PlantTFDB - Plant Transcription Factor Database @ CBI, PKU

PlantRegMap/PlantTFDB v5.0

Plant Transcription Factor Database

Transcription Factor Information

Basic Information | Signature Domain | Sequence |

Basic Information? help Back to Top

TF ID

XP_010925126.1

Organism

Elaeis guineensis

Taxonomic ID

51953

Taxonomic Lineage

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; Liliopsida; Petrosaviidae; commelinids; Arecales; Arecaceae; Arecoideae; Cocoseae; Elaeidinae; Elaeis

Family

GRAS

Protein Properties

Length: 583aa MW: 62374.3 Da PI: 5.3035

Description

GRAS family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
XP_010925126.1	genome	OG	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	GRAS	423.6	1.6e-129	144	515	1	374
GRAS 1 lvelLlecAeavssgdlelaqalLarlsel..aspdgdpmqRlaayfteALaarlarsvselykalppsetseknsseelaalklfsevsPilkf 93 lv+lL++cA+av+ gd la +++++++ + ++g + ++a yf+ AL +r+++ +s+ ++a + + +++ ++ f+evsP+lkf XP_010925126.1 144 LVHLLVTCADAVQRGDSGLAGNIIEEMRVVltRVNTGFGIGKVAGYFVDALCRRIYSPCSSSSSASVAGS-----AADQEILYHHFYEVSPYLKF 233 68*********************9998866888899***************5544443333322.....4556667889****** PP GRAS 94 shltaNqaIleavegeervHiiDfdisqGlQWpaLlqaLasRpegppslRiTgvgspesgskeeleetgerLakfAeelgvpfefnvlvakrled 188 +h++aNqaIlea++g +rvH+iDf+++ GlQWpaL+qaLa R++gpp lR+Tg+g+p+++ +++l+e+g rLa++A +++v+f f+ ++a+r++d XP_010925126.1 234 AHFMANQAILEAFDGYDRVHVIDFNLMDGLQWPALIQALALRAGGPPFLRLTGIGPPSPDGRDALREVGLRLAELALSVRVRFAFRGVAASRIDD 328 ******************************************************************************************* PP GRAS 189 leleeLrvkpgEalaVnlvlqlhrlldesvsles.erdevLklvkslsPkvvvvveqeadhnsesFlerflealeyysalfdsleaklpreseer 282 +++++L+v pgEa+aVn+vlqlhrll ++++ + ++d+vL + +++Pk+v+vveqeadhn++sFl+rf+eal yys++fdslea+ +++++++ XP_010925126.1 329 VRPWMLQVVPGEAVAVNSVLQLHRLLGDPGDDAAaPIDSVLGWIVRIQPKIVTVVEQEADHNRPSFLDRFTEALFYYSTMFDSLEAGGGATQKQQ 423 *************************9988879******************************************************* PP GRAS 283 ikvErellgreivnvvacegaerrerhetlekWrerleeaGFkpvplsekaakqaklllrkvksdgyrveeesgslvlgWkdrpLvsvSaWr 374 + v +++l+re++n+v+cega+r+erhe l +Wr+rl++aG+++v+l+++a kqa++ll ++++gy vee +g+l+lgW++rpL+s+SaWr XP_010925126.1 424 QAVAEVYLQREVCNIVCCEGAARVERHEPLVRWRARLGRAGLRAVHLGSNAFKQASMLLTLFSGEGYCVEEVDGCLTLGWHSRPLISASAWR 515 *****************************************************************************************8 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
Pfam	PF12041	7.3E-22	30	93	IPR021914	Transcriptional factor DELLA, N-terminal
SMART	SM01129	2.3E-11	30	101	No hit	No description
PROSITE profile	PS50985	62.976	118	495	IPR005202	Transcription factor GRAS
Pfam	PF03514	5.7E-127	144	515	IPR005202	Transcription factor GRAS

Sequence ? help Back to Top
Protein Sequence Length: 583 aa Download sequence Send to blast
MGPYPFGSGT AASGWAAADS GPQCSASEID GLLAGAGYRV RSSDLLHVAH SLERLESAIG 60 GGPADHLASA EAVRYNPSDL TTWVNSILSE LSSSLPPLRP PPAAPVAGTW PDLTCFSLPY 120 PQYQTAVIAA TRQREEEEGS AIRLVHLLVT CADAVQRGDS GLAGNIIEEM RVVLTRVNTG 180 FGIGKVAGYF VDALCRRIYS PCSSSSSASV AGSAADQEIL YHHFYEVSPY LKFAHFMANQ 240 AILEAFDGYD RVHVIDFNLM DGLQWPALIQ ALALRAGGPP FLRLTGIGPP SPDGRDALRE 300 VGLRLAELAL SVRVRFAFRG VAASRIDDVR PWMLQVVPGE AVAVNSVLQL HRLLGDPGDD 360 AAAPIDSVLG WIVRIQPKIV TVVEQEADHN RPSFLDRFTE ALFYYSTMFD SLEAGGGATQ 420 KQQQAVAEVY LQREVCNIVC CEGAARVERH EPLVRWRARL GRAGLRAVHL GSNAFKQASM 480 LLTLFSGEGY CVEEVDGCLT LGWHSRPLIS ASAWRADADV APLPDSQLFN PGIAATINST 540 SISGNDNNNT NNFQSMHHGS GNGNAAANNQ QNNATCDGGV IGL

