ID   PRIL_PYRFU              Reviewed;         396 AA.
AC   Q8U4H7;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=DNA primase large subunit PriL {ECO:0000255|HAMAP-Rule:MF_00701};
DE   AltName: Full=DNA primase 46 kDa subunit;
DE            Short=p46;
GN   Name=priL {ECO:0000255|HAMAP-Rule:MF_00701}; Synonyms=priB;
GN   OrderedLocusNames=PF0111;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [2]
RP   FUNCTION AS A PRIMASE, AND SUBUNIT.
RX   PubMed=11584001; DOI=10.1074/jbc.m106391200;
RA   Liu L., Komori K., Ishino S., Bocquier A.A., Cann I.K., Kohda D.,
RA   Ishino Y.;
RT   "The archaeal DNA primase: biochemical characterization of the p41-p46
RT   complex from Pyrococcus furiosus.";
RL   J. Biol. Chem. 276:45484-45490(2001).
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:11584001}.
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). Both participate in formation of the active center, but the
CC       ATP-binding site is exclusively located on the small subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00701, ECO:0000269|PubMed:11584001}.
CC   -!- SIMILARITY: Belongs to the eukaryotic-type primase large subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_00701}.
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DR   EMBL; AE009950; AAL80235.1; -; Genomic_DNA.
DR   RefSeq; WP_014835470.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U4H7; -.
DR   SMR; Q8U4H7; -.
DR   STRING; 186497.PF0111; -.
DR   PRIDE; Q8U4H7; -.
DR   EnsemblBacteria; AAL80235; AAL80235; PF0111.
DR   GeneID; 41711898; -.
DR   KEGG; pfu:PF0111; -.
DR   PATRIC; fig|186497.12.peg.115; -.
DR   eggNOG; arCOG03013; Archaea.
DR   HOGENOM; CLU_691913_0_0_2; -.
DR   OMA; KNIWYHL; -.
DR   OrthoDB; 29893at2157; -.
DR   PhylomeDB; Q8U4H7; -.
DR   BRENDA; 2.7.7.102; 5243.
DR   BRENDA; 2.7.7.B16; 5243.
DR   Proteomes; UP000001013; 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..396
FT                   /note="DNA primase large subunit PriL"
FT                   /id="PRO_0000046785"
FT   BINDING         231
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         340
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         351
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         357
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
SQ   SEQUENCE   396 AA;  46209 MW;  A133205629114C42 CRC64;
     MLDPFSEKAK ELLKEFGSMN EFLQAIPSLV DIEEVMNRLK FAKESEISED ILNIEDIRDL
     ASFYAQIGAL AYSPYGLELE LVKKANLRIY TERIRRRRKI RSDEIGIEVK IAVEFPENDI
     KTLEKVYGGL PEYIVSLREF LDLVPDEKLS SYYVYDGNVY LRKDDLLKVW SKAFERNVEK
     AVNIIYEIRD ELPEFYRRLA GEIRSFAEKE FSDKFREVQA GELKHHLFPP CVKNALRGVP
     QGMRNYAITV LLTSFLSYAR ICPNPPRRNV KIRDCIKDMR VITEEILPII IEAGNRCSPP
     LFEDQPNEIK NIWYHLGFGY TANPTLEDSG NSTWYFPPNC DKIKANAPQL CTPDKHCRYI
     RNPLTYYLRR LYLEEKRRAK HADEGSDKGG KERILQ