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Database: UniProt
Entry: Q21AP6_RHOPB
LinkDB: Q21AP6_RHOPB
Original site: Q21AP6_RHOPB 
ID   Q21AP6_RHOPB            Unreviewed;       680 AA.
AC   Q21AP6;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   31-JUL-2019, entry version 108.
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=RPC_0970 {ECO:0000313|EMBL:ABD86540.1};
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD86540.1, ECO:0000313|Proteomes:UP000001948};
RN   [1] {ECO:0000313|EMBL:ABD86540.1, ECO:0000313|Proteomes:UP000001948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18 {ECO:0000313|EMBL:ABD86540.1,
RC   ECO:0000313|Proteomes:UP000001948};
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-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       Note=Binds 1 zinc ion per monomer.
CC       {ECO:0000256|PIRNR:PIRNR002811};
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; CP000301; ABD86540.1; -; Genomic_DNA.
DR   RefSeq; WP_011471447.1; NC_007925.1.
DR   STRING; 316056.RPC_0970; -.
DR   EnsemblBacteria; ABD86540; ABD86540; RPC_0970.
DR   KEGG; rpc:RPC_0970; -.
DR   eggNOG; ENOG4105C9G; Bacteria.
DR   eggNOG; COG0358; LUCA.
DR   HOGENOM; HOG000014484; -.
DR   KO; K02316; -.
DR   OMA; DEPILCF; -.
DR   OrthoDB; 1071997at2; -.
DR   BioCyc; RPAL316056:G1G6B-983-MONOMER; -.
DR   Proteomes; UP000001948; 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; 2.
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:UP000001948};
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|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709339,
KW   ECO:0000313|EMBL:ABD86540.1};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001948};
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:ABD86540.1};
KW   Zinc {ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      257    339       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   REGION      425    481       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   680 AA;  73816 MW;  825087AF655BF3FE CRC64;
     MRFTPQFLDE LRARLPVSEV VGRRVKLKKA GREWKGLSPF QQEKSPSFTV NDQKGFYHDF
     SSGKHGDIIS FVMETDGCGF TEAVERLAQM AGVPLPAVTP DAARQEQRRK SLYDVMDLAA
     KFFADTLAAR QGARARGYLA DRAMSPATQL KFRIGYAPGE RFALKEHLGK LGIPVEDMVE
     AGLLISGEDI PVPFDRFRDR VMFPIADVRG RVIAFGGRAL EKDVPAKYLN SPETPLFHKG
     DNLYNLAVAR AAAHDGAPLI VVEGYVDVIA MVGAGYAATV APLGTALTEN QLQLLWKMAD
     EPILCFDGDK AGQKAAWRAA DMALPHLAPG KSLRFALLPE GQDPDDLARS GGRAAIDEVI
     GSARGLADVL WTREIQSGSF ATPERRAALE ARINELTNGI RDEVLRRYYR QDMAERLRSA
     FAPQGGFGGR GGYGRGGPRG GGGGGFGGES GRGFPQRSAF TPGAAGRMQP RGGRGAVSAG
     SQTINRMPYQ VASPDLASSP IMRGQRSAIS RREALILLTL LNHPWLLHDR LEEVAALELA
     HPEAHRLRAG IIAAFANDYH HTGSPGEPSA KLRADLAAAG LSEQLQRVER AITTNDVWAA
     GPDAAPEDVL STWHQLVALH RQWHSLLREL KDAELALGDQ QSEANFGWLR DVKARLAEVD
     GTEALIEGFG ESSGRFQRSV
//
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