ID A0A2W2M012_9ACTN Unreviewed; 754 AA.
AC A0A2W2M012;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=C1I97_10830 {ECO:0000313|EMBL:PZH14284.1};
OS Streptomyces sp. NTH33.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1735453 {ECO:0000313|EMBL:PZH14284.1, ECO:0000313|Proteomes:UP000248559};
RN [1] {ECO:0000313|EMBL:PZH14284.1, ECO:0000313|Proteomes:UP000248559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTH33 {ECO:0000313|EMBL:PZH14284.1,
RC ECO:0000313|Proteomes:UP000248559};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequence of Streptomyces sp. NTH33.";
RL Submitted (JAN-2018) 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:PZH14284.1}.
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DR EMBL; POTZ01000079; PZH14284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2M012; -.
DR OrthoDB; 9763659at2; -.
DR Proteomes; UP000248559; 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 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; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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:PZH14284.1};
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:UP000248559}.
FT DOMAIN 368..549
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 379..383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 754 AA; 81361 MW; 254D4A103510BA5A CRC64;
MTTEASRAGQ AGAGERRSAV LEGVLERITY ANEENGYTVA RVDTGRGAGD LLTVVGALLG
AQVGESLRME GRWGSHPQYG KQFQVENYTT VLPATVQGIR RYLGSGLVKG IGPVFADRIT
QHFGLDTLRI IEEEPERLIE VPGLGPKRTK RIADAWEEQK AIKEVMLFLQ TVEVSTSIAV
RIYKKYGDAS ISVVKNQPYR LAADVWGIGF LTADKIAQSV GIPHDSPERV KAGLQYALSQ
SADQGHCFLP EERLIADAVK LLQVDTGLVI ECLAELAQPA EDGGDPGVVR EKVPGHDGGD
PVTAIYLVPF HRAELSLSAQ LLRLLRTDAD RMPSFRDVAW DRALSWLGGR TGTDLAPEQE
AAVKLALTEK VAVLTGGPGC GKSFTVRSIV ELARAKKAKV VLAAPTGRAA KRLSELTGAE
ASTVHRLLEL KPGGDAAYDR DRPLDADLVV VDEASMLDLL LANKLVKAVP PGAHLLFVGD
VDQLPSVGAG EVLRDLLAEA GPIPAVRLTR VFRQAQQSGV VTNAHRINAG QHPLTDGMKD
FFLFVEDDTE EAGRLTVDVA ARRIPARFGL DPRRDVQVLA PMHRGPAGAG TLNGLLQQAV
TPGRPDLPEK RFGGRVFRVG DKVTQIRNNY EKGENGVFNG TVGVVTSLDP VDQRLTVLTD
EDEEVSYEFD ELDELAHAYA VTIHRSQGSE YPAVVIPVTT GAWMMLQRNL LYTAVTRAKK
LVVLVGSRKA IGQAVRTVSA GRRCTALDFR LAGG
//
