ID   PRIL_THEKO              Reviewed;         400 AA.
AC   Q5JJ73;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=DNA primase large subunit PriL {ECO:0000255|HAMAP-Rule:MF_00701};
GN   Name=priL {ECO:0000255|HAMAP-Rule:MF_00701}; OrderedLocusNames=TK1790;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
RN   [2]
RP   FUNCTION AS A PRIMASE, COFACTOR, AND SUBUNIT.
RX   PubMed=22351771; DOI=10.1074/jbc.m111.338145;
RA   Chemnitz Galal W., Pan M., Kelman Z., Hurwitz J.;
RT   "Characterization of DNA primase complex isolated from the archaeon,
RT   Thermococcus kodakaraensis.";
RL   J. Biol. Chem. 287:16209-16219(2012).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00701, ECO:0000269|PubMed:22351771}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000305|PubMed:22351771};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305|PubMed:22351771};
CC   -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit
CC       (PriL). {ECO:0000255|HAMAP-Rule:MF_00701, ECO:0000269|PubMed:22351771}.
CC   -!- SIMILARITY: Belongs to the eukaryotic-type primase large subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_00701}.
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DR   EMBL; AP006878; BAD85979.1; -; Genomic_DNA.
DR   RefSeq; WP_011250741.1; NC_006624.1.
DR   AlphaFoldDB; Q5JJ73; -.
DR   SMR; Q5JJ73; -.
DR   STRING; 69014.TK1790; -.
DR   EnsemblBacteria; BAD85979; BAD85979; TK1790.
DR   GeneID; 3235506; -.
DR   KEGG; tko:TK1790; -.
DR   PATRIC; fig|69014.16.peg.1746; -.
DR   eggNOG; arCOG03013; Archaea.
DR   HOGENOM; CLU_691913_0_0_2; -.
DR   InParanoid; Q5JJ73; -.
DR   OMA; KNIWYHL; -.
DR   OrthoDB; 29893at2157; -.
DR   PhylomeDB; Q5JJ73; -.
DR   BRENDA; 2.7.7.B16; 5246.
DR   Proteomes; UP000000536; 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   4Fe-4S; DNA replication; Iron; Iron-sulfur; Metal-binding; Primosome;
KW   Reference proteome.
FT   CHAIN           1..400
FT                   /note="DNA primase large subunit PriL"
FT                   /id="PRO_0000424554"
FT   BINDING         247
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         356
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         367
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         373
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
SQ   SEQUENCE   400 AA;  46524 MW;  745BB19ACD242E74 CRC64;
     MLDPFGKRAE SLIREEFGDL LALLERVPSA ISVEEPISLV SWMLESENPP QELVEVDNLE
     ELRDLFKFYA LLGAASISPY GLEAEVVKRA TLRLYSERIK ASKNLSETML PVVPVGENEI
     PHNDLNILER RMDRNLSPEE KEKLKIKYKI PIKDLLNLWG SSLKEVYIRN GYAYLRWETA
     LKMWEKAFEK RFERAVNILY EYRDELPEFY HRLREKLEEI AEEYFKERGE MFKGTASPLR
     FDLFPPCVKE ALKGVPAGMR NYAITVLLTS FLSYARICPN PPKKDVRIKD CINDLKIIEE
     EILPVIIEAG NRCKPPLFED QPHEIKNIWY HLGFGLTDSP TMEDSGNSTW YFPPNCDKIR
     ANAPQLCKPD KYCRGIKNPL SYYLKRLYLE GKKKEGETSE