Q99ZM6 (RNH2_STRP1) 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:	SPy_1162, M5005_Spy0883

Organism

Streptococcus pyogenes serotype M1 [Complete proteome] [HAMAP]

Taxonomic identifier

301447 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus pyogenes

Protein attributes

Sequence length	263 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Endonuclease that specifically degrades the RNA of RNA-DNA hybrids By similarity. HAMAP-Rule MF_00052
Catalytic activity	Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP-Rule MF_00052
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-Rule MF_00052.
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
Gene Ontology (GO)
Biological_process	RNA catabolic process Inferred from electronic annotation. Source: HAMAP nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: HAMAP ribonuclease H activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 263	263	Ribonuclease HII HAMAP-Rule MF_00052		PRO_0000111636
Sites
	Metal binding	77	1	Divalent metal cation By similarity
	Metal binding	78	1	Divalent metal cation By similarity
	Metal binding	172	1	Divalent metal cation By similarity
Experimental info
	Sequence conflict	221	1	D → G in AAZ51501. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q99ZM6 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 3E32B7FFD7CFFBAF	FASTA	263	28,762
	10 20 30 40 50 60 MPTSIKAIKE SLEAVTSLLD PLFQELATDT RSGVQKALKS RQKVIQAELA EEERLEAMLS 70 80 90 100 110 120 YEKALYKKGY KAIAGIDEVG RGPLAGPVVA ACVILPKYCK IKGLNDSKKI PKAKHETIYQ 130 140 150 160 170 180 AVKEKALAIG IGIIDNQLID EVNIYEATKL AMLEAIKQLE GQLTQPDYLL IDAMTLDIAI 190 200 210 220 230 240 SQQSILKGDA NSLSIAAASI VAKVTRDQMM ANYDRIFPGY DFAKNAGYGT KEHLQGLKAY 250 260 GITPIHRKSF EPVKSMCCDS TNP

References

[1]

"Complete genome sequence of an M1 strain of Streptococcus pyogenes." Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K., Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P., Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L. , White J., Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E. Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700294 / SF370 / Serotype M1.

[2]

"Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events." Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., Musser J.M. J. Infect. Dis. 192:771-782(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-947 / MGAS5005 / Serotype M1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE004092 Genomic DNA. Translation: AAK34033.1. CP000017 Genomic DNA. Translation: AAZ51501.1.
RefSeq	NP_269312.1. NC_002737.1. YP_282246.1. NC_007297.1.
3D structure databases
ProteinModelPortal	Q99ZM6.
ModBase	Search...
Protein-protein interaction databases
STRING	160490.SPy_1162.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK34033; AAK34033; SPy_1162. AAZ51501; AAZ51501; M5005_Spy0883.
GeneID	3572014. 901277.
KEGG	spy:SPy_1162. spz:M5005_Spy_0883.
PATRIC	19715899. VBIStrPyo79812_1014.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0164.
HOGENOM	HOG000100288.
KO	K03470.
OMA	NRCPKLA.
ProtClustDB	PRK00015.
Family and domain databases
HAMAP	MF_00052_B. RNase_HII_B.
InterPro	IPR022898. RNase_HII. IPR001352. RNase_HII/HIII. IPR024567. RNase_HII/HIII_dom. IPR012337. RNaseH-like_dom. [Graphical view]
PANTHER	PTHR10954. PTHR10954. 1 hit.
Pfam	PF01351. RNase_HII. 1 hit. [Graphical view]
SUPFAM	SSF53098. RNaseH_fold. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RNH2_STRP1

Accession

Primary (citable) accession number: Q99ZM6
Secondary accession number(s): Q48YS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program