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Database: UniProt
Entry: A0A1Q8Q816_9BACI
LinkDB: A0A1Q8Q816_9BACI
Original site: A0A1Q8Q816_9BACI 
ID   A0A1Q8Q816_9BACI        Unreviewed;       792 AA.
AC   A0A1Q8Q816;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=BTO30_05630 {ECO:0000313|EMBL:OLN23441.1};
OS   Domibacillus antri.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX   NCBI_TaxID=1714264 {ECO:0000313|EMBL:OLN23441.1};
RN   [1] {ECO:0000313|EMBL:OLN23441.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XD80 {ECO:0000313|EMBL:OLN23441.1};
RA   Verma A., Krishnamurthi S.;
RT   "Domibacillus antri genome sequencing.";
RL   Submitted (DEC-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}.
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:OLN23441.1}.
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DR   EMBL; MSDU01000008; OLN23441.1; -; Genomic_DNA.
DR   RefSeq; WP_075397732.1; NZ_MSDU01000008.1.
DR   AlphaFoldDB; A0A1Q8Q816; -.
DR   STRING; 1714264.BTO30_05630; -.
DR   OrthoDB; 9803432at2; -.
DR   Proteomes; UP000185568; Unassembled WGS sequence.
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; 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; IPR027785; UvrD-like_helicase_C.
DR   NCBIfam; TIGR01448; recD_rel; 1.
DR   PANTHER; PTHR43788:SF6; DNA HELICASE B; 1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF13604; AAA_30; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01488};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01488}.
FT   DOMAIN          157..248
FT                   /note="RecD helicase-like helix-hairpin-helix"
FT                   /evidence="ECO:0000259|Pfam:PF14490"
FT   DOMAIN          589..658
FT                   /note="RecD-like DNA helicase SH3"
FT                   /evidence="ECO:0000259|Pfam:PF18335"
FT   DOMAIN          677..725
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13538"
FT   BINDING         366..370
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   792 AA;  89259 MW;  798FF842DC07633F CRC64;
     MAQEKRGLFI EDEQFLKGRH IVTIFRNDEN FYTVLRVRVT ETDGNYEEKE AVVTGYFPAV
     HEHEMYVFSG VFKDHPRFGR QFIARTAQKE MPQTKQGVIA YLSGDLFKGI GKKTAESIVE
     TLGEQAISKI IADKNCLKKV PKLSGEKAQF LYETLMKHQG LEQIMIALND FGFGPQLAMK
     IYQMYYDESL SIIQENPYRL VEDIEGIGFI RADEIGAKIG ISGAHPDRLK AAILYSLELQ
     CLQDGHCYVE ADSLLKHVKE LLDKSANGTA EFDIIAKRLI ELEEEGKVSG EEKRIYMPSL
     YFSEKGLVTN IQRVLDQEEQ SFPESEFLLA LGDLEDRTGI AYAPSQKQAI QTALSSPLMI
     LTGGPGTGKT TVIKGIVELY GELHGLSLDP KQYDKEEPFP IKLCAPTGRA AKRMMESTGL
     PAVTIHRLLG FNGQEEPDEE GKEITGRLLI VDEMSMVDIW LAHQLFKAVP DDMQIVLVGD
     EDQLPSVGPG QVLKDMLASG VIPSVRLTDI YRQEEGSSII SLAHSIKDGH VPETLTHPQK
     DRSFIRCRTE QIPEVIEKVV KNAAGKGYEP RDIQVLAPMY KGPAGIDKLN EVLQTVLNPN
     EDGRRKELQF GTVKYRIGDK VLQLVNQPEQ QVFNGDIGEI ISIFFAKENT EKEDMVIVSY
     EGNEVTYTRN DLNQITHAFC CSIHKSQGSE FPIVILPVVK SYYRMLRRNL LYTAITRSKQ
     FLILCGEEEA FHIGIARNDD LIRKTALAQR LAVYDEKEAE HREAEKLTED SWMNIDPMIG
     MEGITPYDFM RA
//
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