ID A0A3Q0FE35_VIGRR Unreviewed; 870 AA.
AC A0A3Q0FE35;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN Name=LOC106772714 {ECO:0000313|RefSeq:XP_022640889.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_022640889.1};
RN [1] {ECO:0000313|RefSeq:XP_022640889.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_022640889.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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=3.6.4.12;
CC Evidence={ECO:0000256|RuleBase:RU364117};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
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DR RefSeq; XP_022640889.1; XM_022785168.1.
DR AlphaFoldDB; A0A3Q0FE35; -.
DR STRING; 3916.A0A3Q0FE35; -.
DR OrthoDB; 1207998at2759; -.
DR Proteomes; UP000087766; Chromosome 8.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF69; ATP-DEPENDENT DNA HELICASE Q-LIKE SIM; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50030; UBA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364117};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364117};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364117};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766}.
FT DOMAIN 5..51
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 156..332
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 487..645
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 386..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..855
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 99381 MW; 794F731A0CACF97D CRC64;
MGRNAMDGND TCWDKVIAEM IEMGFEHSSI VEAIKVVGPS VPSAVEHILN STTEEPSTTH
TSNSHARNGN ALKKRPLRKC LVRQSNIFDH FRSNDDVEEH KKEIPQLGIK PNPIVLSEPF
EAQDLDVESD WEQKTSNLMK KHFGFSSLKS FQKEAISAWV VHKDCLVLAA TGSGKSLCFQ
IPALFSGKVV VVISPLISLM HDQCLKLTRH GISACFLGSG QPDNTVEQKA MRGLYSIVYI
CPETVLRLIQ PLQKLAESRG IALFAIDEVH CVSKWGHDFR PDYRRLSVLR ENFSTSKLKS
LKFDIPLMAL TATATKRVRE DILKSLQMSK ETKVCLTSFF RPNLRFMVKH SRVSQASYAK
DFHELIRVYG RKKNIDEKEK VFISDDSDQI SNSSDASSIS DTDSVSPDDM DDNQDDYAYR
DINIMHSGNS DDFLTGKELS IEFLENDIDA FQSMDNLDVA RGDFCVLPHK ELELSKNTNI
PKKPEGRVKI LNEPLEQGPT IIYVPTRKET LRIAKYLCKF GLKAAAYNAG LPKLHLRKVH
KEFHENGLEV IVATIAFGMG IDKSNVRRII HYGWPQSLEA YYQEAGRAGR DGKLSDCILY
ANLASKPSLL PSRKSEDQKK QAYIMLSDCF RYGMNTSCCR AKILVEYFGE DFGHQKCHLC
DVCIDGPPKK QNLKEEACIF LQTIGAQNQG RRDSKDYSYD DDIHFDYNYR GQRERPNLRM
LVGKIRQQTC FHLKNVRIQF QKFSTTDMLW WRGLARILEV KGYIREGDDK SHVQAKFPEF
VRSMNEEAFW VYPEADMLLA RKLTEKPFSS FSEWGKGWAD PEIRRQRLER MGVKRKSGMV
SSSKRKPKRK VQHDLRTSRG RLTAKLSKYK
//
