P10363 (PRI1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA primase small subunit
EC=2.7.7.-

Alternative name(s):
DNA polymerase alpha:primase complex p48 subunit
Short name=DNA polymerase-primase complex p48 subunit
Short name=Pol alpha-primase complex p48 subunit
DNA primase 48 kDa subunit

Gene names

Name:	PRI1
Ordered Locus Names:	YIR008C
ORF Names:	YIB8C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. In a complex with DNA polymerase alpha (DNA polymerase alpha:primase) constitutes a replicative polymerase. Both primase components participate in formation of the active center, but the ATP-binding site is exclusively located on p48.
Subunit structure	DNA polymerase alpha:primase is a four subunit enzyme complex, which is assembled throughout the cell cycle, and consists of the two DNA polymerase subunits A and B, and the DNA primase large and small subunits.
Miscellaneous	The bound zinc ion is not a cofactor. It is bound to a zinc knuckle motif that may be involved in sequence recognition and the binding of ssDNA By similarity. Present with 197 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the eukaryotic-type primase small subunit family.

Ontologies

Keywords
Biological process	DNA replication Transcription
Cellular component	DNA-directed RNA polymerase Primosome
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication, synthesis of RNA primer Inferred from direct assay. Source: SGD DNA-dependent DNA replication initiation Inferred by curator. Source: SGD lagging strand elongation Inferred by curator. Source: SGD
Cellular component	alpha DNA polymerase:primase complex Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA primase activity Inferred from mutant phenotype. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 409	409	DNA primase small subunit		PRO_0000046736
Regions
	Motif	123 – 133	11	Zinc knuckle motif
Sites
	Active site	46	1	Potential
	Active site	111	1	Potential
	Active site	113	1	Potential
Amino acid modifications
	Modified residue	61	1	Phosphoserine Ref.9
	Modified residue	406	1	Phosphoserine Ref.9
Experimental info
	Mutagenesis	184	1	R → Q: Temperature-sensitive.
	Mutagenesis	316	1	E → K: Cold-sensitive.
	Sequence conflict	231 – 232	2	EQ → DE in CAA68513. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P10363 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: C4B1C82257AA86F2	FASTA	409	47,690
	10 20 30 40 50 60 MTNSVKTNGP SSSDMEYYYK SLYPFKHIFN WLNHSPKPSR DMINREFAMA FRSGAYKRYN 70 80 90 100 110 120 SFNSVQDFKA QIEKANPDRF EIGAIYNKPP RERDTLLKSE LKALEKELVF DIDMDDYDAF 130 140 150 160 170 180 RTCCSGAQVC SKCWKFISLA MKITNTALRE DFGYKDFIWV FSGRRGAHCW VSDKRARALT 190 200 210 220 230 240 DVQRRNVLDY VNVIRDRNTD KRLALKRPYH PHLARSLEQL KPFFVSIMLE EQNPWEDDQH 250 260 270 280 290 300 AIQTLLPALY DKQLIDSLKK YWLDNPRRSS KEKWNDIDQI ATSLFKGPKQ DSHIIKLREC 310 320 330 340 350 360 KEDLVLMTLY PKLDVEVTKQ TIHLLKAPFC IHPATGNVCV PIDESFAPEK APKLIDLQTE 370 380 390 400 MEKNNDVSLT ALQPFINQFQ AYVSSLLKNE LGSVKRERED DDEPASLDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of the PRI1 gene related to DNA primase in Saccharomyces cerevisiae." Plevani P., Francesconi S., Lucchini G. Nucleic Acids Res. 15:7975-7989(1987) [PubMed: 3313275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DBY939.
[2]	"Nucleotide sequence and analysis of the centromeric region of yeast chromosome IX." Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S., Schwager C., Zimmermann J., Sander C., Ansorge W. Yeast 11:61-78(1995) [PubMed: 7762303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:84-87(1997) [PubMed: 9169870] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"The yeast DNA polymerase-primase complex: genes and proteins." Plevani P., Foiani M., Muzi Falconi M., Pizzagalli A., Santocanale C., Francesconi S., Valsasnini P., Comedini A., Piatti S., Lucchini G. Biochim. Biophys. Acta 951:268-273(1988) [PubMed: 3061469] [Abstract] Cited for: COMPOSITION OF THE DNA POLYMERASE ALPHA:PRIMASE COMPLEX.
[7]	"Mutations in conserved yeast DNA primase domains impair DNA replication in vivo." Francesconi S., Longhese M.P., Piseri A., Santocanale C., Lucchini G., Plevani P. Proc. Natl. Acad. Sci. U.S.A. 88:3877-3881(1991) [PubMed: 2023935] [Abstract] Cited for: MUTAGENESIS.
[8]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-406, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z37996 Genomic DNA. Translation: CAA86078.1. X79743 Genomic DNA. Translation: CAB38098.1. Y00458 Genomic DNA. Translation: CAA68513.1. AY692859 Genomic DNA. Translation: AAT92878.1. BK006942 Genomic DNA. Translation: DAA08554.1.
PIR	S48352.
RefSeq	NP_012273.1. NM_001179530.1.
3D structure databases
ProteinModelPortal	P10363.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2534N.
IntAct	P10363. 4 interactions.
MINT	MINT-572443.
STRING	P10363.
Proteomic databases
PeptideAtlas	P10363.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YIR008C; YIR008C; YIR008C.
GeneID	854825.
KEGG	sce:YIR008C.
NMPDR	fig|4932.3.peg.1811.
Organism-specific databases
CYGD	YIR008c.
SGD	S000001447. PRI1.
Phylogenomic databases
eggNOG	fuNOG05421.
GeneTree	EFGT00050000006322.
HOGENOM	HBG397483.
OMA	EDFGFEH.
OrthoDB	EOG4CVKGS.
Gene expression databases
ArrayExpress	P10363.
Genevestigator	P10363.
GermOnline	YIR008C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002755. DNA_primase_S. IPR014052. DNA_primase_ssu_euk/arc. [Graphical view]
KO	K02684.
PANTHER	PTHR10536. DNA_primase_S_euk_arch. 1 hit.
Pfam	PF01896. DNA_primase_S. 1 hit. [Graphical view]
TIGRFAMs	TIGR00335. Primase_sml. 1 hit.
ProtoNet	Search...
Other
NextBio	977680.

Entry information

Entry name

PRI1_YEAST

Accession

Primary (citable) accession number: P10363
Secondary accession number(s): D6VVT8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program