ID A0A1S8D6B5_9PROT Unreviewed; 629 AA.
AC A0A1S8D6B5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=APZ41_011190 {ECO:0000313|EMBL:ONH83140.1};
OS Roseomonas mucosa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Roseomonas.
OX NCBI_TaxID=207340 {ECO:0000313|EMBL:ONH83140.1, ECO:0000313|Proteomes:UP000054844};
RN [1] {ECO:0000313|EMBL:ONH83140.1, ECO:0000313|Proteomes:UP000054844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAVE376 {ECO:0000313|EMBL:ONH83140.1,
RC ECO:0000313|Proteomes:UP000054844};
RA Choudhury M.A., Sidjabat H.E., Wailan A.M., Zhang L., Marsh N.M.,
RA Rickard C.M., Davies M., Mcmillan D.J.;
RT "Draft genome sequence of Roseomonas mucosa strain AU37, isolated from a
RT peripheral intravenous catheter.";
RL Submitted (DEC-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 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:ONH83140.1}.
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; LLWF02000031; ONH83140.1; -; Genomic_DNA.
DR RefSeq; WP_058389840.1; NZ_LLWF02000031.1.
DR AlphaFoldDB; A0A1S8D6B5; -.
DR STRING; 207340.APZ41_011190; -.
DR OrthoDB; 9803773at2; -.
DR Proteomes; UP000054844; 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:UP000054844};
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 254..336
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 425..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 68451 MW; 568D2273F11AD833 CRC64;
MALPPAFLEE LRARTPLPSL VGRRVKLTRN GRQWKGCCPF HNEKTPSFYV YDDHYHCFGC
GAHGDALSFL MGTEGASFRD AVERLAGEAG LEVPKESPRQ VEREARARDL HEVMEAACGV
MRRWLREAEG REALDYLRRR GLGEDTIDRF GLGWSGSSRG ALAAAMKELG VEAARLAETG
LLRANERDGG YSGFFFNRVM FPIRDRRGRI VSFGGRILGD GQPKYLNGPE TELFSKRRNL
YGFDLAREAA FRGRVLVAVE GYMDVIALHQ AGFDGAVAPL GTALTEDQLG EMWRASPEPV
LCFDGDAAGA RAAARTAEIA LPLLSPERSL RFATLPAGED PDTLVVKQGP AAFQAVLDKA
RPLHESLYDI LDAGRSSGTP EQRAALRNDL AAAAAKIPDK ALASEYRSAL LDRFFATRSR
NRPGFAPGGA LGGGAPRARG GEGEWRGGRN GARFGRPPPV RIERRPVDAD AARVEQARCL
LAIILAHPWV LDEVEEACAL LELPPGPCQS LRQGLLGWHG SSPGSSRMLD SATLLAHLHA
AELGEAHAWA ARATGLPAAA RPEAQPAEVL AAWWHFYALL RGKDALIEDR RLALEDWIAT
NDPAAERRAY RLKEALDAVQ RGETGLDGL
//
