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Protein

Ribonuclease Z

Gene

rnz

Organism
Bacillus cereus (strain AH187)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.UniRule annotation

Catalytic activityi

Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 2 Zn2+ ions.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Zinc 1; catalyticUniRule annotation
Metal bindingi65 – 651Zinc 1; catalyticUniRule annotation
Active sitei67 – 671Proton acceptorUniRule annotation
Metal bindingi67 – 671Zinc 2; catalyticUniRule annotation
Metal bindingi68 – 681Zinc 2; catalyticUniRule annotation
Metal bindingi141 – 1411Zinc 1; catalyticUniRule annotation
Metal bindingi212 – 2121Zinc 1; catalyticUniRule annotation
Metal bindingi212 – 2121Zinc 2; catalyticUniRule annotation
Metal bindingi270 – 2701Zinc 2; catalyticUniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBCER405534:GHXM-4209-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease ZUniRule annotation (EC:3.1.26.11UniRule annotation)
Short name:
RNase ZUniRule annotation
Alternative name(s):
tRNA 3 endonucleaseUniRule annotation
tRNase ZUniRule annotation
Gene namesi
Name:rnzUniRule annotation
Ordered Locus Names:BCAH187_A4274
OrganismiBacillus cereus (strain AH187)
Taxonomic identifieri405534 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000002214 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 307307Ribonuclease ZPRO_1000187934Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB7HNQ7.
SMRiB7HNQ7. Positions 1-307.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase Z family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000272419.
KOiK00784.
OMAiSYAFCSD.
OrthoDBiEOG61P6TK.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
HAMAPiMF_01818. RNase_Z_BN.
InterProiIPR001279. Metallo-B-lactamas.
IPR013471. RNase_Z/BN.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
PF12706. Lactamase_B_2. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
TIGRFAMsiTIGR02651. RNase_Z. 1 hit.

Sequencei

Sequence statusi: Complete.

B7HNQ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFVFLGTGA GVPSKGRNVS AIALQLLEER GQTWLFDCGE ATQHQILHTS
60 70 80 90 100
VRPRRIEKIF ITHLHGDHIF GLPGLLGSRS FQGGTTPLTV YGPKGIKQFI
110 120 130 140 150
EVALSVSTTH VKYPLEIVEI TEEGTVFEDN EFHVETKRLS HGIECFGYRI
160 170 180 190 200
IEKDIQGALL VDKLLEMGVK PGPLFKRLKD GEVVELENGT ILNGQDFIGP
210 220 230 240 250
PQKGRIITIL GDTRFCEASR ELAQDADVLV HEATFAAEDE QQAYDYFHST
260 270 280 290 300
SKQAASIALQ ANAKRLILTH ISSRYQGDTY KELLKEAREL FSNTEIATDL

KSFPVER
Length:307
Mass (Da):34,225
Last modified:February 10, 2009 - v1
Checksum:i321573FE331A8644
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001177 Genomic DNA. Translation: ACJ79366.1.
RefSeqiWP_000397447.1. NC_011658.1.

Genome annotation databases

EnsemblBacteriaiACJ79366; ACJ79366; BCAH187_A4274.
KEGGibcr:BCAH187_A4274.
PATRICi18833973. VBIBacCer120511_4457.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001177 Genomic DNA. Translation: ACJ79366.1.
RefSeqiWP_000397447.1. NC_011658.1.

3D structure databases

ProteinModelPortaliB7HNQ7.
SMRiB7HNQ7. Positions 1-307.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACJ79366; ACJ79366; BCAH187_A4274.
KEGGibcr:BCAH187_A4274.
PATRICi18833973. VBIBacCer120511_4457.

Phylogenomic databases

HOGENOMiHOG000272419.
KOiK00784.
OMAiSYAFCSD.
OrthoDBiEOG61P6TK.

Enzyme and pathway databases

BioCyciBCER405534:GHXM-4209-MONOMER.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
HAMAPiMF_01818. RNase_Z_BN.
InterProiIPR001279. Metallo-B-lactamas.
IPR013471. RNase_Z/BN.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
PF12706. Lactamase_B_2. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
TIGRFAMsiTIGR02651. RNase_Z. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Bacillus cereus AH187."
    Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B., Okstad O.A., Ravel J., Sutton G.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AH187.

Entry informationi

Entry nameiRNZ_BACC7
AccessioniPrimary (citable) accession number: B7HNQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: May 11, 2016
This is version 49 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

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.