ID A0A011A9A2_9BACT Unreviewed; 786 AA.
AC A0A011A9A2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=Cloev_0734 {ECO:0000313|EMBL:EXG78606.1};
OS Cloacibacillus evryensis DSM 19522.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Cloacibacillus.
OX NCBI_TaxID=866499 {ECO:0000313|EMBL:EXG78606.1, ECO:0000313|Proteomes:UP000023044};
RN [1] {ECO:0000313|EMBL:EXG78606.1, ECO:0000313|Proteomes:UP000023044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19522 {ECO:0000313|EMBL:EXG78606.1,
RC ECO:0000313|Proteomes:UP000023044};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JUL-2013) 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:EXG78606.1}.
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DR EMBL; JFBR01000001; EXG78606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011A9A2; -.
DR PATRIC; fig|866499.3.peg.784; -.
DR HOGENOM; CLU_007524_0_3_0; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000023044; 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 GO; GO:0006281; P:DNA repair; IEA:InterPro.
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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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 SMART; SM00278; HhH1; 3.
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, ECO:0000313|EMBL:EXG78606.1};
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:UP000023044}.
FT DOMAIN 96..118
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 132..151
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 196..215
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 353..500
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 750..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 364..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 786 AA; 87654 MW; 2B1C6659221B762B CRC64;
MADKEDNQIV SPVLMIELKG QVERITYHNA ENGYTVLRLS VRDHAELITA VGLMAEPAQG
EMLTLSGRWE ENAKYGMQFH IYKCESTLPA TVTGIEKFLG SGLIRGIGPA MAKKIVDKFG
EETIRVLDDE PARLAEIKGI SENKAEAIAE SWREQREIRE VMVFLQSYGV GTGYAMRIFR
QYGSGTVAVL KDNPYRMAID IPGIGFTIAD RIAQKLGISA DSPMRVRAGV QHVLNQLIAE
GHVYAPSELL AAHSAQTLQV TLDMAREGIE QARLAGEIIV ERFADREGKE QEAVYLPAFH
YAEVSSARNL RLLINEPYNS QCVDCDRTLP WLEREMGITL AQAQREAIIT AVNSKVMVIT
GGPGTGKTTI IRAVLRMREE GGFRVMLAAP TGRAAKRMTE ATGHEAKTIH RLLEYVGSPG
TGGSFMRSET NALECDLLIV DEASMIDQIL FHHLLKAVPR GASLIFVGDA NQLPSVSPGN
VLKDLIESGV CPVVMLREIF RQGRESRIIV NAHRVNDGEM PILPEDQSLE LSDFYFIEPR
VDREGLGEDE YKKLFENKVL QTIKKLVAEN IPNRFNFDPV SDIQVLAPMH NGNVGTKRLN
LELQKILNTG KGASVQRLER VFKEGDKVMQ IKNNYDKDVY NGDIGTITKV DGDESRVTVK
MDTGSVSYEF AELEELVHAY AVSIHKSQGS EYPAVVIPLL TQHYVMLQRN LLYTAITRGK
RLVVIVGAKK ALRIAVENDR TRTRYTRLAQ RLSGPEPPSE IPGELSPDED ELERMFEERQ
KKETLR
//
