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Protein

3'-5' exoribonuclease 1

Gene

Eri1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Binds with high affinity to the 3' side of the stem-loop structure and to the downstream cleavage product (DCP) of histone pre-mRNAs. Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA (By similarity).By similarity

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Enzyme regulationi

Although it can bind simultaneously with SLBP to the 3'-end of histone mRNA, the presence of SLBP prevents the exonuclease activity.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi130Magnesium 1By similarity1
Metal bindingi130Magnesium 2By similarity1
Active sitei132Proton acceptorSequence analysis1
Metal bindingi132Magnesium 1By similarity1
Binding sitei132AMPBy similarity1
Binding sitei133AMP; via amide nitrogen and carbonyl oxygenBy similarity1
Metal bindingi230Magnesium 2By similarity1
Active sitei289Proton acceptorSequence analysis1
Binding sitei289AMPBy similarity1
Metal bindingi294Magnesium 1By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

RNA-mediated gene silencing, rRNA processing

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-RNO-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
3'-5' exoribonuclease 1 (EC:3.1.-.-)
Alternative name(s):
Histone mRNA 3'-exonuclease 1
Gene namesi
Name:Eri1
Synonyms:Thex1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi1308378. Eri1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001870091 – 3453'-5' exoribonuclease 1Add BLAST345

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei58PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5FVR4.
PRIDEiQ5FVR4.

Expressioni

Gene expression databases

BgeeiENSRNOG00000011448.
GenevisibleiQ5FVR4. RN.

Interactioni

Subunit structurei

Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Binds to 40S and 60S ribosomal subunits and to 80S assembled ribosomes. Interacts in a cooperative manner with SLBP to the mature 3'-end of histone mRNAs. Found in a ternary complex with SLBP and the stem-loop structure of the 3'-end of histone mRNAs (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015239.

Structurei

3D structure databases

ProteinModelPortaliQ5FVR4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini72 – 106SAPPROSITE-ProRule annotationAdd BLAST35
Domaini126 – 302ExonucleaseSequence analysisAdd BLAST177

Domaini

The SAP domain is necessary for binding to the stem-loop structure of histone mRNAs and to form the ternary complex with SLBP, but not for 3'-end histone mRNA exonuclease activity.By similarity

Sequence similaritiesi

Contains 1 exonuclease domain.Sequence analysis
Contains 1 SAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0542. Eukaryota.
COG5018. LUCA.
GeneTreeiENSGT00530000063205.
HOGENOMiHOG000006635.
HOVERGENiHBG048925.
InParanoidiQ5FVR4.
KOiK18416.
OMAiFLNIQCR.
OrthoDBiEOG091G0ISP.
PhylomeDBiQ5FVR4.
TreeFamiTF313449.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
IPR003034. SAP_dom.
[Graphical view]
PfamiPF00929. RNase_T. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00479. EXOIII. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS50800. SAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5FVR4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDERGREHG GDAAQQKTPR PECEESRPLS VEKKQRCRLD GKDTDGSKFI
60 70 80 90 100
TSNGGDFSDP VYKEIAMTNG CINRMSKEEL RAKLSEFKLE TRGVKDVLKK
110 120 130 140 150
RLKNYYKKQK LMLKESNAVD SYYDYICIID FEATCEEGNP AEFLHEIIEF
160 170 180 190 200
PVVLLNTHSL EIEDTFQQYV RPEVNSQLSE FCIGLTGITQ DQVDRADAFP
210 220 230 240 250
QVLKKVIEWM KSKELGTKYK YCILTDGSWD MSKFLNIQCQ LSRLKYPSFA
260 270 280 290 300
KKWINIRKSY GNFYKVPRSQ TKLTIMLEKL GMDYDGRPHS GLDDSKNIAR
310 320 330 340
IAVRMLQDGC ELRINEKLHG GQLMSVSSSL PVEGAPAPQM PHSRK
Length:345
Mass (Da):39,580
Last modified:March 1, 2005 - v1
Checksum:i50DE97E5A8E60E43
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC089828 mRNA. Translation: AAH89828.1.
RefSeqiNP_001014165.1. NM_001014143.1.
UniGeneiRn.17469.

Genome annotation databases

EnsembliENSRNOT00000015239; ENSRNOP00000015239; ENSRNOG00000011448.
GeneIDi361159.
KEGGirno:361159.
UCSCiRGD:1308378. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC089828 mRNA. Translation: AAH89828.1.
RefSeqiNP_001014165.1. NM_001014143.1.
UniGeneiRn.17469.

3D structure databases

ProteinModelPortaliQ5FVR4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015239.

Proteomic databases

PaxDbiQ5FVR4.
PRIDEiQ5FVR4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015239; ENSRNOP00000015239; ENSRNOG00000011448.
GeneIDi361159.
KEGGirno:361159.
UCSCiRGD:1308378. rat.

Organism-specific databases

CTDi90459.
RGDi1308378. Eri1.

Phylogenomic databases

eggNOGiKOG0542. Eukaryota.
COG5018. LUCA.
GeneTreeiENSGT00530000063205.
HOGENOMiHOG000006635.
HOVERGENiHBG048925.
InParanoidiQ5FVR4.
KOiK18416.
OMAiFLNIQCR.
OrthoDBiEOG091G0ISP.
PhylomeDBiQ5FVR4.
TreeFamiTF313449.

Enzyme and pathway databases

ReactomeiR-RNO-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.

Miscellaneous databases

PROiQ5FVR4.

Gene expression databases

BgeeiENSRNOG00000011448.
GenevisibleiQ5FVR4. RN.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
IPR003034. SAP_dom.
[Graphical view]
PfamiPF00929. RNase_T. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00479. EXOIII. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS50800. SAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiERI1_RAT
AccessioniPrimary (citable) accession number: Q5FVR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: March 1, 2005
Last modified: November 30, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.