ID A0A0D0FB26_9SPHI Unreviewed; 768 AA.
AC A0A0D0FB26;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=TH53_00085 {ECO:0000313|EMBL:KIO79048.1};
OS Pedobacter lusitanus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1503925 {ECO:0000313|EMBL:KIO79048.1, ECO:0000313|Proteomes:UP000032049};
RN [1] {ECO:0000313|EMBL:KIO79048.1, ECO:0000313|Proteomes:UP000032049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL19 {ECO:0000313|EMBL:KIO79048.1,
RC ECO:0000313|Proteomes:UP000032049};
RA Santos T., Caetano T., Covas C., Cruz A., Mendo S.;
RT "Draft genome sequence of Pedobacter sp. NL19 isolated from sludge of an
RT effluent treatment pond in an abandoned uranium mine.";
RL Submitted (JAN-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:KIO79048.1}.
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DR EMBL; JXRA01000001; KIO79048.1; -; Genomic_DNA.
DR RefSeq; WP_041877149.1; NZ_JXRA01000001.1.
DR AlphaFoldDB; A0A0D0FB26; -.
DR STRING; 1503925.TH53_00085; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000032049; 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 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 PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF21196; PcrA_UvrD_tudor; 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 5..289
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 290..566
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 654..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 768 AA; 87201 MW; E7BE4E7BB5D68ABC CRC64;
MDYLAGLNPQ QRAAVENTQG PAMIVAGAGS GKTRVITYRV AHLIEKGVDA FNILVLTFTN
KASKDMRERI SKVVGGEAKN LWMGTFHSVF AKILRVEAEK IGYPSNFTIY DTDDSKSLIR
SILREMQLDD KLYNANFVYN RISSAKNNLV SHVEYMKSAE IQAEDISNKR PLIGSIYETY
TKRCFKAGAM DFDDLLFKTN VLLKDNPDVL NKYQQKFKYL MVDEYQDTNF SQYTIVKKLA
AAYQNICVVG DDAQSIYGFR GANIQNILNF EKDYPDLQVY KLEQNYRSTQ NIVDVANSII
ANNKNQLEKN VFSENESGDR IKVSRAFTDN EEGKLVAESI MQDRSSKGLN YNDFAILYRT
NAQSRAMEEG LRKLNIPYKI FGGLSFYQRK EIKDLIAYFR LTFNPSDEEA IKRVINYPKR
GLGDTTVDKI IVAADQHNIT MWQVVCEPQT YIAGRIANQL NDFSMLIKSF QAESKKLDAY
ETALYIAQHS GILKELHTDD SVEGRSRYEN IQELLNGIKE FAEREDIEDR SLAIFMQDVA
LLTNDDRQDD KEKDTVSLMT IHSAKGLEFK NVYVVGLEEN LFPSQMSLNS RTDLEEERRL
FYVAITRAEK KLTLTYATSR YRWGTLTNCE PSRFISEISA RFLELEVVKA PKTTLGSDSF
DGERRSWSQQ RDSFSKPKPA SSGSATQTVP SRPKTSTMLP TAHIPTPGFT PDAASAFQNG
MDVEHEKFGF GKIINLEGTL PDVKATVFFQ GLGNKQLLLK FAKLRIVK
//
