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Q6NGJ8 (RNH2_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribonuclease HII

Short name=RNase HII
EC=3.1.26.4
Gene names
Name:rnhB
Ordered Locus Names:DIP1515
OrganismCorynebacterium diphtheriae [Complete proteome] [HAMAP]
Taxonomic identifier1717 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Endonuclease that specifically degrades the RNA of RNA-DNA hybrids By similarity. HAMAP MF_00052_B

Catalytic activity

Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP MF_00052_B

Cofactor

Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding By similarity.

Subcellular location

Cytoplasm Potential HAMAP MF_00052_B.

Sequence similarities

Belongs to the RNase HII family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionRNA binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonuclease H activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 229229Ribonuclease HII HAMAP MF_00052_B
PRO_0000111567

Sites

Metal binding401Divalent metal cation By similarity
Metal binding411Divalent metal cation By similarity
Metal binding1341Divalent metal cation By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6NGJ8 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 33F29A0EFFDC6F12

FASTA22925,067
        10         20         30         40         50         60 
MITQEHYCAL PAPKIRTLKH LRTFEVTLDK HGLGPVAGVD EAGRGSCCGP ITIAACIMPQ 

        70         80         90        100        110        120 
RPIAQLQALT DSKKLSAAKR AELYPLIKKY ALAWSIIHIS AAEIDREGIQ HANIFGMRRA 

       130        140        150        160        170        180 
IEKLDVAPGY VLTDAMKVPG LRCPSLPIIG GDAAVRCIAA ASVLAKHSRD LIMDDLGGKY 

       190        200        210        220 
PEYGLEDHKG YGTKSHMDAV RHHGATPEHR YSYSNVKAAH DQWLQEKTQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248358 Genomic DNA. Translation: CAE50042.1.
RefSeqNP_939861.1. NC_002935.2.

3D structure databases

ProteinModelPortalQ6NGJ8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2650399.
GenomeReviewsGene locus DIP1515 in contig BX248353_GR.
KEGGcdi:DIP1515.
NMPDRfig|257309.1.peg.1452.
PATRIC21484240. VBICorDip47633_1496.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG584843.
OMARLGPTPI.
PhylomeDBQ6NGJ8.
ProtClustDBPRK00015.

Enzyme and pathway databases

BioCycCDIP257309:DIP1515-MONOMER.

Family and domain databases

HAMAPMF_00052_B. RNase_HII_B.
[Tree]
InterProIPR022898. RNase_HII.
IPR001352. RNase_HII/HIII.
IPR024567. RNase_HII/HIII_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
KOK03470.
PANTHERPTHR10954. RNase_HII/HIII. 1 hit.
PfamPF01351. RNase_HII. 1 hit.
[Graphical view]
SUPFAMSSF53098. RNaseH_fold. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRNH2_CORDI
AccessionPrimary (citable) accession number: Q6NGJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families