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Q8FP63 (RNH2_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease HII

Short name=RNase HII
EC=3.1.26.4
Gene names
Name:rnhB
Ordered Locus Names:CE1925
OrganismCorynebacterium efficiens [Complete proteome] [HAMAP]
Taxonomic identifier152794 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length231 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 – 231231Ribonuclease HII HAMAP MF_00052_B
PRO_0000111568

Sites

Metal binding291Divalent metal cation By similarity
Metal binding301Divalent metal cation By similarity
Metal binding1231Divalent metal cation By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FP63 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: F723F97E087BB788

FASTA23124,991
        10         20         30         40         50         60 
MATIRRLKQL RTYEVALSRH GLGPVAGVDE AGRGACCGPI SIAACILPDR PIADLAVLTD 

        70         80         90        100        110        120 
SKQLSPPVRA RLMPLVKKHA VAWSVIHISA ADIDRFGIQH ANISGMRRAV AALEVRPGYV 

       130        140        150        160        170        180 
LTDAFRIPGL PCPSLPIPGG DASARCIAAA SVLAKQTRDE IMTDMAQQFP QYGLAGHKGY 

       190        200        210        220        230 
STKVHMDAVR RHGASPQHRY SYANVAKAHR EWALSHSDTE VQNTGKVEHE R 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC18735.1.
RefSeqNP_738535.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FP63.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1034636.
GenomeReviewsGene locus CE1925 in contig BA000035_GR.
KEGGcef:CE1925.
NMPDRfig|196164.1.peg.1925.
PATRIC21489995. VBICorEff9312_1911.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG584843.
OMARLGPTPI.
PhylomeDBQ8FP63.
ProtClustDBPRK00015.

Enzyme and pathway databases

BioCycCEFF196164:CE1925-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_COREF
AccessionPrimary (citable) accession number: Q8FP63
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 51 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