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Database: UniProt
Entry: A0A1V0PVE4_9RHOB
LinkDB: A0A1V0PVE4_9RHOB
Original site: A0A1V0PVE4_9RHOB 
ID   A0A1V0PVE4_9RHOB        Unreviewed;       651 AA.
AC   A0A1V0PVE4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   13-NOV-2019, entry version 15.
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   ORFNames=RGUI_1939 {ECO:0000313|EMBL:ARE40080.1};
OS   Rhodovulum sp. P5.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodovulum; unclassified Rhodovulum.
OX   NCBI_TaxID=1564506 {ECO:0000313|EMBL:ARE40080.1, ECO:0000313|Proteomes:UP000191808};
RN   [1] {ECO:0000313|EMBL:ARE40080.1, ECO:0000313|Proteomes:UP000191808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P5 {ECO:0000313|EMBL:ARE40080.1,
RC   ECO:0000313|Proteomes:UP000191808};
RA   Tang K.;
RT   "Shallow-sea hydrothermal system.";
RL   Submitted (APR-2016) 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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC         ECO:0000256|PIRSR:PIRSR002811-1};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC       ECO:0000256|PIRSR:PIRSR002811-1};
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|PIRNR:PIRNR002811,
CC       ECO:0000256|SAAS:SAAS00709351}.
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DR   EMBL; CP015039; ARE40080.1; -; Genomic_DNA.
DR   KEGG; rhc:RGUI_1939; -.
DR   KO; K02316; -.
DR   BioCyc; GCF_002079305:RGUI_RS08940-MONOMER; -.
DR   Proteomes; UP000191808; 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: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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000191808};
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|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1,
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:ARE40080.1};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191808};
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:ARE40080.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
KW   ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      262    346       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      43     67       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT                                1}.
FT   REGION      432    454       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      603    651       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      568    588       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   651 AA;  71903 MW;  8CDC6B034F487C9E CRC64;
     MSLPPGFLDE LRSRVSLSHV VGRKVTWDMR KSNQGKGDMW APCPFHQEKT ASFHVDDRKG
     YYYCFGCHAK GDAISFVRET ENVDFMEAVE ILAQEVGLPM PARDPQAREK ADRRSRLIEV
     MEQAVRFFRL QLQTGAAAEA RAYLDRRGLG AEVLERWEIG FAPPGWQNLW DHLTGKGVER
     DLILAAGLAR ESDRGRPPYD VFRDRIMFPI RDGRGQAIAF GGRAMDPQDG AKYLNSPETA
     IFDKGRNLFN HAPAREAAGK GQPLIVAEGY MDVIALAEAG FAAAVAPLGT AITEDQLRLL
     WRIHPEPVVA LDGDKAGIAA ARRLIDLALP LLEAGHALRF ALMPPGKDPD DVIRAGGAGA
     MQRILDAACP MVDLLWARET EGRRFDSPER KAALDRDLHA ATSRIKDPTI RRHYEDEIKR
     LSWQLFRPAR TKPGKGAARW NATPATRPST KTSAMVVAPP QFEEEVLESI ILATLIAHPR
     LIARFAGDLE LLHCVSDRHA RIQSALLMAP QIDDAAAFRA EMDNRLGPET LDELFSQNHV
     RTAPPVLYPG DDDAAACLAD DIAKLAAKRG AVQEIEEAMR DLAGLAHEGL TWRLSQAAEA
     RNRAGAASQE DAPEFEIAPN GVALPKDERR RSRELFDSLL GTPPSPDDDQ R
//
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