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Database: UniProt
Entry: F6GTH7_VITVI
LinkDB: F6GTH7_VITVI
Original site: F6GTH7_VITVI 
ID   F6GTH7_VITVI            Unreviewed;       550 AA.
AC   F6GTH7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   OrderedLocusNames=VIT_17s0000g04310 {ECO:0000313|EMBL:CCB43186.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB43186.1, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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|ARBA:ARBA00001556,
CC         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. DDX18/HAS1
CC       subfamily. {ECO:0000256|ARBA:ARBA00024357}.
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DR   EMBL; FN594950; CCB43186.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6GTH7; -.
DR   STRING; 29760.F6GTH7; -.
DR   PaxDb; 29760-VIT_17s0000g04310-t01; -.
DR   EnsemblPlants; Vitvi17g00388_t001; Vitvi17g00388_P001; Vitvi17g00388.
DR   Gramene; Vitvi17g00388_t001; Vitvi17g00388_P001; Vitvi17g00388.
DR   eggNOG; KOG0342; Eukaryota.
DR   HOGENOM; CLU_003041_26_5_1; -.
DR   InParanoid; F6GTH7; -.
DR   Proteomes; UP000009183; Chromosome 17.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   CDD; cd17942; DEADc_DDX18; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR044773; DDX18/Has1_DEADc.
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   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR24031:SF301; ATP-DEPENDENT RNA HELICASE DDX18; 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.
DR   PROSITE; PS51195; Q_MOTIF; 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   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT   DOMAIN          62..90
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          93..268
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          295..442
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           62..90
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        16..37
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   550 AA;  61769 MW;  F8F04889E26CC4FF CRC64;
     MPKESEPAPS DTANNDEDST PEEEEAVAED REEEVAEERE AVESLKEKKK AKKSGSGIMS
     TEAFSALGLS EPTMKAINDM GFGNMTQIQA RAIPPLLLGK DVLGAARTGS GKTLAFLIPA
     VELLYHISFM PRNGTGVVVI CPTRELAIQT HAVAKDLLKY HTQTLGLVIG GSARRGEAER
     LAKGANLLVA TPGRLLDHLQ NTKGFIYKNL KCLIIDEADR ILEANFEEEM KQIIKLLPKE
     RQTALFSATQ TKKVEDLARL SFQTTPVYID VDDGRTKVTN EGLQQGYCVV PSAKRFVLLY
     SFLKRNLSKK VMVFFSSCNS VKYHSELLRY IQVDCLDIHG KQKQQKRTST FFDFCKAEKG
     ILLCTDVAAR GLDIPDVDWI VQYDPPDEPK EYIHRVGRTA RGEGKKGNAL LFLIPEELQF
     LRYLKAAKVP VKEYEYDVKK LANVQSHLEK LVSNNYYLNK SAKDAYRSYI LAYNSHSMKD
     IFNVHRLDLQ AVASSFCFSS PPKVNLSIDS SASKFRKKTH KVEGSRNGFS ESNPYGRQRG
     QDDKRQFVRY
//
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