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O31744 (RNH2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Synonyms:rnh
Ordered Locus Names:BSU16060
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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
Reference 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 – 255255Ribonuclease HII HAMAP MF_00052_B
PRO_0000111542

Sites

Metal binding781Divalent metal cation By similarity
Metal binding791Divalent metal cation By similarity
Metal binding1701Divalent metal cation By similarity

Sequences

Sequence LengthMass (Da)Tools
O31744 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: B2406C40E9C9302F

FASTA25528,355
        10         20         30         40         50         60 
MNTLTVKDIK DRLQEVKDAQ DPFIAQCEND PRKSVQTLVE QWLKKQAKEK ALKEQWVNMT 

        70         80         90        100        110        120 
SYERLARNKG FRLIAGVDEV GRGPLAGPVV ASAVILPEEC EILGLTDSKK LSEKKREEYY 

       130        140        150        160        170        180 
ELIMKEALAV GIGIVEATVI DEINIYEASK MAMVKAIQDL SDTPDYLLVD AMTLPLDTAQ 

       190        200        210        220        230        240 
ASIIKGDAKS VSIAAGACIA KVTRDRMMSA YAETYPMYGF EKNKGYGTKE HLEALAAYGP 

       250 
TELHRKTFAP VQSFR

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[2]"Isolation of RNase H genes that are essential for growth of Bacillus subtilis 168."
Itaya M., Omori A., Kanaya S., Crouch R.J., Tanaka T., Kondo K.
J. Bacteriol. 181:2118-2123(1999) [PubMed: 10094689] [Abstract]
Cited for: CHARACTERIZATION.
[3]"Identification of the genes encoding Mn2+-dependent RNase HII and Mg2+-dependent RNase HIII from Bacillus subtilis: classification of RNases H into three families."
Ohtani N., Haruki M., Morikawa M., Crouch R.J., Itaya M., Kanaya S.
Biochemistry 38:605-618(1999) [PubMed: 9888800] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL009126 Genomic DNA. Translation: CAB13479.1.
PIRC69693.
RefSeqNP_389488.1. NC_000964.3.

3D structure databases

ProteinModelPortalO31744.
SMRO31744. Positions 65-254.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000002382; EBBACP00000002382; EBBACG00000002377.
GeneID940133.
GenomeReviewsGene locus BSU16060 in contig AL009126_GR.
KEGGbsu:BSU16060.
NMPDRfig|224308.1.peg.1608.
PATRIC18975017. VBIBacSub10457_1700.

Organism-specific databases

GenoListBSU16060. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000002677.
HOGENOMHBG584843.
OMARLGPTPI.
PhylomeDBO31744.
ProtClustDBPRK00015.

Enzyme and pathway databases

BioCycBSUB:BSU16060-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_BACSU
AccessionPrimary (citable) accession number: O31744
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents