PRIS_PYRFU
ID PRIS_PYRFU Reviewed; 347 AA.
AC Q9P9H1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=p41;
GN Name=priS {ECO:0000255|HAMAP-Rule:MF_00700}; Synonyms=priA;
GN OrderedLocusNames=PF0110;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=11301257; DOI=10.1016/s0960-9822(01)00119-1;
RA Bocquier A.A., Liu L., Cann I.K.O., Komori K., Kohda D., Ishino Y.;
RT "Archaeal primase: bridging the gap between RNA and DNA polymerases.";
RL Curr. Biol. 11:452-456(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP FUNCTION AS A PRIMASE, AND SUBUNIT.
RX PubMed=11584001; DOI=10.1074/jbc.m106391200;
RA Liu L., Komori K., Ishino S., Bocquier A.A., Cann I.K., Kohda D.,
RA Ishino Y.;
RT "The archaeal DNA primase: biochemical characterization of the p41-p46
RT complex from Pyrococcus furiosus.";
RL J. Biol. Chem. 276:45484-45490(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ZINC, AND ACTIVE
RP SITES.
RX PubMed=11135672; DOI=10.1038/83060;
RA Augustin M.A., Huber R., Kaiser J.T.;
RT "Crystal structure of a DNA-dependent RNA polymerase (DNA primase).";
RL Nat. Struct. Biol. 8:57-61(2001).
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 Binding to the large subunit stabilizes and modulates the activity,
CC increasing the rate of DNA synthesis while decreasing the length of the
CC DNA fragments, and conferring RNA synthesis capability. The DNA
CC polymerase activity may enable DNA primase to also catalyze primer
CC extension after primer synthesis. May also play a role in DNA repair.
CC {ECO:0000255|HAMAP-Rule:MF_00700, ECO:0000269|PubMed:11584001}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00700};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00700};
CC -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit
CC (PriL). Both participate in formation of the active center, but the
CC ATP-binding site is exclusively located on the small subunit.
CC {ECO:0000255|HAMAP-Rule:MF_00700, ECO:0000269|PubMed:11135672,
CC ECO:0000269|PubMed:11584001}.
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 (PubMed:11135672). {ECO:0000305|PubMed:11135672}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00700}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB037376; BAB03293.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL80234.1; -; Genomic_DNA.
DR RefSeq; WP_011011222.1; NC_018092.1.
DR PDB; 1G71; X-ray; 2.30 A; A/B=1-347.
DR PDBsum; 1G71; -.
DR AlphaFoldDB; Q9P9H1; -.
DR SMR; Q9P9H1; -.
DR STRING; 186497.PF0110; -.
DR EnsemblBacteria; AAL80234; AAL80234; PF0110.
DR GeneID; 41711897; -.
DR KEGG; pfu:PF0110; -.
DR PATRIC; fig|186497.12.peg.114; -.
DR eggNOG; arCOG04110; Archaea.
DR HOGENOM; CLU_056123_1_0_2; -.
DR OMA; GYHVHVR; -.
DR OrthoDB; 95578at2157; -.
DR PhylomeDB; Q9P9H1; -.
DR BRENDA; 2.7.7.102; 5243.
DR BRENDA; 2.7.7.B16; 5243.
DR EvolutionaryTrace; Q9P9H1; -.
DR Proteomes; UP000001013; 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 3D-structure; DNA replication; DNA-directed RNA polymerase; Magnesium;
KW Manganese; Metal-binding; Nucleotidyltransferase; Primosome;
KW Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1..347
FT /note="DNA primase small subunit PriS"
FT /id="PRO_0000046750"
FT MOTIF 106..117
FT /note="Zinc knuckle motif"
FT ACT_SITE 95
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700,
FT ECO:0000269|PubMed:11135672"
FT ACT_SITE 97
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700,
FT ECO:0000269|PubMed:11135672"
FT ACT_SITE 280
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700,
FT ECO:0000269|PubMed:11135672"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:11135672"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:11135672"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:11135672"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:11135672"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:1G71"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:1G71"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:1G71"
FT STRAND 69..80
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1G71"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1G71"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 115..134
FT /evidence="ECO:0007829|PDB:1G71"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:1G71"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:1G71"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:1G71"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:1G71"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 261..275
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 281..285
FT /evidence="ECO:0007829|PDB:1G71"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1G71"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:1G71"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:1G71"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:1G71"
FT HELIX 330..343
FT /evidence="ECO:0007829|PDB:1G71"
SQ SEQUENCE 347 AA; 40772 MW; 12FFC4E670346792 CRC64;
MLMREVTKEE RSEFYSKEWS AKKIPKFIVD TLESREFGFD HNGEGPSDRK NQYSDIRDLE
DYIRATSPYA VYSSVAFYEN PREMEGWRGA ELVFDIDAKD LPLKRCNHEP GTVCPICLED
AKELAKDTLI ILREELGFEN IHVVYSGRGY HIRILDEWAL QLDSKSRERI LAFISASEIE
NVEEFRRFLL EKRGWFVLKH GYPRVFRLRL GYFILRVNVP HLLSIGIRRN IAKKILDHKE
EIYEGFVRKA ILASFPEGVG IESMAKLFAL STRFSKAYFD GRVTVDIKRI LRLPSTLHSK
VGLIATYVGT KEREVMKFNP FRHAVPKFRK KEVREAYKLW RESLEYE
