ID S0NHX4_9ENTE Unreviewed; 835 AA.
AC S0NHX4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=OMQ_02007 {ECO:0000313|EMBL:EOT28092.1};
OS Enterococcus saccharolyticus subsp. saccharolyticus ATCC 43076.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1139996 {ECO:0000313|EMBL:EOT28092.1, ECO:0000313|Proteomes:UP000014136};
RN [1] {ECO:0000313|EMBL:EOT28092.1, ECO:0000313|Proteomes:UP000014136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43076 {ECO:0000313|EMBL:EOT28092.1,
RC ECO:0000313|Proteomes:UP000014136};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus saccharolyticus ATCC_43076 (Illumina
RT only assembly).";
RL Submitted (MAR-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:EOT28092.1}.
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DR EMBL; AHYT01000009; EOT28092.1; -; Genomic_DNA.
DR RefSeq; WP_016175776.1; NZ_KE136523.1.
DR AlphaFoldDB; S0NHX4; -.
DR STRING; 41997.RV16_GL001005; -.
DR PATRIC; fig|1139996.3.peg.1977; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_0_1_9; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000014136; 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; 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; 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.
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:EOT28092.1};
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:UP000014136}.
FT DOMAIN 97..113
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 127..146
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 191..210
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 348..496
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 359..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 835 AA; 94335 MW; FA81AEBE4DA82459 CRC64;
MLPEKTYVVG KVAAIFFQNP SNFFKVLLVR IEETNAEYRE KEIVVTGSFG EVQEEESYRF
FGEMVEHPKY GEQLKADTYQ KEQPTSENGL IHYLSSEKFP GIGKKTAERI VDLLGEQAID
RMIAEPELLG QVPGLTEKKQ KMMLETIRLN YGMDQVIVGL NRFGFGSQLA FAIYQAYKNT
AIEMIEENPY RLVEDIEGIG FKKADNIAEQ LGIEATSPKR MRAAILHQIF QQSMQTGNTY
VPAQELLDQT IRLLETSRPV EIHPEQVADV VIQLVDQGKI QQEGTNLYEN SLFFSEWGIA
TSIQRLLQRK KEINYPEKTV EKCLRKIEKR LGIVYGSSQE EAIKQAIRSP LFILTGGPGT
GKTTVINGIV QLFAELNEVD LEPSKYTEET FPILLAAPTG RAAKRMNETT GLPSGTIHRL
LGLNGREKAT AMAPKELEGG LLIVDEMSMV DTWLANTLFK SISTNMQVIF VGDKDQLPSV
GPGQVLHDLL EIDDIPKQEL NEIYRQGDGS SIIPLAHEIK NGRLPQNFTQ NQKDRSFFAC
DAYKIEPIIA QIVQRAKDRG FTPQDIQVLA PMYRGAAGID ALNKMMQEIF NPNPDGKKKE
VHWNETVYRI GDKVLQLVNS PEDNVFNGDM GQIVGITYAK NSEDKVDELT IQFDANEVTY
KRSEWNKITL SYCCSIHKSQ GSEFKMVILP MVHQYQRMLQ RNLLYTAITR SKELLILLGE
LPAYQQCVAN ESNLRYTTLK ERILGIDSLS STMRQRIHQY EEADEEPFAE EDNVAPLPIV
EASEAQTSLF SEEASLIEEA FEQLPEYLTE EVIQTGQIDP MIGMAGISPY DFQTN
//
