PRI1_HUMAN
ID PRI1_HUMAN Reviewed; 420 AA.
AC P49642;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=DNA primase small subunit;
DE EC=2.7.7.102 {ECO:0000269|PubMed:17893144, ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:25550159, ECO:0000269|PubMed:26975377, ECO:0000269|PubMed:31479243, ECO:0000269|PubMed:9705292};
DE AltName: Full=DNA primase 49 kDa subunit;
DE Short=p49;
GN Name=PRIM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8026492; DOI=10.1111/j.1432-1033.1994.tb18925.x;
RA Stadlbauer F., Brueckner A., Rehfuess C., Eckerskorn C., Lottspeich F.,
RA Foerster V., Tseng B.Y., Nasheuer H.-P.;
RT "DNA replication in vitro by recombinant DNA-polymerase-alpha-primase.";
RL Eur. J. Biochem. 222:781-793(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 97-146.
RX PubMed=9268648; DOI=10.1006/geno.1997.4833;
RA Cloutier S., Hamel H., Champagne M., Yotov W.V.;
RT "Mapping of the human DNA primase 1 (PRIM1) to chromosome 12q13.";
RL Genomics 43:398-401(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND IDENTIFICATION IN THE DNA
RP POLYMERASE ALPHA COMPLEX.
RX PubMed=9705292; DOI=10.1074/jbc.273.34.21608;
RA Schneider A., Smith R.W., Kautz A.R., Weisshart K., Grosse F.,
RA Nasheuer H.P.;
RT "Primase activity of human DNA polymerase alpha-primase. Divalent cations
RT stabilize the enzyme activity of the p48 subunit.";
RL J. Biol. Chem. 273:21608-21615(1998).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PRIM2, AND IDENTIFICATION IN
RP DNA PRIMASE COMPLEX.
RX PubMed=17893144; DOI=10.1074/jbc.m705826200;
RA Weiner B.E., Huang H., Dattilo B.M., Nilges M.J., Fanning E., Chazin W.J.;
RT "An iron-sulfur cluster in the C-terminal domain of the p58 subunit of
RT human DNA primase.";
RL J. Biol. Chem. 282:33444-33451(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9] {ECO:0007744|PDB:4BPU, ECO:0007744|PDB:4BPW, ECO:0007744|PDB:4BPX}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH UTP; ZINC AND
RP MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, AND MUTAGENESIS
RP OF GLU-44; TYR-54; ARG-56; LYS-77; ASP-109; ASP-111; ASP-114; ASP-116;
RP HIS-166; ASP-306; HIS-315; LYS-318 AND HIS-324.
RX PubMed=24043831; DOI=10.1073/pnas.1311185110;
RA Kilkenny M.L., Longo M.A., Perera R.L., Pellegrini L.;
RT "Structures of human primase reveal design of nucleotide elongation site
RT and mode of Pol alpha tethering.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:15961-15966(2013).
RN [10] {ECO:0007744|PDB:4LIK, ECO:0007744|PDB:4LIL}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-408 IN COMPLEX WITH NTP AND
RP ZINC, DOMAIN, COFACTOR, AND MUTAGENESIS OF ASP-109; ASP-111; SER-160;
RP ARG-163; HIS-166; ASP-306; HIS-315 AND LYS-318.
RX PubMed=24239947; DOI=10.1016/j.jmb.2013.11.007;
RA Vaithiyalingam S., Arnett D.R., Aggarwal A., Eichman B.F., Fanning E.,
RA Chazin W.J.;
RT "Insights into eukaryotic primer synthesis from structures of the p48
RT subunit of human DNA primase.";
RL J. Mol. Biol. 426:558-569(2014).
RN [11] {ECO:0007744|PDB:4RR2}
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION,
RP CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=25550159; DOI=10.1074/jbc.m114.624742;
RA Baranovskiy A.G., Zhang Y., Suwa Y., Babayeva N.D., Gu J., Pavlov Y.I.,
RA Tahirov T.H.;
RT "Crystal structure of the human primase.";
RL J. Biol. Chem. 290:5635-5646(2015).
RN [12] {ECO:0007744|PDB:5EXR}
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, AND DOMAIN.
RX PubMed=26975377; DOI=10.1074/jbc.m116.717405;
RA Baranovskiy A.G., Babayeva N.D., Zhang Y., Gu J., Suwa Y., Pavlov Y.I.,
RA Tahirov T.H.;
RT "Mechanism of Concerted RNA-DNA Primer Synthesis by the Human Primosome.";
RL J. Biol. Chem. 291:10006-10020(2016).
