ID A0A1V0GU60_9RHOB Unreviewed; 795 AA.
AC A0A1V0GU60;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=A6J80_14375 {ECO:0000313|EMBL:ARC37396.1};
OS Paracoccus yeei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=147645 {ECO:0000313|EMBL:ARC37396.1, ECO:0000313|Proteomes:UP000191257};
RN [1] {ECO:0000313|Proteomes:UP000191257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_252 {ECO:0000313|Proteomes:UP000191257};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Nadendla S.,
RA Geyer C., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (MAR-2017) 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}.
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DR EMBL; CP020442; ARC37396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0GU60; -.
DR STRING; 147645.A6J80_14375; -.
DR KEGG; pye:A6J80_14375; -.
DR eggNOG; COG0210; Bacteria.
DR Proteomes; UP000191257; Chromosome.
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:UP000191257}.
FT DOMAIN 33..318
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 319..594
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 54..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 795 AA; 88461 MW; 566654F65070F8E6 CRC64;
MNEFDDSDAF EAAAAPVPLS QRAMSARPAP YLDGLNDAQR AAVEALDGPV LLLAGAGTGK
TRALTTRIAH LLTQGRARPG QILAVTFTNK AAREMKDRIG RLLGEMVEGM PWLGTFHSVS
VKILRRHAEL VGDATLHLKP SFTILDTDDQ IRLLKQLIAA ENIDEKRWPA RQLAGLIDGW
KNRCITPARL PRGEERAFDG WGGKLYAAYQ RRLLELNAVD FGDLLMHCVT IFQAHPDVLR
QWQDRFRYIL VDEYQDTNVA QYMWLRLLAQ AHRNICCVGD DDQSIYGWRG AEVGNILRFE
ADFPGAQVIR LEQNYRSTPH ILAAASGLIA ANKGRLGKTL WTEAQGGEPV RLIGHWDSEA
EARWIGEEIE TFQGGHRHSI GKRSLNDIAI LVRASHQMRA FEDRFMTIGL PYRVIGGPRF
YERQEVRDAM AYFRLAVSPT DDLAFERIVN VPKRGLGDKA VQTIQREARE RGLSLLEGAA
SVVATQGIGG KGGAALRNFV QGMGRWHADV LDDRVNHVEL AERILDESGY TAMWQNDKSP
DAPGRLDNLK ELIKALEEFE NLQGFLEHVA LVMDNDTGEQ AEQVSIMTLH AAKGLEYPIV
FLPGWEDGLF PSQRSMDESG MKGLEEERRL AYVGITRAEE LATITFAGNR RMYGQWQSSL
PSRFIDELPE EHVEVLTPPG LYGGGYGAAA QPFAASAMHE RAFKADVYNS PGWKRMQQRS
SERTQPVHRT PVVIDAEPAA RYAVGDRVFH QKFGNGTIRG IAEDTLTVEF PTGFKTIKAS
YVQPASGAST GDVPF
//
