ID A0A2C1ZER7_9BACI Unreviewed; 758 AA.
AC A0A2C1ZER7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=ATP-dependent helicase {ECO:0000313|EMBL:PGV55974.1};
GN ORFNames=COD92_00085 {ECO:0000313|EMBL:PGV55974.1};
OS Bacillus sp. AFS037270.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033499 {ECO:0000313|EMBL:PGV55974.1, ECO:0000313|Proteomes:UP000225442};
RN [1] {ECO:0000313|EMBL:PGV55974.1, ECO:0000313|Proteomes:UP000225442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS037270 {ECO:0000313|EMBL:PGV55974.1,
RC ECO:0000313|Proteomes:UP000225442};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:PGV55974.1}.
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DR EMBL; NUNF01000001; PGV55974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C1ZER7; -.
DR Proteomes; UP000225442; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 1.10.275.40; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 1.10.30.20; Bacterial XPD DNA helicase, FeS cluster domain; 1.
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; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR InterPro; IPR042493; XPD_DNA_FeS.
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; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 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:PGV55974.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 181..464
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
SQ SEQUENCE 758 AA; 87166 MW; 1BE1B63C8211F724 CRC64;
MSEDIQISVR KLVEHVFKGG SIDARFRSQT AMIDGTRIHQ KIQKTYQAGD QKEVYLSTEI
RYEGLTFLID GRCDGLLFHD DNVIIDEIKS FSQPLDQLEP EGYPVHWAQA KMYAYIVAMD
RELKDINVQL TYVHVDTEEK KSLIQNYTFS ELESFAWKVI KGYFPYAKLL HDHRKERDES
CKELVFPFKS YRDGQRKLAG AVYKTIVDNK NLFAKAPTGI GKTISTLFPA MKAIGEGQLN
RVFYLTAKTI TRTSAEEAFA RMGSCGLIAK TVTITAKDKV CFQEETKCQK EFCEFANGYY
DRINEAILDI LSNENQLTRE VIESYARKHK VCPFEYSIDL AYSVDAIICD YNYIFDPRVS
LKRLLEEQKK STALLVDEAH NLVDRGREMF SATLNKEPFL QLKKDFKGVN QAIYDAASNM
NAWFIQMKKM NENQKEFVLE QLDDAFLEQT RQFAITAEQI LQLETSPLLL ETYFMVNQFL
KITELLNEHF VIYAEKDRND LKIKLFCIDP SSLLRQMGKG YCAKIFFSAT LSPMPYYQDI
LGGSEGDYSL SIPSPFNEEQ VDVLIKPLST RYRDRERTRD EIISVIQSML KGRPGNHLIF
FPSYQYLLAV YERFKQIDGN TRTLIQEPGM TESKREDFLA AFKPNQTETL LGFAVLGGIF
SEGVDLVGDR LNGVVVIGVG LPQVCFERNI IKDHFSSQGK NGYDYAYVFP GINKVLQAGG
RLIRSEQDHG TIVLVDDRFL QRQYQQLLPS EWIQFTII
//