ID A0A099GB58_9RHOB Unreviewed; 812 AA.
AC A0A099GB58;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=IX56_16195 {ECO:0000313|EMBL:KGJ19418.1};
OS Paracoccus sanguinis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1545044 {ECO:0000313|EMBL:KGJ19418.1, ECO:0000313|Proteomes:UP000029858};
RN [1] {ECO:0000313|EMBL:KGJ19418.1, ECO:0000313|Proteomes:UP000029858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5503 {ECO:0000313|EMBL:KGJ19418.1,
RC ECO:0000313|Proteomes:UP000029858};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ19418.1, ECO:0000313|Proteomes:UP000029858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5503 {ECO:0000313|EMBL:KGJ19418.1,
RC ECO:0000313|Proteomes:UP000029858};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) 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:KGJ19418.1}.
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DR EMBL; JRKQ01000135; KGJ19418.1; -; Genomic_DNA.
DR RefSeq; WP_036712204.1; NZ_JRKQ01000135.1.
DR AlphaFoldDB; A0A099GB58; -.
DR Proteomes; UP000029858; 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:UP000029858}.
FT DOMAIN 41..326
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 327..602
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 62..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 812 AA; 89140 MW; B0959DCBF357FA2D CRC64;
MSQFDDADAF EAAAARAPAP RPSLSARAMG IGAQAAPAYL DGLNPAQRAA VEALDGPVLL
LAGAGTGKTR ALTTRIAHLL TQGRATPGRI LAVTFSNKAA REMKARIAKL LGETIEGMPW
LGTFHSVSVK ILRRHAELVG VGDLHLKSSF TILDTDDQLR LLKQLIAAEN IDEKRWPARM
LAGLIDDWKN RALTPGRVPA SESHAYDGKG VALYTQYQRR LIELNATDFG DLLLHCVTIF
QAHPDVLAQW QDRFRYILVD EYQDTNVAQY LWLRLLAAGH RNICCVGDDD QSIYGWRGAE
VGNILRFETD FPGAQVIRLE QNYRSTPQIL AAASGLIAAN KGRLGKTLWT DAEPGEKVRL
IGHWDSEAEA RWIGEEIEAF HGGHRHSVGR RSLNDIAILV RAAHQMRAFE DRFMTIGLPY
RVIGGPRFYE RLEIRDAMAY FRLAVSPTDD LAFERIANTP KRGLGDKGLQ TIQRVARAEG
LSLLQGAAAA VASGDLGGKA AAQMRLFTEA MGRFHADALD SRVSHVELAE RILDETGYTA
MWQADKSPDA PGRLDNLKEL VKALEEFENL QGFLEHVALV MDAAEGEQAE EVSIMTLHAA
KGLEYPIVFL PGWEDGLFPS QRSMDEQGLK GLEEERRLAY VGLTRAEDLA TISFAGNRRM
YGQWQSSLSS RFIDELPEDQ IEVLTPPGLY GGGYGAAAQG FGQPFTPSAM HDRASRADVY
NSPGWKRMQE RAAARSAPTH RTPIVIDATP GERFAVGERV FHPKFGTGTV QGIAEDTLTV
EFPAGFKTIK AAYVQPAAEA ARDITPSDDV PF
//
