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Database: UniProt
Entry: A0A1H8YXS2_9ACTN
LinkDB: A0A1H8YXS2_9ACTN
Original site: A0A1H8YXS2_9ACTN 
ID   A0A1H8YXS2_9ACTN        Unreviewed;       750 AA.
AC   A0A1H8YXS2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, 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=SAMN05216481_101162 {ECO:0000313|EMBL:SEP57020.1};
OS   Streptomyces radiopugnans.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=403935 {ECO:0000313|EMBL:SEP57020.1, ECO:0000313|Proteomes:UP000199055};
RN   [1] {ECO:0000313|EMBL:SEP57020.1, ECO:0000313|Proteomes:UP000199055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3519 {ECO:0000313|EMBL:SEP57020.1,
RC   ECO:0000313|Proteomes:UP000199055};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOET01000001; SEP57020.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8YXS2; -.
DR   STRING; 403935.SAMN05216481_101162; -.
DR   Proteomes; UP000199055; 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; 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};
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:UP000199055}.
FT   DOMAIN          360..557
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         371..375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   750 AA;  81233 MW;  7B1EFA53EC84C3C2 CRC64;
     MSVPGVTVCD MSFQPAVLEA VLERITYANE ENGYTVARVD TGRGGELLTV VGSLLGAQVG
     ESLRMEGRWG SHPQYGRQFT VENYTTVLPA TVQGIRRYLG SGLIKGIGPK IAERIVDHFG
     LETLEVIENE PERLIEVPGL GPKRTKLIGA AWEEQKAIKE VMVFLQGVGV STSIAVRIYK
     KYGDASISVV RNQPYRLAAD VWGIGFLTAD RIAQAVGIPH DSPDRVKAGL QYALSQSADQ
     GHCYLPEERL IADTVKLLQV DTGLVIDCLG ELAGEEEGVV REQVPDPEHP GQRVSAVYLV
     PFHRAELSLS AQLLRLLRTE EDRIPAFRDV DWEAALSWLA GRTGAELAPE QRDAVKLALT
     QKVAVLTGGP GCGKSFTVRS VVELARAKRA KVVLAAPTGR AAKRLSELTG AEASTVHRLL
     ELRPGGDAAY DRERPLDADL VVVDEASMLD LLLANKLIKA VAPGAHLLLV GDVDQLPSVG
     AGEVLRDLLA EGSPVPAVRL TRIFRQAQQS GVVTNAHRIN SGVPPITQGL PDFFLFVEDD
     TEEAGRLTVD VAARRIPAKF GLDPRRDVQV LAPMHRGPAG AGTLNGLLQQ AITPGRPDLP
     EKRFGGRVFR VGDKVTQIRN NYEKGANGVF NGTVGVVTSL STEEQRLTVR TDEDEEVGYD
     FDELDELAHA YAVTIHRSQG SEYPAVVVPV TTGAWMMLQR NLLYTAVTRA KRLVVLVGSR
     RALGQAVRTV SAGRRCTALD HRLRGTPHPA
//
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