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Database: UniProt
Entry: A0A1E7K173_9ACTN
LinkDB: A0A1E7K173_9ACTN
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ID   A0A1E7K173_9ACTN        Unreviewed;       760 AA.
AC   A0A1E7K173;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=AN217_07195 {ECO:0000313|EMBL:OEU97684.1};
OS   Streptomyces qinglanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=943816 {ECO:0000313|EMBL:OEU97684.1, ECO:0000313|Proteomes:UP000175829};
RN   [1] {ECO:0000313|EMBL:OEU97684.1, ECO:0000313|Proteomes:UP000175829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO M10379 {ECO:0000313|EMBL:OEU97684.1,
RC   ECO:0000313|Proteomes:UP000175829};
RX   PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA   Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA   Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT   "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT   Adaptation to the Marine Environment and Their Diversity at the Genomic
RT   Level.";
RL   Front. Microbiol. 7:998-998(2016).
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:OEU97684.1}.
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DR   EMBL; LJGV01000022; OEU97684.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E7K173; -.
DR   PATRIC; fig|943816.4.peg.811; -.
DR   Proteomes; UP000175829; 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, ECO:0000313|EMBL:OEU97684.1};
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:UP000175829}.
FT   DOMAIN          362..543
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         373..377
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   760 AA;  81644 MW;  CC366EDB60322D17 CRC64;
     MSVLEATVGD MTFQPAVLEG VLERITYANE DNGYTVARVD TGRGAGELLT VVGALLGAQA
     GESLRMEGRW GSHPQYGRQF QVDNYVTVLP ATVQGIRRYL GSGLVKGVGP RIADRIVSHF
     GVDTLEVIEA DARRLIEVPG LGPKRTGLIA AAWEEQKAIK EVMVFLQGVG VSTSIAVRIY
     KQYGDASISV VRGNPYRLAA DVWGIGFLTA DRIAQAVGIP HDSPERVKAG LRHALSQSSD
     QGHCYLPEER LITEAVKLLQ VDTGLVIDCL GELAGDEEGG VVREPVPDPE QPEHSLTAVY
     LVPFQRAEVA LAAQLKRLAR TPEDRLPWFR DVDWEAALGW LARRTGARLA PEQEEAVRLA
     LTSRVAVLTG GPGCGKSFTV RSVVELARAK EARVVLAAPT GRAAKRLAEL TGAEASTVHR
     LLELKPGGDA AYDRDRPLEA DLVVIDEASM LDLLLANKLI KAVPPGAHLL LVGDVDQLPS
     VGAGEVLRDL LAEGGPVPAV RLRRIFRQAQ QSGVVTNAHR INSGTPPLTR GLSDFFFFVE
     EDTEAAGLLT VDVAARRVPA KFGLDPRRDV QVLAPMHRGP AGAGALNGLL QQAVTPARPD
     LPEKRFGGRV FRVGDKVTQI RNNYEKGANG VFNGTVGVVT GLHPDDHRLT VLTDEDEEVG
     YDFDELDELS HAYAMTIHRS QGSEYPAVVI PVTTGAWMML QRNLLYTAVT RAKRLVVLVG
     SRRALGQAVR TASAGRRCTA LDHRLRASAP VPGGGMGAGG
//
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