ID A0A3A8AXR8_9RHOB Unreviewed; 782 AA.
AC A0A3A8AXR8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=D6850_05480 {ECO:0000313|EMBL:RKF17288.1};
OS Roseovarius spongiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=2320272 {ECO:0000313|EMBL:RKF17288.1, ECO:0000313|Proteomes:UP000281128};
RN [1] {ECO:0000313|EMBL:RKF17288.1, ECO:0000313|Proteomes:UP000281128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-E21 {ECO:0000313|EMBL:RKF17288.1,
RC ECO:0000313|Proteomes:UP000281128};
RA Zhuang L., Luo L.;
RT "Roseovarius spongiae sp. nov., isolated from a marine sponge.";
RL Submitted (SEP-2018) 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:RKF17288.1}.
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DR EMBL; RAPE01000001; RKF17288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A8AXR8; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000281128; 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; PF21196; PcrA_UvrD_tudor; 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:UP000281128}.
FT DOMAIN 29..309
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 310..584
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 782 AA; 86917 MW; A57F3DB7D659AD91 CRC64;
MSSSSDSDAF EAASLSARAV GARGAPYLDD LNPEQRRAVE TLDGPVLMLA GAGTGKTKAL
TSRIVHLLNT GRARPNEILA VTFTNKAARE MKERVGRMLG RDIEGMPWLG TFHAVCVKLL
RRHAELAGLK SNFTILDTDD QVRLLRQLVQ AANIDDKRWP PRVLAGIIDN WKNRAWTPDK
LPASEASAFD GKGPALYAQY QARLKELNAV DFGDLLLHVV TIFQTHDDVL QQCRRWFRYI
LVDEYQDTNV AQYLWLRLLA GGHQNICCVG DDDQSIYGWR GAEVGNILRF EKDFPGAHVV
RLEQNYRSTP HILAAASGVI AGNRGRLGKE LWTETEEGEK VRLIGHWDGE EEARWIGEEI
EAMQRGTRRQ RPFGLDEMAI LVRASHQMRA FEDRFLTIGL PYRVIGGPRF YERLEIRDAM
AYFRVVTSPA DDLAFERIVN TPKRGLGDKA QQKIQITARE HGVPLVEGAR ILLEQGGLGG
KGGAELRKLI DGLARWGRLL GEDTVGHVEL AGQILDESGY TEMWQNDKTP EAPGRLENLK
ELVKALEQFE NLQGFLEHVS LIMDNEQAES GEKVSIMTLH AAKGLEFPVV FLPGWEDGLF
PSQRSMDESG EKGLEEERRL AYVGITRAEE VCTISFAGNR RVFGQWQSAL PSRFIDELPE
AHVEVLTPPG LYGGGYGAAA GGVQNSVDAR AARADVYNSP GWKRMQARAG QRPLSQPAET
RNTVIDMKAV SSHTMGERVF HQKFGYGAVV GIEGDKLEVD FEKAGTKKVV ARFISAADDI
PF
//
