PRI1_DROME
ID PRI1_DROME Reviewed; 438 AA.
AC Q24317; Q9VSI0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=DNA primase small subunit {ECO:0000305};
DE EC=2.7.7.- {ECO:0000269|PubMed:6409898, ECO:0000269|PubMed:6806812, ECO:0000269|PubMed:6812052};
DE AltName: Full=DNA polymerase subunit A {ECO:0000303|PubMed:6773966};
DE AltName: Full=DNA polymerase subunit gamma {ECO:0000303|PubMed:6409898};
DE AltName: Full=DNA primase 50 kDa subunit {ECO:0000303|PubMed:7929411};
DE Short=dPRI50;
GN Name=Prim1 {ECO:0000312|FlyBase:FBgn0011762};
GN Synonyms=DNApol-alpha50 {ECO:0000303|PubMed:7929411,
GN ECO:0000312|FlyBase:FBgn0011762}, Pri50 {ECO:0000312|FlyBase:FBgn0011762};
GN ORFNames=CG7108 {ECO:0000312|FlyBase:FBgn0011762};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=7929411; DOI=10.1016/s0021-9258(18)47084-6;
RA Bakkenist C.J., Cotterill S.;
RT "The 50-kDa primase subunit of Drosophila melanogaster DNA polymerase
RT alpha. Molecular characterization of the gene and functional analysis of
RT the overexpressed protein.";
RL J. Biol. Chem. 269:26759-26766(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE DNA POLYMERASE ALPHA COMPLEX, AND TISSUE
RP SPECIFICITY.
RX PubMed=6773966; DOI=10.1016/s0021-9258(19)70587-0;
RA Villani G., Sauer B., Lehman I.R.;
RT "DNA polymerase alpha from Drosophila melanogaster embryos. Subunit
RT structure.";
RL J. Biol. Chem. 255:9479-9483(1980).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6806812; DOI=10.1073/pnas.79.8.2523;
RA Conaway R.C., Lehman I.R.;
RT "A DNA primase activity associated with DNA polymerase alpha from
RT Drosophila melanogaster embryos.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:2523-2527(1982).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6812052; DOI=10.1073/pnas.79.15.4585;
RA Conaway R.C., Lehman I.R.;
RT "Synthesis by the DNA primase of Drosophila melanogaster of a primer with a
RT unique chain length.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:4585-4588(1982).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE DNA POLYMERASE ALPHA
RP COMPLEX, IDENTIFICATION IN DNA PRIMASE COMPLEX, AND TISSUE SPECIFICITY.
RX PubMed=6409898; DOI=10.1016/s0021-9258(17)44626-6;
RA Kaguni L.S., Rossignol J.M., Conaway R.C., Banks G.R., Lehman I.R.;
RT "Association of DNA primase with the beta/gamma subunits of DNA polymerase
RT alpha from Drosophila melanogaster embryos.";
RL J. Biol. Chem. 258:9037-9039(1983).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE DNA POLYMERASE ALPHA COMPLEX,
RP IDENTIFICATION IN DNA PRIMASE COMPLEX, AND TISSUE SPECIFICITY.
RX PubMed=6403945; DOI=10.1073/pnas.80.8.2221;
RA Kaguni L.S., Rossignol J.M., Conaway R.C., Lehman I.R.;
RT "Isolation of an intact DNA polymerase-primase from embryos of Drosophila
RT melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:2221-2225(1983).
CC -!- FUNCTION: Catalytic subunit of the DNA primase complex and component of
CC the DNA polymerase alpha complex (also known as the alpha DNA
CC polymerase-primase complex) which play an essential role in the
CC initiation of DNA synthesis (PubMed:6773966, PubMed:6806812,
CC PubMed:6812052, PubMed:6403945, PubMed:6409898). During the S phase of
CC the cell cycle, the DNA polymerase alpha complex (composed of a
CC catalytic subunit PolA1, an accessory subunit PolA2 and two primase
CC subunits, the catalytic subunit Prim1 and the regulatory subunit Prim2)
CC is recruited to DNA at the replicative forks (By similarity). The
CC primase subunit of the polymerase alpha complex initiates DNA synthesis
CC by oligomerising short RNA primers on both leading and lagging strands
CC (By similarity). These primers are initially extended by the polymerase
CC alpha catalytic subunit and subsequently transferred to polymerase
CC delta and polymerase epsilon for processive synthesis on the lagging
CC and leading strand, respectively (By similarity). In the primase
CC complex, both subunits are necessary for the initial di-nucleotide
CC formation, but the extension of the primer depends only on the
CC catalytic subunit (By similarity). Can add both ribo- and
CC deoxynucleotides during elongation of the primers (PubMed:6812052).
CC Binds single stranded DNA (By similarity).
CC {ECO:0000250|UniProtKB:P09884, ECO:0000250|UniProtKB:P20664,
CC ECO:0000269|PubMed:6403945, ECO:0000269|PubMed:6409898,
CC ECO:0000269|PubMed:6773966, ECO:0000269|PubMed:6806812,
CC ECO:0000269|PubMed:6812052}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P49642};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P49642};
CC -!- ACTIVITY REGULATION: The presence of the regulatory subunit Prim2
CC accelerates the kinetics of initiation and primer extension.
CC {ECO:0000250|UniProtKB:P20664}.
