ID A0A1G6S2S5_9PROT Unreviewed; 930 AA.
AC A0A1G6S2S5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=ATP-dependent DNA helicase DinG {ECO:0000313|EMBL:SDD10457.1};
GN ORFNames=SAMN04487779_1004223 {ECO:0000313|EMBL:SDD10457.1};
OS Belnapia rosea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Belnapia.
OX NCBI_TaxID=938405 {ECO:0000313|EMBL:SDD10457.1, ECO:0000313|Proteomes:UP000198925};
RN [1] {ECO:0000313|EMBL:SDD10457.1, ECO:0000313|Proteomes:UP000198925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 100156 {ECO:0000313|EMBL:SDD10457.1,
RC ECO:0000313|Proteomes:UP000198925};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FMZX01000004; SDD10457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6S2S5; -.
DR STRING; 938405.SAMN02927895_04310; -.
DR Proteomes; UP000198925; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
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; PF13307; Helicase_C_2; 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:SDD10457.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000198925};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 747..769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 200..473
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 206..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 930 AA; 101282 MW; F4933BE0224F43A2 CRC64;
MPQPPRLLLP DAPALVAGLG RATLLTPDGE LLALSASGLA EALGGAAPLL VHAPATARRL
DLPRFDAAFD LLELFAFCMP ARPAAPTPRG LAMALDLTPP ADDAAAAAQL PEMATILLRH
LAAGRHLPLN RDAAILATHL KKVAGWAWAE SVLAALGADQ EKPSLDPYKV WRRLPDWEDP
GPAQPPGSFE VSPGEARTRL AQILGEGSEQ RPQQADYASA ASGAFAPRED RGTPHIVLAE
AGTGTGKTLG YIAPASLWAE RNGAPVWIST FTRNLQRQID QELGRLYPEP EERRRRVVVR
KGRENYLCLL NLDEMLGQAT HPDMAVPLAL VARWALATRD GDLMAGDFPG WVAELHGPAS
IWPLADRRGE CIRSACPRYK QCYVEHSIRR ARTATLVVAN HALVMVQAAQ GGAEDVRPLR
YVFDEGHHLF DAADAAFSAA LCGGETAEMR RWLLGAEGGR SRARGLRRRI EELAGDLPDL
LPPMEAALHA ARALPGLGWV TRLSEEPREP ASEAAAERQS NPTEVFLRAV RRQVLARARE
EDGLYDVQCD LHPLGEDLPE AGEALERALK RIEEPLARLR EKLMARLEDE VEELETTDRI
RYETAAKGIE RRALMPLAAW QGMLRALREP PPSPGERRAF VDWLALTRRE GREVDAGLHR
HWLDPTTPFA LTVAAPAHGL LVTSATLRDA GLGGDQEADW VAAEARTGAS HLATPAIRAA
FPSPFDYAAR TRAFVVTDVD KTRSAQISAA MGALFLAAGG GGLGLFTAIR RLRDGFRHMA
PRLEAAGIPL YAQHMDAMDN ATLVDVFRAE ENSCLLGTDA MRDGVDVPGR SLRLLVFDRV
PWPRPSILHR ERRVHLSGGD PKGYDDALAR HRLRQAFGRL IRRADDRGVF VLLDRSCPSR
LLAGLPEGVP LRRTGLAEVV AETRAFLAEG
//