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DNAG_PSEPU
ID   DNAG_PSEPU              Reviewed;         660 AA.
AC   P0A119; O33470;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974};
DE            EC=2.7.7.101 {ECO:0000255|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2;
RX   PubMed=9224947; DOI=10.1016/s0167-4781(97)00059-6;
RA   Szafranski P., Smith C.L., Cantor C.R.;
RT   "Cloning and analysis of the dnaG gene encoding Pseudomonas putida DNA
RT   primase.";
RL   Biochim. Biophys. Acta 1352:243-248(1997).
CC   -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC       molecules used as primers for DNA polymerase during DNA replication.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00974};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000255|HAMAP-Rule:MF_00974};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC       Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00974};
CC   -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00974}.
CC   -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00974}.
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DR   EMBL; U85774; AAC45508.1; -; Genomic_DNA.
DR   EMBL; AF014397; AAC38072.1; -; Genomic_DNA.
DR   RefSeq; WP_010951735.1; NZ_SPUU01000020.1.
DR   AlphaFoldDB; P0A119; -.
DR   SMR; P0A119; -.
DR   STRING; 1240350.AMZE01000023_gene1355; -.
DR   PATRIC; fig|303.175.peg.3167; -.
DR   eggNOG; COG0358; Bacteria.
DR   BRENDA; 2.7.7.101; 5092.
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; 1.10.860.10; -; 1.
DR   Gene3D; 3.90.580.10; -; 1.
DR   Gene3D; 3.90.980.10; -; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
DR   InterPro; IPR013264; DNA_primase_core_N.
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; IPR034151; TOPRIM_DnaG_bac.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR002694; Znf_CHC2.
DR   Pfam; PF10410; DnaB_bind; 1.
DR   Pfam; PF08278; DnaG_DnaB_bind; 1.
DR   Pfam; PF13662; Toprim_4; 1.
DR   Pfam; PF08275; Toprim_N; 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   TIGRFAMs; TIGR01391; dnaG; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed RNA polymerase; Magnesium;
KW   Metal-binding; Nucleotidyltransferase; Primosome; Transcription;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..660
FT                   /note="DNA primase"
FT                   /id="PRO_0000180514"
FT   DOMAIN          261..343
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   ZN_FING         40..64
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
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"
FT   BINDING         267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   BINDING         313
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
SQ   SEQUENCE   660 AA;  73830 MW;  0D9A88AAA2B81A9C 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 DEIIVVEGYM DVIALAQQGL RNAVATLGTA TSEEHLKRLF
     RVVPSVLFCF DGDQAGRKAA WRALESTLSN LQDGRRARFL FLPEGEDPDS LVRAEGTDAF
     MARINQHSQP LADYFFEQLG VEADPRSLEG KAHMATLAAP LIEKIPGANL RQLMRNRLKE
     ITGLDPQQVE QLAQQAPATS SMPDYDPGYD YDAMASYTPD YGDMPQHDYA PVHQEQAWKP
     NKGGSKKPWS DKPWDKNRKG GKPWQQRDEA PPRVPAPVEP PTLAALRTLL HHPLLAGKVE
     DASHFADEEH LYSQLLVALI EAAQKNPGLS SMQLIARWHG TEQGRLLRAL AEKEWLIVAD
     NLEQQFFDTI TSLSARQRER SLEQLLRKSR QSELTSEEKT QLLALLSRNV PAQTPTSSGA
 
 
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