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Database: UniProt
Entry: M1PP35_DESSD
LinkDB: M1PP35_DESSD
Original site: M1PP35_DESSD 
ID   M1PP35_DESSD            Unreviewed;       612 AA.
AC   M1PP35;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   31-JUL-2019, entry version 49.
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   OrderedLocusNames=UWK_01628 {ECO:0000313|EMBL:AGF78186.1};
OS   Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobulbaceae; Desulfocapsa.
OX   NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF78186.1, ECO:0000313|Proteomes:UP000011721};
RN   [1] {ECO:0000313|Proteomes:UP000011721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX   PubMed=23961312; DOI=10.4056/sigs.3777412;
RA   Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M.,
RA   Amann R., Schreiber L.;
RT   "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT   deltaproteobacterium specialized in disproportionating inorganic
RT   sulfur compounds.";
RL   Stand. Genomic Sci. 8:58-68(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}.
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DR   EMBL; CP003985; AGF78186.1; -; Genomic_DNA.
DR   RefSeq; WP_015403877.1; NC_020304.1.
DR   STRING; 1167006.UWK_01628; -.
DR   EnsemblBacteria; AGF78186; AGF78186; UWK_01628.
DR   KEGG; dsf:UWK_01628; -.
DR   PATRIC; fig|1167006.5.peg.1798; -.
DR   KO; K02316; -.
DR   OMA; RIMFPIY; -.
DR   OrthoDB; 1071997at2; -.
DR   BioCyc; DSUL1167006:G1HFC-1621-MONOMER; -.
DR   Proteomes; UP000011721; Chromosome.
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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011721};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, 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|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:AGF78186.1};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011721};
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:AGF78186.1};
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   DOMAIN      263    355       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      41     65       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT                                1}.
FT   REGION      426    453       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      586    606       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   612 AA;  67912 MW;  3F82BC85221A2534 CRC64;
     MGYTDFDDGL PAKIKEQADI VQVIGECVEL KRAGVRFLGC CPFHNEKTAS FSVHPGQQFF
     HCFGCGASGD IFDFQMKYHN LDFPSAMKEL ARRYNVEIPE RPRSAQEREK SRKRQLLYEV
     NEKVVTIFRR TLLASDMAKS ARAYLEERKI PPAVQERFGL GYAPSPDSAG WNFLGAQLAA
     EEKLVAVEAG LLVEKESGGT YDRFRDRVLF PIYDRRGRVV GFGGRIIGEG QPKYMNSPES
     LVFNKSASLL GLYQQGDEIR RRRKAIVVEG NFDLVSLVVH GCPNVVAPLG TALTAQQLRM
     LKGFSEECVL LFDGDTAGVK AAMRSVPLFL SEQIAGKVAL LPTGHDPDTF VREEGLAALN
     TLLDKAMPLP EFVLQQLVAE YGLTSYDGKI RIIKELQPLI KATTSPLQRS LMLSHFSEAI
     GISPDELGAS MPGREATVRP PVKEPPQERS RERLVPLSAS QKRLVTHMVL YPEAVHELEK
     AGVRECLGGT VGEVLLLQLL ALLEQPGGVE PEELLAKLPQ GGERVMVSEI LLSSSPGSSD
     LGCRGTDEEL KELLTWLERE QLLRESGELV KLISKCALQN DQEEELNRLV LKKMSVDNRL
     QELRQTNVLQ DG
//
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