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DNAG_PSEAE
ID   DNAG_PSEAE              Reviewed;         664 AA.
AC   Q9I5W0;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 123.
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}; OrderedLocusNames=PA0577;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; AE004091; AAG03966.1; -; Genomic_DNA.
DR   PIR; E83572; E83572.
DR   PIR; S15899; S15899.
DR   RefSeq; NP_249268.1; NC_002516.2.
DR   RefSeq; WP_003099594.1; NZ_QZGE01000010.1.
DR   PDB; 5VAZ; X-ray; 2.40 A; A/B=106-486.
DR   PDBsum; 5VAZ; -.
DR   AlphaFoldDB; Q9I5W0; -.
DR   SMR; Q9I5W0; -.
DR   STRING; 287.DR97_3546; -.
DR   PaxDb; Q9I5W0; -.
DR   PRIDE; Q9I5W0; -.
DR   EnsemblBacteria; AAG03966; AAG03966; PA0577.
DR   GeneID; 882047; -.
DR   KEGG; pae:PA0577; -.
DR   PATRIC; fig|208964.12.peg.612; -.
DR   PseudoCAP; PA0577; -.
DR   HOGENOM; CLU_013501_5_4_6; -.
DR   InParanoid; Q9I5W0; -.
DR   OMA; LMWPIRD; -.
DR   PhylomeDB; Q9I5W0; -.
DR   BioCyc; PAER208964:G1FZ6-584-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IBA:GO_Central.
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   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   1: Evidence at protein level;
KW   3D-structure; DNA replication; DNA-binding; DNA-directed RNA polymerase;
KW   Magnesium; Metal-binding; Nucleotidyltransferase; Primosome;
KW   Reference proteome; Transcription; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..664
FT                   /note="DNA primase"
FT                   /id="PRO_0000180512"
FT   DOMAIN          262..344
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          483..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..513
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         268
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         312
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         312
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   BINDING         314
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   HELIX           117..134
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   HELIX           138..146
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   TURN            147..149
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   HELIX           153..157
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   STRAND          165..167
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   HELIX           169..174
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   HELIX           178..186
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   STRAND          189..192
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   TURN            194..196
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   STRAND          199..203
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   STRAND          205..212
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   STRAND          218..228
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   STRAND          232..235
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   TURN            244..246
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   HELIX           251..257
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   STRAND          262..269
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   HELIX           270..278
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   STRAND          284..286
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   STRAND          288..290
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   HELIX           294..301
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   STRAND          305..314
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   HELIX           315..328
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   HELIX           329..331
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   STRAND          337..345
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   HELIX           349..368
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   HELIX           372..383
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   HELIX           389..403
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   HELIX           409..423
FT                   /evidence="ECO:0007829|PDB:5VAZ"
FT   HELIX           427..432
FT                   /evidence="ECO:0007829|PDB:5VAZ"
SQ   SEQUENCE   664 AA;  74176 MW;  8D149A92619214ED CRC64;
     MAGLIPQSFI DDLLNRTDIV EVVSSRIQLK KTGKNYSACC PFHKEKTPSF TVSPDKQFYY
     CFGCGAGGNA LGFVMDHDQL EFPQAVEELA KRAGMDVPRE ERGGRGHTPR QPTDSPLYPL
     LSAAAEFYKQ ALKSHPARKA AVNYLKGRGL TGEIARDFGL GFAPPGWDNL LKHLGGDNLQ
     LKAMLDAGLL VENSDTGKRY DRFRDRVMFP IRDSRGRIIA FGGRVLGDDK PKYLNSPETP
     VFHKGQELYG LYEARQKNRD LDEIMVVEGY MDVIALAQQG IRNAVATLGT ATSEEHIKRL
     FRLVPSILFC FDGDQAGRKA AWRALESVLP NLQDGKRVRF LFLPEGEDPD SLVRAEGEDA
     FRARITQQAQ PLAEYFFQQL MLEADPATLE GKAHLATLAA PLLEKIPGNN LRLLMRQRLS
     EITGLSGENI GQLAHHSPPP SSMDHGASGV LDGDDYFAAS AYYENEPSHA PFDAAPGYVE
     AQPRKSWNKD KKPWDGKKWD GKKKWDKGGR GDFKAPQRTP VSVESTTLNA LRTLLHHPQL
     ALKVDDAGTL AREQDTYAQL LVSLLEALQK NPRQSSMQLI ARWHGTPQGR LLQALGEKEW
     LIVQENLEKQ FFDTITKLSE SQRFGEREER LRSVMQKSYS ELTDEEKALL REHYSVAASS
     PSQS
 
 
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