ID A0A0J9E601_9RHOB Unreviewed; 784 AA.
AC A0A0J9E601;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=AIOL_003056 {ECO:0000313|EMBL:KMW58086.1};
OS Candidatus Rhodobacter lobularis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW58086.1, ECO:0000313|Proteomes:UP000037178};
RN [1] {ECO:0000313|EMBL:KMW58086.1, ECO:0000313|Proteomes:UP000037178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGS {ECO:0000313|EMBL:KMW58086.1};
RA Jourda C., Santini S., Claverie J.-M.;
RT "Draft genome sequence of an Alphaproteobacteria species associated to the
RT Mediterranean sponge Oscarella lobularis.";
RL Submitted (JUN-2015) 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:KMW58086.1}.
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DR EMBL; LFTY01000002; KMW58086.1; -; Genomic_DNA.
DR RefSeq; WP_049643732.1; NZ_LFTY01000002.1.
DR AlphaFoldDB; A0A0J9E601; -.
DR STRING; 1675527.AIOL_003056; -.
DR PATRIC; fig|1675527.3.peg.3197; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000037178; 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:UP000037178}.
FT DOMAIN 32..312
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 313..587
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 53..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 784 AA; 87704 MW; FA3C97EE7D5FBC2C CRC64;
MSHFDESDAF EEAAGLSLSA RAMAARPAPY LDGLNAPQRE AVEALNGPVL MLAGAGTGKT
KALTTRIAHL LNTGTARPNE ILAVTFTNKA AREMKNRVWK LLGQTVEGMP WLGTFHAIGV
KLLRRHAELV GLKSNFTILD TDDTVRLLKQ LILAANIDEK RWPPRMLSSI IDSWKNRAWT
PDKVPAEEAN AFNQRGIELY HLYQRRLLEL NAVDFGDLLL HVLTIFQKHE DVLAQYQRWF
RYILVDEYQD TNVAQYMWLR LLAQGHKNIC CVGDDDQSIY GWRGAEVGNI LRFEKDFPGA
TVIRLEQNYR STPHILGAAS GVIEGNKGRL GKTLFTELDE GEKVRLIGHW DGEEEARWIG
EEIEAMQGGT RGLDPVDLDG MAILVRASHQ MRAFEDRFLT IGLPYRVIGG PRFYERMEIR
DAMAYFRVAC SPDDDLAFER IVNTPKRGAG DKAQQTMQRI ARGNGVSLLE GARIAVAQGE
LSGKAKGEIG KLVDFFDRWH VHALDKSYNH VELAEIMLDE SGYTEMWQLD KTPEAAGRLE
NLKELVKALD QFENLQGFLE HVALIMDNET EGEGSKVSIM TLHAAKGLEF PSVFLPGWED
GLFPSQRSMD ESGVKGLEEE RRLAYVGITR AEALCTISFA ANRRTYGQWQ SAMPSRFIDE
LPEDHVDVLT PPGLYGGGYG AAAPTVEARA AEANVYNSPG WKRLQQRQSR RPMSQPQESG
NTVIDLDAIS AFTQGDRVFH QKFGYGYVMG IEGDKLDIEF EKAGAKKVIS KFIVSAERAD
DVPF
//