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Protein

Ribonuclease 3

Gene

rnc

Organism
Francisella tularensis subsp. novicida (strain U112)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon (By similarity).By similarity
CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). In this organism endogenous ribonuclease 3 and Cas9 are required for correct coprocessing of pre-crRNA and the trans-encoded small RNA (tracrRNA). Cas9, crRNA and tracrRNA are required for cleavage of invading DNA (Probable). Complements pre-crRNA and tracrRNA coprocessing defects in an rnc deletion in S.pyogenes strain 370 (PubMed:24270795).Curated1 Publication

Catalytic activityi

Endonucleolytic cleavage to 5'-phosphomonoester.UniRule annotation

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401MagnesiumUniRule annotation
Active sitei44 – 441UniRule annotation
Metal bindingi111 – 1111MagnesiumUniRule annotation
Active sitei114 – 1141UniRule annotation
Metal bindingi114 – 1141MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

mRNA processing, rRNA processing, tRNA processing

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciFNOV401614:GC4M-1462-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease 3UniRule annotation (EC:3.1.26.3UniRule annotation)
Alternative name(s):
Ribonuclease IIIUniRule annotation
Short name:
RNase IIIUniRule annotation
Gene namesi
Name:rncUniRule annotation
Ordered Locus Names:FTN_1463
OrganismiFrancisella tularensis subsp. novicida (strain U112)
Taxonomic identifieri401614 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
ProteomesiUP000000762 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 230230Ribonuclease 3PRO_1000075757Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA0Q7W6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 125121RNase IIIUniRule annotationAdd
BLAST
Domaini153 – 22371DRBMUniRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 DRBM (double-stranded RNA-binding) domain.UniRule annotation
Contains 1 RNase III domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0571.
HOGENOMiHOG000246809.
KOiK03685.
OMAiSADHNER.
OrthoDBiEOG6T1WVS.

Family and domain databases

Gene3Di1.10.1520.10. 1 hit.
3.30.160.20. 1 hit.
HAMAPiMF_00104. RNase_III.
InterProiIPR014720. dsRNA-bd_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]
PfamiPF00035. dsrm. 1 hit.
PF14622. Ribonucleas_3_3. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 1 hit.
SM00535. RIBOc. 1 hit.
[Graphical view]
SUPFAMiSSF69065. SSF69065. 1 hit.
TIGRFAMsiTIGR02191. RNaseIII. 1 hit.
PROSITEiPS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A0Q7W6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPEYSRFYN ILGYNFKDYT LLIRALTHRS KTKKNYERLE FLGDSVLSFV
60 70 80 90 100
IAEVLYKQFT DLAEGKLSQL RSKLVKGTTL AQLASSLKMD EYIILGASEQ
110 120 130 140 150
GGHKREKILE DVFEAVIGAI YLDSDFATVK KVILKWYQPI ISSINLDTIK
160 170 180 190 200
VKDSKSKLQE ILLQNALSLP EYSIETIDGK DHEQQFTVVA MSKDLNLRVK
210 220 230
AQGTSRKKAE QKAAEKMIEM LSQQGLHEKK
Length:230
Mass (Da):26,229
Last modified:January 9, 2007 - v1
Checksum:iFC742D0460DF4859
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000439 Genomic DNA. Translation: ABK90331.1.
RefSeqiWP_003034807.1. NC_008601.1.
YP_899085.1. NC_008601.1.

Genome annotation databases

EnsemblBacteriaiABK90331; ABK90331; FTN_1463.
KEGGiftn:FTN_1463.
PATRICi17936089. VBIFraNov128299_1496.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000439 Genomic DNA. Translation: ABK90331.1.
RefSeqiWP_003034807.1. NC_008601.1.
YP_899085.1. NC_008601.1.

3D structure databases

ProteinModelPortaliA0Q7W6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK90331; ABK90331; FTN_1463.
KEGGiftn:FTN_1463.
PATRICi17936089. VBIFraNov128299_1496.

Phylogenomic databases

eggNOGiCOG0571.
HOGENOMiHOG000246809.
KOiK03685.
OMAiSADHNER.
OrthoDBiEOG6T1WVS.

Enzyme and pathway databases

BioCyciFNOV401614:GC4M-1462-MONOMER.

Family and domain databases

Gene3Di1.10.1520.10. 1 hit.
3.30.160.20. 1 hit.
HAMAPiMF_00104. RNase_III.
InterProiIPR014720. dsRNA-bd_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]
PfamiPF00035. dsrm. 1 hit.
PF14622. Ribonucleas_3_3. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 1 hit.
SM00535. RIBOc. 1 hit.
[Graphical view]
SUPFAMiSSF69065. SSF69065. 1 hit.
TIGRFAMsiTIGR02191. RNaseIII. 1 hit.
PROSITEiPS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: U112.
  2. "Phylogeny of Cas9 determines functional exchangeability of dual-RNA and Cas9 among orthologous type II CRISPR-Cas systems."
    Fonfara I., Le Rhun A., Chylinski K., Makarova K.S., Lecrivain A.L., Bzdrenga J., Koonin E.V., Charpentier E.
    Nucleic Acids Res. 42:2577-2590(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: U112.

Entry informationi

Entry nameiRNC_FRATN
AccessioniPrimary (citable) accession number: A0Q7W6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 9, 2007
Last modified: June 24, 2015
This is version 58 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.