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B2HJL9 (RNH2_MYCMM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 21. 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:MMAR_1806
OrganismMycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP]
Taxonomic identifier216594 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length239 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 – 239239Ribonuclease HII HAMAP MF_00052_B
PRO_1000091636

Sites

Metal binding361Divalent metal cation By similarity
Metal binding371Divalent metal cation By similarity
Metal binding1301Divalent metal cation By similarity

Sequences

Sequence LengthMass (Da)Tools
B2HJL9 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 2EF0FAB2801AB0D6

FASTA23925,390
        10         20         30         40         50         60 
MATTWPPRTV IRKSSGLRTL ESALQRSGLG PVAGVDEVGR GACAGPLVVA ACALGPNRYE 

        70         80         90        100        110        120 
SLAALDDSKK LTEKTREKLF PLICRYALAY HVVFIPSVEV DRRGVHVANI EGMRRAVAGL 

       130        140        150        160        170        180 
SVRPGYVLSD GFRVPGLSVP SLPVIGGDAA AACIAAASVL AKVSRDRLMV AMDTQYPGYG 

       190        200        210        220        230 
FAEHKGYSTR AHTLALTQLG PCPEHRRSFI NVRRVATRSN GAAAAEREAD PPQERDGTG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000854 Genomic DNA. Translation: ACC40255.1.
RefSeqYP_001850110.1. NC_010612.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB2HJL9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000034376; EBMYCP00000032816; EBMYCG00000034371.
GeneID6226065.
GenomeReviewsGene locus MMAR_1806 in contig CP000854_GR.
KEGGmmi:MMAR_1806.
PATRIC18064489. VBIMycMar75906_1929.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000016477.
HOGENOMHBG584843.
OMARLGPTPI.
ProtClustDBPRK00015.

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_MYCMM
AccessionPrimary (citable) accession number: B2HJL9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: January 25, 2012
This is version 21 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