Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribonuclease T

Gene

rnt

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

Functioni

Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis, especially in strains lacking other exoribonucleases.UniRule annotation3 Publications

Cofactori

Mg2+UniRule annotation4 PublicationsNote: Binds two Mg2+ per subunit. The active form of the enzyme binds two Mg2+ ions in its active site. The first Mg2+ forms only one salt bridge with the protein.UniRule annotation4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi23Magnesium 1; catalytic1
Metal bindingi23Magnesium 2; catalytic1
Metal bindingi25Magnesium 2; catalytic1
Sitei29Important for substrate binding and specificity1
Sitei73Important for substrate binding and specificity1
Sitei77Important for substrate binding and specificity1
Sitei124Important for substrate binding and specificity1
Sitei146Important for substrate binding and specificity1
Active sitei181Proton donor/acceptorUniRule annotation2 Publications1
Metal bindingi181Magnesium 2; catalytic1
Metal bindingi186Magnesium 2; catalytic1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11547-MONOMER.
ECOL316407:JW1644-MONOMER.
MetaCyc:EG11547-MONOMER.
BRENDAi3.1.13.3. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease TUniRule annotation (EC:3.1.13.-UniRule annotation)
Alternative name(s):
Exoribonuclease TUniRule annotation
Short name:
RNase TUniRule annotation
Gene namesi
Name:rntUniRule annotation
Ordered Locus Names:b1652, JW1644
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11547. rnt.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Required for optimal growth.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi13R → A: Strongly reduces affinity for RNA. Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi15R → A: Strongly reduces affinity for RNA. 1 Publication1
Mutagenesisi23D → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi25E → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi29F → A: Abolishes enzyme activity; when associated with A-73 and A-77. 1 Publication1
Mutagenesisi73E → A: Reduces enzyme activity. Abolishes enzyme activity; when associated with A-29 and A-77. 1 Publication1
Mutagenesisi77F → A: Abolishes enzyme activity; when associated with A-29 and A-73. 1 Publication1
Mutagenesisi108K → A: Strongly reduces affinity for RNA. 1 Publication1
Mutagenesisi114R → A: Strongly reduces affinity for RNA. 1 Publication1
Mutagenesisi124F → A: Abolishes enzyme activity; when associated with A-146. 1 Publication1
Mutagenesisi139K → A: Reduces affinity for RNA. 1 Publication1
Mutagenesisi146F → A: Abolishes enzyme activity; when associated with A-124. 1 Publication1
Mutagenesisi150D → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi181H → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi186D → A: Nearly abolishes enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002089601 – 215Ribonuclease TAdd BLAST215

Proteomic databases

PaxDbiP30014.
PRIDEiP30014.

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Protein-protein interaction databases

BioGridi4260267. 143 interactors.
DIPiDIP-10734N.
IntActiP30014. 2 interactors.
MINTiMINT-1248458.
STRINGi511145.b1652.

Structurei

Secondary structure

1215
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 7Combined sources3
Helixi10 – 13Combined sources4
Turni14 – 16Combined sources3
Beta strandi17 – 29Combined sources13
Turni31 – 33Combined sources3
Beta strandi36 – 46Combined sources11
Beta strandi48 – 50Combined sources3
Beta strandi52 – 62Combined sources11
Helixi72 – 78Combined sources7
Helixi85 – 87Combined sources3
Helixi92 – 107Combined sources16
Turni108 – 111Combined sources4
Beta strandi114 – 119Combined sources6
Turni120 – 122Combined sources3
Helixi123 – 135Combined sources13
Beta strandi143 – 150Combined sources8
Helixi151 – 159Combined sources9
Helixi164 – 171Combined sources8
Turni177 – 181Combined sources5
Helixi183 – 203Combined sources21
Helixi211 – 213Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IS3X-ray3.10A/B/C/D1-215[»]
3NGYX-ray2.20A/B/C/D1-215[»]
3NGZX-ray2.10A/B1-215[»]
3NH0X-ray2.30A/B1-215[»]
3NH1X-ray2.11A/B/C/D1-215[»]
3NH2X-ray2.30A/B/E/F1-215[»]
3V9SX-ray2.10A/B1-215[»]
3V9UX-ray2.30A/B/C/D1-215[»]
3V9WX-ray1.70A/B/C/D1-215[»]
3V9XX-ray1.90A/B/C/D1-215[»]
3V9ZX-ray1.80A/B1-215[»]
3VA0X-ray2.20A/B1-215[»]
3VA3X-ray2.71A/B1-215[»]
4KAZX-ray1.90A1-215[»]
4KB0X-ray2.00A/B1-215[»]
4KB1X-ray1.80A/B1-215[»]
ProteinModelPortaliP30014.
SMRiP30014.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30014.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 194ExonucleaseUniRule annotationAdd BLAST175

Sequence similaritiesi

Belongs to the RNase T family.UniRule annotation
Contains 1 exonuclease domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DH5. Bacteria.
COG0847. LUCA.
HOGENOMiHOG000279358.
InParanoidiP30014.
KOiK03683.
OMAiCYMVNHL.
PhylomeDBiP30014.

