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Database: UniProt
Entry: A0A1I5Q1B9_9SPHN
LinkDB: A0A1I5Q1B9_9SPHN
Original site: A0A1I5Q1B9_9SPHN 
ID   A0A1I5Q1B9_9SPHN        Unreviewed;       770 AA.
AC   A0A1I5Q1B9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=SAMN04488060_2693 {ECO:0000313|EMBL:SFP40015.1};
OS   Qipengyuania nanhaisediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Qipengyuania.
OX   NCBI_TaxID=604088 {ECO:0000313|EMBL:SFP40015.1, ECO:0000313|Proteomes:UP000199331};
RN   [1] {ECO:0000313|Proteomes:UP000199331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7715 {ECO:0000313|Proteomes:UP000199331};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FOWZ01000005; SFP40015.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5Q1B9; -.
DR   STRING; 604088.SAMN04488060_2693; -.
DR   OrthoDB; 9806690at2; -.
DR   Proteomes; UP000199331; 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; 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}.
FT   DOMAIN          21..302
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          303..570
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   770 AA;  87007 MW;  81ED20CE95779E73 CRC64;
     MTTPPSPQDL TEDRDVPAYA AMLNEPQRQA VLTTEGPVLM LAGAGTGKTA ALTARLAHLI
     ATRRAWPSEI LCVTFTNKAA REMRERVGRH IGDAVEGMPW LGTFHSIGAK MLRRHAELVG
     LKSNYTILDT DDQLRLLKQL IRDQELDEKR WPARQLAALI DRWKNRGLNP GDLDAVENEA
     YANGRGTQFY KLYQDRLKAL NACDFGDLLL HMLNIFRQHH DVLAQYQKRF KYILVDEYQD
     TNQVQYLWLR LLAQERKNIC VVGDDDQSIY SWRGAEVANI LKFEKDFPGA AVVKLEQNYR
     STPQILAAAS GLINANSERL GKTLWTELPS GEKVRVVGVW DGPEEARRVG EAIERLESEG
     APLDEIAILV RAQYQTREFE DRFIQIGLNY RIVGGFRFYE RAEIRDMLAY LRVISQPADD
     LAFERIYNQP KRGLGAKTLE VMQRHARRTQ APLAAASLDL AETDELPARA RNTLVGLLSQ
     FVHWREQSEK VTPSELLRIV VAESGYEEML QKDRSAESAG RLENLTELAR AMEDYETLGD
     FLEHVGLVMD NDRANDGEKI TIMTMHAAKG LEFDHVFLPG WEEGVFPSQR AIDEGGLASL
     EEERRLAYVA ITRAKRRCTI YHAANRRIYG QWTSSIPSRF IEELPDDYVE SETTMSGGAS
     LWRANWTENE DPFAHVSSNR PGRSSVRGPG WQRALASGYD TTPKRLAEPG KSAASFAAKP
     RTDVAVGARV FHDKFGYGYV MDQEGNKLTI EFETSGEKRV LDSFVKPVSD
//
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