PRIL_METKA
ID PRIL_METKA Reviewed; 406 AA.
AC Q8TVJ5;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=MK1394;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(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; AE009439; AAM02607.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TVJ5; -.
DR SMR; Q8TVJ5; -.
DR STRING; 190192.MK1394; -.
DR EnsemblBacteria; AAM02607; AAM02607; MK1394.
DR KEGG; mka:MK1394; -.
DR HOGENOM; CLU_677258_0_0_2; -.
DR Proteomes; UP000001826; 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 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..406
FT /note="DNA primase large subunit PriL"
FT /id="PRO_0000046781"
FT BINDING 302
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 375
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 384
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 389
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
SQ SEQUENCE 406 AA; 46873 MW; 9F08B3B42B4030D5 CRC64;
MRSWFPHAPT VSVPEIEPEE ALSYRDEIRT RVRSYAFGLD DWRAKVKTRR AYLRKVRDED
ESEILRVYGA LLTVAAAGPR PVRHLIAEGE SAMAETALYA LRHEDESAMS YPEERVLSDL
YLWDVRVLER DLGLYAVHFS FPLIHRSPEG QKLKVLVWER ASLEKVLKEV RSNRVLGVRV
LDPSGWNDVW ICPRCGATRR GGTGDLEQDH ARRCSNCRGR MRKPDPNLLE MLKEPEGYLI
MHFKTLARTF REDVRRLVVS DIESRDDVED EELREFCLKL FPKVRKRLER VEKGAGGRFP
PCIRELLRRA QEGENLPHEA RFALAAFLVN VGWDVDRVVE VFSNLPDFDE ERTQYQVRHI
AGEVGGGTRY LPPNCDKMKA WGLCPGKDCG VKNPLAYYRR PRADDG