ID A0A126RCP8_9SPHN Unreviewed; 1052 AA.
AC A0A126RCP8;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=K663_14835 {ECO:0000313|EMBL:AMK19345.1};
OS Sphingobium sp. MI1205.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=407020 {ECO:0000313|EMBL:AMK19345.1, ECO:0000313|Proteomes:UP000060707};
RN [1] {ECO:0000313|Proteomes:UP000060707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI1205 {ECO:0000313|Proteomes:UP000060707};
RA Tabata M.;
RT "Genome sequence of gamma-HCH degrading bacterium Sphingobium sp. MI1205.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMK19345.1, ECO:0000313|Proteomes:UP000060707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI1205 {ECO:0000313|EMBL:AMK19345.1,
RC ECO:0000313|Proteomes:UP000060707};
RX PubMed=27056230;
RA Tabata M., Ohhata S., Nikawadori Y., Sato T., Kishida K., Ohtsubo Y.,
RA Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of a gamma-Hexachlorocyclohexane-Degrading
RT Bacterium, Sphingobium sp. Strain MI1205.";
RL Genome Announc. 4:0-0(2016).
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00974};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00974};
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. {ECO:0000256|HAMAP-
CC Rule:MF_00974}.
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; CP005188; AMK19345.1; -; Genomic_DNA.
DR RefSeq; WP_062119233.1; NZ_CP005188.1.
DR AlphaFoldDB; A0A126RCP8; -.
DR STRING; 407020.K663_14835; -.
DR KEGG; spmi:K663_14835; -.
DR PATRIC; fig|407020.3.peg.3100; -.
DR OrthoDB; 9763644at2; -.
DR Proteomes; UP000060707; Chromosome 1.
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:0005524; F:ATP binding; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR InterPro; IPR004968; DNA_primase/NTPase_C.
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; IPR006500; Helicase_put_C_phage/plasmid.
DR InterPro; IPR014015; Helicase_SF3_DNA-vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014818; Phage/plasmid_primase_P4_C.
DR InterPro; IPR034151; TOPRIM_DnaG_bac.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR002694; Znf_CHC2.
DR NCBIfam; TIGR01391; dnaG; 1.
DR NCBIfam; TIGR01613; primase_Cterm; 1.
DR PANTHER; PTHR30313; DNA PRIMASE; 1.
DR PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR Pfam; PF08706; D5_N; 1.
DR Pfam; PF08275; DNAG_N; 1.
DR Pfam; PF03288; Pox_D5; 1.
DR Pfam; PF13662; Toprim_4; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR SMART; SM00885; D5_N; 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; PS51206; SF3_HELICASE_1; 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, ECO:0000256|HAMAP-
KW Rule:MF_00974};
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 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|HAMAP-Rule:MF_00974};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_00974}.
FT DOMAIN 247..329
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 732..895
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51206"
FT ZN_FING 38..62
FT /note="CHC2-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00974"
FT REGION 93..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1052 AA; 115292 MW; 811775509013A2DB CRC64;
MSLPQSFLDS IRDRTSLSAL IGASIKLEKA GREHKACCPF HGEKTASFTI NDDKGFYHCF
GCGAHGDAIR WLTDHAGMDF IDAVKELAAK AGIEMPARSP EDAQRERRRS ETSDVMGSAA
EWFQRQLHGE SRALAQLEAR GISTASIARF GLGYAPGQRS IGGSGIAPAQ LVDAGLLIDT
DDGFRDRFRG RLMVPIQDAR GRVIAFGGRA TRPGQEPKYV NSEGGSFDKG ATLYNLHRAA
PAARSARRLI IVEGYFDVIA LDQAGIAEVV APMGTAITPQ QLERAWRVFE RPVLLMDGDA
AGRKAALRAC ERALPLVGPG RSLSIATLPD GSDPDDLVRS QGRAAIDALI DAAVPLADAL
WQGVLADADH ATPEGRAAIW KRLAGMAGAI ADEETRAQYL SDWRARFDVA FPPPPPWARD
IETLPFGRLE ALSEQPEPVQ ARLKAMAVAW FDGRIERLVD SKDAVLRLAF VAGRRVGAGL
LAEVEVKEKL LVRLDALPDL QPADVERALG DGINRAWDIG PDLVTLGCVL HPMTDFGIGE
RLIARHGTAF RFTTAKGWLG WDDRRWRVLD QDKDGPPPSE LQSAIFDTIR AIQAEARAVR
QTGIHDPDSN PHGLDRLIPS GRKNVLLSAL LAKFGRESET AGKPSSIAKL AQKWLTVSIE
AFDCDPFAIN VLNGTLRFER YRDSDGRRRA RFSLEAHRRE DLNTKLAPVA FDPDAICPIY
DDFFAWAHPD GGMRRYLHQV VGYTATGDTG EQKLWFHYGL GANGKSTAMD LWAHVLGDYA
GTIGIETFLD QGIKKRGDAA SPDLARLGGV RLLRASEPER GAKLNEALIK AATGGEPMAV
RALHRGFFDL LPLFKLHIGG NYKPSIPGTD EGIWRRMKLV PWNAHVADGE RDEQLPLKLR
AEAAGVLNHM VRGLLDWLAN GLIEPDAVRE ATAQYREDSD PLARFLKLCT AQDQQGRVQS
SRLYEVFQAW CKAAGEREWT PVGFSKAMLD KGFVKKTSNG VQWLGMRLVR EVGDFVDEHG
RVREVPIETP EEVRAPPAGP PPDADADWVP DF
//
