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Database: UniProt
Entry: A0A3B6FQ41_WHEAT
LinkDB: A0A3B6FQ41_WHEAT
Original site: A0A3B6FQ41_WHEAT 
ID   A0A3B6FQ41_WHEAT        Unreviewed;      1195 AA.
AC   A0A3B6FQ41;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=CFC21_042341 {ECO:0000313|EMBL:KAF7030904.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS3B02G337600.3};
RN   [1] {ECO:0000313|EMBL:KAF7030904.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7030904.1};
RX   PubMed=29069494;
RA   Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT   "The first near-complete assembly of the hexaploid bread wheat genome,
RT   Triticum aestivum.";
RL   Gigascience 6:1-7(2017).
RN   [2] {ECO:0000313|EnsemblPlants:TraesCS3B02G337600.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS3B02G337600.3};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [3] {ECO:0000313|EnsemblPlants:TraesCS3B02G337600.3}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KAF7030904.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7030904.1};
RA   Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT   "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT   aestivum) genome.";
RL   Submitted (MAR-2020) 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=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
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DR   EMBL; CM022218; KAF7030904.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B6FQ41; -.
DR   SMR; A0A3B6FQ41; -.
DR   STRING; 4565.A0A3B6FQ41; -.
DR   PaxDb; 4565-Traes_3B_5D41CB402-1; -.
DR   EnsemblPlants; TraesCS3B02G337600.3; TraesCS3B02G337600.3; TraesCS3B02G337600.
DR   Gramene; TraesCS3B02G337600.3; TraesCS3B02G337600.3; TraesCS3B02G337600.
DR   Gramene; TraesCS3B03G0857800.2; TraesCS3B03G0857800.2.CDS; TraesCS3B03G0857800.
DR   OrthoDB; 53793at2759; -.
DR   Proteomes; UP000019116; Chromosome 3B.
DR   Proteomes; UP000815260; Chromosome 3B.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd17917; DEXHc_RHA-like; 1.
DR   CDD; cd06007; R3H_DEXH_helicase; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR034083; R3H_DEXH_helicase.
DR   InterPro; IPR001374; R3H_dom.
DR   InterPro; IPR036867; R3H_dom_sf.
DR   PANTHER; PTHR18934:SF213; 3'-5' RNA HELICASE YTHDC2; 1.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF01424; R3H; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00393; R3H; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF82708; R3H domain; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51061; R3H; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          25..88
FT                   /note="R3H"
FT                   /evidence="ECO:0000259|PROSITE:PS51061"
FT   DOMAIN          196..373
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REPEAT          456..488
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          543..716
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          994..1026
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1131..1195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1010..1026
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1138..1152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1161..1189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1195 AA;  130936 MW;  7DF3042199A7946F CRC64;
     MGRKGPKGAK NAAALTKAAL AAMSEETTVR ITTLLEDFRA SDAQVHTFEP SLTNQERAAV
     HAMCKKMGMI SKSKGYGERR CLSVYKTKNT QGAVKEEGPS KLGFSEEARQ VLLDLFTHYP
     PDDAELNGDA VKNPGDKAAK ILWKTDTAFS RPAMQKHDIA KKVKMLTSKL NDTRQLRKIG
     EGRSKLPIAS FKDHISSTLE NHQVVLISGE TGCGKTTQVP QYILDHVWGK GESCKIICTQ
     PRRISAMSVA ERISVERGET VGDTVGYKIR LESKGGKNSS IMFCTNGVLL RVLIGRVTNI
     SKRQRAADDV IMGITHIIVD EIHERDRFSD FMLAILRDLL PIYPHLHLVL MSATIDAERF
     SQYFNGCPVI QVPGHTYPVK TFYLEDVLSI LQSVGDNHLN PETNDLGLDS VLTDDYKSSM
     DEAISIALVS DEFDPLIELI SIEQNPEIFN YQHSETGVTP LMVFARKGQL GDVCMLLSFG
     VDCSARDHDG KSALDWAQQE NQVEAYEVIK KHMDCSPAKL PEENELLKKY LATINPEHID
     TVLIERLLRK ICTDSNEGAI LVFLPGWEDI NQTRERLLAS SFRDSSKFLV LSLHSMIPSS
     EQKKVFKRAP AGVRKIILST NIAETAVTID DVVFVIDSGR MKEKSYDPYN NVSTLHTSWV
     SRANARQREG RAGRCQPGTC YHLYSRFRAA SLPEFQIPEI KRMPIEELCL QVKLLDPNSK
     IADFLKKTLD PPVTETVKNA ITVLQDLGAL TQNEQLTDLG EKLGSLPVHP STSKMLLFGI
     LMNCLDPALT LACAADYRDP FVLPMAPDER KRAAAAKVEL ASLYGGYSDQ LAVVAAFDCW
     TCAKVKGQEA LFCSKYFVAS NTMNMLSSMR KQLHSELTQR GFLPADTSAC SLNAKVPGII
     SAVLVAGAYP MVGRLLPPRK NARRAVLETA SGAKVRLHPH SSNFNLSFNK SSGNPLMVFD
     EITRGDGGMY VKNCSVVGSY PLLLLATEIA VAPPDDVSDE DDEGSSGDEA GKSTLGQQKE
     EIMSSPDNTV SVVVDRWLRF DATALDVAQI YCLRERLASA ILFKVKHPQD VLPPALGATM
     YAIACILSYD GLPGNLATRH GSGQSSTDAS GSAEGRKVGF IPPGGFLMSL LSDVPPNAPH
     HQKSSNHPGG GSGHIRSSRA PAGRFNQSQQ HPGRNSSGPG SSASQSFKRQ RDAAR
//
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