CC -!- SUBUNIT: Heterodimer of a catalytic subunit Prim1 and a regulatory
CC subunit Prim2, also known as the DNA primase complex (PubMed:6403945,
CC PubMed:6409898). Component of the alpha DNA polymerase complex (also
CC known as the alpha DNA polymerase-primase complex) consisting of four
CC subunits: the catalytic subunit PolA1, the regulatory subunit PolA2,
CC and the primase complex subunits Prim1 and Prim2 respectively
CC (PubMed:6773966, PubMed:6403945, PubMed:6409898). PolA1 associates with
CC the DNA primase complex before association with PolA2 (PubMed:6409898).
CC {ECO:0000269|PubMed:6403945, ECO:0000269|PubMed:6409898,
CC ECO:0000269|PubMed:6773966}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos (at protein level).
CC {ECO:0000269|PubMed:6403945, ECO:0000269|PubMed:6409898,
CC ECO:0000269|PubMed:6773966}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expression is very low in late embryos, larvae, pupae and adult males.
CC {ECO:0000269|PubMed:7929411}.
CC -!- MISCELLANEOUS: The bound zinc ion is not a cofactor. It is bound to a
CC zinc knuckle motif that may be involved in sequence recognition and the
CC binding of ssDNA (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC family. {ECO:0000305}.
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DR EMBL; X79801; CAA56196.1; -; mRNA.
DR EMBL; AE014296; AAF50439.1; -; Genomic_DNA.
DR EMBL; AY071217; AAL48839.1; -; mRNA.
DR PIR; A55070; A55070.
DR RefSeq; NP_523972.2; NM_079248.4.
DR AlphaFoldDB; Q24317; -.
DR SMR; Q24317; -.
DR BioGRID; 64360; 8.
DR ComplexPortal; CPX-2090; DNA polymerase alpha:primase complex.
DR DIP; DIP-20251N; -.
DR IntAct; Q24317; 4.
DR STRING; 7227.FBpp0076330; -.
DR PaxDb; Q24317; -.
DR PRIDE; Q24317; -.
DR DNASU; 38942; -.
DR EnsemblMetazoa; FBtr0076603; FBpp0076330; FBgn0011762.
DR GeneID; 38942; -.
DR KEGG; dme:Dmel_CG7108; -.
DR CTD; 38942; -.
DR FlyBase; FBgn0011762; Prim1.
DR VEuPathDB; VectorBase:FBgn0011762; -.
DR eggNOG; KOG2851; Eukaryota.
DR GeneTree; ENSGT00390000011466; -.
DR HOGENOM; CLU_028288_3_2_1; -.
DR InParanoid; Q24317; -.
DR OMA; NVTRGFN; -.
DR OrthoDB; 1346165at2759; -.
DR PhylomeDB; Q24317; -.
DR Reactome; R-DME-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-DME-68952; DNA replication initiation.
DR Reactome; R-DME-68962; Activation of the pre-replicative complex.
DR Reactome; R-DME-69091; Polymerase switching.
DR Reactome; R-DME-69166; Removal of the Flap Intermediate.
DR Reactome; R-DME-69183; Processive synthesis on the lagging strand.
DR BioGRID-ORCS; 38942; 0 hits in 1 CRISPR screen.
DR ChiTaRS; DNApol-alpha50; fly.
DR GenomeRNAi; 38942; -.
DR PRO; PR:Q24317; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0011762; Expressed in secondary oocyte and 19 other tissues.
DR Genevisible; Q24317; DM.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IDA:FlyBase.
DR GO; GO:0003896; F:DNA primase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IDA:FlyBase.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:FlyBase.
DR CDD; cd04860; AE_Prim_S; 1.
DR InterPro; IPR002755; DNA_primase_S.
DR InterPro; IPR014052; DNA_primase_ssu_euk/arc.
DR PANTHER; PTHR10536; PTHR10536; 1.
DR Pfam; PF01896; DNA_primase_S; 1.
DR TIGRFAMs; TIGR00335; primase_sml; 1.
PE 1: Evidence at protein level;
KW DNA replication; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Primosome; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..438
FT /note="DNA primase small subunit"
FT /id="PRO_0000046733"
FT MOTIF 139..149
FT /note="Zinc knuckle motif"
FT ACT_SITE 63
FT /evidence="ECO:0000255"
FT ACT_SITE 127
FT /evidence="ECO:0000255"
FT ACT_SITE 129
FT /evidence="ECO:0000255"
FT CONFLICT 165
FT /note="R -> A (in Ref. 1; CAA56196)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="V -> E (in Ref. 1; CAA56196)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="L -> I (in Ref. 1; CAA56196)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="Q -> E (in Ref. 1; CAA56196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 50222 MW; 5A396DF27F040F42 CRC64;
MPEQVTDQEN QAPQQQTTAV HAYNPEVLQD MLPVYYRRLF PHLPFYRWLS YGSSEDAIFS
NREISFTLQD DIYIRYLCFD TQAELEKEIC SRNPIKIDIG PVMHSKPKNH RSIPGGLTPV
QRELVFDIDM TDYDEVRTCC SGAGVCLKCW KFMVLAARVL DVALREDFGF EHIIWIFSGR
RGIHCWVCDY QARHLDGRGR YAVAEYLNII TYASFAGGNS PRCSMGDRPH HSLKRALKIV
EPMFEEIVLE DQNLFGTPKG VTKLLNMVHD DAARGELESY MQKNLEDGAH SRLVWESFIK
YANSMRTSTT SAWSRKLKNI VAEIQLGLLY PRLDINVTRG FNHLLKAPFC IHPATGKVCV
PFSVSAVAKF DPTTVPTITQ LLHEINAFDD KSKSYMEAPE DKSRIKDHKK TSMFKGVVVF
EEFLRKLERS QKSASLQF
