ID J6UEI1_9RHOB Unreviewed; 918 AA.
AC J6UEI1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=A33M_3127 {ECO:0000313|EMBL:EJW11514.1};
OS Rhodovulum sp. PH10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW11514.1, ECO:0000313|Proteomes:UP000002930};
RN [1] {ECO:0000313|EMBL:EJW11514.1, ECO:0000313|Proteomes:UP000002930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH10 {ECO:0000313|EMBL:EJW11514.1,
RC ECO:0000313|Proteomes:UP000002930};
RX PubMed=23105089; DOI=10.1128/JB.01695-12;
RA Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.;
RT "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic
RT Alphaproteobacterium Isolated from a Soil Sample of Mangrove of Namkhana,
RT India.";
RL J. Bacteriol. 194:6363-6363(2012).
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:EJW11514.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKZI01000058; EJW11514.1; -; Genomic_DNA.
DR AlphaFoldDB; J6UEI1; -.
DR STRING; 1187851.A33M_3127; -.
DR PATRIC; fig|1187851.3.peg.2299; -.
DR eggNOG; COG0210; Bacteria.
DR Proteomes; UP000002930; 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; 2.
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:UP000002930}.
FT DOMAIN 60..396
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 397..664
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 918 AA; 100602 MW; D262EA4A3FFFA191 CRC64;
MALPAGENQR ARNGPAGACR RTGTRMAEPH KNRFEPAPPA PRPGGIAARA SGATRAPYLE
GLNPEQREAV ETLDGAVLVL AGAGTGKTRV LTTRIAHILR LGRARAGEIL AVTFTNKAAR
EMKTRIGGMV GEVVEGMPWL GTFHSIGAKI LRRHAELVGL KPDFTILDVD DQIRLLKQLL
AAENIDEKRW PARVLATQID HWKNRGLSPD QVSAGEAGAF ANGRGKDFYT AYQARLKTLN
AADFGDLLLE TIRLFREHPE VLAQYQNRFK FILVDEYQDT NVAQYLWLRL LGQRPRDTTG
GGGLVLRDAA LRAAPQDEAG SMPVPGPRPE EPGRSPGVSK DVATKNAAPQ KNICCVGDDD
QSIYGWRGAE VDNILRFDHD FPGAKVIRLE RNYRSTAHIL AAASHLIAHN EGRLGKTLRS
EGEAGEKVVV SSAWDSEEEA RAIGEEIERL QRQGHRLNEI AILVRASFQM REIEDRFVTL
GLPYRVIGGP RFYERAEIRD AMAYLRLVNQ PADDLAFERI VNVPKRGLGD AALQCLHDFA
RAQGVPLLEA AHRIVATETL KPKPRGALRD LAAAFDRWRE QRDVLPHTEL AEIVLDESGY
TEMWQKDRSA DAAGRLENLK ELVRSMEEFE NLQGFLEHVA LVMDTDRGEE QDAASIMTLH
AAKGLEFDTV FLPGWEEGLL PHQRSLDENG RAGLEEERRL AHVGLTRARK NARISFVSNR
RIHGSWTSSL PSRFLDELPE EDVEVLEGQG AFAGYGGYSN AYGSRFDTTA AFGSGYTTPG
WRRAQQGRGA GAGAGAARDD FPQEYFNQDP AGRFENGSGS GTASSPTTRG RDATGPQNPG
AGRNGFGGAA SPRRAPLTIE GELVARSSGA PSAFSRGDRV FHQKFGNGTV RAVDGNKLTI
QFDRAGEKRV VDSFLTKV
//
