GenomeNet

Database: UniProt
Entry: A0A1N7K7F4_9RHOB
LinkDB: A0A1N7K7F4_9RHOB
Original site: A0A1N7K7F4_9RHOB 
ID   A0A1N7K7F4_9RHOB        Unreviewed;       643 AA.
AC   A0A1N7K7F4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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   ORFNames=SAMN05421774_101256 {ECO:0000313|EMBL:SIS57497.1};
OS   Gemmobacter megaterium.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Gemmobacter.
OX   NCBI_TaxID=1086013 {ECO:0000313|EMBL:SIS57497.1, ECO:0000313|Proteomes:UP000186141};
RN   [1] {ECO:0000313|EMBL:SIS57497.1, ECO:0000313|Proteomes:UP000186141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26375 {ECO:0000313|EMBL:SIS57497.1,
RC   ECO:0000313|Proteomes:UP000186141};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FTOT01000001; SIS57497.1; -; Genomic_DNA.
DR   RefSeq; WP_076527916.1; NZ_FTOT01000001.1.
DR   AlphaFoldDB; A0A1N7K7F4; -.
DR   STRING; 1086013.SAMN05421774_101256; -.
DR   OrthoDB; 9803773at2; -.
DR   Proteomes; UP000186141; Unassembled WGS sequence.
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; 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; PF08275; DNAG_N; 1.
DR   Pfam; PF13662; Toprim_4; 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:UP000186141};
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          262..346
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         43..67
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974"
SQ   SEQUENCE   643 AA;  70275 MW;  406F717F70CBFC31 CRC64;
     MSLPPGFLDE LRNRLSLTQV VGRKVTWDMR KSNQAKGDMW APCPFHQEKS ASFHVDDRKG
     FYYCFGCHAK GDAISFVKET ENVGFMEAVE ILAREAGMPM PARDPRAAEV ADRRSKLAEV
     MEAAVQHYRL MLRSGSGAVA RDYLVRRRLP EAAQDRWHIG WAPDSRTGLL QALGAKGIAP
     ELVVEAGLAI KPDDGGAPYD RFRGRVIFPI RDGRGRAISL GGRSLDPNAR AKYLNGPETA
     LFDKGRNLFN IGPAREAAGK GLPLVVAEGY MDVIALSEAG FRGAVAPLGT AVTEDQLRLM
     WRIHDEPVIA LDGDAAGLRA ALRVIDLALP MLEAGKGLRF AVMPGGMDPD DLIKAEGAGA
     FQRVLEGAQP MVRLLWQRET EGQVFDSPER RAALDKRLRA ALARIADPSI RAHYGTEMKR
     LREDLFGTGV RAPRGFVPRH WQQKVKAAPM PSTRASMLAG SGEAVEERLR EAVVLSVLAL
     HPDLVETFDT ALERMECTDP AHGQLRTALL RAAQAADPRG TLSAMAGPEL ETLRALPHVQ
     IVPAVRNPED AVMARLCLAE EFAKLEARRT ARREIAEGVE EVGEGSTPSD EGLTWRLGQA
     AEAVNRAGRA QNEDSSDLGE DRAAMSGYLQ SLIDGQVWVK KRH
//
DBGET integrated database retrieval system