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Database: UniProt
Entry: A0A0B2P6F6_GLYSO
LinkDB: A0A0B2P6F6_GLYSO
Original site: A0A0B2P6F6_GLYSO 
ID   A0A0B2P6F6_GLYSO        Unreviewed;       643 AA.
AC   A0A0B2P6F6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   ORFNames=glysoja_031886 {ECO:0000313|EMBL:KHN04786.1};
OS   Glycine soja (Wild soybean).
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; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN04786.1};
RN   [1] {ECO:0000313|EMBL:KHN04786.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Root {ECO:0000313|EMBL:KHN04786.1};
RA   Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT   "Identification of a novel salt tolerance gene in wild soybean by whole-
RT   genome sequencing.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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=3.6.4.13;
CC         Evidence={ECO:0000256|RuleBase:RU365068};
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC       {ECO:0000256|RuleBase:RU365068}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4
CC       subfamily. {ECO:0000256|ARBA:ARBA00038002}.
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DR   EMBL; KN668935; KHN04786.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2P6F6; -.
DR   Proteomes; UP000053555; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd17960; DEADc_DDX55; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025313; DUF4217.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   PANTHER; PTHR24031:SF2; ATP-DEPENDENT RNA HELICASE DDX55; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT   DOMAIN          24..202
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          244..400
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          205..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   643 AA;  72243 MW;  98E1BAC6779A360D CRC64;
     MTVKIIAEKD KKNDFLQNQG LTKGFLNLSF KDVAVDAATG SGKTLAFVVP LVEILRRSSS
     HPKPHKVLGI IISPTRELST QIYHVAQSFI STLMNVKSML LVGGAEVKTD IKKIEEEGAN
     ILIGTPGRLY DIMNRMDVLD LKNLEILILD EADRLLDMGF QKQITSIISL LPKLRRTGLF
     SATQTEAIEE LAKAGLRNPV RVEVRAETKS EKGPASSKQP ESSKTPSGLH IEYLECEEDK
     KPSQLLDILI KNRSKKIIIY FMTCACVDYW GAVLPCLSVL KGFSLIPLHG KMKQSAREKA
     LASFTTLSNG ILLCTDVAAR GLDIPGVDCI VQYDPPQDPN VFIHRVGRTA RLGKQGHAVV
     FLLPKEESYV EFLRIRRVPL QERICSDDAT DVVPQIRSAA KKDRDVMEKG IKAFVSYIRA
     YKEHHCSYIF RWKELEIGKL ATGFGLLQLP SMPEVKHHSL STDGFEPVED INLVDIKYRD
     KSREKQRKKN LQAKKEAKER EPKPQKPKKT PIAPTATRKK TARQRRAQQT MEDEEELMQE
     YRLLKKLKKG TIDENEYAKL TGAQGDEIIF PQALLVAENE PPSGLAHSNG WNPLPIFLSI
     ISNSWQPLSY TVTEIAYLIS SPSLKNSKRM SSNPCTGKHR FHL
//
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