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Database: UniProt
Entry: A0A0B4CL98_9RHOB
LinkDB: A0A0B4CL98_9RHOB
Original site: A0A0B4CL98_9RHOB 
ID   A0A0B4CL98_9RHOB        Unreviewed;       667 AA.
AC   A0A0B4CL98;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   11-DEC-2019, entry version 27.
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=RA20_22300 {ECO:0000313|EMBL:KIC13811.1};
OS   Leisingera sp. ANG-Vp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Leisingera.
OX   NCBI_TaxID=1577896 {ECO:0000313|EMBL:KIC13811.1, ECO:0000313|Proteomes:UP000031177};
RN   [1] {ECO:0000313|Proteomes:UP000031177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANG-Vp {ECO:0000313|Proteomes:UP000031177};
RX   PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA   Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT   "Comparative genomics of Roseobacter clade bacteria isolated from the
RT   accessory nidamental gland of Euprymna scolopes.";
RL   Front. Microbiol. 6:123-123(2015).
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:KIC13811.1}.
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DR   EMBL; JWLD01000086; KIC13811.1; -; Genomic_DNA.
DR   RefSeq; WP_039134147.1; NZ_JWLD01000086.1.
DR   EnsemblBacteria; KIC13811; KIC13811; RA20_22300.
DR   Proteomes; UP000031177; 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; 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   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          428..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          591..618
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   667 AA;  73714 MW;  E9AC7C49F70FC74B CRC64;
     MSLPPGFLDE LRTRISISDV VGRKVMWDQR KSQPGKGDYW SPCPFHHEKT ASFHVEDRKG
     FYYCFGCHAK GDALKFVQET ENVGFMEAVE ILAGEAGMEM PKRDPRAQEK QDRRALLADV
     MEQAVQFFRL QLKTGAAQDA RAYLQRRGMT AQALDRWEIG FAPDGWQNLW DALRGKNVPE
     DLIIGAGLAK PSNKGGKPYD TFRNRIMFPI RDARGRAIAF GGRAMDPNDN AKYLNSPETE
     LFDKGRSLYN HGPARSASGR GSTLVVAEGY MDVIALAEGG FQSSVAPLGT AITENQLQML
     WRMSDEPIIA LDGDKAGIRA AMRLIDLALP LLEAGKSLRF AIMPEGKDPD DMIRSEGPEA
     VQAVLDQAMP MVKLLWQRET DGKVFDSPER KAALDKALRE KIKLIRDPSI RKHYGEDVKE
     MRWQLFRGGR DSGGGGGGYQ QRGGKGGGFR DGARASWKPG KGFGPIPQPR ATTRASLVAG
     ADDESFASMR EAVILATAIT TPDVIPEFET SLERLHCADP DLAALRDMVL RHGISAPDRL
     REEIDWSLGP HALENLFALR HVAIIPCLRK PGDAELASMT LAEELAKLEA RRGLDAELAE
     AEEDLDGLAD EALTWRLRQA AEAKNKAVRS ENEDKATYDV GKNGARLNRD ERDAFGALLD
     RIGFSEK
//
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