ID A0A0Q6A4B0_9BRAD Unreviewed; 855 AA.
AC A0A0Q6A4B0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN ORFNames=ASG57_03790 {ECO:0000313|EMBL:KQT21259.1};
OS Bradyrhizobium sp. Leaf396.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT21259.1, ECO:0000313|Proteomes:UP000051536};
RN [1] {ECO:0000313|EMBL:KQT21259.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT21259.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT21259.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT21259.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQT21259.1}.
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DR EMBL; LMQJ01000012; KQT21259.1; -; Genomic_DNA.
DR RefSeq; WP_057196588.1; NZ_LMQJ01000012.1.
DR AlphaFoldDB; A0A0Q6A4B0; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000051536; 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 Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; PF00580; UvrD-helicase; 2.
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 37..366
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 367..634
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 274..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 855 AA; 95120 MW; F5FDA8C2F6F72FFB CRC64;
MIRMTEPSKI TAVPDHQPAA GGIAARARAS VGPKYLSGLN PEQREAVETL DGPVLVLAGA
GTGKTRVLTT RIAHILSQGR ARPAEILSVT FTNKAAREMK HRLGQMLGHA VEGMPWLGTF
HSIGGRILRI HAELAQLKSN FTVLDVDDQV RLLKQLLQAE NIDDKRWPAR MLAGLIDGWK
NRGLMPSQVP SGEAAMFANG KGGKLYASYQ ERLKILNAAD FGDLLLENIR IFREHPDILR
QYQQRFKFIL VDEYQDTNVA QYLWLRLLSQ APSSSSSLPG LTRQSIASSQ DGSPGLDAAR
RPDDERHDAR LVSASEKGPT RNICCVGDDD QSIYGWRGAE VDNILRFEHD FPGAKVIRLE
RNYRSTGHIL AAASHLIAHN EGRLGKTLRT EDQDGEKVTV TGSWDSEEEA RGIGEEIEQL
QRQGEKLNEI AILVRASYQM REFEDRFVTL GLSYRVIGGP RFYERAEIRD ALAYLRVINS
PADDLAFERI VNTPKRGLGD ATVQMLHDHA RKRRIPLFEA ARAVVETDEL KPKARGSLRD
LIAQFDRWRA QREVTAHTDL AQIVLDESGY TEMWQKDRSA DAAGRLENLK ELVRSMEEFE
NLQGFLEHIS LVMDREGGAE DDAVSLMTLH SAKGLEFDNV FLPGWEEGLF PSQRTLDEQG
RAGLEEERRL GHVGLTRARR RAKIYFATNR RIHGTWSTTI PSRFLDELPA ANVEITESKG
GSGWGGSGGY GASRFDDMEA FGSSYSTPGW QRAQANRNRG GGRSGFEEET ATFSSASSSG
PDFGSFSSRR RGPMTIEGEL VAKSTGTTSE FALDDRVFHQ KFGYGRVTRI DGNKLTIAFD
KAGEKKVVDS FVQRA
//
