ID A0A2D0KQW8_9GAMM Unreviewed; 638 AA.
AC A0A2D0KQW8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=ATP-dependent DNA helicase DinG {ECO:0000313|EMBL:PHM65816.1};
GN ORFNames=Xsto_01763 {ECO:0000313|EMBL:PHM65816.1};
OS Xenorhabdus stockiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351614 {ECO:0000313|EMBL:PHM65816.1, ECO:0000313|Proteomes:UP000222366};
RN [1] {ECO:0000313|EMBL:PHM65816.1, ECO:0000313|Proteomes:UP000222366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17904 {ECO:0000313|EMBL:PHM65816.1,
RC ECO:0000313|Proteomes:UP000222366};
RX PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA Ebersberger I., Bode H.B.;
RT "Natural product diversity associated with the nematode symbionts
RT Photorhabdus and Xenorhabdus.";
RL Nat. Microbiol. 2:1676-1685(2017).
CC -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC {ECO:0000256|ARBA:ARBA00038058}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHM65816.1}.
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DR EMBL; NJAJ01000013; PHM65816.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D0KQW8; -.
DR Proteomes; UP000222366; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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 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 InterPro; IPR010614; RAD3-like_helicase_DEAD.
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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:PHM65816.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 10..272
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
SQ SEQUENCE 638 AA; 71386 MW; 2CC71A68B0EDD24C CRC64;
MSDDFAENGI LAKTIQGFKP RDAQREMSSA ITAAIQNKQQ LVVEAGTGTG KTFAYLVPAL
RSGKKVIIST GSKALQDQLY SRDLPAITDS LAFSGRLALL KGRSNYLCLE RLEQQSIGGS
QLEPETLSEI ITLKNWSSQT EDGDISTCHK IAEDSTVWPL VTSTNDNCLG RDCPNYQECF
VLKARRRAME ADIVIVNHHL FMADAVVKDT GFGELIPQAE VMIFDEAHQI PDIASQYFGQ
QLSSRQLLDL SRDIIMAYRT EVRDQAQLQK SADRLSQSTQ DFRLELGENS YRGNLREVLQ
QQHIKRALVR LDDALELCYD VMKLSLGRSA MLDAAFERAT IYRNRLKRLI DVTVPDYSYW
FESYGRHFLL ALTPLSVSDK FSEMIREQSG CWVFTSATLS VNDQLEHFTA RLGLKQAQTL
LLPSPFDYQR QMLLCVPRHL PLPNQNGGAK WLAGMLKPLI ESNKGRCFFL CTSHQMMRSL
AEEFRASMTL PVLVQGETSK GKLLSQFLAA GNALLVATGS FWEGVDVRGD ALSCVIIDKL
PFTAPDDPLF KARIEDCQHK GGDAFSEVQL PDAVLSLKQG VGRLIRDVDD YGVVVICDNR
LVMRPYGEVF LNSLPPSPRT RDLSKAVEFL KSRQSQSQ
//
