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Database: UniProt
Entry: Q1AVW4_RUBXD
LinkDB: Q1AVW4_RUBXD
Original site: Q1AVW4_RUBXD 
ID   Q1AVW4_RUBXD            Unreviewed;       583 AA.
AC   Q1AVW4;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   08-MAY-2019, entry version 109.
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=Rxyl_1502 {ECO:0000313|EMBL:ABG04464.1};
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129).
OC   Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales;
OC   Rubrobacteraceae; Rubrobacter.
OX   NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG04464.1, ECO:0000313|Proteomes:UP000006637};
RN   [1] {ECO:0000313|EMBL:ABG04464.1, ECO:0000313|Proteomes:UP000006637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 {ECO:0000313|Proteomes:UP000006637};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E.,
RA   Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000256|PIRNR:PIRNR002811,
CC         ECO:0000256|PIRSR:PIRSR002811-1};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|PIRNR:PIRNR002811,
CC       ECO:0000256|PIRSR:PIRSR002811-1};
CC   -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC       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: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00974}.
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DR   EMBL; CP000386; ABG04464.1; -; Genomic_DNA.
DR   RefSeq; WP_011564481.1; NC_008148.1.
DR   STRING; 266117.Rxyl_1502; -.
DR   EnsemblBacteria; ABG04464; ABG04464; Rxyl_1502.
DR   KEGG; rxy:Rxyl_1502; -.
DR   eggNOG; ENOG4105C9G; Bacteria.
DR   eggNOG; COG0358; LUCA.
DR   HOGENOM; HOG000014483; -.
DR   KO; K02316; -.
DR   OrthoDB; 1071997at2; -.
DR   BioCyc; RXYL266117:G1G6P-1533-MONOMER; -.
DR   Proteomes; UP000006637; 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:InterPro.
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; PF13662; Toprim_4; 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   Complete proteome {ECO:0000313|Proteomes:UP000006637};
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|PIRNR:PIRNR002811,
KW   ECO:0000256|PIRSR:PIRSR002811-1, 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   Reference proteome {ECO:0000313|Proteomes:UP000006637};
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|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1,
KW   ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|PIRSR:PIRSR002811-1,
KW   ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      257    340       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      38     64       CHC2-type. {ECO:0000256|PIRSR:
FT                                PIRSR002811-1}.
SQ   SEQUENCE   583 AA;  64213 MW;  0814A83930384227 CRC64;
     MRISRQSIEE LREAVDIVEV ASEFTALRRQ GARFVGLCPY PDHQEKTPSF SVSPDKGFYY
     CFGCSRGGDA IKLVEELKSL PFAEAVAHLA ERYNIELRFE GATEPSRDRA NRRRAIHKAL
     AAAAVYYHKV LLKMPSQETE RARRYLAGRG ISSSTIEEFR LGFAPSSGGF VRAAARLGLG
     REVLEAAGLL GRGGRERFAG RITFPISDRR GRIVGFGARV LGEGGPKYLN SPETEVFDKR
     NLLYGFPQVM EAMRRERSAL VVEGYTDVLM LHQAGIKNAV ATLGTAITPS HLRLLSGYAD
     EIYMLFDPDA AGEKAVERAV AAASELKLGL KVLRLPEDPA DWLRGHAGEE FVRLLPGAEP
     ALHYVFRRKA ERARSADTVG RARALEEMKG LVARIEDPVF RHEALRLASE ALGVAPHALF
     AAGAGRAERQ PASAGGLRDP YEEAGRDVLA TMLARPDLAA DLLREGVAVP GLGAPLRLVP
     EDFATDRQGR LFGLLQRRPG VALDRLVVDE ELRPFVDLLA SLSEAGERLQ PSAASARELW
     LRLGILSRQR KKRQTDDISR KETLQAEIQL LREAQRSIAS REA
//
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