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DING_SHIFL
ID   DING_SHIFL              Reviewed;         716 AA.
AC   Q83LU7; Q7UD89;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 4.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=ATP-dependent DNA helicase DinG {ECO:0000255|HAMAP-Rule:MF_02205};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_02205};
GN   Name=dinG {ECO:0000255|HAMAP-Rule:MF_02205};
GN   OrderedLocusNames=SF0748, S0790;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase.
CC       {ECO:0000255|HAMAP-Rule:MF_02205}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02205};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02205};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_02205};
CC   -!- SIMILARITY: Belongs to the helicase family. DinG subfamily. Type 1 sub-
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_02205}.
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DR   EMBL; AE005674; AAN42384.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16261.1; -; Genomic_DNA.
DR   RefSeq; NP_706677.2; NC_004337.2.
DR   RefSeq; WP_005048497.1; NZ_WPGW01000030.1.
DR   AlphaFoldDB; Q83LU7; -.
DR   SMR; Q83LU7; -.
DR   STRING; 198214.SF0748; -.
DR   EnsemblBacteria; AAN42384; AAN42384; SF0748.
DR   EnsemblBacteria; AAP16261; AAP16261; S0790.
DR   GeneID; 1023745; -.
DR   KEGG; sfl:SF0748; -.
DR   KEGG; sfx:S0790; -.
DR   PATRIC; fig|198214.7.peg.870; -.
DR   HOGENOM; CLU_012117_4_1_6; -.
DR   OrthoDB; 679382at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_02205; DinG_proteobact; 1.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR010614; DEAD_2.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR039000; DinG_proteobact.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006554; Helicase-like_DEXD_c2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11472; PTHR11472; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00488; DEXDc2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; DNA-binding; Helicase; Hydrolase; Iron; Iron-sulfur;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..716
FT                   /note="ATP-dependent DNA helicase DinG"
FT                   /id="PRO_0000102002"
FT   DOMAIN          17..294
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT   DOMAIN          487..698
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT   MOTIF           248..251
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT   BINDING         54..61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02205, ECO:0000305"
FT   BINDING         120
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT   BINDING         194
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT   BINDING         199
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT   BINDING         205
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
SQ   SEQUENCE   716 AA;  81615 MW;  7D6402E20DC621DC CRC64;
     MALTAALKAQ IAAWYKALQE QIPDFIPRAP QRQMIADVAK TLAGEEGRHL AIEAPTGVGK
     TLSYLIPGIA IAREEQKTLV VSTANVALQD QIYSKDLPLL KKIIPDLKFT AAFGRGRYVC
     PRNLTALAST EPTQQDLLAF LDDELTPNNQ EEQKRCAKLK GDLDTYKWDG LRDHTDIAID
     DDLWRRLSTD KASCLNRNCY YYRECPFFVT RREIQEAEVV VANHALVMAA MESEAVLPDP
     KNLLLVLDEG HHLPDVARDA LEMSAEITVP WYRLQLDLFT KLVATCMEQF RPKTIPPLAI
     PERLNAHCEE LYELIASLNN ILNLYMPAGQ EAEHRFAMGE LPDELLEICQ RLAKLTEMLR
     GLAELFLNDL SEKTGSHDIV RLHRLILQMN RALGMFEVQS KLWRLASLAQ SSGAPVTKWA
     TREEREGQLH LWFHCVGIRV SDQLERLLWR SIPHIIVTSA TLRSLNSFSR LQEMSGLKEK
     AGDRFVALDS PFNHCEQGKI VIPRMRFEPS IDNEEQHIAE MAAFFREQVE SKKYLGMLVL
     FASGRAMQRF LDYVTDLRLM LLVQGDQPRY RLVELHRKRV ANGERSVLVG LQSFAEGLDL
     KGDLLSQVHI HKIAFPPIDS PVVITEGEWL KSLNRYPFEV QSLPSASFNL IQQVGRLIRS
     HGCWGEVVIY DKRLLTKNYG KRLLDALPVF PIEQPEVPEG IVKKKEKTKS PRRRRR
 
 
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