ID A6VX61_MARMS Unreviewed; 707 AA.
AC A6VX61;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=ATP-dependent DNA helicase DinG {ECO:0000256|HAMAP-Rule:MF_02205};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_02205};
GN Name=dinG {ECO:0000256|HAMAP-Rule:MF_02205};
GN OrderedLocusNames=Mmwyl1_2118 {ECO:0000313|EMBL:ABR71040.1};
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR71040.1};
RN [1] {ECO:0000313|EMBL:ABR71040.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1 {ECO:0000313|EMBL:ABR71040.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_02205};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02205};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_02205};
CC -!- SIMILARITY: Belongs to the helicase family. DinG subfamily. Type 1 sub-
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02205}.
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DR EMBL; CP000749; ABR71040.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VX61; -.
DR STRING; 400668.Mmwyl1_2118; -.
DR KEGG; mmw:Mmwyl1_2118; -.
DR eggNOG; COG1199; Bacteria.
DR HOGENOM; CLU_012117_4_1_6; -.
DR OrthoDB; 9805194at2; -.
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; P-loop containing nucleotide triphosphate hydrolases; 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; IPR045028; DinG/Rad3-like.
DR InterPro; IPR039000; DinG_proteobact.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR PANTHER; PTHR11472:SF59; ATP-DEPENDENT DNA HELICASE DING; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 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; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02205};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02205}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_02205};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_02205};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02205};
KW Iron {ECO:0000256|HAMAP-Rule:MF_02205};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02205};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02205};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02205}.
FT DOMAIN 15..322
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT COILED 279..306
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
FT BINDING 204
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
FT BINDING 209
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
FT BINDING 215
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
SQ SEQUENCE 707 AA; 79512 MW; 37A231C936468CCD CRC64;
MLSDELKKQI QLAYRASLDA KSHKPRAGQR QMIGAIARTL GNIKQGSEGE RLEEKHVAVI
EAGTGTGKTL SYCLAAIPIA KARGLKLIIS TATVALQEQI LHKELPDLLE HTELTFKYTL
AKGRGRYLCL NNLEGFLSSE EQAMDDMFAG LFEQHLHSDD INTVLYQEMD TALQKGDWDG
DKDNWAGIVR DQDWRRLTTD HQQCTNRNCA NYSACPFFKA RAEIEVADVI VANHDLVLAD
LSLGGGAILT PPKETIYIFD EGHHLPDKAI GHFRHEVRLQ QSITWLRQLE KNLVNLKQEL
TDDVSVTGQL LLKIPQQIQS IVNFIQYAQQ GLAPYIQGLG LDQENNQHRF EFGQIPDELR
QLAYSLQTSY QKLFNNIESI QDECKKTKQN EGMGVTPETA ETWQPILGVI LGRLEQCIGL
WCLYSTVDDQ NFPPNARWLV LSGQGMEQDI ELGGSPILAA NTLRQQLWDK CFGAVVTSAT
LTALNQFHRF NMRSGVPRES EYLRVISPFN FQENGLLVVP DMEHEPNRVE QHTAEIVTYL
DKHVNTEKGS LVLFSSRRQM EEVAQSVSVG LQEILLMQGE QSKRVILDSH KSRIDEGKGS
LLLGLASFAE GVDLPGDYLT CVYIAKIPFA VPDDPVEATL AEWIQKRGGN PFMEITIPDA
SLRLVQATGR LLRSEKDSGE IHILDKRLRT KRYGSQLINS LPPYKYQ
//
