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PRIL_ARCFU
ID   PRIL_ARCFU              Reviewed;         370 AA.
AC   O29911;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=AF_0336;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB90898.1; -; Genomic_DNA.
DR   PIR; H69291; H69291.
DR   RefSeq; WP_010877843.1; NC_000917.1.
DR   AlphaFoldDB; O29911; -.
DR   STRING; 224325.AF_0336; -.
DR   DNASU; 1483550; -.
DR   EnsemblBacteria; AAB90898; AAB90898; AF_0336.
DR   GeneID; 24793875; -.
DR   KEGG; afu:AF_0336; -.
DR   eggNOG; arCOG03013; Archaea.
DR   HOGENOM; CLU_052778_0_0_2; -.
DR   OMA; EAYHEEA; -.
DR   OrthoDB; 29893at2157; -.
DR   PhylomeDB; O29911; -.
DR   Proteomes; UP000002199; 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..370
FT                   /note="DNA primase large subunit PriL"
FT                   /id="PRO_0000046777"
FT   BINDING         268
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         341
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         350
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         354
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
SQ   SEQUENCE   370 AA;  42844 MW;  4368F68516EEB90E CRC64;
     MKYLPLYPIL ARYPFLRIAS RVFSFNIEDE LRKFLDTVEA AKRIVDKAID GRVEYDRFTD
     ESEFFCLGCE ENCYDCQKRG TLEGCDLCMG CFENCSLYYP REAVERFYTN AKLSLLTYIA
     SRMIVSAMED WVRMRYAVNE ASYYSRLLRE DVEESGKEPI VRLVAIDLGA KLKGWKMHVS
     TFVRVSARIK DDKWRLVNRK LRNGWVETTK AEVLRGLEEL LRMKLFEKVP VSEAVSEAVR
     ELSRKAKRES EKFAMDLGEV DLNCLPPCMR EILSELQRGM NIPHTARFAI TSFLLNIGMT
     VDEIIALFKS APDFDDEKTR YQVEHIAGER GKGAEYTSPS CDTMRTYSNC VADCRVSHPL
     IYYKKCKSKS
 
 
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