PRIS_PYRAB
ID PRIS_PYRAB Reviewed; 345 AA.
AC Q9V292; G8ZG17;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=DNA primase small subunit PriS {ECO:0000255|HAMAP-Rule:MF_00700};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00700};
DE AltName: Full=DNA primase 41 kDa subunit;
DE Short=Pabp41;
DE Short=p41;
GN Name=priS {ECO:0000255|HAMAP-Rule:MF_00700}; Synonyms=priA;
GN OrderedLocusNames=PYRAB01820; ORFNames=PAB2236;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
RN [3]
RP FUNCTION, COFACTOR, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=GE5 / Orsay;
RX PubMed=17991487; DOI=10.1016/j.jmb.2007.10.015;
RA Le Breton M., Henneke G., Norais C., Flament D., Myllykallio H.,
RA Querellou J., Raffin J.P.;
RT "The heterodimeric primase from the euryarchaeon Pyrococcus abyssi: a
RT multifunctional enzyme for initiation and repair?";
RL J. Mol. Biol. 374:1172-1185(2007).
CC -!- FUNCTION: Catalytic subunit of DNA primase, an RNA polymerase that
CC catalyzes the synthesis of short RNA molecules used as primers for DNA
CC polymerase during DNA replication. The small subunit contains the
CC primase catalytic core and has DNA synthesis activity on its own,
CC synthesizing DNA strands up to 3 kB. Binding to the large subunit
CC stabilizes and modulates the activity, increasing the rate of DNA
CC synthesis while decreasing the length of the DNA fragments, and
CC conferring RNA synthesis capability for RNA fragments up to 150 bases.
CC The DNA polymerase activity may enable DNA primase to also catalyze
CC primer extension after primer synthesis. May also play a role in DNA
CC repair. Displays gap-filling and strand-displacement activities.
CC {ECO:0000269|PubMed:17991487}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00700,
CC ECO:0000269|PubMed:17991487};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00700,
CC ECO:0000269|PubMed:17991487};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60.5 mM for dNTPs (in the presence of 5 mM Mg(2+)
CC {ECO:0000269|PubMed:17991487};
CC KM=5.0 mM for dNTPs (in the presence of 10 mM Mg(2+)
CC {ECO:0000269|PubMed:17991487};
CC KM=198.0 mM for dNTPs (in the presence of 10 mM Mg(2+) and 5 mM
CC Mn(2+) {ECO:0000269|PubMed:17991487};
CC KM=27.5 mM for NTPs (in the presence of 10 mM Mg(2+)
CC {ECO:0000269|PubMed:17991487};
CC Vmax=1.12 pmol/min/mg enzyme for dNTPs (in the presence of 5 mM
CC Mg(2+) {ECO:0000269|PubMed:17991487};
CC Vmax=0.7 pmol/min/mg enzyme for dNTPs (in the presence of 10 mM
CC Mg(2+) {ECO:0000269|PubMed:17991487};
CC Vmax=5.9 pmol/min/mg enzyme for dNTPs (in the presence of 10 mM
CC Mg(2+) and 5 mM Mn(2+) {ECO:0000269|PubMed:17991487};
CC Vmax=0.88 pmol/min/mg enzyme for NTPs (in the presence of 5 mM Mg(2+)
CC {ECO:0000269|PubMed:17991487};
CC -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit
CC (PriL). {ECO:0000255|HAMAP-Rule:MF_00700, ECO:0000269|PubMed:17991487}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00700}.
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DR EMBL; AJ248283; CAB49106.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69558.1; -; Genomic_DNA.
DR PIR; C75207; C75207.
DR RefSeq; WP_010867306.1; NC_000868.1.
DR AlphaFoldDB; Q9V292; -.
DR SMR; Q9V292; -.
DR STRING; 272844.PAB2236; -.
DR EnsemblBacteria; CAB49106; CAB49106; PAB2236.
DR GeneID; 1495069; -.
DR KEGG; pab:PAB2236; -.
DR PATRIC; fig|272844.11.peg.196; -.
DR eggNOG; arCOG04110; Archaea.
DR HOGENOM; CLU_056123_1_0_2; -.
DR OMA; GFDHTGE; -.
DR OrthoDB; 95578at2157; -.
DR PhylomeDB; Q9V292; -.
DR BRENDA; 2.7.7.102; 5242.
DR BRENDA; 2.7.7.B16; 5242.
DR SABIO-RK; Q9V292; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd04860; AE_Prim_S; 1.
DR HAMAP; MF_00700; DNA_primase_sml_arc; 1.
DR InterPro; IPR002755; DNA_primase_S.
DR InterPro; IPR014052; DNA_primase_ssu_euk/arc.
DR InterPro; IPR023639; DNA_primase_ssu_PriS.
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; Magnesium; Manganese;
KW Metal-binding; Nucleotidyltransferase; Primosome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..345
FT /note="DNA primase small subunit PriS"
FT /id="PRO_0000046748"
FT MOTIF 106..117
FT /note="Zinc knuckle motif"
FT /evidence="ECO:0000250"
FT ACT_SITE 95
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 97
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 280
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 345 AA; 40508 MW; 782D8FBA1D71FEDF CRC64;
MLLREVTKEE RKEFYSNEWN AKQIPDFILQ NLDKREFGFD HTGEGPSDRK NSYTDVRDLE
DYIKATAPYA VYSSVAFYEK PQEMEGWLGA ELVFDIDAKD LPLRRCNHEP GKVCPICLND
AKEIARDTLI VLKEELGFED VHVVYSGRGY HIRVMDGWAL SLDSKSRERI LSFISASEIE
DHSEFRKMLL ERRGWFVLNH GYPRVFRLRF GYFILRVKVE HLINFGIRKN IAKRILDNKE
TIYEEFVRKG ILAAFPDGVG IESLAKLFAL STRFSKAYFD GRVTVDLKRI LRLPSTLHSK
VGLIAKYIGN NERDVMRFNP FKHAVPKFRR KEVKEEYKRF LEENF
