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Database: UniProt
Entry: A0A437MF03_9PROT
LinkDB: A0A437MF03_9PROT
Original site: A0A437MF03_9PROT 
ID   A0A437MF03_9PROT        Unreviewed;       574 AA.
AC   A0A437MF03;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974};
DE            EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=EOD42_13830 {ECO:0000313|EMBL:RVT96192.1};
OS   Rhodovarius crocodyli.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Rhodovarius.
OX   NCBI_TaxID=1979269 {ECO:0000313|EMBL:RVT96192.1, ECO:0000313|Proteomes:UP000282957};
RN   [1] {ECO:0000313|EMBL:RVT96192.1, ECO:0000313|Proteomes:UP000282957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCP-6 {ECO:0000313|EMBL:RVT96192.1,
RC   ECO:0000313|Proteomes:UP000282957};
RA   Chen W.-M.;
RL   Submitted (JAN-2019) 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 replication.
CC       {ECO:0000256|HAMAP-Rule:MF_00974}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC         EC=2.7.7.101; Evidence={ECO:0000256|HAMAP-Rule:MF_00974};
CC   -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC       Rule:MF_00974}.
CC   -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00974}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00974}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RVT96192.1}.
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DR   EMBL; SACL01000004; RVT96192.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A437MF03; -.
DR   OrthoDB; 9803773at2; -.
DR   Proteomes; UP000282957; Unassembled WGS sequence.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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; 3.40.1360.10; -; 1.
DR   Gene3D; 3.90.980.10; DNA primase, catalytic core, N-terminal domain; 1.
DR   Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
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; IPR013264; DNAG_N.
DR   InterPro; IPR034151; TOPRIM_DnaG_bac.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR002694; Znf_CHC2.
DR   NCBIfam; TIGR01391; dnaG; 1.
DR   PANTHER; PTHR30313; DNA PRIMASE; 1.
DR   PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR   Pfam; PF08275; DNAG_N; 1.
DR   Pfam; PF13662; Toprim_4; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   SUPFAM; SSF56731; DNA primase core; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_00974};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00974};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282957};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00974}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          251..333
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   574 AA;  62144 MW;  0BB0E994FEA28B8D CRC64;
     MLPSTFLDEL RGRTPLHTLV GRKVKLERRG RQWKGCCPFH SEKSASFYVY PDHYHCFGCG
     AHGDAIAFLT EGEGLPFREA VERLAAEAGM DVPQDSPKAA QRAEEAKSLQ DVLAAAQDAF
     TRRLKLPEGA EGLAYLRKRG LSDETIARFG LGWSGSGRGA LTADLRAQGI TPEQMLAAGL
     LLERDGRLVD LYFDRVTFPI RNERGRVIAF GGRVLGDAKP KYINGSESPV FSKRRSLYGL
     DLAREGIFRG AAPVVVEGYL DVIALHEAGF RGAVAPLGTA LTEEQLQLLW GINPEPVLCF
     DGDSAGSKAA ARAVELAMGL LEPGRSIRIM TLPVGQDPDS LVRERGAAAF QQHMAVARPL
     HEVLYTVIER SIPAGTPEAR AQLRHRLETA AGQIKDKALA QEYRKALLDQ FYRAARPGAP
     SRGAKGMRYA RPTEVGDQVR VALARIVLHA AAHHPDVLDE LEEQLAMASL PRGRCADLRD
     ALLRDRTLPA SDLGWLQGAD IPPEVTAHAA PDEAVAIAQG VLTRLQSEQV LTADLEAAVE
     AFAAGDAAAE ARLITLNREL LALRAGEPLE DALC
//
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