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Database: UniProt
Entry: M5T6F9_9PLAN
LinkDB: M5T6F9_9PLAN
Original site: M5T6F9_9PLAN 
ID   M5T6F9_9PLAN            Unreviewed;       692 AA.
AC   M5T6F9;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   31-JUL-2019, entry version 43.
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=RRSWK_02750 {ECO:0000313|EMBL:EMI44684.1};
OS   Rhodopirellula sp. SWK7.
OC   Bacteria; Planctomycetes; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Rhodopirellula.
OX   NCBI_TaxID=595460 {ECO:0000313|EMBL:EMI44684.1, ECO:0000313|Proteomes:UP000012028};
RN   [1] {ECO:0000313|EMBL:EMI44684.1, ECO:0000313|Proteomes:UP000012028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SWK7 {ECO:0000313|EMBL:EMI44684.1,
RC   ECO:0000313|Proteomes:UP000012028};
RX   PubMed=23273849;
RA   Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C.,
RA   Richter M., Achstetter T., Glockner F.O., Harder J.;
RT   "Expression of sulfatases in Rhodopirellula baltica and the diversity
RT   of sulfatases in the genus Rhodopirellula.";
RL   Mar. Genomics 0:0-0(2012).
CC   -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC       molecules used as primers for DNA polymerase during DNA
CC       replication. {ECO:0000256|HAMAP-Rule:MF_00974,
CC       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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00974};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       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.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709351}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EMI44684.1}.
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DR   EMBL; ANOQ01000049; EMI44684.1; -; Genomic_DNA.
DR   RefSeq; WP_009097299.1; NZ_ANOQ01000049.1.
DR   STRING; 595460.RRSWK_02750; -.
DR   EnsemblBacteria; EMI44684; EMI44684; RRSWK_02750.
DR   PATRIC; fig|595460.3.peg.3006; -.
DR   Proteomes; UP000012028; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000012028};
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};
KW   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,
KW   ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012028};
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       24     78       ZnF_CHCC. {ECO:0000259|SMART:SM00400}.
FT   DOMAIN      273    344       Toprim. {ECO:0000259|SMART:SM00493}.
FT   ZN_FING      28     52       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
FT   REGION      452    501       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      516    550       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    522    550       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   692 AA;  76394 MW;  5E27CFA20275D714 CRC64;
     MRNASDIVDV IGRDLELRPQ GRNFVARCPF HNDTKPSMTV NQERQSWKCW VCDIGGDVFS
     FVMQREGVDF PGALRMLAER AGIELPEYRK GPKTQPGDPD DKATLAAAIE EVAQAYYEQL
     DARKSDDAKA AWDYLASRGI NDENRQRFRI GFAPDSWDFA VNLLKRKNFT EQVAVACGVA
     KSRGNRSGNQ SGNDGCYDFF RGRLMFPINN AHGKVISLGG RIIPAIAERT VAASGGKVTA
     GAKYFNGPET LLYRKSSELY GLDLARDAIR SAGEVLVMEG YTDVVATRMA GIENAVAVLG
     TALTAQHVRI LKRFAPRVVL VLDGDDAGRR RAEEVLELFV TADADLRILT LPDNADPADF
     LAAHSAPALL DMAANAPDAV DHKIARLTEG VDITRDTHRV TSAIETLLSL FVKVPQNDDH
     ASLKVDQLLM RMSRTFELPV DRLSRRLDAL RADRKESEAK KARYQKKPNG PAQHNAPSKP
     SSAPAPSAPP PHDDYADFGF DDPFASAAME DAAMFGIDDS MPPSSSVPST PSRSFSPSQR
     TNDSQSQPLS GVERELFETL LESPEVAAMA IEAIDPDWLR STTAKMLLSA YQDLDLQGHD
     LDSASLLTLL ENEFLKNQII TLQQRVDTRA DRIAESPHER YAAILTRFHE REFEAEKSRQ
     IVQLESATLP EDEELAVLQA IIAAERIRHN PR
//
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