ID C5T270_ACIDE Unreviewed; 821 AA.
AC C5T270;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=AcdelDRAFT_1000 {ECO:0000313|EMBL:EER61411.1};
OS Acidovorax delafieldii 2AN.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER61411.1, ECO:0000313|Proteomes:UP000003856};
RN [1] {ECO:0000313|EMBL:EER61411.1, ECO:0000313|Proteomes:UP000003856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2AN {ECO:0000313|EMBL:EER61411.1,
RC ECO:0000313|Proteomes:UP000003856};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA Picardal F., Roden E., Emerson D.;
RT "The draft genome of Acidovorax delafieldii 2AN.";
RL Submitted (MAY-2009) 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:EER61411.1}.
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DR EMBL; ACQT01000017; EER61411.1; -; Genomic_DNA.
DR RefSeq; WP_005794019.1; NZ_ACQT01000017.1.
DR AlphaFoldDB; C5T270; -.
DR PATRIC; fig|573060.9.peg.4171; -.
DR OrthoDB; 5905204at2; -.
DR Proteomes; UP000003856; 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; 2.
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; 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:UP000003856}.
FT DOMAIN 30..315
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 316..635
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 821 AA; 90101 MW; A618ED7025AD10B4 CRC64;
MFPQDPFSGV PDPLVPPHPG AASAASPLLA NLNDEQLAAV TLPAGHALIL AGAGSGKTRV
LTTRIAWLLQ NGYATPGGIL AVTFTNKAAK EMVARLSAML PVNVRGMWIG TFHGLCNRLL
RAHHKAAGLP QAFQILDTQD QLSAIKRLCK QHNVDDERFP PKQLAYFIAN CKEEGMRPGD
VPTHDSDSRK KVEIYQLYEE QCQREGVVDF GELMLRSYEL LRDNDPIREH YQRRFQHILV
DEFQDTNKLQ YAWLKQLAGN DVGGRYEARG SVIAVGDDDQ SIYAFRGARV GNMTDFVREF
DVQRQIKLEQ NYRSYSNILD SANALISHNS RRLGKNLRTT QGAGEPVRVY EASSDLAEAQ
WMLDEIKQLV RNDGFERKEI AVLYRSNAQS RVIESALFNA SVPYRVYGGL RFFERAEIKH
ALAYLRLLEN PHDDTSFTRV VNFPPRGIGA RSIEVLQDAA RAAGCSLHDA VSAVPGKAGA
NLGAFVAMVD VLREQTQGLN LRGIIEQMLE STGLVEHFRT EKEGADRIEN LQELVNAAES
FVTQEGFGRD AVALPLDEHG TPLTQSAVSQ GIDPHAPLLD EPLKPAVPGI VDADTGETLS
PLAAFLTHAA LEAGDNQAQA GQDAVQLMTV HASKGLEFDC VFIGGMEEGL FPHDNSSSDR
DGLEEERRLM YVAITRARKR LYLSHSQTRM LHGQTRYNAK SRFFDELPEG ALKWITPKQQ
GFGSFMPGSA PYSGAGGAYG ASARGQFGFK SETFASPPVP PQKAAPSHGL RAGIAVFHTK
FGEGKVLAIE GTGDDARAQV NFPRHGTKWL ALSVAKLTVV E
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