product."
Cormack R.S., Genereaux J.L., Mackie G.A.
Proc. Natl. Acad. Sci. U.S.A. 90:9006-9010(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 844-1061, CHARACTERIZATION.
Strain: K12.
[8]"Maturation of 5-S rRNA: ribonuclease E cleavages and their dependence on precursor sequences."
Roy M.K., Singh B., Ray B.K., Apirion D.
Eur. J. Biochem. 131:119-127(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN 5S RRNA MATURATION.
[9]"Escherichia coli cell division inhibitor DicF-RNA of the dicB operon. Evidence for its generation in vivo by transcription termination and by RNase III and RNase E-dependent processing."
Faubladier M., Cam K., Bouche J.P.
J. Mol. Biol. 212:461-471(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PROCESSING OF DICF-RNA.
[10]"RNase E, an endoribonuclease, has a general role in the chemical decay of Escherichia coli mRNA: evidence that rne and ams are the same genetic locus."
Mudd E.A., Krisch H.M., Higgins C.F.
Mol. Microbiol. 4:2127-2135(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome."
Vanzo N.F., Li Y.S., Py B., Blum E., Higgins C.F., Raynal L.C., Krisch H.M., Carpousis A.J.
Genes Dev. 12:2770-2781(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RHLB; PNPASE AND ENOLASE, DOMAIN.
[12]"RNase G (CafA protein) and RNase E are both required for the 5' maturation of 16S ribosomal RNA."
Li Z., Pandit S., Deutscher M.P.
EMBO J. 18:2878-2885(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN 16S RRNA MATURATION.
Strain: K12.
[13]"RNA degradosomes exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E."
Liou G.G., Jane W.N., Cohen S.N., Lin N.S., Lin-Chao S.
Proc. Natl. Acad. Sci. U.S.A. 98:63-68(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[14]"Cleavage of poly(A) tails on the 3'-end of RNA by ribonuclease E of Escherichia coli."
Walsh A.P., Tock M.R., Mallen M.H., Kaberdin V.R., Gabain Av A., McDowall K.J.
Nucleic Acids Res. 29:1864-1871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CLEAVAGE OF POLY(A).
[15]"RNase E plays an essential role in the maturation of Escherichia coli tRNA precursors."
Li Z., Deutscher M.P.
RNA 8:97-109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRNA MATURATION.
Strain: K12.
[16]"Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock degradosome'."
Prud'homme-Genereux A., Beran R.K., Iost I., Ramey C.S., Mackie G.A., Simons R.W.
Mol. Microbiol. 54:1409-1421(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DEAD.
Strain: CF881.
[17]"'Zn-link': a metal-sharing interface that organizes the quaternary structure and catalytic site of the endoribonuclease, RNase E."
Callaghan A.J., Redko Y., Murphy L.M., Grossmann J.G., Yates D., Garman E., Ilag L.L., Robinson C.V., Symmons M.F., McDowall K.J., Luisi B.F.
Biochemistry 44:4667-4675(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, RNA-BINDING, SUBUNIT, ZINC-BINDING, COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF CYS-404 AND CYS-407.
[18]"RNaseE and RNA helicase B play central roles in the cytoskeletal organization of the RNA degradosome."
Taghbalout A., Rothfield L.
J. Biol. Chem. 283:13850-13855(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RHLB; PNPASE AND ENOLASE.
[19]"Rapid cleavage of RNA by RNase E in the absence of 5' monophosphate stimulation."
Kime L., Jourdan S.S., Stead J.A., Hidalgo-Sastre A., McDowall K.J.
Mol. Microbiol. 76:590-604(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF THR-170.
[20]"Membrane binding of Escherichia coli RNase E catalytic domain stabilizes protein structure and increases RNA substrate affinity."
Murashko O.N., Kaberdin V.R., Lin-Chao S.
Proc. Natl. Acad. Sci. U.S.A. 109:7019-7024(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION.
[21]"Structural characterization of the RNase E S1 domain and identification of its oligonucleotide-binding and dimerization interfaces."
Schubert M., Edge R.E., Lario P., Cook M.A., Strynadka N.C., Mackie G.A., McIntosh L.P.
J. Mol. Biol. 341:37-54(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 35-125, STRUCTURE BY NMR OF 35-125, SUBUNIT, RNA-BINDING, DOMAIN, MUTAGENESIS OF GLY-66.
[22]"Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover."
Callaghan A.J., Marcaida M.J., Stead J.A., McDowall K.J., Scott W.G., Luisi B.F.
Nature 437:1187-1191(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-510 IN COMPLEXES WITH RNA; ZINC AND MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF PHE-57; PHE-67; LYS-112; THR-170; ASP-303; ASN-305; ASP-346 AND ARG-373.
[23]"Recognition of enolase in the Escherichia coli RNA degradosome."
Chandran V., Luisi B.F.
J. Mol. Biol. 358:8-15(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 833-850 IN COMPLEX WITH ENO, SUBUNIT.
[24]"The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation."
Koslover D.J., Callaghan A.J., Marcaida M.J., Garman E.F., Martick M., Scott W.G., Luisi B.F.
Structure 16:1238-1244(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-515 IN COMPLEX WITH RNA AND ZINC IONS, SUBUNIT.
[25]"Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: implications for catalytic mechanism and RNA degradosome assembly."
Nurmohamed S., Vaidialingam B., Callaghan A.J., Luisi B.F.
J. Mol. Biol. 389:17-33(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1021-1061 IN COMPLEXES WITH PNP AND RNA, SUBUNIT.
[26]"Molecular recognition between Escherichia coli enolase and ribonuclease E."
Nurmohamed S., McKay A.R., Robinson C.V., Luisi B.F.
Acta Crystallogr. D 66:1036-1040(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 823-850 IN COMPLEX WITH ENO, INTERACTION WITH ENO, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS27311. A64852.
RefSeqNP_415602.1. NC_000913.3.
YP_489352.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
DisProtDP00207.
ProteinModelPortalP21513.
SMRP21513. Positions 1-510, 823-850.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10727N.
IntActP21513. 61 interactions.
MINTMINT-1220086.
STRING511145.b1084.

