ID A0A0N8GHA0_9BACI Unreviewed; 740 AA.
AC A0A0N8GHA0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=AM506_05495 {ECO:0000313|EMBL:KPL60714.1};
OS Rossellomorea vietnamensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=218284 {ECO:0000313|EMBL:KPL60714.1, ECO:0000313|Proteomes:UP000050398};
RN [1] {ECO:0000313|EMBL:KPL60714.1, ECO:0000313|Proteomes:UP000050398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-SED5 {ECO:0000313|EMBL:KPL60714.1,
RC ECO:0000313|Proteomes:UP000050398};
RA Lee R.D., Jospin G., Lang J.M., Coil D.A., Eisen J.A.;
RT "Draft Genome Sequence of Bacillus vietnamensis UCD-SED5.";
RL Submitted (AUG-2015) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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:KPL60714.1}.
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DR EMBL; LIXZ01000003; KPL60714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8GHA0; -.
DR PATRIC; fig|218284.4.peg.2216; -.
DR eggNOG; COG0210; Bacteria.
DR Proteomes; UP000050398; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 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; IPR014016; UvrD-like_ATP-bd.
DR InterPro; IPR025916; YdjO.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR Pfam; PF14169; YdjO; 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000050398}.
FT DOMAIN 44..315
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 316..589
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 740 AA; 85676 MW; 83984A3070AF0871 CRC64;
MYPYEADKKE IPVAPLHKGE TTKQLISSRD EDAFFFRTME EAGIHLNAAQ IEAVRHVKGP
CLTLAGAGTG KTTVLVCRAG YLMAVKNIQP RNILLVTFTK KASEEMKQRI ARLPGAEHGG
QVHASTFHAL FLYLLRSRHY TQEVIGNERY KQIILKQIQR EMNIYDPYDS ETLLAKLSHY
KLNQKDIREL PEKSKSEKEV RSILLKYEEW KRMNHKMDFD DILTEAYQLL LGNPNLLTSL
QHRFQYVMVD EFQDTNLVQY ELIKLIAAHR NLFVVGDDDQ TIYTFNGARN EFILDFDEEF
PDAKVVTLKE NYRSDAYIIG LGNEVIGRND HRRKKELIAT KVEGQKPLYS RPATADEEAV
WITEEIQRLL DEGYGYGDMT ILHRTMSSGR AVFEQLLLKE IPFTPYNQKD SLFYDNWTVK
PVVDYLRLSI VPRNFSAMES LLPTLFIRRD RGMAHILEEE QKERKKYPLI HLTTLSGLKP
FQVKNVKERM KFLKEIGDQS PESAIKRIRK EFYHQYIDAQ ESHVVTEQKE LIKEMLDELE
GSAKRFDTIS SFITFIDEMK AKYEEIYSNQ RRNKDTNSVS LMTIHRSKGL EFPVVFLIGA
IEGNLPHSSA LNANKLEDKV YKDPNQKEKM TGAVEEERRL AYVAITRAKE KLFISSPAYY
QGEQRKSSRF ISDLFKQTPH AEPRPSKKAR VGKVSKILAW VCTSSECIAW QRPETHEDTE
SKVCPLCSSP MKLGEKDIIE
//
