ID M1ZYQ3_CLOBO Unreviewed; 569 AA.
AC M1ZYQ3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE Flags: Fragment;
GN ORFNames=CFSAN001627_06049 {ECO:0000313|EMBL:EKN42550.1};
OS Clostridium botulinum CFSAN001627.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1232189 {ECO:0000313|EMBL:EKN42550.1, ECO:0000313|Proteomes:UP000011944};
RN [1] {ECO:0000313|EMBL:EKN42550.1, ECO:0000313|Proteomes:UP000011944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFSAN001627 {ECO:0000313|EMBL:EKN42550.1,
RC ECO:0000313|Proteomes:UP000011944};
RA Strain E.A., Brown E., Allard M.W., Gonzalez-Escalona N., Timme R.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EKN42550.1, ECO:0000313|Proteomes:UP000011944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFSAN001627 {ECO:0000313|EMBL:EKN42550.1,
RC ECO:0000313|Proteomes:UP000011944};
RA Timme R.E., Allard M., Luo Y., Strain E., Gonzalez-Escalona N., Brown E.;
RT "Diversity in Clostridium botulinum.";
RL Submitted (MAR-2013) 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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
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:EKN42550.1}.
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DR EMBL; AMXI01000347; EKN42550.1; -; Genomic_DNA.
DR AlphaFoldDB; M1ZYQ3; -.
DR Proteomes; UP000011944; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR048228; HelD_bacillota.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; NF041464; HelD_BACSU; 1.
DR PANTHER; PTHR11070:SF17; DNA HELICASE IV; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 69..452
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT BINDING 90..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT NON_TER 569
FT /evidence="ECO:0000313|EMBL:EKN42550.1"
SQ SEQUENCE 569 AA; 66764 MW; 689A0F8A281C6AFF CRC64;
MFYDYEIGEA NYKCPEGRVN GKLTLKRQYK INNGEIKYMF DSNLKIDDEV LQDILGKSTD
SKMNAIVTTI QREQNKVIRN EEYKNLIVQG PAGSGKTSVA LHRIAYLLYK HRDKISPKNI
VIFSPNDILN DYISNVLPQL GEDNMCQTTF KEYMHKVLGN GLIKENYSEM MEYILVSKKD
GAYEKRINNI KFKSSMEFMN ILKAYVGYLE KMDRNFTDIT FRGDLIISSK DIEELFFKDY
VKLPLKRRLE KIRRRILFLM EPYEKHWVKE ESEELKNSGN YIDNVEIMER SINIVKDEIK
DIYHEINRMT DFDLVDVYKK LFENLEFFLK KSNIEYHEKN IDEIKNYTLE ILRIGKLNYE
DQPPLLYLKG ALGDLPKNSE IKYVIIDEAQ DYTPLQYEIF SQLFNHANMT ILGDLHQSIN
PFMNVGDYSN ISNVFPKDNT CIINLTKSYR STMEITEFSR RILNKKITDQ WVERSGDKPL
VLGFPNEEAI KERLLKDIKI YKEKGYKSIG IITRTIKEAQ EVHSFLKDKI HVKAIMKDDD
EYVSDTLVIP AYLAKGLEFD VVLIYNAGD
//
