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Database: UniProt
Entry: A0A0R0MF68_9BURK
LinkDB: A0A0R0MF68_9BURK
Original site: A0A0R0MF68_9BURK 
ID   A0A0R0MF68_9BURK        Unreviewed;       624 AA.
AC   A0A0R0MF68;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   31-JUL-2019, entry version 20.
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=AO057_13930 {ECO:0000313|EMBL:KRI00267.1};
OS   Curvibacter sp. PAE-UM.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Curvibacter.
OX   NCBI_TaxID=1714344 {ECO:0000313|EMBL:KRI00267.1, ECO:0000313|Proteomes:UP000051912};
RN   [1] {ECO:0000313|EMBL:KRI00267.1, ECO:0000313|Proteomes:UP000051912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAE-UM {ECO:0000313|EMBL:KRI00267.1,
RC   ECO:0000313|Proteomes:UP000051912};
RA   Ma D.;
RT   "The whole genome sequence of a typical ultramicrobacteria PAE-UM from
RT   river sediment.";
RL   Submitted (SEP-2015) 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
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:KRI00267.1}.
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DR   EMBL; LKCX01000019; KRI00267.1; -; Genomic_DNA.
DR   RefSeq; WP_057676505.1; NZ_KQ483358.1.
DR   EnsemblBacteria; KRI00267; KRI00267; AO057_13930.
DR   OrthoDB; 1071997at2; -.
DR   Proteomes; UP000051912; 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; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000051912};
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:UP000051912};
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       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      38     62       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
FT   REGION      434    469       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   624 AA;  68794 MW;  378ABA1D1B6412BF CRC64;
     MAIPQSFIQE LLARADVVEI VGRTVQLKKG GANFMGLCPF HAEKSPSFTV SPTKQFYHCF
     GCGKHGDAIN FLMEQTGMSF IEAVKDLAQH YGLQVPEDDA SPQDRARAAE QRQKQATLND
     VLEKAGEAWR KQLKSSAKAV DYLKGRGLSG EIARQFGLGY APEGWRSLAS VFPQYDDPLL
     VESGLVITNA DDNSGEEKRY DRFRDRIMFP IRNVKGECIG FGGRVLGDEK PKYLNSPETP
     VFSKGHELYG LFEARNAIRD AGYVLVTEGY MDVVALAQLG FPNAVATLGT ACTTDHVQKL
     FRFTDSVVFS FDGDAAGRRA ARRALDGALP YATDVRSIKF LFLPAEHDPD SYIRENGKEA
     FARCVGEAVP LSRFLIEAAR EGCDLSSAEG RARLASNAKP LWSQLPDGAL KRQLLKEIAG
     QVKVETQELQ ELWGSAKSKE GSPPAGAGAA PRRDNRPAPR NSRRLPIRPA MEAGASNIAR
     LVFRNPGFWE QLTAADHEVL CQLEGTFGDL FRWIDSQVHE HGAQPMAALL AGMGGQPFEA
     QARQLIEFDN LQPLGRQIED PETPLSDLRV AVTRLHLEAI DMELKQVQSL PSGDGTRIEQ
     EKQLIQQQLA YKKSLHDLGK SVRT
//
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