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Database: UniProt
Entry: A0A0H4UWD4_9COXI
LinkDB: A0A0H4UWD4_9COXI
Original site: A0A0H4UWD4_9COXI 
ID   A0A0H4UWD4_9COXI        Unreviewed;       566 AA.
AC   A0A0H4UWD4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   05-DEC-2018, entry version 22.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993444};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974,
GN   ECO:0000313|EMBL:AKQ33268.1};
GN   ORFNames=CleRT_02750 {ECO:0000313|EMBL:AKQ33268.1};
OS   Coxiella-like endosymbiont.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Coxiellaceae.
OX   NCBI_TaxID=1592897 {ECO:0000313|EMBL:AKQ33268.1};
RN   [1] {ECO:0000313|EMBL:AKQ33268.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRt {ECO:0000313|EMBL:AKQ33268.1};
RX   PubMed=26025560; DOI=10.1093/gbe/evv108;
RA   Gottlieb Y., Lalzar I., Klasson L.;
RT   "Distinctive Genome Reduction Rates Revealed by Genomic Analyses of
RT   Two Coxiella-Like Endosymbionts in Ticks.";
RL   Genome Biol. Evol. 7:1779-1796(2015).
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|PIRNR:PIRNR002811, 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, ECO:0000256|PIRNR:PIRNR002811,
CC         ECO:0000256|PIRSR:PIRSR002811-1};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC       ECO:0000256|PIRSR:PIRSR002811-1};
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|PIRNR:PIRNR002811,
CC       ECO:0000256|SAAS:SAAS00709351}.
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DR   EMBL; CP011126; AKQ33268.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKQ33268; AKQ33268; CleRT_02750.
DR   KEGG; cey:CleRT_02750; -.
DR   PATRIC; fig|1592897.3.peg.609; -.
DR   KO; K02316; -.
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; 1.10.860.10; -; 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; IPR016136; DNA_helicase_N/primase_C.
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; IPR013173; DNA_primase_DnaG_DnaB-bd_dom.
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; PF08278; DnaG_DnaB_bind; 1.
DR   Pfam; PF08275; Toprim_N; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   PIRSF; PIRSF002811; DnaG; 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   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00740714};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00740674};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709327};
KW   Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709339};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993442};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
KW   ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      250    332       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      39     63       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT                                1}.
SQ   SEQUENCE   566 AA;  64629 MW;  47ADFA1BE37310FC CRC64;
     MRRIPQSFIQ DLLSRIDIVE LIQSRVNLKK RGHNYLGLCP FHNEKTPSFT VSPAKQFYYC
     FGCGASGNAI NFLMAFDRTE FVETITDLSA QLGLEIPLEA RHSNSPEREE YYSLLAKIAR
     YYQQQLKRSP IAINYLKSRG LTGEIAKQFA LGYAPSNWEN LKAFTKNSKI KAQLISNGLL
     IKKDHHLFDR FRHRIIFPIR DVRGRIIAFG GRALGNKQPK YMNSPETPIF HKGNELYGLY
     EACKKQANLS CFLIVEGYMD VISLHQHQIP YAVATMGTAT NAQHLKKLLR YVNEIVYCFD
     GDNAGRRAAW RALTESLPLM RDGIHIRFLF LPEEEDPDSL IRKIGKDAFE GKIKAAFPLS
     EVFFEHLQRE IPLHSIADKA NFSKKVLEYL STMPKGLFYQ LLVDELAKRL AIEIDEIHSL
     IEDNSEKGGR TSPNHSPSPS QVLSLAYHAI SILAQIPSLV TLIPKDFLPI SKMPDMQLLF
     KVVTLLTKQQ INSTAELLAL WPDSQERQLI ADLVGRHLLE EARLSPDDLA IELKDAIQRL
     KEQAEKENTW QLLRRKNLTK QSTDLI
//
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