ID A0A1X9YBW9_9SPHN Unreviewed; 765 AA.
AC A0A1X9YBW9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=KC8_03240 {ECO:0000313|EMBL:ARS26305.1};
OS Sphingomonas sp. KC8.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1030157 {ECO:0000313|EMBL:ARS26305.1, ECO:0000313|Proteomes:UP000194475};
RN [1] {ECO:0000313|EMBL:ARS26305.1, ECO:0000313|Proteomes:UP000194475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KC8 {ECO:0000313|EMBL:ARS26305.1};
RA Chen Y.-L., Yu C.-P., Hu A., Lee T.-H., Yang F.-C., Ismail W., Wang P.-H.,
RA Wang C.-H., Goh K.-S., Shih C.-J., Chiang Y.-R.;
RT "Bacteria use an extradiol dioxygenase-mediated pathway to degrade natural
RT estrogens in aquatic ecosystems.";
RL Submitted (JUN-2016) 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}.
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DR EMBL; CP016306; ARS26305.1; -; Genomic_DNA.
DR RefSeq; WP_050805382.1; NZ_CP016306.1.
DR AlphaFoldDB; A0A1X9YBW9; -.
DR STRING; 1030157.GCA_000214335_02423; -.
DR KEGG; spkc:KC8_03240; -.
DR eggNOG; COG0210; Bacteria.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000194475; 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 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; 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:UP000194475}.
FT DOMAIN 23..304
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 305..572
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 765 AA; 85342 MW; C336DC7AB0967201 CRC64;
MFPNCSRVTQ PLPTTASEPA YLTGLNPPQR EAVLTTEGPV LVLAGAGTGK TAALTARLAH
LVATRRAWPS EILAVTFTNK AAREMKERVG RMLGDAVEGL PWLGTFHAIA AKMLRRHAEL
VGLQANFTIL DTDDQLRLMK QLIVAADLDE KRWTPRMLGG LIDRWKNRGW TPADVDAGES
EAFANGRGQE FYQAYQDRLR AVNACDFGDL LLHMLTILKK HRDVLESYQD RFRYVMVDEY
QDTNSAQYLW LRLIAQTRKN ICCVGDDDQS IYSWRGAEVA NILRFEQDFP GAKIIRLEQN
YRSTPHILGA AGGVIAHNGG RLGKELWTEM DAGDKVRVIG VWDGPEEARR IGDEIEAHQR
HGGALDEVAI LVRAQFQTRE FEDRFIAIGL PYRIVGGFRF YERAEIRDAL AYLRVIHQPA
DDLAFERIVN TPKRGLGDKA VAKVHQLARA QGIPLTLAAT RVLDTDELTP QARRAMGNLI
GDIMRWRDRL NDLPHAELTR LMLDESGYTG MLQAERTADA AGRLENLVEL TRAMEEYETL
PAFLEHVSLV MDNDADRDTA KVTVMTIHAA KGLEFDTVFL PGWEEGVFPS QRAIDEGGLA
SLEEERRLAY VAITRARRRA TILHAANRRI YGQWTSSIPS RFVGELPPEH VDGETTMSGG
ESLWRAQWAE QSDPFAHGGR ATGRGPGWQR AAAAGYDPAP KRVAETRAST ATFAARPRSD
IAIGQRVFHT KFGYGAVAEI DGNKLEIDFE LSGRKRVLDS FISLA
//
