Q24317 (PRI1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
DNA polymerase subunit A
DNA primase 50 kDa subunit
Short name=dPRI50

Gene names

Name:	DNApol-alpha50
Synonyms:	Pri50
ORF Names:	CG7108

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. Ref.1
Subunit structure	Heterodimer of a small subunit and a large subunit.
Developmental stage	Expressed both maternally and zygotically. Expression is very low in late embryos, larvae, pupae and adult males. Ref.1
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.
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	Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication, synthesis of RNA primer Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	alpha DNA polymerase:primase complex Inferred from direct assay. Source: FlyBase
Molecular function	DNA primase activity Inferred from electronic annotation. Source: InterPro 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 – 438	438	DNA primase small subunit		PRO_0000046733
Regions
	Motif	139 – 149	11	Zinc knuckle motif
Sites
	Active site	63	1	Potential
	Active site	127	1	Potential
	Active site	129	1	Potential
Experimental info
	Sequence conflict	165	1	R → A in CAA56196. Ref.1
	Sequence conflict	203	1	V → E in CAA56196. Ref.1
	Sequence conflict	233	1	L → I in CAA56196. Ref.1
	Sequence conflict	431	1	Q → E in CAA56196. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q24317 [UniParc]. Last modified March 15, 2004. Version 2. Checksum: 5A396DF27F040F42	FASTA	438	50,222
	10 20 30 40 50 60 MPEQVTDQEN QAPQQQTTAV HAYNPEVLQD MLPVYYRRLF PHLPFYRWLS YGSSEDAIFS 70 80 90 100 110 120 NREISFTLQD DIYIRYLCFD TQAELEKEIC SRNPIKIDIG PVMHSKPKNH RSIPGGLTPV 130 140 150 160 170 180 QRELVFDIDM TDYDEVRTCC SGAGVCLKCW KFMVLAARVL DVALREDFGF EHIIWIFSGR 190 200 210 220 230 240 RGIHCWVCDY QARHLDGRGR YAVAEYLNII TYASFAGGNS PRCSMGDRPH HSLKRALKIV 250 260 270 280 290 300 EPMFEEIVLE DQNLFGTPKG VTKLLNMVHD DAARGELESY MQKNLEDGAH SRLVWESFIK 310 320 330 340 350 360 YANSMRTSTT SAWSRKLKNI VAEIQLGLLY PRLDINVTRG FNHLLKAPFC IHPATGKVCV 370 380 390 400 410 420 PFSVSAVAKF DPTTVPTITQ LLHEINAFDD KSKSYMEAPE DKSRIKDHKK TSMFKGVVVF 430 EEFLRKLERS QKSASLQF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The 50-kDa primase subunit of Drosophila melanogaster DNA polymerase alpha. Molecular characterization of the gene and functional analysis of the overexpressed protein." Bakkenist C.J., Cotterill S. J. Biol. Chem. 269:26759-26766(1994) [PubMed: 7929411] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE. Tissue: Embryo.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X79801 mRNA. Translation: CAA56196.1. AE014296 Genomic DNA. Translation: AAF50439.1. AY071217 mRNA. Translation: AAL48839.1.
PIR	A55070.
RefSeq	NP_523972.2. NM_079248.3.
3D structure databases
ProteinModelPortal	Q24317.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-20251N.
IntAct	Q24317. 3 interactions.
MINT	MINT-776576.
STRING	Q24317.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0076603; FBpp0076330; FBgn0011762.
GeneID	38942.
KEGG	dme:Dmel_CG7108.
NMPDR	fig|7227.3.peg.8841.
Organism-specific databases
CTD	38942.
FlyBase	FBgn0011762. DNApol-alpha50.
Phylogenomic databases
eggNOG	inNOG06812.
GeneTree	EMGT00050000017360.
InParanoid	Q24317.
OMA	EDFGFEH.
OrthoDB	EOG42NGFV.
PhylomeDB	Q24317.
Gene expression databases
Bgee	Q24317.
GermOnline	CG7108. Drosophila melanogaster.
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	811126.

Entry information

Entry name

PRI1_DROME

Accession

Primary (citable) accession number: Q24317
Secondary accession number(s): Q9VSI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 15, 2004
Last modified:	January 25, 2012
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project