RN [13] {ECO:0007744|PDB:6R4S, ECO:0007744|PDB:6R4T, ECO:0007744|PDB:6R4U, ECO:0007744|PDB:6R5D, ECO:0007744|PDB:6R5E, ECO:0007744|PDB:6RB4}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-407 IN COMPLEXES WITH ZINC;
RP MANGANESE; ATP; DATP AND INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RX PubMed=31479243; DOI=10.1021/acschembio.9b00367;
RA Holzer S., Rzechorzek N.J., Short I.R., Jenkyn-Bedford M., Pellegrini L.,
RA Kilkenny M.L.;
RT "Structural Basis for Inhibition of Human Primase by Arabinofuranosyl
RT Nucleoside Analogues Fludarabine and Vidarabine.";
RL ACS Chem. Biol. 14:1904-1912(2019).
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 - primosome/replisome) which play an
CC essential role in the initiation of DNA synthesis (PubMed:9268648,
CC PubMed:9705292, PubMed:17893144, PubMed:24043831, PubMed:26975377,
CC PubMed:25550159, PubMed:31479243). During the S phase of the cell
CC cycle, the DNA polymerase alpha complex (composed of a catalytic
CC subunit POLA1, an accessory subunit POLA2 and two primase subunits, the
CC catalytic subunit PRIM1 and the regulatory subunit PRIM2) is recruited
CC to DNA at the replicative forks via direct interactions with MCM10 and
CC WDHD1 (By similarity). The primase subunit of the polymerase alpha
CC complex initiates DNA synthesis by oligomerising short RNA primers on
CC both leading and lagging strands (PubMed:17893144). These primers are
CC initially extended by the polymerase alpha catalytic subunit and
CC subsequently transferred to polymerase delta and polymerase epsilon for
CC processive synthesis on the lagging and leading strand, respectively
CC (By similarity). In the primase complex, both subunits are necessary
CC for the initial di-nucleotide formation, but the extension of the
CC primer depends only on the catalytic subunit (PubMed:17893144).
CC Synthesizes 9-mer RNA primers (also known as the 'unit length' RNA
CC primers). Incorporates only ribonucleotides in the presence of
CC ribo- and deoxy-nucleotide triphosphates (rNTPs, dNTPs)
CC (PubMed:26975377). Requires template thymine or cytidine to start the
CC RNA primer synthesis, with an adenine or guanine at its 5'-end
CC (PubMed:25550159, PubMed:26975377). Binds single stranded DNA (By
CC similarity). {ECO:0000250|UniProtKB:P09884,
CC ECO:0000250|UniProtKB:P20664, ECO:0000269|PubMed:17893144,
CC ECO:0000269|PubMed:25550159, ECO:0000269|PubMed:26975377,
CC ECO:0000269|PubMed:9268648, ECO:0000269|PubMed:9705292}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC EC=2.7.7.102; Evidence={ECO:0000269|PubMed:17893144,
CC ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:25550159,
CC ECO:0000269|PubMed:26975377, ECO:0000269|PubMed:31479243,
CC ECO:0000269|PubMed:9705292};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9705292};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:24239947, ECO:0000269|PubMed:9705292};
CC -!- ACTIVITY REGULATION: The presence of the regulatory subunit PRIM2/p58
CC accelerates the kinetics of initiation and primer extension (By
CC similarity). Inhibited by arabinose nucleoside derivatives such as
CC fludarabine and vidarabine (PubMed:31479243).
CC {ECO:0000250|UniProtKB:P20664, ECO:0000269|PubMed:31479243}.
CC -!- SUBUNIT: Heterodimer of a catalytic subunit PRIM1 and a regulatory
CC subunit PRIM2, also known as the DNA primase complex (PubMed:9705292,
CC PubMed:17893144). Interacts with PRIM2 (via C-terminus)
CC (PubMed:17893144). 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:9705292, PubMed:26975377, PubMed:24043831). Within the complex,
CC POLA1 directly interacts with PRIM2 (By similarity).
CC {ECO:0000250|UniProtKB:P20664, ECO:0000269|PubMed:17893144,
CC ECO:0000269|PubMed:9705292}.
