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Database: UniProt
Entry: K8EKP2_9FIRM
LinkDB: K8EKP2_9FIRM
Original site: K8EKP2_9FIRM 
ID   K8EKP2_9FIRM            Unreviewed;       603 AA.
AC   K8EKP2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   05-JUN-2019, entry version 44.
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   ORFNames=DESHY_60288 {ECO:0000313|EMBL:CCO09116.1};
OS   Desulfotomaculum hydrothermale Lam5 = DSM 18033.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=1121428 {ECO:0000313|EMBL:CCO09116.1, ECO:0000313|Proteomes:UP000009315};
RN   [1] {ECO:0000313|EMBL:CCO09116.1, ECO:0000313|Proteomes:UP000009315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lam5 / DSM 18033 {ECO:0000313|Proteomes:UP000009315};
RX   PubMed=23405336; DOI=10.1128/genomeA.00114-12;
RA   Amin O., Fardeau M.L., Valette O., Hirschler-Rea A., Barbe V.,
RA   Medigue C., Vacherie B., Ollivier B., Bertin P.N., Dolla A.;
RT   "Genome Sequence of the Sulfate-Reducing Bacterium Desulfotomaculum
RT   hydrothermale Lam5(T).";
RL   Genome Announc. 1:e00114-e00112(2013).
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}.
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:CCO09116.1}.
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DR   EMBL; CAOS01000013; CCO09116.1; -; Genomic_DNA.
DR   RefSeq; WP_008412937.1; NZ_FQXF01000012.1.
DR   STRING; 1121428.DESHY_60288___1; -.
DR   EnsemblBacteria; CCO09116; CCO09116; DESHY_60288.
DR   OrthoDB; 1071997at2; -.
DR   Proteomes; UP000009315; 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; 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; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000009315};
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   ECO:0000313|EMBL:CCO09116.1};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009315};
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   ECO:0000313|EMBL:CCO09116.1};
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   ZN_FING      40     64       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT                                1}.
SQ   SEQUENCE   603 AA;  66854 MW;  77C3899CDB74E89F CRC64;
     MAGRIPEAVL EEIRQRSDIV EIVARYVPLE KRGKNYLALC PFHQEKTPSF NVSQEKQAFH
     CFGCGVGGNV FSFIMMVEGL SFLDAVRFLA ARAGVKIPAE ASPAEQARQG KRDRAFKIYG
     LVRDFYRLLL GKEIGAGARR YLESRRLAES AAETFQLGYA PAGWDNLVKF LAARGIKTEE
     MVQLGLAQTR ESGGCYDRFR NRVMFPIWDS QGRVVGFGGR TMGDDNPKYL NSPEGEFFNK
     GRLLYGLHIA RRSIRELGYA ILMEGYMDVV SAYQHGVANA VASLGTAFTR EQAGLLTAYT
     NEVVIAYDAD AAGIKAALRA AEILQQVGCQ VRIASITGAK DPDEFIQKYG LAGWQKIIQQ
     AAPLVQFKLL QAVKAHGLSN KRKILQEVLP NLAAVASPIE LEEAVKQTAT VLQVNWETVL
     EEIKSFKKNT RKISQIGDNS VKNSHNIAST RPAVPQQPRD ARSQAEAGIL RMALENRSWL
     ERILAELGQQ FFQNSDYQSI FNAYLAGGSD RSAAALFNLL DEPRQKILSS ILLQELPGPI
     TEQMLADFIN TIKKLSDKAR LEDLLARLAA AEQSGDTAQV RDLSQQIHIL MNKLKWPERG
     VAT
//
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