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ECOLI:RNE

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) rne (ECO:0000255 with HAMAP-Rule:MF_00970) (synonyms: ams, hmp1)
Protein Name(s) Ribonuclease E (ECO:0000255 with HAMAP-Rule:MF_00970)

RNase E (ECO:0000255 with HAMAP-Rule:MF_00970)

External Links
UniProt P21513
EMBL U00096
AP009048
X67470
M62747
X54309
L23942
PIR A64852
RefSeq NP_415602.1
YP_489352.1
PDB 1SLJ
1SMX
1SN8
2BX2
2C0B
2C4R
2FYM
2VMK
2VRT
3GCM
3GME
3H1C
3H8A
PDBsum 1SLJ
1SMX
1SN8
2BX2
2C0B
2C4R
2FYM
2VMK
2VRT
3GCM
3GME
3H1C
3H8A
DisProt DP00207
ProteinModelPortal P21513
SMR P21513
DIP DIP-10727N
IntAct P21513
MINT MINT-1220086
STRING 511145.b1084
PaxDb P21513
PRIDE P21513
EnsemblBacteria AAC74168
BAA35893
GeneID 12932029
945641
KEGG ecj:Y75_p1054
eco:b1084
PATRIC 32117409
EchoBASE EB0852
EcoGene EG10859
eggNOG COG1530
HOGENOM HOG000258027
InParanoid P21513
KO K08300
OMA ENTKEVH
OrthoDB EOG6PCPTH
BioCyc EcoCyc:EG10859-MONOMER
ECOL316407:JW1071-MONOMER
MetaCyc:EG10859-MONOMER
EvolutionaryTrace P21513
PRO PR:P21513
Proteomes UP000000318
UP000000625
Genevestigator P21513
GO GO:0005737
GO:0009898
GO:0004521
GO:0000287
GO:0008995
GO:0003723
GO:0008270
GO:0006402
GO:0006401
GO:0000967
GO:0006364
GO:0008033
Gene3D 2.40.50.140
HAMAP MF_00970
InterPro IPR012340
IPR021968
IPR003029
IPR019307
IPR028878
IPR004659
IPR022967
Pfam PF12111
PF10150
PF00575
SMART SM00316
SUPFAM SSF50249
TIGRFAMs TIGR00757
PROSITE PS50126

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004519

endonuclease activity

PMID:9790196[1]

ECO:0000314

F

Two forms of RNA were used, linear and circular. The circular RNA did not have a 5' end and thus could not be digested by RNase E as shown in Figure 2a. The circular RNA was then digested by RNase H and thus linearized as shown in Figure 2b. The now linearized RNA was then digested by RNase E which since the RNA was linear could be digested by RNase E as shown in Figure 2d and Figure 2e. The bands shown in Figures 2d,e are consistent with the digestion sites of both RNase H and RNase E.

complete

enables

GO:0017151

DEAD/H-box RNA helicase binding

PMID:15236960[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A8J8

F

Seeded From UniProt

complete

involved_in

GO:1902280

regulation of ATP-dependent RNA helicase activity

PMID:15236960[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

PMID:15236960[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008312

7S RNA binding

PMID:15236960[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006364

rRNA processing

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11299
PANTHER:PTN001246338

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:18682225[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P21513

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:15236960[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P21513

F

Seeded From UniProt

complete

involved_in

GO:0051289

protein homotetramerization

PMID:14636052[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P21513

P

Seeded From UniProt

complete

enables

GO:0008995

ribonuclease E activity

PMID:12417756[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0008033

tRNA processing

PMID:11871663[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006402

mRNA catabolic process

PMID:1846032[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006401

RNA catabolic process

PMID:8415644[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000967

rRNA 5'-end processing

PMID:10329633[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:25404697[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004519

P

Seeded From UniProt

complete

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004518

P

Seeded From UniProt

complete

involved_in

GO:0090501

RNA phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004540

P

Seeded From UniProt

complete

involved_in

GO:0090501

RNA phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0008995

P

Seeded From UniProt

complete

involved_in

GO:0090501

RNA phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0008995

P

Seeded From UniProt

complete

involved_in

GO:0090502

RNA phosphodiester bond hydrolysis, endonucleolytic

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004521

P

Seeded From UniProt

complete

enables

GO:0003676

nucleic acid binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003029

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004659
InterPro:IPR019307

F

Seeded From UniProt

complete

enables

GO:0004540

ribonuclease activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004659

F

Seeded From UniProt

complete

involved_in

GO:0006396

RNA processing

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004659
InterPro:IPR028878

P

Seeded From UniProt

complete

enables

GO:0008995

ribonuclease E activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR028878

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000112759

C

Seeded From UniProt

complete

enables

GO:0004521

endoribonuclease activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000112759

F

Seeded From UniProt

complete

involved_in

GO:0006402

mRNA catabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000112759

P

Seeded From UniProt

complete

part_of

GO:0009898

cytoplasmic side of plasma membrane

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000112759

C

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000112759

F

Seeded From UniProt

complete

involved_in

GO:0006364

rRNA processing

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000112759

P

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000112759

F

Seeded From UniProt

complete

involved_in

GO:0008033

tRNA processing

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000112759

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000112759

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-KW:KW-0997
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0694

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0004519

endonuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0255

F

Seeded From UniProt

complete

involved_in

GO:0006364

rRNA processing

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0698

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0004518

nuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0540

F

Seeded From UniProt

complete

involved_in

GO:0008033

tRNA processing

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0819

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Mackie, GA (1998) Ribonuclease E is a 5'-end-dependent endonuclease. Nature 395 720-3 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 2.4 Callaghan, AJ et al. (2004) Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. J. Mol. Biol. 340 965-79 PubMed GONUTS page
  3. Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. Koslover, DJ et al. (2008) The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation. Structure 16 1238-44 PubMed GONUTS page
  5. Callaghan, AJ et al. (2003) Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain. Biochemistry 42 13848-55 PubMed GONUTS page
  6. Feng, Y et al. (2002) The catalytic domain of RNase E shows inherent 3' to 5' directionality in cleavage site selection. Proc. Natl. Acad. Sci. U.S.A. 99 14746-51 PubMed GONUTS page
  7. Li, Z & Deutscher, MP (2002) RNase E plays an essential role in the maturation of Escherichia coli tRNA precursors. RNA 8 97-109 PubMed GONUTS page
  8. Babitzke, P & Kushner, SR (1991) The Ams (altered mRNA stability) protein and ribonuclease E are encoded by the same structural gene of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 88 1-5 PubMed GONUTS page
  9. Cormack, RS et al. (1993) RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product. Proc. Natl. Acad. Sci. U.S.A. 90 9006-10 PubMed GONUTS page
  10. Li, Z et al. (1999) RNase G (CafA protein) and RNase E are both required for the 5' maturation of 16S ribosomal RNA. EMBO J. 18 2878-85 PubMed GONUTS page
  11. Thompson, KJ et al. (2015) Altering the divalent metal ion preference of RNase E. J. Bacteriol. 197 477-82 PubMed GONUTS page