ID C1FLL7_CLOBJ Unreviewed; 588 AA.
AC C1FLL7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN OrderedLocusNames=CLM_1540 {ECO:0000313|EMBL:ACO83475.1};
OS Clostridium botulinum (strain Kyoto / Type A2).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536232 {ECO:0000313|EMBL:ACO83475.1, ECO:0000313|Proteomes:UP000001374};
RN [1] {ECO:0000313|EMBL:ACO83475.1, ECO:0000313|Proteomes:UP000001374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyoto / Type A2 {ECO:0000313|Proteomes:UP000001374};
RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the helicase family.
CC {ECO:0000256|ARBA:ARBA00008708}.
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DR EMBL; CP001581; ACO83475.1; -; Genomic_DNA.
DR RefSeq; WP_012703710.1; NC_012563.1.
DR AlphaFoldDB; C1FLL7; -.
DR KEGG; cby:CLM_1540; -.
DR eggNOG; COG4581; Bacteria.
DR HOGENOM; CLU_010647_4_1_9; -.
DR Proteomes; UP000001374; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17913; DEXQc_Suv3; 1.
DR Gene3D; 1.20.272.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022192; SUV3_C.
DR InterPro; IPR044774; Suv3_DEXQc.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF1; ATP-DEPENDENT RNA HELICASE SUPV3L1, MITOCHONDRIAL; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF12513; SUV3_C; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ACO83475.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 136..250
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 290..445
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 588 AA; 69368 MW; 3081F3B1B5BF9445 CRC64;
MKKASIDRNF RKIKNSYSQT EDIVQHSKIN SLWEQEASIR KKLKKLESMK DKNIRDFKEV
YNNYSHLLDY ISKKLVKDYN IKHNTNFDFH EIIKGNRKNY LKSGIMSVLI TRHIPTMIFK
EFDRIFPKNP KDEYKKVRHM NRKFYLHLGE TNTGKTYNSM ERLKESKKGI YLSPLRILAL
ENFEKLNKEG IMCNLITGEE EIKKEKAQHV CCTIEKLDIN EEYDVAIIDE IQMIDDDQRG
SAWTRAILAL RCKEIHVCGA LNTKELIINI IEDCGDEYEL KEYFRNIPLK IEEEAFKLKD
IKKGDALVTF SKKKVLQLAD YYGDLGIKTS VIYGNLPPEV RKKQYEQFMS GDTNILITTD
AIGMGVNLPI RRIVFMDIRK FDGNDMRYLT SQEIKQIGGR AGRLGIYDIG YLASYGNTQN
FVKEMIEVYD RKIYEAVIEP SEAILDVKSL PLREKLALWS TREEKSLLYR KMDIGEKILV
LDSIKNYKLP EKYQWQLLKV PFDVTNINIM NAFLKYVNEI FIGNFKSISK PRLNSKDLYD
LELYYQKLNL YYSLSKNFNL DFDESWVYDE RTKLSIEINK VLRKRFSF
//
