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Database: UniProt
Entry: A0A1S3V8T7_VIGRR
LinkDB: A0A1S3V8T7_VIGRR
Original site: A0A1S3V8T7_VIGRR 
ID   A0A1S3V8T7_VIGRR        Unreviewed;       858 AA.
AC   A0A1S3V8T7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
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_014514758.1};
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_014514758.1};
RN   [1] {ECO:0000313|RefSeq:XP_014514758.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014514758.1};
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_014514758.1; XM_014659272.2.
DR   AlphaFoldDB; A0A1S3V8T7; -.
DR   GeneID; 106772714; -.
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          818..858
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        827..843
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   858 AA;  97912 MW;  307474BC106622DE 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 LQTIGAQNGR RDSKDYSYDD DIHFDYNYRG QRERPNLRML
     VGKIRQQFQK FSTTDMLWWR GLARILEVKG YIREGDDKSH VQAKFPEFVR SMNEEAFWVY
     PEADMLLARK LTEKPFSSFS EWGKGWADPE IRRQRLERMG VKRKSGMVSS SKRKPKRKVQ
     HDLRTSRGRL TAKLSKYK
//
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