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 HIII

Gene

rnhC

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.UniRule annotation

Catalytic activityi

Endonucleolytic cleavage to 5'-phosphomonoester.UniRule annotation

Cofactori

Mn2+UniRule annotation, Mg2+UniRule annotationNote: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi101 – 1011Divalent metal cationUniRule annotation
Metal bindingi102 – 1021Divalent metal cationUniRule annotation
Metal bindingi206 – 2061Divalent metal cationUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-1043-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease HIIIUniRule annotation (EC:3.1.26.4UniRule annotation)
Short name:
RNase HIIIUniRule annotation
Gene namesi
Name:rnhCUniRule annotation
Ordered Locus Names:SA0987
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000751 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 – 312312Ribonuclease HIIIPRO_0000111693Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ7A647.
SMRiQ7A647. Positions 24-310.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase HII family. RnhC subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000292531.
OMAiTGDYFGP.
OrthoDBiEOG6W723H.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
HAMAPiMF_00053. RNase_HIII.
InterProiIPR001352. RNase_HII/HIII.
IPR024567. RNase_HII/HIII_dom.
IPR004641. RNase_HIII.
IPR024568. RNase_HIII_N.
IPR012337. RNaseH-like_dom.
[Graphical view]
PANTHERiPTHR10954. PTHR10954. 1 hit.
PfamiPF11858. DUF3378. 1 hit.
PF01351. RNase_HII. 1 hit.
[Graphical view]
PIRSFiPIRSF037748. RnhC. 1 hit.
SUPFAMiSSF53098. SSF53098. 1 hit.
TIGRFAMsiTIGR00716. rnhC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7A647-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANIVFKLSD KDITTLMSRI TFDTENLPQG MKARAKYQNT TVNIYQSGKV
60 70 80 90 100
MFQGNHAEAV SKELLPQHSQ LNTNKTKKKN MANSSLEQTL MYDQFNCIGS
110 120 130 140 150
DEAGSGDYFG PLTVCAAFVT KEHVPILKTL GVDDSKKLTD TKIVELAEQL
160 170 180 190 200
VAFIPHSLLT LHNDKYNIQQ AKGWTQVKMK AVLHNEAIKN VLEKIDSSQL
210 220 230 240 250
DYIVIDQFAK REVYSHYALS DIPLPKKTKF ETKGESKSLA IAVASIISRY
260 270 280 290 300
AFITYMDQIS KYINMTIPKG AGAKVDVIAA KIIKKYGLSR LDTISKKHFK
310
NREKAQKILK PL
Length:312
Mass (Da):35,055
Last modified:July 5, 2004 - v1
Checksum:i3CEFB18CAE99A567
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB42236.1.
PIRiH89884.
RefSeqiWP_001284282.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB42236; BAB42236; BAB42236.
PATRICi19574172. VBIStaAur116463_1056.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB42236.1.
PIRiH89884.
RefSeqiWP_001284282.1. NC_002745.2.

3D structure databases

ProteinModelPortaliQ7A647.
SMRiQ7A647. Positions 24-310.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB42236; BAB42236; BAB42236.
PATRICi19574172. VBIStaAur116463_1056.

Phylogenomic databases

HOGENOMiHOG000292531.
OMAiTGDYFGP.
OrthoDBiEOG6W723H.

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-1043-MONOMER.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
HAMAPiMF_00053. RNase_HIII.
InterProiIPR001352. RNase_HII/HIII.
IPR024567. RNase_HII/HIII_dom.
IPR004641. RNase_HIII.
IPR024568. RNase_HIII_N.
IPR012337. RNaseH-like_dom.
[Graphical view]
PANTHERiPTHR10954. PTHR10954. 1 hit.
PfamiPF11858. DUF3378. 1 hit.
PF01351. RNase_HII. 1 hit.
[Graphical view]
PIRSFiPIRSF037748. RnhC. 1 hit.
SUPFAMiSSF53098. SSF53098. 1 hit.
TIGRFAMsiTIGR00716. rnhC. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: N315.

Entry informationi

Entry nameiRNH3_STAAN
AccessioniPrimary (citable) accession number: Q7A647
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 5, 2004
Last modified: March 16, 2016
This is version 79 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.