ID A0A2N6SM64_9LACT Unreviewed; 787 AA.
AC A0A2N6SM64;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CJ205_05785 {ECO:0000313|EMBL:PMC58153.1};
OS Dolosicoccus paucivorans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Dolosicoccus.
OX NCBI_TaxID=84521 {ECO:0000313|EMBL:PMC58153.1, ECO:0000313|Proteomes:UP000235682};
RN [1] {ECO:0000313|EMBL:PMC58153.1, ECO:0000313|Proteomes:UP000235682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0852 {ECO:0000313|EMBL:PMC58153.1,
RC ECO:0000313|Proteomes:UP000235682};
RA Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT "Bacterial strain isolated from the female urinary microbiota.";
RL Submitted (SEP-2017) 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:PMC58153.1}.
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DR EMBL; PNHE01000023; PMC58153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6SM64; -.
DR STRING; 84521.SAMN04487994_10044; -.
DR Proteomes; UP000235682; 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:RHEA.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01488; RecD_like; 1.
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; 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; PF13604; AAA_30; 1.
DR Pfam; PF14490; HHH_4; 1.
DR Pfam; PF18335; SH3_13; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
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:PMC58153.1};
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:UP000235682}.
FT DOMAIN 150..240
FT /note="RecD helicase-like helix-hairpin-helix"
FT /evidence="ECO:0000259|Pfam:PF14490"
FT DOMAIN 576..646
FT /note="RecD-like DNA helicase SH3"
FT /evidence="ECO:0000259|Pfam:PF18335"
FT DOMAIN 663..711
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 359..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 787 AA; 88935 MW; 05646653A86536FF CRC64;
MPQEEYIVGQ VEAIYFENPS NLYKVFRIQV DASESSIIVD DTIVCTGYFA ELDYDLPYQF
FGSIVNHPKF GEQFKVERYQ QMEPTSKQGL IDYLSGHKFK GIGPVLATRI VDELGQDAIN
KIIEDSNALI NVQGLSKTKQ EELRNTLLQT QGTERIFITL GQWGFTAKMA DKIYKAFQSK
TIDLLQENPY LLVEKVEGIG FQKADQLAQT LDIKADSPDR LKAALLVVVQ QYSLAEGDTY
VEKETLLQET QKLLEKSRSF MVEEFLIEES LETAIEEELL MTLDNGVMLP SLYYAELGCV
QLLSDLMEHT TFTPPSKKRI DEGIKAVINQ VGIPYDKQQQ AAIKTAMQSP VSIITGGPGT
GKTTLVNGMI HLHEWLNPSK GDEQTTVLLA APTGRAAKRL SEMTDRPATT IHRLVGYTRE
SRRDEFVPLE LEGTLLVVDE MSMVDTWLLY WLLQSIPFGL QVIFVGDRHQ LPSVGPGQVF
TDLILSKTLP TIELTHIYRQ EEGSSIVELA HSIQKGELPS DFLDKRDDRS FIPCTADQVP
QVVERVVQFA LQKGYDAQTM QVLAPMYKGP AGINRLNELL QEEMNPLKGQ MREIKSFNHS
FRHADKVLQL ENDAELGIYN GDIGMIEGVY RGEETESKSD ELVVDFDGLE ITYTRSNFDQ
LTLAYCTSIH KSQGSEYPLV ILALVNTYSK MLRRDLLYTA ITRAKGSLVL LGNPQDFVTA
VNNGGQERRT LLKELLQVKF ETQEEVFEEE EQAIIQQQLE EPIRLTEETW DQIDPMIGMN
NVTPYTI
//
