PRIS_PYRHO
ID PRIS_PYRHO Reviewed; 346 AA.
AC O57934;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=PH0195;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP SUBUNIT.
RX PubMed=17286576; DOI=10.1111/j.1742-4658.2007.05690.x;
RA Ito N., Matsui I., Matsui E.;
RT "Molecular basis for the subunit assembly of the primase from an archaeon
RT Pyrococcus horikoshii.";
RL FEBS J. 274:1340-1351(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION, AND
RP ACTIVE SITES.
RX PubMed=14750947; DOI=10.1111/j.1365-2443.2003.00693.x;
RA Ito N., Nureki O., Shirouzu M., Yokoyama S., Hanaoka F.;
RT "Crystal structure of the Pyrococcus horikoshii DNA primase-UTP complex:
RT implications for the mechanism of primer synthesis.";
RL Genes Cells 8:913-923(2003).
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:14750947}.
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). {ECO:0000255|HAMAP-Rule:MF_00700, ECO:0000269|PubMed:14750947,
CC ECO:0000269|PubMed:17286576}.
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:14750947). {ECO:0000305|PubMed:14750947}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00700}.
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DR EMBL; BA000001; BAA29264.1; -; Genomic_DNA.
DR PIR; A71242; A71242.
DR RefSeq; WP_010884304.1; NC_000961.1.
DR PDB; 1V33; X-ray; 1.80 A; A=1-346.
DR PDB; 1V34; X-ray; 2.70 A; A=1-346.
DR PDBsum; 1V33; -.
DR PDBsum; 1V34; -.
DR AlphaFoldDB; O57934; -.
DR SMR; O57934; -.
DR STRING; 70601.3256581; -.
DR EnsemblBacteria; BAA29264; BAA29264; BAA29264.
DR GeneID; 1444086; -.
DR KEGG; pho:PH0195; -.
DR eggNOG; arCOG04110; Archaea.
DR OMA; GFDHTGE; -.
DR OrthoDB; 95578at2157; -.
DR BRENDA; 2.7.7.B16; 5244.
DR EvolutionaryTrace; O57934; -.
DR Proteomes; UP000000752; 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; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..346
FT /note="DNA primase small subunit PriS"
FT /id="PRO_0000046751"
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:14750947"
FT ACT_SITE 97
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700,
FT ECO:0000269|PubMed:14750947"
FT ACT_SITE 280
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700,
FT ECO:0000269|PubMed:14750947"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:14750947"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:14750947"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:14750947"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:14750947"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:1V33"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:1V33"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:1V33"
FT STRAND 69..80
FT /evidence="ECO:0007829|PDB:1V33"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:1V33"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1V33"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 115..134
FT /evidence="ECO:0007829|PDB:1V33"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1V33"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:1V33"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:1V33"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 260..276
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 281..285
FT /evidence="ECO:0007829|PDB:1V33"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1V33"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:1V33"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:1V33"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:1V33"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:1V33"
SQ SEQUENCE 346 AA; 40405 MW; 04BA4B6ED8FC92FD CRC64;
MLLREVTREE RKNFYTNEWK VKDIPDFIVK TLELREFGFD HSGEGPSDRK NQYTDIRDLE
DYIRATAPYA VYSSVALYEK PQEMEGWLGT ELVFDIDAKD LPLRRCEHEP GTVCPICLND
AKEIVRDTVI ILREELGFND IHIIYSGRGY HIRVLDEWAL KLDSKSRERI LSFVSASEIE
DVEEFRKLLL NKRGWFVLNH GYPRAFRLRF GYFILRIKLP HLINAGIRKS IAKSILKSKE
EIYEEFVRKA ILAAFPQGVG IESLAKLFAL STRFSKSYFD GRVTVDLKRI LRLPSTLHSK
VGLIAKYVGT NERDVMRFNP FKHAVPKFRK EEVKVEYKKF LESLGT
