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Database: UniProt
Entry: R9B7J9_9GAMM
LinkDB: R9B7J9_9GAMM
Original site: R9B7J9_9GAMM 
ID   R9B7J9_9GAMM            Unreviewed;       627 AA.
AC   R9B7J9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   13-NOV-2019, entry version 38.
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   ORFNames=I593_00663 {ECO:0000313|EMBL:EOR10494.1};
OS   Acinetobacter tandoii DSM 14970 = CIP 107469.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=1120927 {ECO:0000313|EMBL:EOR10494.1, ECO:0000313|Proteomes:UP000016201};
RN   [1] {ECO:0000313|EMBL:EOR10494.1, ECO:0000313|Proteomes:UP000016201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 107469 {ECO:0000313|EMBL:EOR10494.1,
RC   ECO:0000313|Proteomes:UP000016201};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter tandoii CIP 107469.";
RL   Submitted (MAR-2013) 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   -!- 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}.
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:EOR10494.1}.
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DR   EMBL; AQFM01000025; EOR10494.1; -; Genomic_DNA.
DR   RefSeq; WP_016165804.1; NZ_KK211210.1.
DR   STRING; 202954.BBNK01000042_gene83; -.
DR   EnsemblBacteria; EOR10494; EOR10494; I593_00663.
DR   PATRIC; fig|1120927.3.peg.629; -.
DR   OrthoDB; 1071997at2; -.
DR   Proteomes; UP000016201; 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; 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; PF13662; Toprim_4; 1.
DR   Pfam; PF08275; Toprim_N; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000016201};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00993445};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00974};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00974};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016201};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00993442};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974}.
FT   DOMAIN      307    389       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      38     62       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
FT   REGION      111    133       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   627 AA;  71998 MW;  AEB397CE0F14C931 CRC64;
     MAIPQHTIDQ ILDRTDIVDL IGQRVKLKKT GRTYSGCCPF HQEKSPSFHV YRDKQYYHCF
     GCQANGNAIR FLMDIDNRNF VDVMKDLSSQ TGIELPKDNQ DSKRLSYKRE AKTVAEPSKT
     APVTPVQSPP TTELQIDHDP FEEFRNVDDP FAQFEPFQTF NEAPAQEGNL YDLLENVAQF
     YERQLPQSQS AQQYFRHRGL GVETIQFWRL GYAPEDWQHL EKAFPQDVQG LKLLGLIRTS
     DKGRDFDLLR DRVIFPIRDA KGRVVGFGGR ALNDEIKPKY INSPDSEVFH KNQLLYGLYE
     GRKQKAQDWL MVEGYMDVIA LQQNGIYGAV ATLGTASNTE HLNILFKQNN RITIAFDGDA
     AGQKAARRTL EIALPLLNDG RELKFFVLPN DHDPDSLIRR EGLENFQRLL QQAPLLSDFV
     FAHLTQNQDI SSPEGKSLVM AELRQLTELL PKTGSFRYLL NQSFKEKLGF GKRWTPQLSN
     DASLSFNIRT KDEDFAIAIL MHHPFLYIHF ETLRAFVPSH ELLSHILNIL NRIFDNLPDD
     QELATYYVLG ACSTFSLEIA DIMRRTNIEV LTHAPEMADK LATEYALGLQ EKYLRQKLKD
     PNSLLESRNL RQQLNELTKK IGLRLLS
//
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