P10442 (RNH2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease HII
Short name=RNase HII
EC=3.1.26.4

Gene names

Name:	rnhB
Ordered Locus Names:	b0183, JW0178

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Endonuclease that specifically degrades the RNA of RNA-DNA hybrids By similarity. Ref.6
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 component	Cytoplasm
Ligand	Manganese Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid binding Inferred from electronic annotation. Source: InterPro ribonuclease H activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 198	198	Ribonuclease HII HAMAP MF_00052_B		PRO_0000111571
Sites
	Metal binding	16	1	Divalent metal cation By similarity
	Metal binding	17	1	Divalent metal cation By similarity
	Metal binding	108	1	Divalent metal cation By similarity
Experimental info
	Sequence conflict	196 – 198	3	LAS → TCVLILVSRLSKPESEDV Ref.1
	Sequence conflict	196 – 198	3	LAS → TCVLILVSRLSKPESEDV Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P10442 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 25350722EB5D7864	FASTA	198	21,526
	10 20 30 40 50 60 MIEFVYPHTQ LVAGVDEVGR GPLVGAVVTA AVILDPARPI AGLNDSKKLS EKRRLALYEE 70 80 90 100 110 120 IKEKALSWSL GRAEPHEIDE LNILHATMLA MQRAVAGLHI APEYVLIDGN RCPKLPMPAM 130 140 150 160 170 180 AVVKGDSRVP EISAASILAK VTRDAEMAAL DIVFPQYGFA QHKGYPTAFH LEKLAEHGAT 190 EHHRRSFGPV KRALGLAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the Escherichia coli dnaE gene." Tomasiewicz H.G., McHenry C.S. J. Bacteriol. 169:5735-5744(1987) [PubMed: 3316192] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region." Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 196-198. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Isolation and characterization of a second RNase H (RNase HII) of Escherichia coli K-12 encoded by the rnhB gene." Itaya M. Proc. Natl. Acad. Sci. U.S.A. 87:8587-8591(1990) [PubMed: 2172991] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-11, FUNCTION. Strain: K12.
[7]	"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	M19334 Genomic DNA. No translation available. U70214 Genomic DNA. Translation: AAB08612.1. U00096 Genomic DNA. Translation: AAC73294.1. AP009048 Genomic DNA. Translation: BAA77858.2.
PIR	QQECBE. G64742.
RefSeq	NP_414725.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P10442.
SMR	P10442. Positions 3-196.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10442. 5 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000003492; EBESCP00000003492; EBESCG00000002866. EBESCT00000014844; EBESCP00000014135; EBESCG00000013904.
GeneID	944852.
GenomeReviews	Gene locus JW0178 in contig AP009048_GR. Gene locus b0183 in contig U00096_GR.
KEGG	ecj:JW0178. eco:b0183.
PATRIC	32115477. VBIEscCol129921_0190.
Organism-specific databases
EchoBASE	EB0854.
EcoGene	EG10861. rnhB.
Phylogenomic databases
eggNOG	COG0164.
GeneTree	EBGT00050000010966.
HOGENOM	HBG584843.
OMA	RLGPTPI.
PhylomeDB	P10442.
ProtClustDB	PRK00015.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10861-MONOMER. MetaCyc:EG10861-MONOMER.
BRENDA	3.1.26.4. 2026.
Gene expression databases
Genevestigator	P10442.
Family and domain databases
HAMAP	MF_00052_B. RNase_HII_B. [Tree]
InterPro	IPR022898. RNase_HII. IPR024567. RNase_HII/HIII_dom. IPR012337. RNaseH-like_dom. [Graphical view]
KO	K03470.
Pfam	PF01351. RNase_HII. 1 hit. [Graphical view]
SUPFAM	SSF53098. RNaseH_fold. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RNH2_ECOLI

Accession

Primary (citable) accession number: P10442
Secondary accession number(s): P78265

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program