ID A0A0G3UKC4_9ACTN Unreviewed; 743 AA.
AC A0A0G3UKC4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=M444_13220 {ECO:0000313|EMBL:AKL66211.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL66211.1, ECO:0000313|Proteomes:UP000035653};
RN [1] {ECO:0000313|EMBL:AKL66211.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL66211.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
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; CP011664; AKL66211.1; -; Genomic_DNA.
DR RefSeq; WP_037793336.1; NZ_DS570412.1.
DR AlphaFoldDB; A0A0G3UKC4; -.
DR KEGG; strm:M444_13220; -.
DR PATRIC; fig|465541.12.peg.2873; -.
DR OrthoDB; 9763659at2; -.
DR Proteomes; UP000035653; 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 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:AKL66211.1};
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:UP000035653}.
FT DOMAIN 350..547
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 743 AA; 80234 MW; C9E7CC1551B99C17 CRC64;
MAQQAVVEGV LERITYANEE SGYTVARVDT GRGAGDLLTV VGALLGAQPG ESLRMEGRWG
SHPQYGRQFT VENYSTLLPA TIQGIRRYLG SGLIKGIGPK IADRIVEHFG LDTLEVIESE
PKRLIEVPGL GPKRTRMIGA AWEEQKAIKE VMVFLQGVGV STSIAVRIYK KYGDASISVV
RNQPYRLAAD VWGIGFLTAD RIAQAVGIPH DSPERVKAGL QYALSQSTDQ GHCFLPEERL
IADGVKLLQV DTGLVIDCLS ELAADPEGVV RESVPDPQGG PDPLTAVYLV PFHRAELSLV
GQVRRLLNAE EDRMPGFQDV DWAKALEWLA GRTGAKLAPE QRDAVRLALT RRVAVLTGGP
GCGKSFTVRS IVELARAKKA KVVLAAPTGR AAKRLAELTG AEASTVHRLL ELKPGGDAAY
DRERPLDADL VVVDEASMLD LLLANKLVKA VAPGAHLLLV GDVDQLPSVG AGEVLRDLLA
QDGPVPAVRL TRIFRQAQQS GVVTNAHRIN TGLPPITDGL PDFFLFPVED TEEAGRLTVD
VAARRIPARF GLDPRRDIQV LAPMHRGPAG AGTLNGLLQQ AITPARPDLT EKRFGGRVFR
VGDKVTQIRN NYEKGANGVF NGTVGVVTGL DLDEQRLTVR TEEDEEVAYE FSELDELAHA
YAVTIHRSQG SEYPAVVIPV TTGAWMMLQR NLLYTAVTRA KKLVVLVGSR KALGQAVRTV
SAGRRYTAVA PRLSGRIPVG IFP
//
