ID C5AP49_METEA Unreviewed; 733 AA.
AC C5AP49;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 96.
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=recD {ECO:0000313|EMBL:ACS37981.1};
GN Synonyms=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN OrderedLocusNames=MexAM1_META1p0008 {ECO:0000313|EMBL:ACS37981.1};
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630 {ECO:0000313|EMBL:ACS37981.1, ECO:0000313|Proteomes:UP000009081};
RN [1] {ECO:0000313|EMBL:ACS37981.1, ECO:0000313|Proteomes:UP000009081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
RC {ECO:0000313|Proteomes:UP000009081};
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
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; CP001510; ACS37981.1; -; Genomic_DNA.
DR RefSeq; WP_003601039.1; NC_012808.1.
DR AlphaFoldDB; C5AP49; -.
DR STRING; 272630.MexAM1_META1p0008; -.
DR KEGG; mea:Mex_1p0008; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_0_3_5; -.
DR OrthoDB; 1826980at2; -.
DR Proteomes; UP000009081; 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: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; PF14520; HHH_5; 1.
DR Pfam; PF18335; SH3_13; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00278; HhH1; 2.
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:ACS37981.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:ACS37981.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000009081}.
FT DOMAIN 133..152
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 197..216
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 350..530
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 361..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 733 AA; 79665 MW; 53BE37F56EBE9592 CRC64;
MNTPLRSSAI DGAASLDMLA GSVERVTFHS AETGFCVLKI HARGRRDLVP VVGHAPAIAA
GEWLTASGRW VTDREHGLQF RADTLQVTPP TGIEGIERYL ASGQMRGIGP MMAKRIVARF
GEAVFEIIEA EPARLTEVEG IGRKRAARIV KGWAEQKAVR EIMIFLHAHG VGTARATRIF
RTYGGDSLKV MAEDPYRLAR DIRGIGFRTA DAIALRLGLA RDAPQRLAAG VSYALQTAMD
EGHCGLPVER LVRLAAELLD VAPDLVRLAA ALVLREGREV VADTLRGEPC LFLKGLHGAE
RVIAMRLAER AAGPPPWAAI DFALARPWVE AKTGKTLSAS QAEAVGLVLR SKLCVLTGGP
GVGKTSTLDA ILRILTAKGV RVLLAAPTGR AAKRMAEQTG LEARTLHRLL EIDPRNGGFQ
RNEDNPLDCD LLVIDETSMV DVPLMHALLK AVPERAGLIL VGDVDQLPSV GPGQVLADVI
ASGTVPVARL TEIFRQAAQS RIVVNAHSIN TGRMPAAPAK GEDSDFYLID IEDADEGVET
LIELVTRRIP RRFGLDPTRD IQVLTPMIRG SLGSRNLNNA LQRVLNPSPS AEVERFGWRF
APGDRVMETR NDYDRDVFNG DLGTISAIDA EDEALVVDFD GRAVIYPFNE LDTLVPAFAT
TIHKAQGSEY PAVVIPVVTQ HRTMLARNLL YTGVTRGRRL VVLIGQRRAL AMAVREGASR
RRWTKLREWL DAA
//
