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Protein

Exoribonuclease 2

Gene

rnb

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

Functioni

Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction.1 Publication

Catalytic activityi

Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.

Cofactori

Mg2+1 Publication

Enzyme regulationi

Stimulated by the presence of a monovalent cation.1 Publication

Kineticsi

    1. Vmax=109800 nmol/min/mg enzyme with Poly(A) as substrate1 Publication
    2. Vmax=160 nmol/min/mg enzyme with 23S rRNA as substrate1 Publication
    3. Vmax=30 nmol/min/mg enzyme with 16S rRNA as substrate1 Publication
    4. Vmax=20 nmol/min/mg enzyme with 5S rRNA as substrate1 Publication

    pH dependencei

    Optimum pH is 7.5-9.5.1 Publication

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius.1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Exonuclease, Hydrolase, Nuclease

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11620-MONOMER.
    ECOL316407:JW1279-MONOMER.
    MetaCyc:EG11620-MONOMER.
    BRENDAi3.1.13.1. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exoribonuclease 2 (EC:3.1.13.1)
    Alternative name(s):
    Exoribonuclease II
    Short name:
    RNase II
    Short name:
    Ribonuclease II
    Gene namesi
    Name:rnb
    Ordered Locus Names:b1286, JW1279
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11620. rnb.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    • exosome (RNase complex) Source: GO_Central
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001663801 – 644Exoribonuclease 2Add BLAST644

    Proteomic databases

    PaxDbiP30850.
    PRIDEiP30850.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rpsEP0A7W12EBI-557325,EBI-543949

    Protein-protein interaction databases

    BioGridi4263341. 12 interactors.
    DIPiDIP-10724N.
    IntActiP30850. 10 interactors.
    MINTiMINT-1248196.
    STRINGi511145.b1286.

    Structurei

    Secondary structure

    1644
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi6 – 17Combined sources12
    Beta strandi21 – 27Combined sources7
    Beta strandi30 – 32Combined sources3
    Beta strandi34 – 37Combined sources4
    Beta strandi39 – 41Combined sources3
    Beta strandi43 – 46Combined sources4
    Helixi48 – 51Combined sources4
    Beta strandi59 – 65Combined sources7
    Beta strandi68 – 70Combined sources3
    Beta strandi72 – 80Combined sources9
    Beta strandi84 – 93Combined sources10
    Beta strandi96 – 103Combined sources8
    Beta strandi110 – 114Combined sources5
    Beta strandi127 – 134Combined sources8
    Helixi136 – 138Combined sources3
    Beta strandi144 – 152Combined sources9
    Helixi159 – 167Combined sources9
    Beta strandi198 – 201Combined sources4
    Beta strandi210 – 214Combined sources5
    Beta strandi218 – 220Combined sources3
    Beta strandi222 – 229Combined sources8
    Helixi231 – 233Combined sources3
    Helixi240 – 248Combined sources9
    Beta strandi252 – 254Combined sources3
    Beta strandi257 – 259Combined sources3
    Helixi264 – 267Combined sources4
    Turni268 – 270Combined sources3
    Beta strandi278 – 288Combined sources11
    Beta strandi300 – 306Combined sources7
    Beta strandi310 – 312Combined sources3
    Helixi313 – 319Combined sources7
    Helixi331 – 354Combined sources24
    Beta strandi364 – 368Combined sources5
    Beta strandi374 – 379Combined sources6
    Helixi384 – 407Combined sources24
    Beta strandi413 – 416Combined sources4
    Turni421 – 423Combined sources3
    Helixi424 – 434Combined sources11
    Helixi440 – 443Combined sources4
    Helixi446 – 457Combined sources12
    Beta strandi459 – 462Combined sources4
    Helixi463 – 468Combined sources6
    Helixi469 – 471Combined sources3
    Beta strandi476 – 480Combined sources5
    Turni485 – 488Combined sources4
    Beta strandi489 – 491Combined sources3
    Turni498 – 500Combined sources3
    Helixi502 – 514Combined sources13
    Helixi527 – 554Combined sources28
    Helixi555 – 557Combined sources3
    Beta strandi564 – 572Combined sources9
    Beta strandi575 – 580Combined sources6
    Turni581 – 583Combined sources3
    Beta strandi586 – 590Combined sources5
    Helixi591 – 593Combined sources3
    Helixi598 – 600Combined sources3
    Beta strandi601 – 604Combined sources4
    Turni605 – 608Combined sources4
    Beta strandi609 – 612Combined sources4
    Beta strandi615 – 619Combined sources5
    Beta strandi623 – 632Combined sources10
    Turni633 – 636Combined sources4
    Beta strandi637 – 642Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2ID0X-ray2.35A/B/C/D1-644[»]
    2IX0X-ray2.44A6-644[»]
    2IX1X-ray2.74A6-644[»]
    ProteinModelPortaliP30850.
    SMRiP30850.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30850.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini561 – 643S1 motifAdd BLAST83

