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Protein

Ribonuclease I

Gene

rna

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

One of the few RNases that cleaves the phosphodiester bond between any two nucleotide. Shows a preference for cytidylic or guanylic acid.

Catalytic activityi

Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei78By similarity1
Active sitei152By similarity1
Active sitei156By similarity1

GO - Molecular functioni

  • endonuclease activity Source: EcoCyc
  • Enterobacter ribonuclease activity Source: UniProtKB-EC
  • ribonuclease T2 activity Source: InterPro
  • RNA binding Source: InterPro

GO - Biological processi

  • RNA catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Enzyme and pathway databases

BioCyciEcoCyc:EG10856-MONOMER.
ECOL316407:JW0603-MONOMER.
MetaCyc:EG10856-MONOMER.
BRENDAi3.1.27.5. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease I (EC:3.1.27.6)
Short name:
RNase I
Alternative name(s):
Enterobacter ribonuclease
Gene namesi
Name:rna
Synonyms:rnsA
Ordered Locus Names:b0611, JW0603
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10856. rna.

Subcellular locationi

  • Periplasm
  • Cytoplasm

  • Note: RNase I (periplasmic) and RNase I* (cytoplasmic) appear to be isoforms apparently encoded by the same gene. The cytoplasmic form is less active towards natural polymer RNA.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 231 PublicationAdd BLAST23
ChainiPRO_000003096124 – 268Ribonuclease IAdd BLAST245

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi103 ↔ 159By similarity

Post-translational modificationi

Contains four disulfide bonds.By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP21338.
PRIDEiP21338.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4259901. 6 interactors.
IntActiP21338. 1 interactor.
MINTiMINT-1292710.
STRINGi511145.b0611.

Structurei

Secondary structure

1268
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 31Combined sources3
Beta strandi36 – 43Combined sources8
Helixi44 – 53Combined sources10
Helixi60 – 63Combined sources4
Helixi71 – 74Combined sources4
Beta strandi75 – 82Combined sources8
Helixi86 – 89Combined sources4
Turni90 – 92Combined sources3
Helixi95 – 101Combined sources7
Helixi102 – 104Combined sources3
Turni106 – 109Combined sources4
Helixi116 – 121Combined sources6
Helixi129 – 138Combined sources10
Turni144 – 146Combined sources3
Helixi148 – 156Combined sources9
Helixi158 – 160Combined sources3
Helixi164 – 180Combined sources17
Helixi182 – 189Combined sources8
Turni190 – 192Combined sources3
Beta strandi193 – 196Combined sources4
Helixi197 – 208Combined sources12
Helixi210 – 215Combined sources6
Beta strandi216 – 221Combined sources6
Turni222 – 225Combined sources4
Beta strandi226 – 235Combined sources10
Helixi236 – 238Combined sources3
Beta strandi255 – 257Combined sources3
Beta strandi259 – 262Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EA1X-ray1.80A24-268[»]
2PQXX-ray1.42A24-268[»]
2PQYX-ray2.30A24-268[»]
2Z70X-ray1.70A24-268[»]
ProteinModelPortaliP21338.
SMRiP21338.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21338.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase T2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105KTS. Bacteria.
COG3719. LUCA.
HOGENOMiHOG000117890.
InParanoidiP21338.
KOiK01169.
OMAiTRPIPNM.

Family and domain databases

Gene3Di3.90.730.10. 1 hit.
InterProiIPR001568. RNase_T2-like.
IPR018188. RNase_T2_His_AS_1.
IPR033130. RNase_T2_His_AS_2.
[Graphical view]
PfamiPF00445. Ribonuclease_T2. 1 hit.
[Graphical view]
SUPFAMiSSF55895. SSF55895. 1 hit.
PROSITEiPS00530. RNASE_T2_1. 1 hit.
PS00531. RNASE_T2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21338-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAFWRNAAL LAVSLLPFSS ANALALQAKQ YGDFDRYVLA LSWQTGFCQS
60 70 80 90 100
QHDRNRNERD ECRLQTETTN KADFLTVHGL WPGLPKSVAA RGVDERRWMR
110 120 130 140 150
FGCATRPIPN LPEARASRMC SSPETGLSLE TAAKLSEVMP GAGGRSCLER
160 170 180 190 200
YEYAKHGACF GFDPDAYFGT MVRLNQEIKE SEAGKFLADN YGKTVSRRDF
210 220 230 240 250
DAAFAKSWGK ENVKAVKLTC QGNPAYLTEI QISIKADAIN APLSANSFLP
260
QPHPGNCGKT FVIDKAGY
Length:268
Mass (Da):29,618
Last modified:May 1, 1991 - v1
Checksum:i56BC290438EE3DD0
GO

Sequence cautioni

The sequence AAB40811 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55687 Genomic DNA. Translation: AAA24548.1.
U82598 Genomic DNA. Translation: AAB40811.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73712.1.
AP009048 Genomic DNA. Translation: BAA35240.1.
PIRiJQ0777.
RefSeqiNP_415144.1. NC_000913.3.
WP_000643397.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73712; AAC73712; b0611.
BAA35240; BAA35240; BAA35240.
GeneIDi949065.
KEGGiecj:JW0603.
eco:b0611.
PATRICi32116402. VBIEscCol129921_0641.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55687 Genomic DNA. Translation: AAA24548.1.
U82598 Genomic DNA. Translation: AAB40811.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73712.1.
AP009048 Genomic DNA. Translation: BAA35240.1.
PIRiJQ0777.
RefSeqiNP_415144.1. NC_000913.3.
WP_000643397.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EA1X-ray1.80A24-268[»]
2PQXX-ray1.42A24-268[»]
2PQYX-ray2.30A24-268[»]
2Z70X-ray1.70A24-268[»]
ProteinModelPortaliP21338.
SMRiP21338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259901. 6 interactors.
IntActiP21338. 1 interactor.
MINTiMINT-1292710.
STRINGi511145.b0611.

Proteomic databases

PaxDbiP21338.
PRIDEiP21338.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73712; AAC73712; b0611.
BAA35240; BAA35240; BAA35240.
GeneIDi949065.
KEGGiecj:JW0603.
eco:b0611.
PATRICi32116402. VBIEscCol129921_0641.

Organism-specific databases

EchoBASEiEB0849.
EcoGeneiEG10856. rna.

Phylogenomic databases

eggNOGiENOG4105KTS. Bacteria.
COG3719. LUCA.
HOGENOMiHOG000117890.
InParanoidiP21338.
KOiK01169.
OMAiTRPIPNM.

Enzyme and pathway databases

BioCyciEcoCyc:EG10856-MONOMER.
ECOL316407:JW0603-MONOMER.
MetaCyc:EG10856-MONOMER.
BRENDAi3.1.27.5. 2026.

Miscellaneous databases

EvolutionaryTraceiP21338.
PROiP21338.

Family and domain databases

Gene3Di3.90.730.10. 1 hit.
InterProiIPR001568. RNase_T2-like.
IPR018188. RNase_T2_His_AS_1.
IPR033130. RNase_T2_His_AS_2.
[Graphical view]
PfamiPF00445. Ribonuclease_T2. 1 hit.
[Graphical view]
SUPFAMiSSF55895. SSF55895. 1 hit.
PROSITEiPS00530. RNASE_T2_1. 1 hit.
PS00531. RNASE_T2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRNI_ECOLI
AccessioniPrimary (citable) accession number: P21338
Secondary accession number(s): P77101
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: November 2, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.