DNAG_SYNE7
ID DNAG_SYNE7 Reviewed; 694 AA.
AC P74893; Q31NP7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974};
DE EC=2.7.7.101 {ECO:0000255|HAMAP-Rule:MF_00974};
GN Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974};
GN OrderedLocusNames=Synpcc7942_1292;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-616, AND MUTAGENESIS OF CYS-597.
RX PubMed=9694883; DOI=10.1074/jbc.273.33.21246;
RA Bird A.J., Turner-Cavet J.S., Lakey J.H., Robinson N.J.;
RT "A carboxyl-terminal Cys2/His2-type zinc-finger motif in DNA primase
RT influences DNA content in Synechococcus PCC 7942.";
RL J. Biol. Chem. 273:21246-21252(1998).
CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC molecules used as primers for DNA polymerase during DNA replication.
CC {ECO:0000255|HAMAP-Rule:MF_00974}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC EC=2.7.7.101; Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000255|HAMAP-Rule:MF_00974};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00974};
CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000255|HAMAP-
CC Rule:MF_00974}.
CC -!- DOMAIN: Contains an N-terminal zinc-binding domain, a central core
CC domain that contains the primase activity, and a C-terminal DnaB-
CC binding domain. {ECO:0000255|HAMAP-Rule:MF_00974}.
CC -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000255|HAMAP-
CC Rule:MF_00974}.
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DR EMBL; CP000100; ABB57322.1; -; Genomic_DNA.
DR EMBL; X94247; CAA63931.1; -; Genomic_DNA.
DR PIR; T11850; T11850.
DR RefSeq; WP_011377965.1; NC_007604.1.
DR AlphaFoldDB; P74893; -.
DR SMR; P74893; -.
DR STRING; 1140.Synpcc7942_1292; -.
DR PRIDE; P74893; -.
DR EnsemblBacteria; ABB57322; ABB57322; Synpcc7942_1292.
DR KEGG; syf:Synpcc7942_1292; -.
DR eggNOG; COG0358; Bacteria.
DR HOGENOM; CLU_013501_3_1_3; -.
DR OMA; LWLDWQI; -.
DR OrthoDB; 1071997at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1292-MON; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd03364; TOPRIM_DnaG_primases; 1.
DR Gene3D; 3.90.580.10; -; 1.
DR Gene3D; 3.90.980.10; -; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR InterPro; IPR013264; DNA_primase_core_N.
DR InterPro; IPR037068; DNA_primase_core_N_sf.
DR InterPro; IPR019475; DNA_primase_DnaB-bd.
DR InterPro; IPR006295; DNA_primase_DnaG.
DR InterPro; IPR036977; DNA_primase_Znf_CHC2.
DR InterPro; IPR030846; DnaG_bac.
DR InterPro; IPR034151; TOPRIM_DnaG_bac.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR002694; Znf_CHC2.
DR Pfam; PF10410; DnaB_bind; 1.
DR Pfam; PF08275; Toprim_N; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SMART; SM00400; ZnF_CHCC; 1.
DR TIGRFAMs; TIGR01391; dnaG; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW DNA replication; DNA-binding; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Primosome; Transcription;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..694
FT /note="DNA primase"
FT /id="PRO_0000180528"
FT DOMAIN 265..348
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT ZN_FING 41..65
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT MUTAGEN 597
FT /note="C->S: Cell contains less chromosomes than the
FT equivalent wild-type, but grows at the same rate."
FT /evidence="ECO:0000269|PubMed:9694883"
FT CONFLICT 223
FT /note="G -> A (in Ref. 2; CAA63931)"
FT /evidence="ECO:0000305"
FT CONFLICT 615..616
FT /note="CI -> LH (in Ref. 2; CAA63931)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 694 AA; 78524 MW; A3417991A7863BE9 CRC64;
MDTPRLHPET IAAVKERADI VDIVSEQVVL KKRGKDFVGL CPFHDDKSPS FTVSPAKQFY
YCFSCGAGGN PIKFLMELGK QSFSEVVLDL AKRYQVPVRT LEVQQHQELQ RQLSRRERLY
EVLAVATQFY EQSLRRPEGA AALDYLRRSR QLQESTIQKF QLGYAPAQWA SLATHLIEQK
RFPADLVEEA GLVVARRNGQ GYYDRFRDRL MIPIHDLQGR VVGFGGRTLT GEEPKYLNSP
ETTLFEKGKL LFGLDKARAA IAKQDQAVVV EGYFDVIALH AAGIDHAVAS LGTALSRQQV
KLLSRYSESN QIVLNFDADR AGAKAAERAI GEVEDLAYQG QVQLRVLNLP GGKDADEYLQ
RHSVADYREL LARSPLWLDW QIDQLLRDRN LDQADQFQAV VQAIVQLLGK LPNTPLRTHY
VHQVAERLSQ GEARTAVQLA SDLRAQVRGQ RWHGQASRWE KPGDVSIREQ AEAQILKVYL
HCPRLRLAVR KTLHDREIQG FSLQPHRLLW QAIAEIEEAH LGFAAMYQVE RGEGNGDDLA
AIDLVPILRD RLDQLTGVSL GGFLELSEND HADLTHPLPL LRGAVALVER LRCEKRCRHL
LDSWARQSIH TFEHCIEQLL QAGIGEDVDA EAQITALHEQ LNQEALHFQK LYYNERRYLQ
QLDQERCLNP QAFLGMTEHD ATAIAPTTPQ PISA
