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Q55801 (RNH_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 HI

Short name=RNase HI
EC=3.1.26.4
Gene names
Name:rnhA
Ordered Locus Names:slr0080
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Endonuclease that specifically degrades the RNA of RNA-DNA hybrids By similarity. HAMAP-Rule MF_00042

Catalytic activity

Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP-Rule MF_00042

Cofactor

Binds 1 magnesium ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding By similarity.

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00042

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00042.

Sequence similarities

Belongs to the RNase H family.

Contains 1 RNase H domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA-DNA hybrid ribonuclease activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 160160Ribonuclease HI HAMAP-Rule MF_00042
PRO_0000195408

Regions

Domain4 – 147144RNase H

Sites

Metal binding131Magnesium 1 By similarity
Metal binding131Magnesium 2 By similarity
Metal binding521Magnesium 1 By similarity
Metal binding741Magnesium 1 By similarity
Metal binding1391Magnesium 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q55801 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F25924F536CBF766

FASTA16017,856
        10         20         30         40         50         60 
MASTPNSVTL YTDGACSMNP GPGGYGAVIL YGDGRREELS AGYKMTTNNR MEIMGAIAAL 

        70         80         90        100        110        120 
SHLQEPSQVL LYTDSRYMVD AMSKGWAKKW KANGWQRNAK EKAKNPDLWE TMLTLCEKHQ 

       130        140        150        160 
VTFQWVKAHA GNKENERCDR LAVAAYQNNP NLVDEGFGKF 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27184 / PCC 6803 / N-1.
[2]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA10553.1.
PIRS76609.
RefSeqNP_442483.1. NC_000911.1.
YP_005652544.1. NC_017277.1.
YP_007452359.1. NC_020286.1.

3D structure databases

ProteinModelPortalQ55801.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ55801. 1 interaction.
STRING1148.slr0080.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA10553; BAA10553; BAA10553.
GeneID12253856.
14618040.
952423.
KEGGsyn:slr0080.
syy:SYNGTS_2591.
syz:MYO_126160.
PATRIC23842672. VBISynSp132158_2875.

Phylogenomic databases

eggNOGCOG0328.
HOGENOMHOG000040465.
KOK03469.
OMAITSWIHN.
OrthoDBEOG696BTR.
PhylomeDBQ55801.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
HAMAPMF_00042. RNase_H.
InterProIPR022892. RNaseH.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
[Graphical view]
PfamPF00075. RNase_H. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 1 hit.
PROSITEPS50879. RNASE_H. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRNH_SYNY3
AccessionPrimary (citable) accession number: Q55801
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families