ID A0A1G9XTH1_9BACI Unreviewed; 774 AA.
AC A0A1G9XTH1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05216244_3957 {ECO:0000313|EMBL:SDN00030.1};
OS Sediminibacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Sediminibacillus.
OX NCBI_TaxID=482461 {ECO:0000313|EMBL:SDN00030.1, ECO:0000313|Proteomes:UP000182347};
RN [1] {ECO:0000313|EMBL:SDN00030.1, ECO:0000313|Proteomes:UP000182347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6199 {ECO:0000313|EMBL:SDN00030.1,
RC ECO:0000313|Proteomes:UP000182347};
RA de Groot N.N.;
RL Submitted (OCT-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; FNHF01000007; SDN00030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9XTH1; -.
DR STRING; 482461.SAMN05216244_3957; -.
DR Proteomes; UP000182347; 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; 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; 2.
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};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}.
FT DOMAIN 157..247
FT /note="RecD helicase-like helix-hairpin-helix"
FT /evidence="ECO:0000259|Pfam:PF14490"
FT DOMAIN 589..659
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 REGION 755..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..774
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 365..369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 774 AA; 88079 MW; EE8FF7F9A4485CCC CRC64;
MAMEDKNGQL QQNSYVKGEL LHHIFINEEE HFSIARIKVL ETNESFKEKD MVVKGYFSRL
NEGETYVFHG TFEQHKKFGL QYQVNHFKRF IPETEDGLVA YLSSDLFYGI GKKTAQRIVK
ELGETAVSKI LQDPGVLNSI PGLTQEKAEQ LSKDLAEHQG FEHIVVHLSN YGFGLKMAQK
IYQAYKDEAI TILEQDPYQY VFDIEGFGFQ RADEVARQNH IPMDHPSRVQ AACIYTLQQS
IQEGHVYLPL ENHLQAVDEL LHGEEHQIEP ETITAQIAEL NKRKKIIVVD SRVYLPSLYY
SESGFCTNID RIIKQAISEQ PADAELLKIV GRIEEEESLS YGKEQYQAIE KAIGSKLMVL
TGGPGTGKTT VIKGIINAYA EIHGLSLDPD DYDNDATYPF ILTAPTGRAA KRMKESTGLP
AVTIHRLLGW NGHETFEKDE DNQLEGKLLV IDEFSMVDIW LAHQLFKAIP NNMQVLIVGD
EDQLPSVGPG QVLADLLKSG LVPFVQLNEV YRQKEGSKII QLAHEIKNNQ CRHDSLQQET
DFNFIECPEY QVVDVIIQIV KRAHDKGVDL RDLQVLAPMY RSKAGIHRIN EEIQKLINPK
TNQRREIRTK DITFRTGDKV IQLVNQPEDG VFNGDIGEIS AIFEEDEGSG QAEEVVVAFE
EKEVAYERKD LANIMHAYCT SIHKSQGSEF PIVIIPVIQG YRRMLRKNLL YTAVTRCKKS
LILCGNKQAF IQGVNEQDTN RRFTSLEEQL RELIENVPQP EQEEEGELSP YDFL
//