Proteomic databases

PaxDbP21513.
PRIDEP21513.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74168; AAC74168; b1084.
BAA35893; BAA35893; BAA35893.
GeneID12932029.
945641.
KEGGecj:Y75_p1054.
eco:b1084.
PATRIC32117409. VBIEscCol129921_1127.

Organism-specific databases

EchoBASEEB0852.
EcoGeneEG10859. rne.

Phylogenomic databases

eggNOGCOG1530.
HOGENOMHOG000258027.
KOK08300.
OMAENTKEVH.
OrthoDBEOG6PCPTH.
ProtClustDBPRK10811.

Enzyme and pathway databases

BioCycEcoCyc:EG10859-MONOMER.
ECOL316407:JW1071-MONOMER.
MetaCyc:EG10859-MONOMER.

Gene expression databases

GenevestigatorP21513.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
HAMAPMF_00970. RNase_E.
InterProIPR012340. NA-bd_OB-fold.
IPR021968. PNPase_C.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR019307. RNA-bd_AU-1/RNase_E/G.
IPR022967. RNA-binding_domain_S1.
IPR028878. RNase_E.
IPR004659. RNase_E/G.
[Graphical view]
PfamPF12111. PNPase_C. 1 hit.
PF10150. RNase_E_G. 1 hit.
PF00575. S1. 1 hit.
[Graphical view]
SMARTSM00316. S1. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00757. RNaseEG. 1 hit.
PROSITEPS50126. S1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21513.
PROP21513.

Entry information

Entry nameRNE_ECOLI
AccessionPrimary (citable) accession number: P21513
Secondary accession number(s): P77591
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: August 29, 2003
Last modified: April 16, 2014
This is version 142 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene