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O33022 (RNH2_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. 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:ML1611
ORF Names:MLCB250.40
OrganismMycobacterium leprae [Complete proteome] [HAMAP]
Taxonomic identifier1769 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length240 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 – 240240Ribonuclease HII HAMAP MF_00052_B
PRO_0000111591

Sites

Metal binding391Divalent metal cation By similarity
Metal binding401Divalent metal cation By similarity
Metal binding1311Divalent metal cation By similarity

Sequences

Sequence LengthMass (Da)Tools
O33022 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 3789259F169454C2

FASTA24025,600
        10         20         30         40         50         60 
MATTWPPCRI IRKSGGLRGM WTLEYELQRS GLGPVAGVDE VGRGACAGPL VVAACVLGPG 

        70         80         90        100        110        120 
RLEESLDDSK KLSAKGREML FPLICRYALA YHVVFIPSVE VDRHGVQVAN IEGMRRAVAG 

       130        140        150        160        170        180 
LSVRPGYVLS DGFRVPGLSV PSLPVVGGDA VVACIAAASV LAKVSRDRLM VAMDADYPGY 

       190        200        210        220        230        240 
GFAAHKGYCT RAHSLALTQL GPCPEHRYSF INVRRIVTRS NTRAVAGFTP APPAEHGECR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z97369 Genomic DNA. Translation: CAB10634.1.
AL583922 Genomic DNA. Translation: CAC30562.1.
PIRE87110.
RefSeqNP_302110.1. NC_002677.1.

3D structure databases

ProteinModelPortalO33022.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000028081; EBMYCP00000027687; EBMYCG00000028076.
GeneID909811.
GenomeReviewsGene locus ML1611 in contig AL450380_GR.
KEGGmle:ML1611.
NMPDRfig|272631.1.peg.982.
PATRIC18056210. VBIMycLep78757_3037.

Organism-specific databases

LepromaML1611.
CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000016477.
HOGENOMHBG584843.
OMARLGPTPI.
ProtClustDBPRK00015.

Enzyme and pathway databases

BioCycMLEP272631:ML1611-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_MYCLE
AccessionPrimary (citable) accession number: O33022
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 73 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