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Database: UniProt
Entry: A0A238KZF6_9RHOB
LinkDB: A0A238KZF6_9RHOB
Original site: A0A238KZF6_9RHOB 
ID   A0A238KZF6_9RHOB        Unreviewed;       650 AA.
AC   A0A238KZF6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   31-JUL-2019, entry version 10.
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   ECO:0000313|EMBL:SMX47592.1};
GN   ORFNames=MAA8898_03699 {ECO:0000313|EMBL:SMX47592.1};
OS   Maliponia aquimaris.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Maliponia.
OX   NCBI_TaxID=1673631 {ECO:0000313|EMBL:SMX47592.1, ECO:0000313|Proteomes:UP000207598};
RN   [1] {ECO:0000313|EMBL:SMX47592.1, ECO:0000313|Proteomes:UP000207598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8898 {ECO:0000313|EMBL:SMX47592.1,
RC   ECO:0000313|Proteomes:UP000207598};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) 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; FXYF01000011; SMX47592.1; -; Genomic_DNA.
DR   Proteomes; UP000207598; 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; 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; 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:UP000207598};
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:SMX47592.1};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000207598};
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:SMX47592.1};
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      434    453       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      607    627       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   650 AA;  71553 MW;  4BDBF142E24A9F37 CRC64;
     MSLPPGFLDE LRNRLSLSQV VGRKVLWDNR KSNQGKGDLW APCPFHHEKT ASFHVDDRKG
     YYYCFGCHAK GDAISFVRET ENVSFIEAIE ILAAEAGMEV PKQDPRAQEK ADRRTQLTEV
     MEQAVGFFRL MLKTGAAAEA RAYLARRGLN EAALARWEIG FAPSGWDNLR NALAAKGVPV
     DLMLAAGLVK TSEKGRQPYD VFRDRIMFPI RDGRGRAIAF GGRAMDPADN AKYLNSPETE
     LFDKSRNLYN LKPAREASGK GQPLVVAEGY MDVIALSEAG FGASVAPLGT AVTEPQLQLM
     WRLSPEPVIA LDGDTAGLRA AFRVIDLALP LLESGKGLRF ALMPEGKDPD DLLRAEGPEA
     VKKVLDAAIP MVDLLWRQET EGKVFDSPER RAALEASLDL RIGKIQDQNL RYHYGQALKK
     MRFEAFRSPR SERMPGVQRA PWRPKGAPLP ASQGAKASLL VTAGDAGERR LREEVILSAI
     LSAPEIVEEF EGELEAMDCS DGQLAALRDA LVTGSGTPEE RRARVEAAIG AEALENLLAR
     GHVAVVPCIR TPGNADLARL TVAEELAKLA AYEGWHAELK EAEEYLEASA DEALTWRLAE
     AARVRAQAGR RRDEDDTDYE IGPNGAQIDR EERTAFDSLL SQIRFDKGRK
//
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