ID Q46L65_PROMT Unreviewed; 675 AA.
AC Q46L65;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974};
DE EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN OrderedLocusNames=PMN2A_0271 {ECO:0000313|EMBL:AAZ57763.1};
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59920 {ECO:0000313|EMBL:AAZ57763.1, ECO:0000313|Proteomes:UP000002535};
RN [1] {ECO:0000313|EMBL:AAZ57763.1, ECO:0000313|Proteomes:UP000002535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A {ECO:0000313|EMBL:AAZ57763.1,
RC ECO:0000313|Proteomes:UP000002535};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC molecules used as primers for DNA polymerase during DNA replication.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00974};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00974};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00974};
CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00974}.
CC -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000256|HAMAP-
CC Rule:MF_00974}.
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DR EMBL; CP000095; AAZ57763.1; -; Genomic_DNA.
DR RefSeq; WP_011293805.1; NC_007335.2.
DR AlphaFoldDB; Q46L65; -.
DR STRING; 59920.PMN2A_0271; -.
DR KEGG; pmn:PMN2A_0271; -.
DR HOGENOM; CLU_013501_3_1_3; -.
DR OrthoDB; 9803773at2; -.
DR PhylomeDB; Q46L65; -.
DR Proteomes; UP000002535; Chromosome.
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; 3.40.1360.10; -; 1.
DR Gene3D; 3.90.980.10; DNA primase, catalytic core, N-terminal domain; 1.
DR Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
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; IPR013264; DNAG_N.
DR InterPro; IPR034151; TOPRIM_DnaG_bac.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR002694; Znf_CHC2.
DR NCBIfam; TIGR01391; dnaG; 1.
DR PANTHER; PTHR30313; DNA PRIMASE; 1.
DR PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR Pfam; PF10410; DnaB_bind; 1.
DR Pfam; PF08275; DNAG_N; 1.
DR Pfam; PF13155; Toprim_2; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SMART; SM00400; ZnF_CHCC; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00974};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00974};
KW Reference proteome {ECO:0000313|Proteomes:UP000002535};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00974};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_00974}.
FT DOMAIN 265..350
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT ZN_FING 41..65
FT /note="CHC2-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00974"
SQ SEQUENCE 675 AA; 76986 MW; 3417248923C0E66C CRC64;
MASARLHPKT IESVKERVDI VDVVGEHVVL KKKGKEYVGI CPFHDDSKPS MSVIPGKQFY
YCFSCGAGGN AIKFLMEFQR QSFSDVVLEL AKKYQVPIDT IEGPQQERLK QQLSRRDTLY
RVLKTATGWF RNQLNSPCGE NALNYLKNKR NLSDGTLINF ELGFAPDNWD SLLKYFVDIE
KVSVEILESA GLIVPRKGGN GFYDRFRNRI IVPIHDRQKR VIGFGGRSLD GSEPKYLNSP
ETEIFEKGKN LFGFDKSTLS IRKKDYAVVV EGYFDVMALH DSGITNVVAS LGTALSRNQI
TLLSRATDSK KILLNFDSDN AGIRAANRAI SEVENLAIQG QLDLRVLQLP SGKDPDEFLK
DNSPSEYEAL AAKSPLWMDW QIDQSLKDLD LSKSDQFQEA VSSLVSLLGK LPQTAIRTHY
LQKVAQRLSG GQGRFSLQLE EDLRNQISGQ RWHGRSKKID KPQEISLRER SEADILFTYI
HCPNYRSFIR YELRLRDLDD FAINHHRAIW STISNIEENM FGPEIVEKIN RFNDSNNILA
DVDLIKKLLD NFLSSDNEHL PKLTPLLDVN ELRLATLNDP ESLIRGALAA LEKQKSLKRC
RHLIDAWSSQ RLQTLENCIA SLIVQEKSEP SDSSDMEQRV ISMFEDLNND AINFQQLYYA
ERKHILNLDQ QRCYK
//
