ID Q47SK6_THEFY Unreviewed; 1044 AA.
AC Q47SK6;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=Tfu_0523 {ECO:0000313|EMBL:AAZ54561.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54561.1};
RN [1] {ECO:0000313|EMBL:AAZ54561.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YX {ECO:0000313|EMBL:AAZ54561.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of Thermobifida fusca YX.";
RL Submitted (JUL-2005) 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};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; CP000088; AAZ54561.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47SK6; -.
DR STRING; 269800.Tfu_0523; -.
DR KEGG; tfu:Tfu_0523; -.
DR eggNOG; COG0210; Bacteria.
DR eggNOG; COG2887; Bacteria.
DR HOGENOM; CLU_004900_0_0_11; -.
DR OrthoDB; 5240387at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; 1.10.10.160; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
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; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF59; 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; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
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 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}.
FT DOMAIN 19..319
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 330..630
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1044 AA; 115344 MW; 444F726655840EDB CRC64;
MDNPPYRLVR RIRHRAPAPE LDDDQRRVVD HEGGPLLVLA GPGTGKTTTI VEAIVDRVEN
RGVDPAHVLV LTFSRKAAQE LRERITARLR RTVREPLALT FHSYAYALIR REFQRVGDHA
PRLLSGPEQL MEVRELLKGE LADGAPGWPE QLRPMLHTRG FAEELRDFLM RVQERGLHAD
DVRELGRRHG REDWVAAGGF LERYTGRFDI APVPTFNYAE LVRVAANLLN DPDIQARERA
ARKVVFVDEY QDTDPAQEEL LHALAGDGRD LVVVGDPDQS IYGFRGAEVR NILNFPDRFR
TPTGDPAPVV ALHTCRRSGA ELLRVSRALA QRLPAVPGPG GEGVNAHRNL VPAEGTPPGR
ARMLLAESPV HEAAVIADLL RRAHLIDGVP WSRMAVLVRS VTRHVPVLRR ALIAADVPVT
VDGDDLPLAS EPLVRSMLLL LRCAFHPERL DEEAAHNLLT SAFGEADALG LRRLGRALRQ
LELDAGGRRP AAALLAEILH DPRDLVMVDP EVRAPAERIA TLLRLVRDSI AEGANAEEVL
WRMWHHSGLA DTLLRASQAG GRHGAAADRE LDSVMALFER AARYCDRLPP GSPEGFLEDL
EAQEIPGDTL AEQAPQGETV RILTAHRSKG LEWDLVVVAG VQEGTWPDLR LRGSLLGVEQ
LLDTVGGFAE TSPAAVVSKQ LDEERRLFYV ALTRARRELV VTAVGGEDVE ERPSRFLTEL
GLGEPERLAT GYRWLSLPAL VADLRATLLD PHTDEPVRRA AAAHLARLAD AGVRGADPAE
WYALTELSDS SPLVLEGEQI RISPSQVEKF TTCELRWLLE TAAGAEKRRA ASGIGSIVHA
LARIAAENPD LPELLRRMDQ IWSDLDFGGP WYAEKQRERA EEMLQRFLDW QKENPRELVA
TEKKFRVEVG NIEISGQVDR LERDAEGRGV IVDIKTGTAV PDREISRHPQ LGVYQLALLM
AAFEHYGLVE PGGAALLQIG DRKTAKEQTQ PALADDADPE WPQRLVQKVA AGMAGARFRA
KATPSCRHCS VRASCPVQSE GDHV
//
