PRIL_SACS2
ID PRIL_SACS2 Reviewed; 307 AA.
AC Q9UWW1;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=DNA primase large subunit PriL {ECO:0000255|HAMAP-Rule:MF_00701};
GN Name=priL {ECO:0000255|HAMAP-Rule:MF_00701}; Synonyms=priB;
GN OrderedLocusNames=SSO0557; ORFNames=C21_042;
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=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [2]
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 [3]
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 [4]
RP IRON-SULFUR-BINDING, AND COFACTOR.
RX PubMed=17704817; DOI=10.1038/nsmb1288;
RA Klinge S., Hirst J., Maman J.D., Krude T., Pellegrini L.;
RT "An iron-sulfur domain of the eukaryotic primase is essential for RNA
RT primer synthesis.";
RL Nat. Struct. Mol. Biol. 14:875-877(2007).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.33 ANGSTROMS) OF 1-212, AND SUBUNIT.
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: Regulatory 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. Stabilizes and modulates the
CC activity of the small subunit, increasing the rate of DNA synthesis,
CC and conferring RNA synthesis capability. The DNA polymerase activity
CC may enable DNA primase to also catalyze primer extension after primer
CC synthesis. May also play a role in DNA repair. Possesses a template-
CC independent 3'-terminal nucleotidyl transferase activity.
CC {ECO:0000255|HAMAP-Rule:MF_00701, ECO:0000269|PubMed:15561142}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00701,
CC ECO:0000269|PubMed:17704817};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00701,
CC ECO:0000269|PubMed:17704817};
CC -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit
CC (PriL). {ECO:0000255|HAMAP-Rule:MF_00701, ECO:0000269|PubMed:15561142,
CC ECO:0000269|PubMed:16273105}.
CC -!- INTERACTION:
CC Q9UWW1; Q97Z83: priS; NbExp=5; IntAct=EBI-8081454, EBI-8081502;
CC Q9UWW1; Q9UXG0: ORF-c40_009; Xeno; NbExp=3; IntAct=EBI-8081454, EBI-8081318;
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase large subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00701}.
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DR EMBL; Y18930; CAB57742.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK40874.1; -; Genomic_DNA.
DR PIR; C90202; C90202.
DR RefSeq; WP_009991067.1; NC_002754.1.
DR PDB; 1ZT2; X-ray; 3.33 A; B/D=1-212.
DR PDB; 5OF3; X-ray; 2.91 A; B/E=1-307.
DR PDB; 5OFN; X-ray; 3.00 A; B/C=1-271.
DR PDBsum; 1ZT2; -.
DR PDBsum; 5OF3; -.
DR PDBsum; 5OFN; -.
DR AlphaFoldDB; Q9UWW1; -.
DR SMR; Q9UWW1; -.
DR DIP; DIP-42888N; -.
DR IntAct; Q9UWW1; 2.
DR MINT; Q9UWW1; -.
DR STRING; 273057.SSO0557; -.
DR EnsemblBacteria; AAK40874; AAK40874; SSO0557.
DR GeneID; 44129563; -.
DR KEGG; sso:SSO0557; -.
DR PATRIC; fig|273057.12.peg.567; -.
DR eggNOG; arCOG03013; Archaea.
DR HOGENOM; CLU_052778_1_0_2; -.
DR InParanoid; Q9UWW1; -.
DR OMA; PSCATMQ; -.
DR PhylomeDB; Q9UWW1; -.
DR BRENDA; 2.7.7.102; 6163.
DR BRENDA; 2.7.7.B16; 6163.
DR EvolutionaryTrace; Q9UWW1; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003896; F:DNA primase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06560; PriL; 1.
DR HAMAP; MF_00701; DNA_primase_lrg_arc; 1.
DR InterPro; IPR007238; DNA_primase_lsu_euk/arc.
DR InterPro; IPR023642; DNA_primase_lsu_PriL.
DR Pfam; PF04104; DNA_primase_lrg; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; DNA replication; Iron; Iron-sulfur; Metal-binding;
KW Primosome; Reference proteome.
FT CHAIN 1..307
FT /note="DNA primase large subunit PriL"
FT /id="PRO_0000046787"
FT BINDING 216
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 280
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 289
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 293
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:5OFN"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 63..77
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 80..98
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:5OF3"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 132..141
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:5OF3"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 172..191
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:5OF3"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:5OF3"
FT TURN 219..223
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 229..241
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:5OF3"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:5OF3"
SQ SEQUENCE 307 AA; 35734 MW; 5EF09A913B4ABAC3 CRC64;
MALDVKKYPF IKSLDDELKK YGGGITLTDL LLNSTTLIDQ AKDRIQKTKS GDELPHYVSY
NEPVLVFYTT LLSLAILNDV KLIRRYAYAE AKQFRSLLHT ENEENLLEIS KLLDLKINRC
DPIKFYLEKK RRIIQKEFCV HFIDYLKYTK DLKEDWKLSG QILHKGYVYL DKNQLIGLIA
ESIKSKIVEM IRPLNLKEIP EKLKSLIERR GIIPPCIENI LAKEKLNEEE IRTLITFYID
IGKGLSGIVS IMKKYNVSNV EDLYRKYRGD KGTRYIVYSC AKMKQLGLCV SSCNVKNPLQ
LYFLSNE
