ID A0A244EGE6_9BURK Unreviewed; 787 AA.
AC A0A244EGE6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=A8M77_05650 {ECO:0000313|EMBL:OUM03540.1};
OS Variovorax sp. JS1663.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1851577 {ECO:0000313|EMBL:OUM03540.1, ECO:0000313|Proteomes:UP000195166};
RN [1] {ECO:0000313|EMBL:OUM03540.1, ECO:0000313|Proteomes:UP000195166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1663 {ECO:0000313|EMBL:OUM03540.1};
RX PubMed=28526789;
RA Mahan K.M., Zheng H., Fida T.T., Parry R.J., Graham D.E., Spain J.C.;
RT "A novel, iron-dependent enzyme that catalyzes the initial step in the
RT biodegradation of N-nitroglycine by Variovorax sp. strain JS1663.";
RL Appl. Environ. Microbiol. 83:0-0(2017).
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:OUM03540.1}.
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DR EMBL; LYMK01000004; OUM03540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A244EGE6; -.
DR OrthoDB; 5905204at2; -.
DR Proteomes; UP000195166; 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}; Reference proteome {ECO:0000313|Proteomes:UP000195166}.
FT DOMAIN 15..301
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 302..610
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 787 AA; 87732 MW; 9FD2E498171A84D0 CRC64;
MLTPPAASAE SPLLHNLNPE QRAAVTLPAG NSLILAGAGS GKTRVLTTRI AWLLQTGQVS
AGGVLAVTFT NKAAKEMMAR LGAMLPVNVR GMWIGTFHGL CNRFLRAHWK LAGLPSTFQI
LDTQDQLSAI KRLMKQFNVD EERFPAKQTQ WFISGAKEDG LRPRDIEVRS EDDRKKVELY
QLYEEQCQRE GVVDFGELML RSYELLRDND PVREHYQRRF RHILIDEFQD TNRLQYAWLK
MLAGETVDGR FVPGDNSVLA VGDDDQSIYA FRGARVGNMA DFVREFEVAH QIKLEQNYRS
YSNILDSANT LISHNKKRLG KNLRTDQGPG EPVRVYESVS DFAEAQWMVE EMRQLVRDGI
ERKEMAVLYR SNAQSRVIET ALFNAAVPYR VYGGLRFFER AEIKHALAYL RLLENKDDDT
SFLRIVNFPP RGIGARSIEQ LQDAAGAARG SLHDAVSAVG GKAGANLSAF VAKIDVLREQ
TQGLSLREII ELVLQHSGLI EHYRNERDGA DRIENLEELV NAAESFVTQE GFGRDAVAMP
VDELRQSPAS QGLDPNLPIV DEPLAPDAET GETMSPLAAF LTHAALESGD NQAQAGQDAV
QLMTVHAAKG LEFDCVFITG MEEGLFPHEN SMSDYESLEE ERRLMYVAIT RARQRLYLSH
SQTRMLHGQT RYNVKSRFFE ELPESALKWL TPKNQGFTPS AFGYGGGYAS TRGSYGSKEV
FASPPVPPQK AAPSHGLRSG MQVFHNKFGE GTVMALEGSG DDARAQINFP RHGVKWLALS
VAKLTPV
//
