GenomeNet

Database: UniProt
Entry: A0A0E9LT68_9BACT
LinkDB: A0A0E9LT68_9BACT
Original site: A0A0E9LT68_9BACT 
ID   A0A0E9LT68_9BACT        Unreviewed;       482 AA.
AC   A0A0E9LT68;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   31-JUL-2019, entry version 20.
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=JCM15548_1522 {ECO:0000313|EMBL:GAO28429.1};
OS   Geofilum rubicundum JCM 15548.
OC   Bacteria; Bacteroidetes; Bacteroidia; Marinilabiliales;
OC   Marinilabiliaceae; Geofilum.
OX   NCBI_TaxID=1236989 {ECO:0000313|EMBL:GAO28429.1, ECO:0000313|Proteomes:UP000032900};
RN   [1] {ECO:0000313|EMBL:GAO28429.1, ECO:0000313|Proteomes:UP000032900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15548 {ECO:0000313|EMBL:GAO28429.1};
RX   PubMed=25736980;
RA   Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S.,
RA   Hongoh Y., Hattori M., Ohkuma M.;
RT   "Distribution and evolution of nitrogen fixation genes in the phylum
RT   bacteroidetes.";
RL   Microbes Environ. 30:44-50(2015).
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:GAO28429.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; BAZW01000002; GAO28429.1; -; Genomic_DNA.
DR   EnsemblBacteria; GAO28429; GAO28429; JCM15548_1522.
DR   Proteomes; UP000032900; 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; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000032900};
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:UP000032900};
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      261    342       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      39     63       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
FT   REGION      436    469       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED       11     31       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    436    458       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   482 AA;  54847 MW;  86F26E28562BE089 CRC64;
     MIDSATVDRI MEAAQGQITD VISEYVNLKR RGINYIGNCP FHNEKTPSFI VSPHKGIFKC
     FGCGKGGNAV NFLMEHEQIT FVEAIKSLGR KFHIHIEERE PSPEALQHQN ERESMMVVTE
     YAAKYFAQTL YETDEGQSVG LGYFRQRGFR DDIIKKFQLG YSPEQRDALT RQAQQHGYKI
     EFLEKTGLSI VRDDYKADRF RGRVIFPIHS LSGKVIAFGG RVLKSDAKTA KYLNSPESEI
     YHKSRILYGI YQARQEMVRQ DRTYLVEGYT DVLSFHQAGI TNVVASSGTA LTVDQIRLMA
     RFTPNITIIY DGDPAGIKAS IRGIDLVLEE GMNVKVLLLP EGEDPDSFAK KLGKEKLLQY
     IRDNETDFIK FKTSILLEDT HNDPIKRAQL IQDIVRTISV IPDSIVRAVY IKECSKLMNV
     EEPVLYTEIG KIKKKKQEKE ALRPAVRPPV HEAPPRRIRI PRPCPSSPAI RWSRKNGKYC
     AS
//
DBGET integrated database retrieval system