Family and domain databases

CDDicd06134. RNaseT. 1 hit.
Gene3Di3.30.420.10. 1 hit.
HAMAPiMF_00157. RNase_T. 1 hit.
InterProiIPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR005987. RNase_T.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF00929. RNase_T. 1 hit.
[Graphical view]
SMARTiSM00479. EXOIII. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
TIGRFAMsiTIGR01298. RNaseT. 1 hit.

Sequencei

Sequence statusi: Complete.

P30014-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDNAQLTGL CDRFRGFYPV VIDVETAGFN AKTDALLEIA AITLKMDEQG
60 70 80 90 100
WLMPDTTLHF HVEPFVGANL QPEALAFNGI DPNDPDRGAV SEYEALHEIF
110 120 130 140 150
KVVRKGIKAS GCNRAIMVAH NANFDHSFMM AAAERASLKR NPFHPFATFD
160 170 180 190 200
TAALAGLALG QTVLSKACQT AGMDFDSTQA HSALYDTERT AVLFCEIVNR
210
WKRLGGWPLS AAEEV
Length:215
Mass (Da):23,523
Last modified:April 1, 1993 - v1
Checksum:i502C1CCEFABF4B05
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01622 Genomic DNA. Translation: AAC37008.1.
U00096 Genomic DNA. Translation: AAC74724.1.
AP009048 Genomic DNA. Translation: BAA15418.2.
PIRiA45065.
RefSeqiNP_416169.1. NC_000913.3.
WP_001282283.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74724; AAC74724; b1652.
BAA15418; BAA15418; BAA15418.
GeneIDi946159.
KEGGiecj:JW1644.
eco:b1652.
PATRICi32118606. VBIEscCol129921_1723.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01622 Genomic DNA. Translation: AAC37008.1.
U00096 Genomic DNA. Translation: AAC74724.1.
AP009048 Genomic DNA. Translation: BAA15418.2.
PIRiA45065.
RefSeqiNP_416169.1. NC_000913.3.
WP_001282283.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IS3X-ray3.10A/B/C/D1-215[»]
3NGYX-ray2.20A/B/C/D1-215[»]
3NGZX-ray2.10A/B1-215[»]
3NH0X-ray2.30A/B1-215[»]
3NH1X-ray2.11A/B/C/D1-215[»]
3NH2X-ray2.30A/B/E/F1-215[»]
3V9SX-ray2.10A/B1-215[»]
3V9UX-ray2.30A/B/C/D1-215[»]
3V9WX-ray1.70A/B/C/D1-215[»]
3V9XX-ray1.90A/B/C/D1-215[»]
3V9ZX-ray1.80A/B1-215[»]
3VA0X-ray2.20A/B1-215[»]
3VA3X-ray2.71A/B1-215[»]
4KAZX-ray1.90A1-215[»]
4KB0X-ray2.00A/B1-215[»]
4KB1X-ray1.80A/B1-215[»]
ProteinModelPortaliP30014.
SMRiP30014.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260267. 143 interactors.
DIPiDIP-10734N.
IntActiP30014. 2 interactors.
MINTiMINT-1248458.
STRINGi511145.b1652.

Proteomic databases

PaxDbiP30014.
PRIDEiP30014.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74724; AAC74724; b1652.
BAA15418; BAA15418; BAA15418.
GeneIDi946159.
KEGGiecj:JW1644.
eco:b1652.
PATRICi32118606. VBIEscCol129921_1723.

Organism-specific databases

EchoBASEiEB1509.
EcoGeneiEG11547. rnt.

Phylogenomic databases

eggNOGiENOG4105DH5. Bacteria.
COG0847. LUCA.
HOGENOMiHOG000279358.
InParanoidiP30014.
KOiK03683.
OMAiCYMVNHL.
PhylomeDBiP30014.

Enzyme and pathway databases

BioCyciEcoCyc:EG11547-MONOMER.
ECOL316407:JW1644-MONOMER.
MetaCyc:EG11547-MONOMER.
BRENDAi3.1.13.3. 2026.

Miscellaneous databases

EvolutionaryTraceiP30014.
PROiP30014.

Family and domain databases

CDDicd06134. RNaseT. 1 hit.
Gene3Di3.30.420.10. 1 hit.
HAMAPiMF_00157. RNase_T. 1 hit.
InterProiIPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR005987. RNase_T.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF00929. RNase_T. 1 hit.
[Graphical view]
SMARTiSM00479. EXOIII. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
TIGRFAMsiTIGR01298. RNaseT. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRNT_ECOLI
AccessioniPrimary (citable) accession number: P30014
Secondary accession number(s): P76896
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 2, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Member of the DEDD group of RNAses that are characterized by the presence of four acidic residues in the active site. These residues are conserved even when the proteins have highly divergent sequences.

Keywords - Technical termi

3D-structure, Complete proteome, 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.