ID   PRIL_METAC              Reviewed;         371 AA.
AC   Q8TUF8;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=MA_0109;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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; AE010299; AAM03563.1; -; Genomic_DNA.
DR   RefSeq; WP_011020168.1; NC_003552.1.
DR   AlphaFoldDB; Q8TUF8; -.
DR   STRING; 188937.MA_0109; -.
DR   EnsemblBacteria; AAM03563; AAM03563; MA_0109.
DR   GeneID; 1472001; -.
DR   KEGG; mac:MA_0109; -.
DR   HOGENOM; CLU_052778_0_0_2; -.
DR   InParanoid; Q8TUF8; -.
DR   OMA; PSCATMQ; -.
DR   OrthoDB; 29893at2157; -.
DR   PhylomeDB; Q8TUF8; -.
DR   Proteomes; UP000002487; 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..371
FT                   /note="DNA primase large subunit PriL"
FT                   /id="PRO_0000046780"
FT   REGION          337..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         230
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         317
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
SQ   SEQUENCE   371 AA;  42277 MW;  E3D4AEA8C019DA5A CRC64;
     MQAEKLAYYP FISEASAHVG DLGISLESLL NSRAYRTARA RGIERVKEAL EGEIKKPPVS
     EEAQVLSELL SYPFARMLVA CVDDQLFTRR YALAEAKAAY TFLRNETPDF LLEFGEDFGI
     SAEIRDSHFS MHFTDYIRFS NSLKEPSWKL TNRQFRAGKI KITKEEFARL LEEAVRERIE
     QSFPIPEIPP EVSAFCAPYV AEIKEQFEVQ KKKFGATDFG AVEPELFPPC ISHALANVQG
     GVNLAHSMRF AMTSFLLNVG MSVEEILNLF NVSPDFDAEK TLYQIEHIAG ATGNEYKPPA
     CDTMRTYGNC IGKDGLCAKI SHPLGYYERR IFLKNKEREK EEGKEKGNEE KKEKREEHEK
     KNEKGNEIKE K