ID I3UWN5_PSEPU Unreviewed; 660 AA.
AC I3UWN5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
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=YSA_05786 {ECO:0000313|EMBL:AFK69906.1};
OS Pseudomonas putida ND6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=231023 {ECO:0000313|EMBL:AFK69906.1, ECO:0000313|Proteomes:UP000005268};
RN [1] {ECO:0000313|EMBL:AFK69906.1, ECO:0000313|Proteomes:UP000005268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND6 {ECO:0000313|EMBL:AFK69906.1,
RC ECO:0000313|Proteomes:UP000005268};
RX PubMed=22933774; DOI=10.1128/JB.01190-12;
RA Li S., Zhao H., Li Y., Niu S., Cai B.;
RT "Complete Genome Sequence of the Naphthalene-Degrading Pseudomonas putida
RT Strain ND6.";
RL J. Bacteriol. 194:5154-5155(2012).
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|HAMAP-Rule:MF_00974,
CC ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00974,
CC ECO:0000256|PIRNR:PIRNR002811, 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. {ECO:0000256|HAMAP-
CC Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
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DR EMBL; CP003588; AFK69906.1; -; Genomic_DNA.
DR RefSeq; WP_014755126.1; NC_017986.1.
DR AlphaFoldDB; I3UWN5; -.
DR KEGG; ppi:YSA_05786; -.
DR PATRIC; fig|231023.4.peg.2782; -.
DR HOGENOM; CLU_013501_5_4_6; -.
DR Proteomes; UP000005268; Chromosome.
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: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; 1.20.50.20; DnaG, RNA polymerase domain, helical bundle; 1.
DR Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR InterPro; IPR016136; DNA_helicase_N/primase_C.
DR InterPro; IPR037068; DNA_primase_core_N_sf.
DR InterPro; IPR019475; DNA_primase_DnaB-bd.
DR InterPro; IPR006295; DNA_primase_DnaG.
DR InterPro; IPR013173; DNA_primase_DnaG_DnaB-bd_dom.
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; PF08278; DnaG_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; SM00766; DnaG_DnaB_bind; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SMART; SM00400; ZnF_CHCC; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR SUPFAM; SSF117023; DNA primase DnaG, C-terminal domain; 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, 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 261..343
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT ZN_FING 40..64
FT /note="CHC2-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00974,
FT ECO:0000256|PIRSR:PIRSR002811-1"
FT REGION 94..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 73858 MW; FABAA577F51593F5 CRC64;
MAGLIPQSFI DDLINRLDIV DVVSSRVQLK KTGKNYSACC PFHKEKTPSF TVSPDKQFYY
CFGCGAGGNA LGFVMDHDNL DFPQAVEELA RAAGMEVPRE QGRRDQKPRQ PTDSPLYPLL
DAASEFYRQA LRSHPSRKAA VDYLKGRGLS GEIARDFGLG FAPPGWDNLL KHLGADTLQQ
KVMIDAGLLI ENAESGKRYD RFRDRVMFPI RDSRGRIIAF GGRVLGDDKP KYLNSPETPV
FHKGQELYGL YEARKHNRNL EEIIVVEGYM DVIALAQQGL RNAVATLGTA TSEEHLKRLF
RVVPSVLFCF DGDQAGRKAA WRALESTLSN LQDGRRARFL FLPEGEDPDS LVRAEGTDAF
MARINQHAQP LADYFFEQLG VEADPRSLEG KAHMATLAAP LIEKIPGANL RQLMRNRLKE
ITGLDPQQVE QLAQQAPATS SMPDYDPGYD YDAMASYTPD YGDMPQHDYA PVHQEQAWKP
NKGGSKKPWS DKPWDKNRKS GKPWQQRDEA PPRVPAPVEP PTLAALRTLL HHPLLAGKVE
DASHFADEEH LYSQLLVALI EAAQKNPGLS SMQLIARWHG TEQGRLLRAL AEKEWLIVAD
NLEQQFFDTI TSLSARQRER SLEQLLRKSR QSELTSEEKT QLLALLSRNV PAQTPTSSGA
//
