ID   PRIL_HALMA              Reviewed;         358 AA.
AC   Q5UYQ8;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=DNA primase large subunit PriL {ECO:0000255|HAMAP-Rule:MF_00701};
GN   Name=priL {ECO:0000255|HAMAP-Rule:MF_00701}; Synonyms=pri2, priB;
GN   OrderedLocusNames=rrnAC2844;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY596297; AAV47595.1; -; Genomic_DNA.
DR   RefSeq; WP_011224464.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UYQ8; -.
DR   STRING; 272569.rrnAC2844; -.
DR   EnsemblBacteria; AAV47595; AAV47595; rrnAC2844.
DR   GeneID; 40153692; -.
DR   KEGG; hma:rrnAC2844; -.
DR   PATRIC; fig|272569.17.peg.3415; -.
DR   eggNOG; arCOG03013; Archaea.
DR   HOGENOM; CLU_052778_0_0_2; -.
DR   OMA; PSCATMQ; -.
DR   Proteomes; UP000001169; Chromosome I.
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..358
FT                   /note="DNA primase large subunit PriL"
FT                   /id="PRO_0000046778"
FT   REGION          335..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..358
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         234
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         306
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         315
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         322
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
SQ   SEQUENCE   358 AA;  39976 MW;  901E60B6A55815A6 CRC64;
     MEPLHARYPF LARSREAVEA AAVDLGEIVA TDETVTARAL ERVESAITDG TVGEPHRRTR
     VELLSYPVAR VLVSLVDVHI CTRKYAQAEA EAAYDRFTEE FATTTELKST QRETLDRTEL
     LGEFDLASAV SDAGDGYRVE VGAYLDLAAD QRGDSWRLVN RPLTDGEVRV TAEELNVLLK
     QAIRHRVTDG LPFTVPDAIA DELTAEVEQL EEVLSELELT REIDTVVPEL FPPCMKSLLD
     QVQKGEHLEH HSRFAIATFL VGIGMTTDEI VDLFQVNPGF GEEATRYQVD HIRGDTSPTE
     YSTPACSTMQ SYGDCVNMDD LCEAISHPMG YYEQKLDDTD EEELVDWRED EGEEEADA