GenomeNet

Database: UniProt
Entry: A3JWN0_9RHOB
LinkDB: A3JWN0_9RHOB
Original site: A3JWN0_9RHOB 
ID   A3JWN0_9RHOB            Unreviewed;       647 AA.
AC   A3JWN0;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 91.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993444};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=RB2150_00512 {ECO:0000313|EMBL:EBA01935.1};
OS   Rhodobacteraceae bacterium HTCC2150.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae.
OX   NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA01935.1, ECO:0000313|Proteomes:UP000004731};
RN   [1] {ECO:0000313|EMBL:EBA01935.1, ECO:0000313|Proteomes:UP000004731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA01935.1,
RC   ECO:0000313|Proteomes:UP000004731};
RX   PubMed=20889754; DOI=10.1128/JB.01088-10;
RA   Kang I., Oh H.M., Vergin K.L., Giovannoni S.J., Cho J.C.;
RT   "Genome sequence of the marine alphaproteobacterium HTCC2150, assigned to
RT   the Roseobacter clade.";
RL   J. Bacteriol. 192:6315-6316(2010).
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, ECO:0000256|SAAS:SAAS00709340}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00709317};
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, ECO:0000256|SAAS:SAAS00709351}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EBA01935.1}.
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; AAXZ01000016; EBA01935.1; -; Genomic_DNA.
DR   RefSeq; WP_008193053.1; NZ_AAXZ01000016.1.
DR   STRING; 388401.RB2150_00512; -.
DR   EnsemblBacteria; EBA01935; EBA01935; RB2150_00512.
DR   eggNOG; ENOG4105C9G; Bacteria.
DR   eggNOG; COG0358; LUCA.
DR   OrthoDB; 1071997at2; -.
DR   Proteomes; UP000004731; Unassembled WGS sequence.
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; 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; PF13662; Toprim_4; 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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00993445};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709369};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709327}; Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709339};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004731};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00993442};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN          262..344
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"
FT   REGION          430..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          575..595
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   647 AA;  71155 MW;  BCFD3B8B4666C321 CRC64;
     MSLPPGFLDE LRTRTSLTQV VGRKVTWDQR KSNQAKGDMW SPCPFHEEKT ASFHVDDRKG
     FYYCFGCHAK GDALGFIRET ENVSFMEAVE ILARENGMPM PARDPQAQKK ADRNAQLAEV
     MEMAVQFYRL QLQTGAAGNA RDYLLRRGLD EAAQARFDIG FAPEQRQILF SHLTGKNVAP
     DLIIEAGLAA KPDDGGAPYD RFRGRILFPI RDARGRAIGL GGRAMDQNAR AKYLNSPETP
     LFDKGRSLYN HGPAREAAGK GAPLIVAEGY MDVIALVEAG FGAAVAPLGT AVTENQLALM
     WRISPEPIIA LDGDKAGIRA AMRLIDIAFP LIEAGKSLRF CIMPEGQDPD DVIKAQGAGA
     MQALLDQAEP MVNLLWRRET DGKNFDSPER RAALDKSLRD ALMLIKDPSI QRHYGEAVKN
     LRWELFDPRQ GKTPQKREWT PGGKGKWNKA PTKPLASTKT SLLASAGAGV EDQLREAVIL
     AALICHPSII PEFEADMDTL HMSPEHAGIR DALLRLPTDT DTESAREIIA QEHRSALDKL
     FALNHVQIAP PVRNTENHSQ AAKCVAEELA KLTSIRGAEL EISEAAEDLQ GIADEGLTWR
     LGQAAEARNA ASRSQDDDSG VMNEDQAALS SKLQDFLDSE IWVKKKR
//
DBGET integrated database retrieval system