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B1MDH9 (RNH2_MYCA9) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:MAB_3222c
OrganismMycobacterium abscessus (strain ATCC 19977 / DSM 44196) [Complete proteome] [HAMAP]
Taxonomic identifier561007 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium abscessus

Protein attributes

Sequence length234 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 – 234234Ribonuclease HII HAMAP MF_00052_B
PRO_1000091635

Sites

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

Sequences

Sequence LengthMass (Da)Tools
B1MDH9 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: F4A86FCCD225D041

FASTA23424,620
        10         20         30         40         50         60 
MSTSWPPRTV IRKASGLRTL ELTLDRVGLG PVAGVDEAGR GACAGPLVIA ACVLGSNQRK 

        70         80         90        100        110        120 
SLAALNDSKK LTEKMRETLF PLICRYAEAY HVVSVPADEV DRIGVHVANI EGMRRAVAGL 

       130        140        150        160        170        180 
GVKPGYVLTD GFRVPGLPVP SLPVIGGDAS AACIAAASVL AKVSRDRVMV NMDSDHPGYG 

       190        200        210        220        230 
FAVHKGYSTA VHTEALRRLG PSAQHRQSFV NVRNAAMGSS LMRPLAPRES DTGG 

« Hide

References

[1]"Acquisition of foreign virulence genes by the cystic fibrosis pathogen Mycobacterium abscessus."
Genoscope
Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., Gaillard J.L.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19977 / DSM 44196.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU458896 Genomic DNA. Translation: CAM63298.1.
RefSeqYP_001703952.1. NC_010397.1.

3D structure databases

ProteinModelPortalB1MDH9.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1MDH9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000004298; EBMYCP00000004237; EBMYCG00000004296.
GeneID5965725.
GenomeReviewsGene locus MAB_3222c in contig CU458896_GR.
KEGGmab:MAB_3222c.
PATRIC17978214. VBIMycAbs55940_3280.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000016477.
HOGENOMHBG584843.
OMARLGPTPI.
ProtClustDBPRK00015.

Enzyme and pathway databases

BioCycMABS561007:MAB_3222C-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_MYCA9
AccessionPrimary (citable) accession number: B1MDH9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 27 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