ID Q1GX41_SPHAL Unreviewed; 1112 AA.
AC Q1GX41;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=Sala_0055 {ECO:0000313|EMBL:ABF51781.1};
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655 {ECO:0000313|EMBL:ABF51781.1, ECO:0000313|Proteomes:UP000006578};
RN [1] {ECO:0000313|EMBL:ABF51781.1, ECO:0000313|Proteomes:UP000006578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256
RC {ECO:0000313|Proteomes:UP000006578};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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 -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; CP000356; ABF51781.1; -; Genomic_DNA.
DR RefSeq; WP_011540396.1; NC_008048.1.
DR AlphaFoldDB; Q1GX41; -.
DR STRING; 317655.Sala_0055; -.
DR KEGG; sal:Sala_0055; -.
DR eggNOG; COG0210; Bacteria.
DR eggNOG; COG2856; Bacteria.
DR HOGENOM; CLU_008930_0_0_5; -.
DR Proteomes; UP000006578; Chromosome.
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; 1.10.10.2910; -; 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; IPR010359; IrrE_HExxH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF55; DNA HELICASE; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF06114; Peptidase_M78; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
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:UP000006578}.
FT DOMAIN 188..487
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 488..769
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 209..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1112 AA; 119274 MW; BF36ADF2691587FB CRC64;
MAAFDLARLH ARALREAKIA GRATGPAAVK SAAAAEGFVI KPVPPGDPVI GTSDAKLLRE
WCSIYVRNDV SDAEAAAFVA HELGHLKLHR PQDNCTGPNP DAGTSRALSR VEAYGPRERR
ELQANVFARE LLLPRALARQ LFLVERLGAG SIAQLLELPV PLVRRQLFDS LLGPDASAPT
VNAQKPKFGR DDSQEAAAGF ADPALLLEAG PGSGKTRTLV KRIEHLLDFD EAVPNEILAL
TFSNKAAGEL ADRIATARPD AAADMWIGTF HAFGLDLIRR YYELLDLPSN VQLIDKAQAI
ELLEDQLPLM GLNHYHDLRN PDQGLVKILS AISRAKDELV THAEFTRRAR EALAAAVSAE
QVEVAERACE AARVYEIYAD ALGKAGAVDF GDLVMLPTLL MMRNDCVRAQ VAQRHSMVLV
DEYQDVNRAS ARLLMELYRE GARLWVVGDA RQSLYRWRGA SSANMAQFER DFSGGKRLPL
DRNYRSTEHI VGLGRGFARD MRAGKNGLAY NAKSAREEPG SATRLLVGLD DRCEGELLAA
EITSLKQAGV PLSQQAVLAP TNNRLDIVAG ILAEHGIATT HLGSFFEREE VRDLLSVIAL
LAEANGGALV RVAALREIGV GASDIGVIVR AAQAARVPLL SLLATASTLT GMSPTGGEAL
EQLGLQMAGL DQFTPAFEVA ASWLLDRSDY LRDLAVAPDA SGSLSRAALL ALLGFLDQRE
LGGQPLTPAR ALKRMRSTVL LADDRDLRDA TLGADADAVR LMTIHGAKGL EFPAVHVVGL
HDQCLPGAFR RDDSPLPPGL VEPETREGHL EEEECLFFVA ISRAEDHLRL YHSELANVRG
RKPSPFLGRL GALERRHLPA AATAAGAAGS PLSPISTDRI NLFDVRDFDS CPLRIAYRRF
FGVEGRRHET PYLKTSGVLY ALVDRITEVS GPGVEERLQV LLGEIWAIRG PAEHGLAADY
LAHAAGRAAA LGRLMSGFDS PGYSQIELPI NGGLLTVAAP LVRSTAAGTE IRFLEAGRVR
SKTGNDLTAG LLLAAARHTF GPNVSVTIGH VTDGATVPVK RQDDKAAGDV EAAAAILAAI
NKGALPAKPA MRVCGRCPHF VACPAVGRAE TA
//