ID A0A0B4BI31_9RHOB Unreviewed; 809 AA.
AC A0A0B4BI31;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=RA29_11605 {ECO:0000313|EMBL:KIC48409.1};
OS Tateyamaria sp. ANG-S1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tateyamaria.
OX NCBI_TaxID=1577905 {ECO:0000313|EMBL:KIC48409.1, ECO:0000313|Proteomes:UP000031171};
RN [1] {ECO:0000313|Proteomes:UP000031171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S1 {ECO:0000313|Proteomes:UP000031171};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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:KIC48409.1}.
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DR EMBL; JWLL01000006; KIC48409.1; -; Genomic_DNA.
DR RefSeq; WP_039686179.1; NZ_JWLL01000006.1.
DR AlphaFoldDB; A0A0B4BI31; -.
DR STRING; 1577905.RA29_11605; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000031171; 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; 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:UP000031171}.
FT DOMAIN 29..309
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 310..609
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 809 AA; 89826 MW; 66FCD3381EE54E5D CRC64;
MSSFDEFDAF EGASLSARAM QARPQPYLDG LNPAQREAVE TLDGPVLMLA GAGTGKTRAL
TARIVHLLNT GRARPNEILA VTFTNKAARE MKNRVGQMLG QQIEGMPWLG TFHAICVKLL
RRHAELVGLK TNFTILDTDD QIRLLKQLIS AANIDDKRWP ARQLASIIDG WKNRALTPDK
VPAADAGAYN HKGVDLYAQY QARLKELNAC DFGDLLLHMV TIFQTHSDVL AQYQRWFAFI
LVDEYQDTNV AQYLWLRLLA QGHKNICCVG DDDQSIYGWR GAEVGNILRF EKDFPGAHVV
RLEQNYRSTP HILAAASGVI DGNENRLGKT LWTDKNDGEK VRLIGHWDGE EEARWIGEEI
EASQKGTRGV RPMSLEDIAI LVRASHQMRA FEDRFLTIGL PYRVIGGPRF YERMEIRDAM
AYLRVVVSPD DDLAFERIVN TPKRGLGDKA QQTIQITARA NGVPLVEGAR LAVEQGLIKG
KGGNELRALV DGIARWHSKL RGPRIEVAED DSVLDDGAGP LRVEYGPPPV SHIELAEIIL
DESGYTAHWQ NDKTPEAPGR LENLKELVKA LESFENLQGF LEHVSLVMDN ASEDDEAKVS
IMTLHAAKGL EFPQVFLPGW EDGLFPSQRS MDESGVKGLE EERRLAYVGI TRAEEVCTIS
FASNRRMFGQ WQSSMPSRFV DELPEDHVDV LTPPGLYGGG FGAAAPNMGA ESRLHQAAAD
ANVYNSPGWK RLQARAGERP LSQPQESRNT VIDLNAVSAF TVGERVFHQK FGYGAIVGIE
GDKLEVDFEK AGLKKVVSRF VSGTDDIPF
//