Sequence ? help Back to Top

Protein Sequence Length: 583 aa Download sequence Send to blast

MGPYPFGSGT AASGWAAADS GPQCSASEID GLLAGAGYRV RSSDLLHVAH SLERLESAIG  60
GGPADHLASA EAVRYNPSDL TTWVNSILSE LSSSLPPLRP PPAAPVAGTW PDLTCFSLPY  120
PQYQTAVIAA TRQREEEEGS AIRLVHLLVT CADAVQRGDS GLAGNIIEEM RVVLTRVNTG  180
FGIGKVAGYF VDALCRRIYS PCSSSSSASV AGSAADQEIL YHHFYEVSPY LKFAHFMANQ  240
AILEAFDGYD RVHVIDFNLM DGLQWPALIQ ALALRAGGPP FLRLTGIGPP SPDGRDALRE  300
VGLRLAELAL SVRVRFAFRG VAASRIDDVR PWMLQVVPGE AVAVNSVLQL HRLLGDPGDD  360
AAAPIDSVLG WIVRIQPKIV TVVEQEADHN RPSFLDRFTE ALFYYSTMFD SLEAGGGATQ  420
KQQQAVAEVY LQREVCNIVC CEGAARVERH EPLVRWRARL GRAGLRAVHL GSNAFKQASM  480
LLTLFSGEGY CVEEVDGCLT LGWHSRPLIS ASAWRADADV APLPDSQLFN PGIAATINST  540
SISGNDNNNT NNFQSMHHGS GNGNAAANNQ QNNATCDGGV IGL

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
5b3g_A	1e-62	132	514	9	378	Protein SCARECROW
5b3h_A	1e-62	132	514	8	377	Protein SCARECROW
5b3h_D	1e-62	132	514	8	377	Protein SCARECROW
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Functional Description ? help Back to Top
Source	Description
UniProt	Transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. Transcription coactivator of the zinc finger transcription factors GAF1/IDD2 and ENY/IDD1 in regulation of gibberellin homeostasis and signaling (PubMed:25035403). No effect of the BOI proteins on its stability. Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes. Positively regulates XERICO expression. In contrast to RGA, it is less sensitive to GA. Its activity is probably regulated by other phytohormones such as auxin and ethylene. {ECO:0000269\|PubMed:11487693, ECO:0000269\|PubMed:11606551, ECO:0000269\|PubMed:11606552, ECO:0000269\|PubMed:14973286, ECO:0000269\|PubMed:15128937, ECO:0000269\|PubMed:16034591, ECO:0000269\|PubMed:17933900, ECO:0000269\|PubMed:25035403, ECO:0000269\|PubMed:9389651}.

Regulation -- PlantRegMap ? help Back to Top
Source	Upstream Regulator	Target Gene
PlantRegMap	Retrieve	-

Annotation -- Protein ? help Back to Top
Source	Hit ID	E-value	Description
Refseq	XP_010925126.1	0.0	DELLA protein DWARF8
Swissprot	Q9LQT8	1e-150	GAI_ARATH; DELLA protein GAI
TrEMBL	A0A2H3Z6Z7	0.0	A0A2H3Z6Z7_PHODC; DELLA protein RHT-1-like
STRING	XP_008809331.1	0.0	(Phoenix dactylifera)

Orthologous Group ? help Back to Top
Lineage	Orthologous Group ID	Taxa Number	Gene Number
Monocots	OGMP998	38	138

Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID	E-value	Description
AT1G14920.1	1e-117	GRAS family protein

