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Database: UniProt
Entry: H1QQL8_9ACTN
LinkDB: H1QQL8_9ACTN
Original site: H1QQL8_9ACTN 
ID   H1QQL8_9ACTN            Unreviewed;       641 AA.
AC   H1QQL8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   31-JUL-2019, entry version 52.
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=SMCF_7289 {ECO:0000313|EMBL:EHN73277.1};
OS   Streptomyces coelicoflavus ZG0656.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1120227 {ECO:0000313|EMBL:EHN73277.1, ECO:0000313|Proteomes:UP000003638};
RN   [1] {ECO:0000313|EMBL:EHN73277.1, ECO:0000313|Proteomes:UP000003638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZG0656 {ECO:0000313|EMBL:EHN73277.1,
RC   ECO:0000313|Proteomes:UP000003638};
RX   PubMed=22691180; DOI=10.1111/j.1472-765X.2012.03274.x;
RA   Guo X., Geng P., Bai F., Bai G., Sun T., Li X., Shi L., Zhong Q.;
RT   "Draft genome sequence of Streptomyces coelicoflavus ZG0656 reveals
RT   the putative biosynthetic gene cluster of acarviostatin family alpha-
RT   amylase inhibitors.";
RL   Lett. Appl. Microbiol. 55:162-169(2012).
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:EHN73277.1}.
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DR   EMBL; AHGS01001467; EHN73277.1; -; Genomic_DNA.
DR   RefSeq; WP_007449387.1; NZ_AHGS01001467.1.
DR   EnsemblBacteria; EHN73277; EHN73277; SMCF_7289.
DR   PATRIC; fig|1120227.3.peg.5982; -.
DR   Proteomes; UP000003638; 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; 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; PF13662; Toprim_4; 1.
DR   Pfam; PF08275; Toprim_N; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   PIRSF; PIRSF002811; DnaG; 1.
DR   SMART; SM00766; DnaG_DnaB_bind; 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:UP000003638};
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   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      262    346       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      444    479       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   641 AA;  69740 MW;  6BDE763179E32A46 CRC64;
     MAGRINDEDV KAVRDAVPID AVVSEYLQLR NAGGGNLKGL CPFHDEKSPS FQVSPSKGFF
     HCFGCQEGGD TITFVMKIDH LTFSEAVERL AGQAGITLRY EEGGYNPSHQ RGERIRLVEA
     HKIAAQWYAE QLATGPEADT GRAFLADRGF DQAAAEHFGV GYSPQGWDHL TRFLRGKGFS
     DKELLLSGLS QEGRRGPIDR FRGRLMWPIR DIGGDVVGFG ARKLYEADNG PKYLNTPETA
     IYKKSQVLYG IDLAKKDIAK ASRAVVVEGY TDVMACHLAG VTTAIATCGT AFGGDHIKIL
     RRLLMDNGSA RVIFTFDGDA AGQKAALRAF EDDQKFAAET YIAIAPDGMD PCDLRLAKGD
     DAVADLVEPR TPLFEFALRQ IVARYDLDTP AGRASALDEA APVVARIKNS GAQHEVAVQL
     AGMLGILDTQ FVVKRIAQLA RWARDRGGKG PAPDQRQRGG APHQQSGPTA SAPRGPALNL
     RNPVFATERE LLKLALQRPE LVSPAFDAYG VDEFTAQPYA AVREAIMEAG GAEFGVQDPQ
     DYLVRVREAA PDDAVRAMVT ELAVEAIMLH RGVKGVDEVY AGAQLVTVRR RAVERRIRDI
     TGRLTRLSGH GDPAELAAVQ NELWILQQYD QNLREHGAAA L
//
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