DING_PHOPR
ID DING_PHOPR Reviewed; 692 AA.
AC P29741;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 119.
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}; OrderedLocusNames=PBPRA1011;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-151.
RX PubMed=8396546; DOI=10.1016/0378-1119(93)90680-2;
RA Bartlett D.H., Chi E., Wright M.E.;
RT "Sequence of the ompH gene from the deep-sea bacterium Photobacterium
RT SS9.";
RL Gene 131:125-128(1993).
RN [3]
RP SIMILARITY TO DING.
RX PubMed=8385320; DOI=10.1093/nar/21.6.1497;
RA Koonin E.V.;
RT "Escherichia coli dinG gene encodes a putative DNA helicase related to a
RT group of eukaryotic helicases including Rad3 protein.";
RL Nucleic Acids Res. 21:1497-1497(1993).
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; CR378666; CAG19422.1; -; Genomic_DNA.
DR EMBL; X67094; CAA47468.1; -; Genomic_DNA.
DR PIR; S23215; S23215.
DR RefSeq; WP_011217756.1; NC_006370.1.
DR AlphaFoldDB; P29741; -.
DR SMR; P29741; -.
DR STRING; 298386.PBPRA1011; -.
DR EnsemblBacteria; CAG19422; CAG19422; PBPRA1011.
DR KEGG; ppr:PBPRA1011; -.
DR eggNOG; COG1199; Bacteria.
DR HOGENOM; CLU_012117_4_1_6; -.
DR OMA; PRRAQNY; -.
DR OrthoDB; 679382at2; -.
DR Proteomes; UP000000593; Chromosome 1.
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; 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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11472; PTHR11472; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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..692
FT /note="ATP-dependent DNA helicase DinG"
FT /id="PRO_0000102005"
FT DOMAIN 16..293
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT DOMAIN 514..692
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT MOTIF 247..250
FT /note="DEAH box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT BINDING 56..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205, ECO:0000305"
FT BINDING 123
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT BINDING 202
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT CONFLICT 118
FT /note="R -> A (in Ref. 2; CAA47468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 692 AA; 78056 MW; CF5ED56922B75989 CRC64;
MLHSQIKSDI KQCYENLGNQ LDNFIPRRAQ NYLVAEIAKT LAGEYHQKHR MLVGEAGTGI
GKSLAYLLGG IPFALFNNKK LLISTATVAL QEQLINKDLP LFNRIYPKEF SFILAKGRQR
YCCNHKLEAC CATNNDQQVT LWEEKPKKSD LDLLRRMLKA TRDGKWDGDR DSWPTTIPDR
VWPQIMADKH SCHAGLPQHR SCPFAKAREH LDKADVIIAN HALLMADIEL GGGVILPEPE
QTIYVIDEAH HLPKVARDFS SAASSLKGAA TWLEKLNQTI GKLAELAEYK KAARFQDAIL
ENIQHLIPTL RQVANNVDVG MFSKDGIYRF EHGELPAWLE QEAKGCKDAS KKALQSLGKI
HDLISERLKD NEIQQRLGEQ ALAESGVYLQ RLENLEKVWA LMAQPKKDKG APLARWIEKN
PDNEGDYIIQ VSPLEVGYRL DQLLWSRAAG AILVSATLRA LNQFTYFCRQ VGIYEMDSTR
FLALASPFDY QNNARLVIPA LSLEPQADKF TDLLIKTLPE YLEGETASLV LFSSYWQMNK
VADELRPLAK KNKWELLVQG EESRHITLKK HKDNCKSGKP SILFGTGSFS EGLDLPGDLL
KNLIITKIPF GVPTSPVEEA HAEYIESCGG NPFMQISVPE ASKKLIQSVG RLIRKEDDMG
RVVLLDRRII NRRYGKALLD SLPPFKRVIE YS
