PRIS_SACS2
ID PRIS_SACS2 Reviewed; 330 AA.
AC Q97Z83;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
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};
GN Name=priS {ECO:0000255|HAMAP-Rule:MF_00700}; Synonyms=priA;
GN OrderedLocusNames=SSO1048;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, SUBUNIT, AND GENE NAME.
RX PubMed=15561142; DOI=10.1016/j.jmb.2004.10.018;
RA Lao-Sirieix S.H., Bell S.D.;
RT "The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus
RT solfataricus possesses DNA and RNA primase, polymerase and 3'-terminal
RT nucleotidyl transferase activities.";
RL J. Mol. Biol. 344:1251-1263(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.33 ANGSTROMS) IN COMPLEX WITH ZINC, SUBUNIT, AND
RP MUTAGENESIS OF PHE-164 AND GLY-165.
RX PubMed=16273105; DOI=10.1038/nsmb1013;
RA Lao-Sirieix S.H., Nookala R.K., Roversi P., Bell S.D., Pellegrini L.;
RT "Structure of the heterodimeric core primase.";
RL Nat. Struct. Mol. Biol. 12:1137-1144(2005).
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 Possesses a template-independent 3'-terminal nucleotidyl transferase
CC activity. {ECO:0000255|HAMAP-Rule:MF_00700,
CC ECO:0000269|PubMed:15561142}.
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:15561142,
CC ECO:0000269|PubMed:16273105}.
CC -!- INTERACTION:
CC Q97Z83; Q9UWW1: priL; NbExp=5; IntAct=EBI-8081502, EBI-8081454;
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:16273105). {ECO:0000305|PubMed:16273105}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00700}.
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DR EMBL; AE006641; AAK41310.1; -; Genomic_DNA.
DR PIR; G90256; G90256.
DR RefSeq; WP_009989180.1; NC_002754.1.
DR PDB; 1ZT2; X-ray; 3.33 A; A/C=1-330.
DR PDB; 5OF3; X-ray; 2.91 A; A/D=1-330.
DR PDB; 5OFN; X-ray; 3.00 A; A=1-330.
DR PDBsum; 1ZT2; -.
DR PDBsum; 5OF3; -.
DR PDBsum; 5OFN; -.
DR AlphaFoldDB; Q97Z83; -.
DR SMR; Q97Z83; -.
DR DIP; DIP-42889N; -.
DR IntAct; Q97Z83; 2.
DR MINT; Q97Z83; -.
DR STRING; 273057.SSO1048; -.
DR EnsemblBacteria; AAK41310; AAK41310; SSO1048.
DR GeneID; 44129977; -.
DR KEGG; sso:SSO1048; -.
DR PATRIC; fig|273057.12.peg.1042; -.
DR eggNOG; arCOG04110; Archaea.
DR HOGENOM; CLU_056123_0_0_2; -.
DR InParanoid; Q97Z83; -.
DR OMA; GYHVHVR; -.
DR PhylomeDB; Q97Z83; -.
DR BRENDA; 2.7.7.102; 6163.
DR BRENDA; 2.7.7.B16; 6163.
DR EvolutionaryTrace; Q97Z83; -.
DR Proteomes; UP000001974; 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 GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IBA:GO_Central.
DR CDD; cd04860; AE_Prim_S; 1.
DR HAMAP; MF_00700; DNA_primase_sml_arc; 1.
DR InterPro; IPR014052; DNA_primase_ssu_euk/arc.
DR InterPro; IPR023639; DNA_primase_ssu_PriS.
DR PANTHER; PTHR10536; PTHR10536; 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..330
FT /note="DNA primase small subunit PriS"
FT /id="PRO_0000046754"
FT ACT_SITE 101
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 103
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 235
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16273105"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16273105"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16273105"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16273105"
FT MUTAGEN 164
FT /note="F->E: Strong decrease in interaction with PriL."
FT /evidence="ECO:0000269|PubMed:16273105"
FT MUTAGEN 165
FT /note="G->I: Partial destabilization of PriS-PriL complex."
FT /evidence="ECO:0000269|PubMed:16273105"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 70..82
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:5OF3"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:5OF3"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:5OF3"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 143..162
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:5OF3"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:5OF3"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1ZT2"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:5OFN"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 280..288
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 311..319
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:5OF3"
SQ SEQUENCE 330 AA; 37598 MW; E9B3C556E619B66E CRC64;
MGTFTLHQGQ TNLIKSFFRN YYLNAELELP KDMELREFAL QPFGSDTYVR HLSFSSSEEL
RDYLVNRNLP LHLFYSSARY QLPSARNMEE KAWMGSDLLF DIDADHLCKL RSIRFCPVCG
NAVVSEKCER DNVETLEYVE MTSECIKRGL EQTRNLVEIL EDDFGLKPKV YFSGNRGFHV
QVDCYGNCAL LDSDERKEIA EYVMGIGVPG YPGGSENAPG WVGRKNRGIN GVTIDEQVTI
DVKRLIRIPN SLHGKSGLIV KRVPNLDDFE FNETLSPFTG YTIFLPYITI ETEVLGSIIK
LNRGIPIKIK SSIGIYLHLR NLGEVKAYVR
