ID A0A1T1AQ26_RHOFE Unreviewed; 809 AA.
AC A0A1T1AQ26;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=RF819_05255 {ECO:0000313|EMBL:OOV06211.1};
OS Rhodoferax fermentans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=28066 {ECO:0000313|EMBL:OOV06211.1, ECO:0000313|Proteomes:UP000190750};
RN [1] {ECO:0000313|EMBL:OOV06211.1, ECO:0000313|Proteomes:UP000190750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 7819 {ECO:0000313|EMBL:OOV06211.1,
RC ECO:0000313|Proteomes:UP000190750};
RA Kim Y.J., Farh M.E.-A., Yang D.-C.;
RT "Genome sequencing of Rhodoferax fermentans JCM 7819.";
RL Submitted (JAN-2017) 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:OOV06211.1}.
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DR EMBL; MTJN01000002; OOV06211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T1AQ26; -.
DR STRING; 28066.RF819_05255; -.
DR OrthoDB; 5905204at2; -.
DR Proteomes; UP000190750; 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:UP000190750}.
FT DOMAIN 17..306
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 307..618
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 809 AA; 89175 MW; 12A64DF8839F8926 CRC64;
MFSSPPSEPV SNSSLLHNLN PEQLAAVTLP AEHALILAGA GSGKTRVLTT RIAWLLQTGE
VSPGGILAVT FTNKAAKEMM TRLGAMLPVN VRGMWIGTFH GLCNRFLRAH YKLANLPQAF
QILDTQDQLS SIKRLYKQFN IDDERFPAKQ MQWFIGGCKE DGLRPNAVVA RDDETRKKIE
IYQLYEDQCQ REGVVDFGEL MLRSYELLRD NDPIREHYQR RFRHILIDEF QDTNKLQYAW
VKMLAGTGAH SSVDGAFQPT GCVLAVGDDD QSIYAFRGAR VGNMADFVRE FGVRHQIKLE
ENYRSGSNIL DSANALISHN SKRLGKNLRT SQGPGEPVRV FEATSDFAEA QWMVDEMKQL
VREGHERKEI AVLYRSNAQS RVIETALFNA SMPYKVYGGL RFFERAEIKN ALAYLRLLEN
PRDDTSFMRA VNFPPRGIGA RSLEQLQDLA RASGCALSDA VSGLSGKAGT NIGAFLAGID
VLREQTQGMS LRDTIVATLE HSNLLTHYKA DREGADRLEN LAELVNAAES FVSIEGFGRD
AVALPVDELG QALTQSPASQ GLDLNQPVLD IPAPDAETGE TLSPLAAFLT HAALEAGDNQ
AQAGQDAIQL MTVHASKGLE FDAVFITGME EGLFPHENSM NDRDGLEEER RLMYVAITRA
RKRLYLSHSQ TRMLHGQTRY NLKSRFFEEL PEEALKWITP KQSGFGGGSG FGGGASYSGA
GGPYSERARG QFGTDYTKYN TAATAAPVPA QKETPGGLKV KQKVFHPKFG EGTVTALEGT
GEDARAQINF PRHGVKWLAL SVAKLTPVP
//