CC -!- INTERACTION:
CC P49642; P42858: HTT; NbExp=3; IntAct=EBI-726050, EBI-466029;
CC P49642; P49643: PRIM2; NbExp=7; IntAct=EBI-726050, EBI-850004;
CC -!- DOMAIN: The catalytic domain (residues 1-190 and 303-408) adopts a
CC typical 'prim' fold structure formed by two three strand beta-sheets
CC that line the inside of the lower and upper parts, each surrounded by
CC alpha-helices on the outside (PubMed:24043831, PubMed:24239947). It
CC comprises a highly conserved catalytic triad, a structural zinc-binding
CC motif and the nucleotide-binding motifs. The Asp-109, Asp-111 and Asp-
CC 306 catalytic triad binds two Mn2+ or Mg2+ ions which activate for
CC nucleophilic attack the 3'-hydroxyl of the growing RNA primer or of the
CC first NTP bound at the initiation site (PubMed:24043831,
CC PubMed:24239947, PubMed:25550159, PubMed:26975377). The nucleotide-
CC binding motifs coordinate the phosphates, the ribose and the base of a
CC NTP molecule (PubMed:24043831). The interaction between O2' of the
CC initiating NTP and Asp-306 stabilizes the ribose during the di-
CC nucleotide synthesis (PubMed:26975377). It is proposed that the first
CC nucleotide binds to the elongation site, followed by binding to the
CC initiation site of a second NTP, which will become the 5'-terminal
CC nucleotide of the primer (PubMed:26975377).
CC {ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:24239947,
CC ECO:0000269|PubMed:25550159, ECO:0000269|PubMed:26975377}.
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; X74330; CAA52377.1; -; mRNA.
DR EMBL; BC005266; AAH05266.1; -; mRNA.
DR EMBL; U89689; AAC51726.1; -; Genomic_DNA.
DR CCDS; CCDS44926.1; -.
DR PIR; S45630; S45630.
DR RefSeq; NP_000937.1; NM_000946.2.
DR PDB; 4BPU; X-ray; 2.70 A; A/C=1-420.
DR PDB; 4BPW; X-ray; 3.00 A; A/C=1-420.
DR PDB; 4BPX; X-ray; 3.40 A; A/C=1-420.
DR PDB; 4LIK; X-ray; 1.70 A; A=1-408.
DR PDB; 4LIL; X-ray; 2.60 A; A=1-408.
DR PDB; 4MHQ; X-ray; 2.20 A; A=1-420.
DR PDB; 4RR2; X-ray; 2.65 A; A/C=1-420.
DR PDB; 5EXR; X-ray; 3.60 A; A/E=1-420.
DR PDB; 6R4S; X-ray; 2.75 A; A/E=1-407.
DR PDB; 6R4T; X-ray; 2.35 A; A/D=1-407.
DR PDB; 6R4U; X-ray; 2.20 A; A/E=1-407.
DR PDB; 6R5D; X-ray; 1.95 A; A/E=1-407.
DR PDB; 6R5E; X-ray; 1.85 A; A/E=1-407.
DR PDB; 6RB4; X-ray; 1.50 A; A=1-407.
DR PDB; 7OPL; EM; 4.12 A; C=1-420.
DR PDBsum; 4BPU; -.
DR PDBsum; 4BPW; -.
DR PDBsum; 4BPX; -.
DR PDBsum; 4LIK; -.
DR PDBsum; 4LIL; -.
DR PDBsum; 4MHQ; -.
DR PDBsum; 4RR2; -.
DR PDBsum; 5EXR; -.
DR PDBsum; 6R4S; -.
DR PDBsum; 6R4T; -.
DR PDBsum; 6R4U; -.
DR PDBsum; 6R5D; -.
DR PDBsum; 6R5E; -.
DR PDBsum; 6RB4; -.
DR PDBsum; 7OPL; -.
DR AlphaFoldDB; P49642; -.
DR SMR; P49642; -.
DR BioGRID; 111547; 203.
DR ComplexPortal; CPX-2087; DNA polymerase alpha:primase complex.
DR CORUM; P49642; -.
DR IntAct; P49642; 34.
DR MINT; P49642; -.
DR STRING; 9606.ENSP00000350491; -.
DR ChEMBL; CHEMBL2363042; -.
DR iPTMnet; P49642; -.
DR PhosphoSitePlus; P49642; -.
DR BioMuta; PRIM1; -.
DR DMDM; 1346792; -.
DR EPD; P49642; -.
DR jPOST; P49642; -.
DR MassIVE; P49642; -.
DR MaxQB; P49642; -.
DR PaxDb; P49642; -.
DR PeptideAtlas; P49642; -.
DR PRIDE; P49642; -.
DR ProteomicsDB; 56040; -.
DR Antibodypedia; 8376; 203 antibodies from 32 providers.
DR DNASU; 5557; -.
DR Ensembl; ENST00000338193.11; ENSP00000350491.5; ENSG00000198056.15.
DR GeneID; 5557; -.
DR KEGG; hsa:5557; -.
DR MANE-Select; ENST00000338193.11; ENSP00000350491.5; NM_000946.3; NP_000937.1.
