P53942 (RNH2A_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease H2 subunit A
Short name=RNase H2 subunit A
EC=3.1.26.4

Alternative name(s):
RNase H(201)
RNase H(35)
Ribonuclease HI large subunit
Short name=RNase HI large subunit
Ribonuclease HI subunit A

Gene names

Name:	RNH201
Synonyms:	RNH35
Ordered Locus Names:	YNL072W
ORF Names:	N2369

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	307 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
Catalytic activity	Endonucleolytic cleavage to 5'-phosphomonoester.
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.
Subunit structure	The RNase 2 complex is a heterotrimer composed of the catalytic subunit RNH201 and of the non-catalytic subunits RNH202 and RNH203.
Subcellular location	Cytoplasm. Nucleus Ref.5.
Miscellaneous	Present with 623 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the RNase HII family. Eukaryotic subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication, removal of RNA primer Inferred from direct assay PubMed 10567561. Source: SGD
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay PubMed 11029655. Source: SGD ribonuclease H2 complex Inferred from direct assay Ref.7. Source: SGD
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribonuclease H activity Inferred from mutant phenotype Ref.7. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RNH202	Q05635	2	EBI-15663,EBI-33940

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 307	307	Ribonuclease H2 subunit A		PRO_0000111718
Sites
	Metal binding	39	1	Divalent metal cation
	Metal binding	40	1	Divalent metal cation By similarity
	Metal binding	155	1	Divalent metal cation
Experimental info
	Mutagenesis	39	1	D → A: Abolishes enzyme activity. Ref.7
	Mutagenesis	155	1	D → A: Abolishes enzyme activity. Ref.7
	Mutagenesis	183	1	D → A: Strongly impairs enzyme activity. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P53942 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 60B1005F674ECC88	FASTA	307	34,875
	10 20 30 40 50 60 MVPPTVEASL ESPYTKSYFS PVPSALLEQN DSPIIMGIDE AGRGPVLGPM VYAVAYSTQK 70 80 90 100 110 120 YQDETIIPNY EFDDSKKLTD PIRRMLFSKI YQDNEELTQI GYATTCITPL DISRGMSKFP 130 140 150 160 170 180 PTRNYNLNEQ AHDVTMALID GVIKQNVKLS HVYVDTVGPP ASYQKKLEQR FPGVKFTVAK 190 200 210 220 230 240 KADSLYCMVS VASVVAKVTR DILVESLKRD PDEILGSGYP SDPKTVAWLK RNQTSLMGWP 250 260 270 280 290 300 ANMVRFSWQT CQTLLDDASK NSIPIKWEEQ YMDSRKNAAQ KTKQLQLQMV AKPVRRKRLR TLDNWYR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV reveals 12 new open reading frames (ORFs) and an ancient duplication of six ORFs." Poehlmann R., Philippsen P. Yeast 12:391-402(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Yeast RNase H(35) is the counterpart of the mammalian RNase HI, and is evolutionarily related to prokaryotic RNase HII." Frank P., Braunshofer-Reiter C., Wintersberger U. FEBS Lett. 421:23-26(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"RNase H2 of Saccharomyces cerevisiae is a complex of three proteins." Jeong H.-S., Backlund P.S., Chen H.-C., Karavanov A.A., Crouch R.J. Nucleic Acids Res. 32:407-414(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RNH202 AND RNH203, MUTAGENESIS OF ASP-39; ASP-155 AND ASP-183.
[8]	Erratum Jeong H.-S., Backlund P.S., Chen H.-C., Karavanov A.A., Crouch R.J. Nucleic Acids Res. 32:1616-1616(2004)
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X86470 Genomic DNA. Translation: CAA60188.1. Z71348 Genomic DNA. Translation: CAA95946.1. BK006947 Genomic DNA. Translation: DAA10473.1.
PIR	S53908.
RefSeq	NP_014327.1. NM_001182910.1.
3D structure databases
ProteinModelPortal	P53942.
SMR	P53942. Positions 20-275.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4565N.
IntAct	P53942. 2 interactions.
MINT	MINT-532801.
STRING	4932.YNL072W.
Proteomic databases
PaxDb	P53942.
PeptideAtlas	P53942.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL072W; YNL072W; YNL072W.
GeneID	855652.
KEGG	sce:YNL072W.
Organism-specific databases
CYGD	YNL072w.
SGD	S000005016. RNH201.
Phylogenomic databases
eggNOG	COG0164.
GeneTree	ENSGT00390000010768.
HOGENOM	HOG000100290.
KO	K10743.
OMA	IAEVYVD.
OrthoDB	EOG4HMNKD.
Gene expression databases
Genevestigator	P53942.
GermOnline	YNL072W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.10.10.460. 1 hit.
InterPro	IPR004649. RNase_H2_suA. IPR001352. RNase_HII/HIII. IPR024567. RNase_HII/HIII_dom. IPR023160. RNase_HII_hlx-loop-hlx_cap_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.
TIGRFAMs	TIGR00729. TIGR00729. 1 hit.
ProtoNet	Search...
Other
NextBio	979902.

Entry information

Entry name

RNH2A_YEAST

Accession

Primary (citable) accession number: P53942
Secondary accession number(s): D6W1A7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program