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Q7TXM7 (RNH2_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:Mb2926c
OrganismMycobacterium bovis [Complete proteome] [HAMAP]
Taxonomic identifier1765 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length264 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 – 264264Ribonuclease HII HAMAP MF_00052_B
PRO_0000111590

Sites

Metal binding391Divalent metal cation By similarity
Metal binding401Divalent metal cation By similarity
Metal binding1331Divalent metal cation By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7TXM7 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: F4E2459915376361

FASTA26427,627
        10         20         30         40         50         60 
MTKTWPPRTV IRKSGGLRGM RTLESALHRG GLGPVAGVDE VGRGACAGPL VVAACVLGPG 

        70         80         90        100        110        120 
RIASLAALDD SKKLSEQARE KLFPLICRYA VAYHVVFIPS AEVDRHGVHV ANIEGMRRAV 

       130        140        150        160        170        180 
AGLAVRPGYV LSDGFRVPGL PMPSLPVIGG DAAAACIAAA SVLAKVSRDR VMVALDADHP 

       190        200        210        220        230        240 
GYGFAEHKGY STPAHSRALA RLGPCPQHRY SFINVRRVAS GSNTAEVADG QPDPRDGTAQ 

       250        260 
TGEGRWSKSS HPATMRATGR AQGT 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248344 Genomic DNA. Translation: CAD96613.1.
RefSeqNP_856571.1. NC_002945.3.

3D structure databases

ProteinModelPortalQ7TXM7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000016724; EBMYCP00000016559; EBMYCG00000016719.
GeneID1092182.
GenomeReviewsGene locus Mb2926c in contig BX248333_GR.
KEGGmbo:Mb2926c.
PATRIC18008160. VBIMycBov88188_3212.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000016477.
HOGENOMHBG584843.
OMARLGPTPI.
ProtClustDBPRK00015.

Enzyme and pathway databases

BioCycMBOV233413:MB2926C-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_MYCBO
AccessionPrimary (citable) accession number: Q7TXM7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 50 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