    Sequence similaritiesi

    Contains 1 S1 motif domain.Curated

    Phylogenomic databases

    eggNOGiENOG4108IEC. Bacteria.
    COG4776. LUCA.
    HOGENOMiHOG000271427.
    InParanoidiP30850.
    KOiK01147.
    OMAiICLSRGE.
    PhylomeDBiP30850.

    Family and domain databases

    HAMAPiMF_01036. RNase_II. 1 hit.
    InterProiIPR011129. Cold_shock_prot.
    IPR012340. NA-bd_OB-fold.
    IPR013223. RNase_B_OB_dom.
    IPR011804. RNase_II.
    IPR022966. RNase_II/R_CS.
    IPR004476. RNase_II/RNase_R.
    IPR003029. S1_domain.
    [Graphical view]
    PfamiPF08206. OB_RNB. 1 hit.
    PF00575. S1. 1 hit.
    [Graphical view]
    SMARTiSM00357. CSP. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 4 hits.
    TIGRFAMsiTIGR00358. 3_prime_RNase. 1 hit.
    TIGR02062. RNase_B. 1 hit.
    PROSITEiPS01175. RIBONUCLEASE_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P30850-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MFQDNPLLAQ LKQQLHSQTP RAEGVVKATE KGFGFLEVDA QKSYFIPPPQ
    60 70 80 90 100
    MKKVMHGDRI IAVIHSEKER ESAEPEELVE PFLTRFVGKV QGKNDRLAIV
    110 120 130 140 150
    PDHPLLKDAI PCRAARGLNH EFKEGDWAVA EMRRHPLKGD RSFYAELTQY
    160 170 180 190 200
    ITFGDDHFVP WWVTLARHNL EKEAPDGVAT EMLDEGLVRE DLTALDFVTI
    210 220 230 240 250
    DSASTEDMDD ALFAKALPDD KLQLIVAIAD PTAWIAEGSK LDKAAKIRAF
    260 270 280 290 300
    TNYLPGFNIP MLPRELSDDL CSLRANEVRP VLACRMTLSA DGTIEDNIEF
    310 320 330 340 350
    FAATIESKAK LVYDQVSDWL ENTGDWQPES EAIAEQVRLL AQICQRRGEW
    360 370 380 390 400
    RHNHALVFKD RPDYRFILGE KGEVLDIVAE PRRIANRIVE EAMIAANICA
    410 420 430 440 450
    ARVLRDKLGF GIYNVHMGFD PANADALAAL LKTHGLHVDA EEVLTLDGFC
    460 470 480 490 500
    KLRRELDAQP TGFLDSRIRR FQSFAEISTE PGPHFGLGLE AYATWTSPIR
    510 520 530 540 550
    KYGDMINHRL LKAVIKGETA TRPQDEITVQ MAERRRLNRM AERDVGDWLY
    560 570 580 590 600
    ARFLKDKAGT DTRFAAEIVD ISRGGMRVRL VDNGAIAFIP APFLHAVRDE
    610 620 630 640
    LVCSQENGTV QIKGETVYKV TDVIDVTIAE VRMETRSIIA RPVA
    Length:644
    Mass (Da):72,491
    Last modified:November 1, 1997 - v3
    Checksum:i36B16712CDF14394
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti384I → N in CAA48112 (PubMed:8497196).Curated1
    Sequence conflicti399C → G in CAA48112 (PubMed:8497196).Curated1
    Sequence conflicti513A → R in CAA48112 (PubMed:8497196).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X67913 Genomic DNA. Translation: CAA48112.1.
    U00096 Genomic DNA. Translation: AAC74368.1.
    AP009048 Genomic DNA. Translation: BAA14840.1.
    PIRiA64877.
    RefSeqiNP_415802.1. NC_000913.3.
    WP_000484984.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74368; AAC74368; b1286.
    BAA14840; BAA14840; BAA14840.
    GeneIDi945864.
    KEGGiecj:JW1279.
    eco:b1286.
    PATRICi32117840. VBIEscCol129921_1340.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X67913 Genomic DNA. Translation: CAA48112.1.
    U00096 Genomic DNA. Translation: AAC74368.1.
    AP009048 Genomic DNA. Translation: BAA14840.1.
    PIRiA64877.
    RefSeqiNP_415802.1. NC_000913.3.
    WP_000484984.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2ID0X-ray2.35A/B/C/D1-644[»]
    2IX0X-ray2.44A6-644[»]
    2IX1X-ray2.74A6-644[»]
    ProteinModelPortaliP30850.
    SMRiP30850.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263341. 12 interactors.
    DIPiDIP-10724N.
    IntActiP30850. 10 interactors.
    MINTiMINT-1248196.
    STRINGi511145.b1286.

