ID A0A286GDI8_9ACTN Unreviewed; 1109 AA.
AC A0A286GDI8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=SAMN06272739_0345 {ECO:0000313|EMBL:SOD93570.1};
OS Blastococcus haudaquaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1938745 {ECO:0000313|EMBL:SOD93570.1, ECO:0000313|Proteomes:UP000219482};
RN [1] {ECO:0000313|Proteomes:UP000219482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44270 {ECO:0000313|Proteomes:UP000219482};
RA Varghese N., Submissions S.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
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DR EMBL; OCNK01000001; SOD93570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286GDI8; -.
DR OrthoDB; 4812256at2; -.
DR Proteomes; UP000219482; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF55; DNA HELICASE; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000219482}.
FT DOMAIN 46..381
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 382..693
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1109 AA; 117893 MW; 43FE87A03F521673 CRC64;
MTPRAGASAE QLSFDDLFSV AVPEQPAARR WLTPAEVAAR CGLSYAPSPE QARVVEAPAD
RPLVVVAGAG SGKTETMAAR VSWLVANGVV APEEILGLTF TRKAASELNE RIRLRLGALA
RHPDTERDLR ERLEIAQPTV STYHGYAAAL VAEHGLRIGV EPGAGVLGPA MCWGQAAQVV
TAYTGDMSDV PLTLLTTVED VLALAADLGE HDISPAALRA WTARLESHIA GYADAPRKKG
PYAPVVEMLA RQKARVALLP LVEAFEARKR SAGAIDYADQ VAYAARIAVA SAEVGRRERA
RWKAVLLDEY QDTSVGQLRM LEALFGGDSG HPVLAVGDPR QSIYGWRGAS AGTIERFDRT
FPGLPGRAAE RLTLATSWRN DDAVLAVANA VSGMLPPPEQ PLPDLAPAPT AGRGAVTVGL
YDTIADETEA LADRLAACWL GTDPEFGGRD GKRPTVAVLV RARKQLPGIA AALRERGLPV
EVVGLGGLLE VPEVSDVIAT LTVLVDPTAG DALGRLLTGA RWRIGPRDLA ALEARARALV
HSRRPAAPAD GQPVVEAPAE RGSIVEALDD LGGPDAYSQA GYRRLRRLGG ELAHLRNRLS
ESLPDLVDEV ARALGLETEL ASAPGASPAG ARAHLDALHG VAAEFTELAE LPSLPAFLGY
LRDAEERERG LEPGEVAVNP EAVQLLTGHS AKGLEWDVVA VPGLTTDQFP SKADTSDSWI
RDPGAVPADL RLTDREELPR LRLPVPGSGD QAAVRQALED YVQEWKDFGT AEEIRLGYVA
VTRARHLLLC SGSWWRDGVK PCGPSSLLLT ARQACEDGAG TVVHWAEPPA DDATNPALAE
WPVGIWPADP LSFGRRRALT AAADLVTGTA AHPLDAEQVL DGGDPLVEQW VRDADLLLRE
RARHASPTVD VPLPSHLSVS ALVTLRRDPA ELARRLRRPM PAAPAPQARR GTAFHAWLEE
RFGAAKLVDL DELPGSGDEF AAPDGALAEL QAAFLASEWA DRQPAEVEVP FETPLGPLTL
RGRIDAVFQR EDGGFEVIDW KTGPPPSGAE LAAAAVQLAA YRLGWARLTG VPVERVSAGF
HHVAANVTLR PVDLLGEAGL LNLVTGADD
//