Publications ? help Back to Top
Duarte JM, et al. Expression pattern shifts following duplication indicative of subfunctionalization and neofunctionalization in regulatory genes of Arabidopsis. Mol. Biol. Evol., 2006. 23(2): p. 469-78 [PMID:16280546] Ding Y, et al. Four distinct types of dehydration stress memory genes in Arabidopsis thaliana. BMC Plant Biol., 2013. 13: p. 229 [PMID:24377444] Gallego-Giraldo C, et al. Role of the gibberellin receptors GID1 during fruit-set in Arabidopsis. Plant J., 2014. 79(6): p. 1020-1032 [PMID:24961590] Fukazawa J, et al. DELLAs function as coactivators of GAI-ASSOCIATED FACTOR1 in regulation of gibberellin homeostasis and signaling in Arabidopsis. Plant Cell, 2014. 26(7): p. 2920-38 [PMID:25035403] Marín-de la Rosa N, et al. Genome Wide Binding Site Analysis Reveals Transcriptional Coactivation of Cytokinin-Responsive Genes by DELLA Proteins. PLoS Genet., 2015. 11(7): p. e1005337 [PMID:26134422] Shi H,Wei Y,Wang Q,Reiter RJ,He C Melatonin mediates the stabilization of DELLA proteins to repress the floral transition in Arabidopsis. J. Pineal Res., 2016. 60(3): p. 373-9 [PMID:26887824] Lee SA, et al. Interplay between ABA and GA Modulates the Timing of Asymmetric Cell Divisions in the Arabidopsis Root Ground Tissue. Mol Plant, 2016. 9(6): p. 870-84 [PMID:26970019] Qu J,Kang SG,Hah C,Jang JC Molecular and cellular characterization of GA-Stimulated Transcripts GASA4 and GASA6 in Arabidopsis thaliana. Plant Sci., 2016. 246: p. 1-10 [PMID:26993231] Shahnejat-Bushehri S,Nobmann B,Devi Allu A,Balazadeh S JUB1 suppresses Pseudomonas syringae-induced defense responses through accumulation of DELLA proteins. Plant Signal Behav, 2016. 11(6): p. e1181245 [PMID:27159137] Shahnejat-Bushehri S,Tarkowska D,Sakuraba Y,Balazadeh S Arabidopsis NAC transcription factor JUB1 regulates GA/BR metabolism and signalling. Nat Plants, 2016. 2: p. 16013 [PMID:27249348] Wang H, et al. The DELLA-CONSTANS Transcription Factor Cascade Integrates Gibberellic Acid and Photoperiod Signaling to Regulate Flowering. Plant Physiol., 2016. 172(1): p. 479-88 [PMID:27406167] Li W,Wang H,Yu D Arabidopsis WRKY Transcription Factors WRKY12 and WRKY13 Oppositely Regulate Flowering under Short-Day Conditions. Mol Plant, 2016. 9(11): p. 1492-1503 [PMID:27592586] Liu B,De Storme N,Geelen D Gibberellin Induces Diploid Pollen Formation by Interfering with Meiotic Cytokinesis. Plant Physiol., 2017. 173(1): p. 338-353 [PMID:27621423] Matsuoka K, et al. Differential Cellular Control by Cotyledon-Derived Phytohormones Involved in Graft Reunion of Arabidopsis Hypocotyls. Plant Cell Physiol., 2016. 57(12): p. 2620-2631 [PMID:27986917] Zentella R, et al. The Arabidopsis O-fucosyltransferase SPINDLY activates nuclear growth repressor DELLA. Nat. Chem. Biol., 2017. 13(5): p. 479-485 [PMID:28244988] Zhang Y, et al. GA-DELLA pathway is involved in regulation of nitrogen deficiency-induced anthocyanin accumulation. Plant Cell Rep., 2017. 36(4): p. 557-569 [PMID:28275852] Zhang L,Chen L,Yu D Transcription Factor WRKY75 Interacts with DELLA Proteins to Affect Flowering. Plant Physiol., 2018. 176(1): p. 790-803 [PMID:29133369] Nelson SK,Ariizumi T,Steber CM Biology in the Dry Seed: Transcriptome Changes Associated with Dry Seed Dormancy and Dormancy Loss in the Arabidopsis GA-Insensitive sleepy1-2 Mutant. Front Plant Sci, 2017. 8: p. 2158 [PMID:29312402] Liu B,De Storme N,Geelen D Cold-Induced Male Meiotic Restitution in Arabidopsis thaliana Is Not Mediated by GA-DELLA Signaling. Front Plant Sci, 2018. 9: p. 91 [PMID:29459879] Zhang Y, et al. DELLA proteins negatively regulate dark-induced senescence and chlorophyll degradation in Arabidopsis through interaction with the transcription factor WRKY6. Plant Cell Rep., 2018. 37(7): p. 981-992 [PMID:29574486] Felipo-Benavent A, et al. Regulation of xylem fiber differentiation by gibberellins through DELLA-KNAT1 interaction. Development, 2019. [PMID:30389856] Wright DA, et al. Recovery of YAC-end sequences through complementation of an Escherichia coli pyrF mutation. Nucleic Acids Res., 1997. 25(13): p. 2679-80 [PMID:9185581]