ID F4JEL4_ARATH Unreviewed; 415 AA. AC F4JEL4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 08-NOV-2023, entry version 86. DE SubName: Full=Eukaryotic translation initiation factor 4A1 {ECO:0000313|EMBL:AEE75439.1}; GN Name=EIF4A1 {ECO:0000313|EMBL:AEE75439.1, ECO:0000313|TAIR:AT3G13920}; GN Synonyms=RH4 {ECO:0000313|EMBL:AEE75439.1}, TIF4A1 GN {ECO:0000313|EMBL:AEE75439.1}; GN OrderedLocusNames=At3g13920 {ECO:0000313|Araport:AT3G13920, GN ECO:0000313|EMBL:AEE75439.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702 {ECO:0000313|EMBL:AEE75439.1, ECO:0000313|Proteomes:UP000006548}; RN [1] {ECO:0000313|EMBL:AEE75439.1, ECO:0000313|Proteomes:UP000006548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RX PubMed=11130713; DOI=10.1038/35048706; RG European Union Chromosome 3 Arabidopsis Sequencing Consortium; RG Institute for Genomic Research; RG Kazusa DNA Research Institute; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., RA Valle G., Blocker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., RA Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., RA Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., RA Weissenbach J., Saurin W., Quetier F., Schafer M., Muller-Auer S., RA Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., RA Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., RA Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., RA Simionati B., Conrad A., Hornischer K., Kauer G., Lohnert T.H., RA Nordsiek G., Reichelt J., Scharfe M., Schon O., Bargues M., Terol J., RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwalder B., RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., flores M., Liguori R., Vitale D., Mannhaupt G., RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.W., Mayer K.F., Kaul S., RA Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."; RL Nature 408:820-822(2000). RN [2] {ECO:0007829|PubMed:22223895} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [3] {ECO:0000313|Proteomes:UP000006548} RP GENOME REANNOTATION. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CC {ECO:0000256|RuleBase:RU000492}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002686; AEE75439.1; -; Genomic_DNA. DR RefSeq; NP_001319547.1; NM_001338092.1. DR AlphaFoldDB; F4JEL4; -. DR SMR; F4JEL4; -. DR IntAct; F4JEL4; 1. DR EnsemblPlants; AT3G13920.2; AT3G13920.2; AT3G13920. DR GeneID; 820605; -. DR Gramene; AT3G13920.2; AT3G13920.2; AT3G13920. DR Araport; AT3G13920; -. DR TAIR; AT3G13920; EIF4A1. DR eggNOG; KOG0327; Eukaryota. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; F4JEL4; baseline and differential. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0005730; C:nucleolus; HDA:TAIR. DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR. DR GO; GO:0009506; C:plasmodesma; HDA:TAIR. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0003729; F:mRNA binding; IDA:TAIR. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. DR GO; GO:0006413; P:translational initiation; ISS:TAIR. DR CDD; cd17939; DEADc_EIF4A; 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; 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; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1. DR PANTHER; PTHR47958:SF117; EUKARYOTIC INITIATION FACTOR 4A-15; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 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 1: Evidence at protein level; 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 Initiation factor {ECO:0000313|EMBL:AEE75439.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU000492}; KW Protein biosynthesis {ECO:0000313|EMBL:AEE75439.1}; KW Proteomics identification {ECO:0007829|PeptideAtlas:F4JEL4, KW ECO:0007829|ProteomicsDB:F4JEL4}; KW Reference proteome {ECO:0000313|Proteomes:UP000006548}. FT DOMAIN 39..67 FT /note="DEAD-box RNA helicase Q" FT /evidence="ECO:0000259|PROSITE:PS51195" FT DOMAIN 70..240 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 251..415 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT MOTIF 39..67 FT /note="Q motif" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552" SQ SEQUENCE 415 AA; 46950 MW; C8D90B25E1C16501 CRC64; MAGSAPEGTQ FDARQFDQKL NEVLEGQDEF FTSYDDVHES FDAMGLQENL LRGIYAYGFE KPSAIQQRGI VPFCKGLDVI QQAQSGTGKT ATFCSGVLQQ LDFSLIQCQA LVLAPTRELA QQIEKVMRAL GDYLGVKVHA CVGGTSVRED QRILQAGVHV VVGTPGRVFD MLKRQSLRAD NIKMFVLDEA DEMLSRGFKD QIYDIFQLLP PKIQVGVFSA TMPPEALEIT RKFMSKPVRI LVKRDELTLE GIKQFYVNVE KEEWKLETLC DLYETLAITQ SVIFVNTRRK VDWLTDKMRS RDHTVSATHG DMDQNTRDII MREFRSGSSR VLITTDLLAR GIDVQQVSLV INFDLPTQPE NYLHRIGRSG RFGRKGVAIN FVTRDDERML CLRTWPICCE GRKEVGSVAV FALPY //