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Database: UniProt
Entry: A0A098R5A9_9SPIO
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ID   A0A098R5A9_9SPIO        Unreviewed;       614 AA.
AC   A0A098R5A9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811};
DE            EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=DC28_01730 {ECO:0000313|EMBL:KGE73927.1};
OS   Spirochaeta lutea.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Spirochaeta.
OX   NCBI_TaxID=1480694 {ECO:0000313|EMBL:KGE73927.1, ECO:0000313|Proteomes:UP000029692};
RN   [1] {ECO:0000313|EMBL:KGE73927.1, ECO:0000313|Proteomes:UP000029692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC230 {ECO:0000313|EMBL:KGE73927.1,
RC   ECO:0000313|Proteomes:UP000029692};
RA   Shivani Y., Subhash Y., Tushar L., Sasikala C., Ramana C.V.;
RT   "De novo Genome Sequence of Spirocheata sp.";
RL   Submitted (MAY-2014) 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, ECO:0000256|PIRNR:PIRNR002811}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR002811};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|PIRNR:PIRNR002811};
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, ECO:0000256|PIRNR:PIRNR002811}.
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:KGE73927.1}.
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DR   EMBL; JNUP01000001; KGE73927.1; -; Genomic_DNA.
DR   RefSeq; WP_037544408.1; NZ_JNUP01000001.1.
DR   AlphaFoldDB; A0A098R5A9; -.
DR   STRING; 1480694.DC28_01730; -.
DR   eggNOG; COG0358; Bacteria.
DR   OrthoDB; 9803773at2; -.
DR   Proteomes; UP000029692; 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; IPR019475; DNA_primase_DnaB-bd.
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; PF10410; DnaB_bind; 1.
DR   Pfam; PF08275; DNAG_N; 1.
DR   Pfam; PF13155; Toprim_2; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   PIRSF; PIRSF002811; DnaG; 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   ECO:0000256|PIRNR:PIRNR002811};
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:UP000029692};
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};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR002811};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          254..335
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   614 AA;  69732 MW;  6B6A26261F351E88 CRC64;
     MRIPSHIVQE ILERARIEEI VSDYVTLTPK GGRLWGLSPF KNEKTPSFTV TPEKNAYYCF
     STQKGGGVVQ FVMEMEGLTY PEALEYLAQK LGIELTMEGS EQNDAQKKRL SLQQLNARVA
     GMFHHLLVKS KDGAKALDYI SGRGIDIETI TRFQLGYAPR DPFWLKKFLV SKGYSEGFLQ
     DSGLFTRKNS SRSLFSNRLM FPILDNSGRV VAFGGRILEG DGPKYLNSPE TILYHKSSTI
     YGLWQAKEEI RKKKEAIVCE GYMDVLALSQ GGLHHAVAPL GTAFTPEQAT LLHRYAKEVL
     LLFDGDQAGI NASQKALQLL ESKNFTISVG LLSSGEDPSD ILEKSGSQGV QNIVYSTSNA
     LDFLLKQAVS RFPVSTPEGK RQAVEQLFDY IESINSAVKR EGVFKQIAEY FELSVESLKT
     DFNQRLEVSK PAPRGVNKAT RFEKNDSDFI EKESESSKRQ IVPSKLTGDL FLMIAVVLNF
     QYFQKVRREV HQEDLRDPWA MELYIVLEES FRANELTQES ILARIEDEDL ISFLLEKQAL
     EEFLVNPEAL ILDGIRQVKI DKLLRQRREI EMQLKKVFMS TDEQKKLHEL LTEKIYIDQA
     LNKLKVTIHD RPAE
//
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