DR UCSC; uc001smd.4; human.
DR CTD; 5557; -.
DR DisGeNET; 5557; -.
DR GeneCards; PRIM1; -.
DR HGNC; HGNC:9369; PRIM1.
DR HPA; ENSG00000198056; Tissue enhanced (bone).
DR MalaCards; PRIM1; -.
DR MIM; 176635; gene.
DR neXtProt; NX_P49642; -.
DR OpenTargets; ENSG00000198056; -.
DR PharmGKB; PA33739; -.
DR VEuPathDB; HostDB:ENSG00000198056; -.
DR eggNOG; KOG2851; Eukaryota.
DR GeneTree; ENSGT00390000011466; -.
DR HOGENOM; CLU_028288_0_1_1; -.
DR InParanoid; P49642; -.
DR OMA; NVTRGFN; -.
DR OrthoDB; 1346165at2759; -.
DR PhylomeDB; P49642; -.
DR TreeFam; TF312823; -.
DR BRENDA; 2.7.7.102; 2681.
DR PathwayCommons; P49642; -.
DR Reactome; R-HSA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-HSA-174430; Telomere C-strand synthesis initiation.
DR Reactome; R-HSA-68952; DNA replication initiation.
DR Reactome; R-HSA-68962; Activation of the pre-replicative complex.
DR Reactome; R-HSA-69091; Polymerase switching.
DR Reactome; R-HSA-69166; Removal of the Flap Intermediate.
DR Reactome; R-HSA-69183; Processive synthesis on the lagging strand.
DR Reactome; R-HSA-9710421; Defective pyroptosis.
DR SignaLink; P49642; -.
DR SIGNOR; P49642; -.
DR BioGRID-ORCS; 5557; 762 hits in 1094 CRISPR screens.
DR ChiTaRS; PRIM1; human.
DR GenomeRNAi; 5557; -.
DR Pharos; P49642; Tbio.
DR PRO; PR:P49642; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P49642; protein.
DR Bgee; ENSG00000198056; Expressed in ganglionic eminence and 104 other tissues.
DR ExpressionAtlas; P49642; baseline and differential.
DR Genevisible; P49642; HS.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003896; F:DNA primase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0032553; F:ribonucleotide binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IDA:UniProtKB.
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 3D-structure; Acetylation; DNA replication; DNA-directed RNA polymerase;
KW Magnesium; Manganese; Metal-binding; Nucleotidyltransferase; Primosome;
KW Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1..420
FT /note="DNA primase small subunit"
FT /id="PRO_0000046730"
FT REGION 363..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 121..131
FT /note="Zinc knuckle motif"
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0000269|PubMed:25550159, ECO:0000269|PubMed:26975377"
FT ACT_SITE 44
FT /evidence="ECO:0000255"
FT ACT_SITE 109
FT /evidence="ECO:0000255"
FT ACT_SITE 111
FT /evidence="ECO:0000255"
FT BINDING 109..111
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0000269|PubMed:31479243"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0007744|PDB:4BPW"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0007744|PDB:4BPW"
FT BINDING 109
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:31479243,
FT ECO:0007744|PDB:6R4S"
FT BINDING 109
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:31479243,
FT ECO:0007744|PDB:6R4S"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0007744|PDB:4BPW"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0007744|PDB:4BPW"
FT BINDING 111
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:31479243,
FT ECO:0007744|PDB:6R4S"
FT BINDING 111
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:31479243,
FT ECO:0007744|PDB:6R4S"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0000269|PubMed:25550159, ECO:0000269|PubMed:26975377,
FT ECO:0000269|PubMed:31479243"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0000269|PubMed:25550159, ECO:0000269|PubMed:26975377,
FT ECO:0000269|PubMed:31479243"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0000269|PubMed:25550159, ECO:0000269|PubMed:26975377,
FT ECO:0000269|PubMed:31479243"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0000269|PubMed:25550159, ECO:0000269|PubMed:26975377,
FT ECO:0000269|PubMed:31479243"
FT BINDING 160..166
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0000269|PubMed:24239947, ECO:0000269|PubMed:31479243"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0007744|PDB:4BPW"
FT BINDING 306
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:31479243,
FT ECO:0007744|PDB:6R4S"
FT BINDING 315..318
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0000269|PubMed:31479243"
FT BINDING 324
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000269|PubMed:31479243"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VARIANT 5
FT /note="D -> A (in dbSNP:rs2277339)"
FT /id="VAR_021898"
FT MUTAGEN 44
FT /note="E->A: Strongly decreases primase activity, which can
FT be partially rescued by increasing primase concentration."
