ID   A9BWB5_DELAS            Unreviewed;       724 AA.
AC   A9BWB5;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Helicase c2 {ECO:0000313|EMBL:ABX36135.1};
GN   OrderedLocusNames=Daci_3499 {ECO:0000313|EMBL:ABX36135.1};
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX36135.1, ECO:0000313|Proteomes:UP000000784};
RN   [1] {ECO:0000313|EMBL:ABX36135.1, ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX   PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA   Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT   "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT   defined pairs of heterotrophic bacteria.";
RL   Appl. Environ. Microbiol. 70:4053-4063(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC       {ECO:0000256|ARBA:ARBA00038058}.
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DR   EMBL; CP000884; ABX36135.1; -; Genomic_DNA.
DR   RefSeq; WP_012205335.1; NC_010002.1.
DR   AlphaFoldDB; A9BWB5; -.
DR   STRING; 398578.Daci_3499; -.
DR   GeneID; 24119207; -.
DR   KEGG; dac:Daci_3499; -.
DR   eggNOG; COG1199; Bacteria.
DR   HOGENOM; CLU_012117_2_0_4; -.
DR   Proteomes; UP000000784; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   PANTHER; PTHR11472:SF47; FANCONI ANEMIA GROUP J PROTEIN; 1.
DR   Pfam; PF00270; DEAD; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:ABX36135.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000784}.
FT   DOMAIN          17..294
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   REGION          404..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..423
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   724 AA;  78550 MW;  2C758D183C8CD116 CRC64;
     MHSLTAAVQA AFAPQGLLSR AEALFLPREG QTRMALAVAQ AIEQRQTLVV EAGTGVGKTY
     AYLVPALLSG QRVLVSTATR ALQDQLYARD LPRLVAALGM PLRMARLKGR SAYLCMERLE
     RVRQGRTAPQ DPQVLRSVAL VERWARTTRT GDLGELPALD ERSPALPLVT STRDNCLGSD
     CPHWQDCHVN VARRAALEAD VVVINHHLMF ADLDVRESGV AQLLPSVGVV VVDEAHQLND
     TGVQFAGQSL SGQQLTGYAR DVLRAGQELA RGMADWMQLS ARVEQALREL RLAAGKPPAG
     GRLPWQGVTP QGLDAQRWRT ALVTLGRSLR ALLEPLVQLQ VSDPELRRLF ERGNELLRRL
     ATFAAAAVQD TVRWLELGSQ QMRMLESPLT IAHIMRTRLL GLTQEQEGSE DQEREDAQPE
     PEPQEQEEGA PAPVHEAAGL PRQPSGTAWI FTSATLGDDE RLSWFTEPCG LREAQVLRVD
     SPFDYARQAA LYVPRPFAQA GSATHSTEVA RLALDAAQRL GGRTLVLTTT LRALHAIGDA
     LQQSLGLFGE LDVLVQGQAP KLALIERFIA AGEGREGTGA SPGRGCILVA SATFWEGVDL
     PGDALQLVVI DKLPFPPPDD PLVEARSRSL ESVGRQAFAD YMLPEAAMAL KQGAGRLIRR
     ETDRGVLVVC DSRLATMGYG RRLRAALPPM RTLVDEAAFV QALQALAQPA PQITTASTTT
     SALP
//