ID A0A167TXI5_9BACI Unreviewed; 785 AA.
AC A0A167TXI5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=ATP-dependent RecD-like DNA helicase {ECO:0000256|HAMAP-Rule:MF_01488};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01488};
GN Name=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN ORFNames=GFC29_1842 {ECO:0000313|EMBL:ANB62690.1};
OS Anoxybacillus sp. B7M1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=1490057 {ECO:0000313|EMBL:ANB62690.1, ECO:0000313|Proteomes:UP000076753};
RN [1] {ECO:0000313|EMBL:ANB62690.1, ECO:0000313|Proteomes:UP000076753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=b7m1 {ECO:0000313|Proteomes:UP000076753};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase.
CC Has no activity on blunt DNA or DNA with 3'-overhangs, requires at
CC least 10 bases of 5'-ssDNA for helicase activity. {ECO:0000256|HAMAP-
CC Rule:MF_01488}.
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=3.6.4.12;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01488};
CC -!- SIMILARITY: Belongs to the RecD family. RecD-like subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01488}.
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DR EMBL; CP015436; ANB62690.1; -; Genomic_DNA.
DR RefSeq; WP_044744637.1; NZ_CP015436.1.
DR AlphaFoldDB; A0A167TXI5; -.
DR KEGG; anl:GFC29_1842; -.
DR PATRIC; fig|1490057.3.peg.2093; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000076753; Chromosome.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd17933; DEXSc_RecD-like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 1.10.10.2220; -; 1.
DR Gene3D; 2.30.30.940; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01488; RecD_like; 1.
DR InterPro; IPR006345; DNA_helicase_RecD-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029493; RecD-like_HHH.
DR InterPro; IPR041451; RecD-like_SH13.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR NCBIfam; TIGR01448; recD_rel; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF14490; HHH_4; 1.
DR Pfam; PF18335; SH3_13; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01488}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01488};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:ANB62690.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000076753}.
FT DOMAIN 156..247
FT /note="RecD helicase-like helix-hairpin-helix"
FT /evidence="ECO:0000259|Pfam:PF14490"
FT DOMAIN 589..656
FT /note="RecD-like DNA helicase SH3"
FT /evidence="ECO:0000259|Pfam:PF18335"
FT DOMAIN 676..724
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 365..369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 785 AA; 88546 MW; F70610D79C0F38E7 CRC64;
MQQQESWALG EKSFIKGTHI VTIFHNESNL YSVVRIHVEE TNEGYDEQEV VVTGYFPRMN
EHDVYVFYGA FKDHPRFGRQ YVAEYFRKEM PQTKEGLIYY LSSDLFKGIG KKTAEQIVEA
LGDQAISVIL ADPEALAKVP KLPKNKAKEL YETLKEHQGL EQIMIALSQF GFGPQLSMKI
YQVYKEAALD VIQKNPYQLV EDVEGIGFRR ADELGQQLGL SGSHPDRVRA ACLYVIESDC
LQEGHVYVTK EQLLFKAKQL LESKRGEDIP PDMIERELLD LAKEEKVIHE DGRFYIPTLY
FAEKGIITNI KRLLEQKVTR FPEAEFLLAL GRLEERLDVQ YGPLQKEAIQ QAISSPLFIL
TGGPGTGKTT VIKGIVEIFA DLHGVSLDPK DYHKENPFPI LLAAPTGRAA KRMSEATGLP
AMTIHRLLGY NAAEGFTHHE DEPIEGNLLI VDEMSMVDTW LANQLLKSLP TGMQVILVGD
EDQLPSVGPG QVLKDLLKTS RIPTIRLTEV YRQAEGSSII ELAHCMKKGE LPADLSSPKT
DRSFIRCKAE QVVDVVRQIA DNAWKKGYSV KDIQVLAPMY RGPAGIDRLN RTLQELFNPK
SPQKRELSSG ETVYRVGDKV LQLVNQPDQN VFNGDIGEIV AIFYAKENTE QQDLVVVSFD
GNEVTYTRQD LTQITHAYCC SIHKAQGSEF PIVILPVVKS YYRMLQRNLL YTAVTRSKKF
LILCGEEEAF RIGTARCDDG VRQTTLAEKI QQLFEPADET ELPLDDAGIG MENVSPYDFM
IEETK
//
