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Database: UniProt
Entry: W8GFA1_9MOLU
LinkDB: W8GFA1_9MOLU
Original site: W8GFA1_9MOLU 
ID   W8GFA1_9MOLU            Unreviewed;       613 AA.
AC   W8GFA1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   10-APR-2019, entry version 31.
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   ECO:0000313|EMBL:AHK22439.1};
GN   ORFNames=X271_00333 {ECO:0000313|EMBL:AHK22439.1};
OS   Candidatus Hepatoplasma crinochetorum Av.
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae;
OC   Candidatus Hepatoplasma.
OX   NCBI_TaxID=1427984 {ECO:0000313|EMBL:AHK22439.1};
RN   [1] {ECO:0000313|EMBL:AHK22439.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Av {ECO:0000313|EMBL:AHK22439.1};
RX   PubMed=24482531; DOI=10.1093/gbe/evu020;
RA   Leclercq S., Dittmer J., Bouchon D., Cordaux R.;
RT   "Phylogenomics of "Candidatus Hepatoplasma crinochetorum," a Lineage
RT   of Mollicutes Associated with Noninsect Arthropods.";
RL   Genome Biol. Evol. 6:407-415(2014).
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|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};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       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.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709351}.
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DR   EMBL; CP006932; AHK22439.1; -; Genomic_DNA.
DR   STRING; 1427984.X271_00333; -.
DR   EnsemblBacteria; AHK22439; AHK22439; X271_00333.
DR   KEGG; hcr:X271_00333; -.
DR   PATRIC; fig|1427984.3.peg.321; -.
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; 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   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};
KW   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, ECO:0000313|EMBL:AHK22439.1};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   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, ECO:0000313|EMBL:AHK22439.1};
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      260    341       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      41     65       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
SQ   SEQUENCE   613 AA;  72333 MW;  D21288875C4DD585 CRC64;
     MTAKKDLNEL IEKITNDLNI EDVISHYISL EKKGNSFVAI CPFHQDSNPS LSISSTKKIF
     KCFVCNVGGN AITFVQKYKK VNYLEAIKII SEDFNLNWND YFVKKERQED PKIKEIKNIN
     LEALNFYKYN LQIEIEKNKK LKDYLNERKF TEKLIEVFNI GWAGSNDGLK KYLLKKNFKE
     QEILRASLIK NNNGNLRDLF FNRLIFPIFN QFNDVLGFSG RVIDQKSPIK YLNSSQNLLF
     NKSKIIYNLN NATEEILLKD NVIIVEGFMD VISFYKIGIK NVVASMGTAF NINHIDKLKS
     FTKNFILSFD NDQAGIQTTI KTYNILKNHN INLSVINFSD GKDIDEIINN NLNINKKYFE
     DNKISFLDFY YQKVIVKEKL ETLTEEKLKE ILLIVLSYND LVKKEIILLK IKEKFGKDFI
     NSFIQNLNFK PLVKKEIIIN NKINLKITNI NKNKNFSSLN NTLNKYLGKY YQEEFKFLLY
     SLLSSSFFNN LIFENFIFIN KYYKEIFDLF KNNKALLKSN DDKINYLKTL LQKFSSQREE
     NIIKSLLENF QENIKNENLL KTIKNINVED FISNLHEKWR IINKEKHKKK FIENINANDD
     EEYNYMINKL KIS
//
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