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Database: UniProt
Entry: A0A1G8N9D9_9BACI
LinkDB: A0A1G8N9D9_9BACI
Original site: A0A1G8N9D9_9BACI 
ID   A0A1G8N9D9_9BACI        Unreviewed;       764 AA.
AC   A0A1G8N9D9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=SAMN05216352_111158 {ECO:0000313|EMBL:SDI76733.1};
OS   Alteribacillus bidgolensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX   NCBI_TaxID=930129 {ECO:0000313|EMBL:SDI76733.1, ECO:0000313|Proteomes:UP000199017};
RN   [1] {ECO:0000313|EMBL:SDI76733.1, ECO:0000313|Proteomes:UP000199017}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P4B,CCM 7963,CECT 7998,DSM 25260,IBRC-M 10614,KCTC 13821
RC   {ECO:0000313|Proteomes:UP000199017};
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; FNDU01000011; SDI76733.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8N9D9; -.
DR   STRING; 930129.SAMN05216352_111158; -.
DR   OrthoDB; 9803432at2; -.
DR   Proteomes; UP000199017; 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:InterPro.
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; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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};
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:UP000199017}.
FT   DOMAIN          355..519
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         366..370
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   764 AA;  86608 MW;  0622F72CA65DEB93 CRC64;
     MSSVSYENDL PSKSFISGTV VHVIFRNEEN GYTVLIVKVR KSHPKADEKK VTVVGYFPSV
     ETDERYYFEG VFKEHPRFGK QYHVQIYKKE IPTEKEALIA YLSSERFPGI GKKTASVLVE
     NFGENVIEKI LNDPDKLKKL SGLNQKRRQN IYQTMLENQG MEQAMTMLTR YGFGMELAVK
     IYNAYRERTF DVIQDTPYQL VWDIEGVGFY KADKLGKSLG IKRDDPERVK AGMLYILYEK
     TMQDGHVYVP WSLLTQESRH LLNDSQNKIS NELLESALLE LAEEDKLIQE DDRVYMASLY
     FAEKGFVTKV KKLLEREEEA AFSEAEFLKA LGKTEEQFGI EYADHQKEAI QKAVHSPLMI
     LTGGPGTGKT TVIRAIVEIF SKLHGFSLDR STYKKEEPFP VLLAAPTGRA AKRMKESTGL
     KASTIHKLLG YNGVDGDEAF EKDEEEPLEG KLLIIDEVSM VDMWLANQLF RSVPEDMQVI
     LVGDEDQLPS VGPGQVLGDL LETNIVPIVS LSVVYRQAEG SSIINLAHSI KKGMLPHDLM
     SPCKDRRFFS CNKIQTSDVI EKVCEGAVKK GYSPLDIQVL APMYKGPAGV DALNKTLQQL
     YNPHEDKKRK VLFGETTYSK GDVILQLINN PEEGVFNGDR GVVEAIFEAK ETADKQMQIV
     LSFEGKEVTY TRQDLNQITL AYCTTIHKAQ GSEFPIVVVP MLMAYKRMLQ RNLLYTAITR
     ARDYLILCGE NSAVEFAVDN KHRENRHTTL KEKLLEKDNA SFHE
//
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