P21513

EV
Gene name
rne (ams, hmp1, b1804, JW1071)
Protein name
Ribonuclease E
Names
RNase E
Species
Escherichia coli (strain K12)
KEGG Pathway
ecj:JW1071,eco:b1084
EC number
3.1.26.12: Endoribonucleases producing 5'-phosphomonoesters
Protein Class
RIBONUCLEASE (PTHR30001)

Descriptions

Ribonuclease E (RNase E) is a metal-dependent hydrolytic enzyme that cleaves polymeric ribonucleic acid internally and serves as a central element in RNA metabolism of diverse bacteria. RNase E has a RNase H-like domain that is a pocket of unknown function consisting of acidic residues, which is considered functionally important. The charge-neutralizing changes within RNase H-like domain substantially boost the rate at which substrates are cleaved, indicating that the region provides an autoinhibitory function.

Autoinhibitory domains (AIDs)

216-279 (RNase H-like domain) EV

Target domain

1-529 (RNase catalytic domain)

Relief mechanism

Others

Assay

Structural analysis, Mutagenesis experiment

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

17 structures for P21513

Entry ID Method Resolution Chain Position Source
1SLJ NMR - A 35-125 PDB
1SMX X-ray 180 A A/B 35-125 PDB
1SN8 X-ray 200 A A/B 35-125 PDB
2BX2 X-ray 285 A L 1-510 PDB
2C0B X-ray 318 A L 1-510 PDB
2C4R X-ray 360 A L 1-510 PDB
2FYM X-ray 160 A B/E 833-850 PDB
2VMK X-ray 330 A A/B/C/D 1-515 PDB
2VRT X-ray 350 A A/B/C/D 1-509 PDB
3GCM X-ray 250 A D/E/F 1021-1061 PDB
3GME X-ray 240 A D 1021-1061 PDB
3H1C X-ray 357 A D/E/F/H/J/L/N/P/S/U/W/Y 1021-1061 PDB
3H8A X-ray 190 A E/F 823-850 PDB
5F6C X-ray 300 A PDB
6G63 X-ray 395 A A/G/L/N 1-510 PDB
8B0J EM 399 A L/N 1-598 PDB
AF-P21513-F1 Predicted AlphaFoldDB

No variants for P21513

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P21513

No associated diseases with P21513

14 regional properties for P21513

Type Name Position InterPro Accession
domain Protein kinase domain 825 - 1097 IPR000719
domain EGF-like domain 216 - 252 IPR000742-1
domain EGF-like domain 267 - 299 IPR000742-2
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 825 - 1092 IPR001245
domain Laminin-type EGF domain 230 - 275 IPR002049-1
domain Laminin-type EGF domain 314 - 342 IPR002049-2
domain Fibronectin type III 444 - 541 IPR003961-1
domain Fibronectin type III 543 - 637 IPR003961-2
domain Fibronectin type III 640 - 735 IPR003961-3
domain Immunoglobulin-like domain 350 - 440 IPR007110
active_site Tyrosine-protein kinase, active site 961 - 973 IPR008266
binding_site Protein kinase, ATP binding site 831 - 856 IPR017441
domain Tyrosine-protein kinase, receptor Tie-2, Ig-like domain 1, N-terminal 24 - 118 IPR018941
domain Tyrosine-protein kinase, catalytic domain 825 - 1093 IPR020635

Functions

Description
EC Number 3.1.26.12 Endoribonucleases producing 5'-phosphomonoesters
Subcellular Localization
  • Cytoplasm
  • Cell inner membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Associated with the cytoplasmic membrane via the N- and C-terminal regions
PANTHER Family PTHR30001 RIBONUCLEASE
PANTHER Subfamily PTHR30001:SF1 RIBONUCLEASE E_G-LIKE PROTEIN, CHLOROPLASTIC
PANTHER Protein Class endoribonuclease
RNA metabolism protein
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
bacterial degradosome The degradosome is a protein complex playing a key role in mRNA degradation and RNA processing. It includes a RNA helicase, a 3'-5' phosphate-dependent PNPase and a RNase E bound-enolase.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoplasmic side of plasma membrane The leaflet the plasma membrane that faces the cytoplasm and any proteins embedded or anchored in it or attached to its surface.
endoribonuclease complex A protein complex which is capable of endoribonuclease activity.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

13 GO annotations of molecular function

Name Definition
7S RNA binding Binding to a 7S RNA, the RNA component of the signal recognition particle (SRP).
DEAD/H-box RNA helicase binding Binding to a DEAD/H-box RNA helicase.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
endoribonuclease activity Catalysis of the hydrolysis of ester linkages within ribonucleic acid by creating internal breaks.
identical protein binding Binding to an identical protein or proteins.
magnesium ion binding Binding to a magnesium (Mg) ion.
molecular adaptor activity The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.
ribonuclease activity Catalysis of the hydrolysis of phosphodiester bonds in chains of RNA.
ribonuclease E activity Catalysis of the cleavage of single-stranded RNA that is monophosphorylated at its 5'-end; cleavage occurs predominantly at 5 nucleotides from the 5'-end and in A + U-rich regions, and is blocked by the presence of a 5'-triphosphate group.
RNA binding Binding to an RNA molecule or a portion thereof.
rRNA binding Binding to a ribosomal RNA.
tRNA binding Binding to a transfer RNA.
zinc ion binding Binding to a zinc ion (Zn).

7 GO annotations of biological process

Name Definition
mRNA catabolic process The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes.
regulation of RNA helicase activity Any process that modulates the frequency, rate or extent of ATP-dependent RNA helicase activity.
RNA catabolic process The chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage.
RNA processing Any process involved in the conversion of one or more primary RNA transcripts into one or more mature RNA molecules.
rRNA 5'-end processing Any process involved in forming the mature 5' end of an rRNA molecule.
rRNA processing Any process involved in the conversion of a primary ribosomal RNA (rRNA) transcript into one or more mature rRNA molecules.
tRNA processing The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
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