PRI1_PLAF7
ID PRI1_PLAF7 Reviewed; 452 AA.
AC Q7KQM1; A0A144A659;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=DNA primase small subunit {ECO:0000250|UniProtKB:Q25998};
DE EC=2.7.7.102 {ECO:0000250|UniProtKB:Q25998};
DE AltName: Full=DNA primase 53 kDa subunit {ECO:0000250|UniProtKB:Q25998};
GN ORFNames=PF14_0366, PF3D7_1438700;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
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 (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). {ECO:0000250|UniProtKB:Q25998}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ssDNA + n dNTP = ssDNA/pppdN(pdN)n-1 hybrid + (n-1)
CC diphosphate.; EC=2.7.7.102; Evidence={ECO:0000250|UniProtKB:Q25998};
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 accelerates
CC the kinetics of initiation and primer extension.
CC {ECO:0000250|UniProtKB:P20664}.
CC -!- SUBUNIT: Heterodimer of a catalytic subunit and a regulatory subunit,
CC also known as the DNA primase complex. {ECO:0000250|UniProtKB:P49642}.
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; LN999946; CZU00083.1; -; Genomic_DNA.
DR RefSeq; XP_001348540.1; XM_001348504.1.
DR AlphaFoldDB; Q7KQM1; -.
DR SMR; Q7KQM1; -.
DR STRING; 5833.PF14_0366; -.
DR PRIDE; Q7KQM1; -.
DR EnsemblProtists; CZU00083; CZU00083; PF3D7_1438700.
DR GeneID; 811948; -.
DR KEGG; pfa:PF3D7_1438700; -.
DR VEuPathDB; PlasmoDB:PF3D7_1438700; -.
DR HOGENOM; CLU_028288_3_2_1; -.
DR InParanoid; Q7KQM1; -.
DR OMA; NVTRGFN; -.
DR PhylomeDB; Q7KQM1; -.
DR Reactome; R-PFA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-PFA-68952; DNA replication initiation.
DR Reactome; R-PFA-68962; Activation of the pre-replicative complex.
DR Reactome; R-PFA-69091; Polymerase switching.
DR Reactome; R-PFA-69166; Removal of the Flap Intermediate.
DR Reactome; R-PFA-69183; Processive synthesis on the lagging strand.
DR Proteomes; UP000001450; Chromosome 14.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; ISS:GeneDB.
DR GO; GO:0003896; F:DNA primase activity; IDA:GeneDB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; ISS:GeneDB.
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 3: Inferred from homology;
KW DNA replication; DNA-directed RNA polymerase; Magnesium; Manganese;
KW Metal-binding; Nucleotidyltransferase; Primosome; Reference proteome;
KW Transcription; Transferase; Zinc.
FT CHAIN 1..452
FT /note="DNA primase small subunit"
FT /id="PRO_0000233399"
FT MOTIF 142..152
FT /note="Zinc knuckle motif"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT ACT_SITE 59
FT /evidence="ECO:0000255"
FT ACT_SITE 130
FT /evidence="ECO:0000255"
FT ACT_SITE 132
FT /evidence="ECO:0000255"
FT BINDING 130..132
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 130
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 130
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 181..187
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 356..359
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:P49642"
FT BINDING 365
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000250|UniProtKB:P49642"
SQ SEQUENCE 452 AA; 53489 MW; D80289257445E8D6 CRC64;
MKMEIVGDIK DSIVNENDLI FYYRSLCPIN DLYNWLNYKN DIKGKYTKLN DPHFFSKREF
SFTCKKSDQG KEEIYIRWLS FSNPEEFKNK LLSDLVPIKF DIGAIYNFPV SQKDQKGDIF
LPVQKELIFD IDMNDYDDIR TCCTDKKVCK LCWKFLTVAI VLLDTALRED FSFEHILWVY
SGRRGIHCWV ADESCRYYTT DARAALADYL NILSGSDTKK KKVSIWGKDK YPMFERAFDI
CYKYFDVLME EQDFFKKGSP HVQKLIDYLP YASGKVTDPL KAMKLNELKE YINNNNFNSR
EIFEKFSSIY NFLTPSNYFK RKNVSGNINM PSFVKEIVFH FTYPRLDINV SKEINHLLKS
PFCIHNSTGR VCVPLDIKNI NNFNPQSVPT LKLLREQFDD PKNSHIEAEN RTSLKPYIDY
FRRHFIENIL LSCVEKKKRL NENSKYVDYN NI