FT /evidence="ECO:0000269|PubMed:24043831"
FT MUTAGEN 54
FT /note="Y->A: Decreases primase activity."
FT /evidence="ECO:0000269|PubMed:24043831"
FT MUTAGEN 56
FT /note="R->A: Loss of primase activity."
FT /evidence="ECO:0000269|PubMed:24043831"
FT MUTAGEN 77
FT /note="K->A: Decreases primase activity."
FT /evidence="ECO:0000269|PubMed:24043831"
FT MUTAGEN 109
FT /note="D->A: Loss of primase activity."
FT /evidence="ECO:0000269|PubMed:24043831"
FT MUTAGEN 109
FT /note="D->N: Decreases the binding affinity for NTPs."
FT /evidence="ECO:0000269|PubMed:24239947"
FT MUTAGEN 111
FT /note="D->A: Loss of primase activity."
FT /evidence="ECO:0000269|PubMed:24043831"
FT MUTAGEN 111
FT /note="D->N: Decreases the binding affinity for NTPs."
FT /evidence="ECO:0000269|PubMed:24239947"
FT MUTAGEN 114
FT /note="D->A: Slightly decreases primase activity."
FT /evidence="ECO:0000269|PubMed:24043831"
FT MUTAGEN 116
FT /note="D->A: Slightly decreases primase activity."
FT /evidence="ECO:0000269|PubMed:24043831"
FT MUTAGEN 160
FT /note="S->A: Abolishes NTP binding."
FT /evidence="ECO:0000269|PubMed:24239947"
FT MUTAGEN 163
FT /note="R->A: Abolishes NTP binding."
FT /evidence="ECO:0000269|PubMed:24239947"
FT MUTAGEN 166
FT /note="H->A: Abolishes NTP binding. Loss of primase
FT activity."
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0000269|PubMed:24239947"
FT MUTAGEN 306
FT /note="D->A: Loss of primase activity."
FT /evidence="ECO:0000269|PubMed:24043831"
FT MUTAGEN 306
FT /note="D->N: Decreases the binding affinity for NTPs."
FT /evidence="ECO:0000269|PubMed:24239947"
FT MUTAGEN 315
FT /note="H->A: Decreases the binding affinity for NTPs. Loss
FT of primase activity."
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0000269|PubMed:24239947"
FT MUTAGEN 318
FT /note="K->A: Decreases the binding affinity for NTPs. Loss
FT of primase activity."
FT /evidence="ECO:0000269|PubMed:24043831,
FT ECO:0000269|PubMed:24239947"
FT MUTAGEN 324
FT /note="H->A: Strongly decreases primase activity, which can
FT be partially rescued by increasing primase concentration."
FT /evidence="ECO:0000269|PubMed:24043831"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:6RB4"
FT TURN 37..42
FT /evidence="ECO:0007829|PDB:6RB4"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:6RB4"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:6RB4"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:6RB4"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:4LIK"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6RB4"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:6RB4"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6RB4"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 132..148
FT /evidence="ECO:0007829|PDB:6RB4"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:6RB4"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 210..227
FT /evidence="ECO:0007829|PDB:6RB4"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:6RB4"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6R5D"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:6RB4"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 291..301
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 307..311
FT /evidence="ECO:0007829|PDB:6RB4"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 350..357
FT /evidence="ECO:0007829|PDB:6RB4"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:4RR2"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:6RB4"
FT HELIX 389..404
FT /evidence="ECO:0007829|PDB:6RB4"
SQ SEQUENCE 420 AA; 49902 MW; 9B5AC900E0C3CCE8 CRC64;
METFDPTELP ELLKLYYRRL FPYSQYYRWL NYGGVIKNYF QHREFSFTLK DDIYIRYQSF
NNQSDLEKEM QKMNPYKIDI GAVYSHRPNQ HNTVKLGAFQ AQEKELVFDI DMTDYDDVRR
CCSSADICPK CWTLMTMAIR IIDRALKEDF GFKHRLWVYS GRRGVHCWVC DESVRKLSSA
VRSGIVEYLS LVKGGQDVKK KVHLSEKIHP FIRKSINIIK KYFEEYALVN QDILENKESW
DKILALVPET IHDELQQSFQ KSHNSLQRWE HLKKVASRYQ NNIKNDKYGP WLEWEIMLQY
CFPRLDINVS KGINHLLKSP FSVHPKTGRI SVPIDLQKVD QFDPFTVPTI SFICRELDAI
STNEEEKEEN EAESDVKHRT RDYKKTSLAP YVKVFEHFLE NLDKSRKGEL LKKSDLQKDF
