ID   PRIL_THEAC              Reviewed;         340 AA.
AC   Q9HJD1;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Ta1038;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
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}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00701};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00701};
CC   -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit
CC       (PriL). {ECO:0000255|HAMAP-Rule:MF_00701}.
CC   -!- SIMILARITY: Belongs to the eukaryotic-type primase large subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_00701}.
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DR   EMBL; AL445066; CAC12167.1; -; Genomic_DNA.
DR   RefSeq; WP_010901449.1; NC_002578.1.
DR   AlphaFoldDB; Q9HJD1; -.
DR   STRING; 273075.Ta1038; -.
DR   DNASU; 1456559; -.
DR   EnsemblBacteria; CAC12167; CAC12167; CAC12167.
DR   GeneID; 1456559; -.
DR   KEGG; tac:Ta1038; -.
DR   eggNOG; arCOG03013; Archaea.
DR   HOGENOM; CLU_052778_0_0_2; -.
DR   OMA; ITRYQIK; -.
DR   OrthoDB; 29893at2157; -.
DR   Proteomes; UP000001024; 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   PANTHER; PTHR10537; PTHR10537; 1.
DR   Pfam; PF04104; DNA_primase_lrg; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; DNA replication; Iron; Iron-sulfur; Metal-binding; Primosome;
KW   Reference proteome.
FT   CHAIN           1..340
FT                   /note="DNA primase large subunit PriL"
FT                   /id="PRO_0000046789"
FT   BINDING         229
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         301
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         310
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         318
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
SQ   SEQUENCE   340 AA;  39049 MW;  E1A13EBF1B06CCCC CRC64;
     MILPDRKQIL DRELIRRIAD TTISGSGHSD GLSEYASIRK AAFAFVESAV LGDQAYSPIE
     NAELAFIVWI LAALDENIIT ARTIIKARDT VEKQLRLVEH YEDLEEFGSR LGIEISVFGE
     QIGKDHLYRI GVADFATYAS RVTGSKYRLS NQIVREGYVY VDEDVMAKVL REAFVSFMFD
     TLDQIRKEDA IETIKSVLDD LEKIRESYRK AHNVRMIAGK GDASMFPPCM KEIIKNLESG
     VNVSHMGRLA LASFLHKAGY SEDEIVPYFR NAPDFDENIT RYQIKHISGE ISGTEYTPPK
     CETMRSNHLC YMDDDPLCHR EWMKHPLTYY EVKRRNRKIR