    Proteomic databases

    PaxDbiP30850.
    PRIDEiP30850.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74368; AAC74368; b1286.
    BAA14840; BAA14840; BAA14840.
    GeneIDi945864.
    KEGGiecj:JW1279.
    eco:b1286.
    PATRICi32117840. VBIEscCol129921_1340.

    Organism-specific databases

    EchoBASEiEB1577.
    EcoGeneiEG11620. rnb.

    Phylogenomic databases

    eggNOGiENOG4108IEC. Bacteria.
    COG4776. LUCA.
    HOGENOMiHOG000271427.
    InParanoidiP30850.
    KOiK01147.
    OMAiICLSRGE.
    PhylomeDBiP30850.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11620-MONOMER.
    ECOL316407:JW1279-MONOMER.
    MetaCyc:EG11620-MONOMER.
    BRENDAi3.1.13.1. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP30850.
    PROiP30850.

    Family and domain databases

    HAMAPiMF_01036. RNase_II. 1 hit.
    InterProiIPR011129. Cold_shock_prot.
    IPR012340. NA-bd_OB-fold.
    IPR013223. RNase_B_OB_dom.
    IPR011804. RNase_II.
    IPR022966. RNase_II/R_CS.
    IPR004476. RNase_II/RNase_R.
    IPR003029. S1_domain.
    [Graphical view]
    PfamiPF08206. OB_RNB. 1 hit.
    PF00575. S1. 1 hit.
    [Graphical view]
    SMARTiSM00357. CSP. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 4 hits.
    TIGRFAMsiTIGR00358. 3_prime_RNase. 1 hit.
    TIGR02062. RNase_B. 1 hit.
    PROSITEiPS01175. RIBONUCLEASE_II. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiRNB_ECOLI
    AccessioniPrimary (citable) accession number: P30850
    Secondary accession number(s): P78280
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: November 1, 1997
    Last modified: November 2, 2016
    This is version 152 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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.