PRIL_PYRAB
ID PRIL_PYRAB Reviewed; 393 AA.
AC Q9V291; G8ZG18;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=DNA primase large subunit PriL {ECO:0000255|HAMAP-Rule:MF_00701};
DE AltName: Full=DNA primase 46 kDa subunit;
DE Short=Pabp46;
DE Short=p46;
GN Name=priL {ECO:0000255|HAMAP-Rule:MF_00701}; Synonyms=priB;
GN OrderedLocusNames=PYRAB01830; ORFNames=PAB2235;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
RN [3]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=GE5 / Orsay;
RX PubMed=17991487; DOI=10.1016/j.jmb.2007.10.015;
RA Le Breton M., Henneke G., Norais C., Flament D., Myllykallio H.,
RA Querellou J., Raffin J.P.;
RT "The heterodimeric primase from the euryarchaeon Pyrococcus abyssi: a
RT multifunctional enzyme for initiation and repair?";
RL J. Mol. Biol. 374:1172-1185(2007).
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. Displays gap-filling and
CC strand-displacement activities. {ECO:0000255|HAMAP-Rule:MF_00701,
CC ECO:0000269|PubMed:17991487}.
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, ECO:0000269|PubMed:17991487}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase large subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00701}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCE69559.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ248283; CAB49107.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69559.1; ALT_INIT; Genomic_DNA.
DR PIR; D75207; D75207.
DR RefSeq; WP_048146502.1; NC_000868.1.
DR AlphaFoldDB; Q9V291; -.
DR SMR; Q9V291; -.
DR STRING; 272844.PAB2235; -.
DR EnsemblBacteria; CAB49107; CAB49107; PAB2235.
DR GeneID; 1495070; -.
DR KEGG; pab:PAB2235; -.
DR PATRIC; fig|272844.11.peg.197; -.
DR eggNOG; arCOG03013; Archaea.
DR HOGENOM; CLU_691913_0_0_2; -.
DR OMA; KNIWYHL; -.
DR OrthoDB; 29893at2157; -.
DR PhylomeDB; Q9V291; -.
DR BRENDA; 2.7.7.102; 5242.
DR BRENDA; 2.7.7.B16; 5242.
DR SABIO-RK; Q9V291; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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.
FT CHAIN 1..393
FT /note="DNA primase large subunit PriL"
FT /id="PRO_0000046784"
FT BINDING 230
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT BINDING 339
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 356
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
SQ SEQUENCE 393 AA; 45486 MW; 9448642FBB3FBF43 CRC64;
MLDPFSEKAK ELLKEFGSIN DFLNSIPRIV DVEEVIERVK IASDRKLLEG FVDIEDIKDL
AQFYALLGAL SYSPYGLELE LVKKANILLY SERIRREKEI RPEEISLRIN KAIEFPIDDL
KKIERVFGKL PEYTIHLAEF LDLIPGERLS EYYIYNGNVY LRKEDLIKVW MKAFERNIEK
SVNMLYEIRD ELPGFFREVL GGIKEVAEQE FGKSGEVKAG TLRPDLFPPC VKNALKGVPQ
GLRNYAITVL LTSFLSYARI CPNPPRRNVR VKDCIDDIRI ITDEILPLII EAANRCSPPL
FEDQPNEIKN IWYHLGFGYT ANPKLEDSGN STWYFPPNCD KIRANAPQLC TPDKHCKYVR
NPLTYYLRRL YLEGRKNASK GGNERGEKRV LQQ
