ID A0A1S9I6N3_9CLOT Unreviewed; 784 AA.
AC A0A1S9I6N3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=ATP-dependent helicase {ECO:0000313|EMBL:OOO65979.1};
GN ORFNames=BS638_07975 {ECO:0000313|EMBL:OOO65979.1};
OS Clostridium tepidum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1962263 {ECO:0000313|EMBL:OOO65979.1, ECO:0000313|Proteomes:UP000190256};
RN [1] {ECO:0000313|EMBL:OOO65979.1, ECO:0000313|Proteomes:UP000190256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IEH 97212 {ECO:0000313|EMBL:OOO65979.1,
RC ECO:0000313|Proteomes:UP000190256};
RA Dobritsa A.P., Kutumbaka K.K., Werner K., Wiedmann M., Asmus A.,
RA Samadpour M.;
RT "Clostridium tepidum sp. nov., a close relative of Clostridium sporogenes
RT and Clostridium botulinum Group I.";
RL Submitted (DEC-2016) 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:OOO65979.1}.
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DR EMBL; MRAE01000016; OOO65979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9I6N3; -.
DR STRING; 1962263.BS637_06570; -.
DR OrthoDB; 9765586at2; -.
DR Proteomes; UP000190256; 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:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
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; 1.10.275.30; -; 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; IPR038726; PDDEXK_AddAB-type.
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; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR Pfam; PF12705; PDDEXK_1; 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 Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:OOO65979.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 189..445
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
SQ SEQUENCE 784 AA; 92329 MW; 13791EFAFC62B807 CRC64;
MESTREVNIS VRNLVEFILR NGDIDIGYLS GSRAQEGIKA HKKIQKIRME GATPLLMTEY
EKEVLLKYSV EYKNFLFNVE GRADGIIIEN GFITIEEIKT TTRNLEEIKD NLLHWAQAKC
YAFIYSKQKN LEKINIKLTY YNIKNENIKS IDKTFDILEL EKFFLDIIHK YYVWIDFNYR
FKEKRNKDIK LLKFPFKEYR SGQRKLAVSV YKTISEGKNI FIEAPTGIGK TISTIFPSIK
AIGEGYIDKI FYLTAKNTTR DFVLSNFKSI VDEDTSFKVI TLISKEKICF KEEFKCTPDN
CEFADGHFDR INEAILDVLN NENIIDESII KKYALKHKVC PFEFSLDISL WCDGIICDYN
YVFDPRVYLR RFFSDVKEDF VLLIDEAHNL LDRSREMFSS SISKNNVLNL RKSSKEKNKA
LYRILGKINK ELLEIKKIYE IDNYYIEKEK PEKLQILLSN FTSEFEVIMM KGNFQINDEL
LNFYFEALYF LKICDLYGDN YITYGEEYNN DFKIKLFAID TSSLLNEILK KSKSSIFFSG
TLSPIKYFRE VLGGEEEDYI LKLNSPFPID NHRILIGHNI STKYKYRCKS YENICDYINT
VFKIKEGNYM VFFPSYKYMN EVFLIYKEKY PFENIIVQNS SMDEKEREEF INKFEKGMDN
IIGFCVLGGI FSEGIDLTGD KIIGAIIIGV GLPQICMERN LIKNYYDEKK QAGFDYSYIY
PGMTKVMQAA GRVIRTEIDQ GIILLIDERF NSYSYKKLFP KHWYPNINIR NKKELEIALK
EFWS
//
