ID B4SFL8_PELPB Unreviewed; 738 AA.
AC B4SFL8;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
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 OrderedLocusNames=Ppha_0989 {ECO:0000313|EMBL:ACF43273.1};
OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=324925 {ECO:0000313|EMBL:ACF43273.1, ECO:0000313|Proteomes:UP000002724};
RN [1] {ECO:0000313|EMBL:ACF43273.1, ECO:0000313|Proteomes:UP000002724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5477 / BU-1 {ECO:0000313|Proteomes:UP000002724};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL Submitted (JUN-2008) 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; CP001110; ACF43273.1; -; Genomic_DNA.
DR RefSeq; WP_012507767.1; NC_011060.1.
DR AlphaFoldDB; B4SFL8; -.
DR STRING; 324925.Ppha_0989; -.
DR KEGG; pph:Ppha_0989; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_0_3_10; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000002724; 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:ACF43273.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:ACF43273.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000002724}.
FT DOMAIN 128..147
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 192..211
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 344..466
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 355..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 738 AA; 80373 MW; 6E5248E865A6F77D CRC64;
MNASSTLSPG EKRITGIVEK VSFFSELSGF SVLRLSRKGE SDAVTVVGYV ASVTMGQHIE
AVGCWHNDKS WGLQFKATHL VVVPPDTLEG ITKYLSSGMV KGVGHRLAKV LVRTYGMEVF
TVIEDHPEQL LGLPGVGKKK LQQIVAGWAE QKAIKKIMLF LHSHGVSTSR IVRIFRVYGD
EAVAVVSANP YRLILDIPGI GFRTADQIAR NLGMTSDSPL RARAGISYAL QELSLEGHCR
VPELMLLAAC RKLLDIPEPV LEDALRQELS IGTIVAVEEE GEKSYYLASL YKAERGVAKS
ISRIMQGALP WGTLDPATVI PEAEKLSALE LSESQRNAVA LALSSKFMVI TGGPGVGKTT
IINTILKILD SGKLKFVLCA PTGRAAKRLA ESTGMEAKTI HRLLEFDPFA REFRRGSSYP
LEADLVIVDE ASMIDVVLMN RLLAAVSRRS ALIFAGDVDQ LPPVGPGFVL ADMINSGVLP
VVRLTEIFRQ AESSLIIVNA HRINRGEFVV SPPDSTAGAE LSDFYVVPSE STADIQRRLL
LVVAERIPGR FGMDPLQDIQ VLTPMNKGPL GTVALNSLLQ ERLNPGAVRK IVRFGTTYAE
GDKVIQVVNN YDKEVFNGDI GRIAVVDEEE STIRVLYDGR EVLYESGSLD EIALAYAITI
HKSQGSEYPA VVIPLSMQHY TLLERNLIYT AVTRAKKLVM LIGDPKAISM AVGNKRSSQR
LTGLAALLAE GTDDHLRQ
//
