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Plant Transcription
Factor Database
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Transcription Factor Information
Basic
Information? help
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TF ID |
PGSC0003DMP400000652 |
Organism |
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Taxonomic ID |
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Taxonomic Lineage |
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum
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Family |
bHLH |
Protein Properties |
Length: 700aa MW: 79315 Da PI: 8.5379 |
Description |
bHLH family protein |
Gene Model |
Gene Model ID |
Type |
Source |
Coding Sequence |
PGSC0003DMP400000652 | genome | PGSC | View CDS |
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Signature Domain? help Back to Top |
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No. |
Domain |
Score |
E-value |
Start |
End |
HMM Start |
HMM End |
1 | HLH | 37.8 | 3.5e-12 | 536 | 581 | 4 | 54 |
HHHHHHHHHHHHHHHHHHHHHCTSCCC...TTS-STCHHHHHHHHHHHHHH CS
HLH 4 ahnerErrRRdriNsafeeLrellPkaskapskKlsKaeiLekAveYIksL 54
h + ErrRR+++N+ f+ Lr+llP+ K +Ka++L ++eY++sL
PGSC0003DMP400000652 536 HHMISERRRREKLNENFQHLRSLLPPE-----IKKDKASVLASTTEYLSSL 581
68899*********************8.....699**************99 PP
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Protein Features
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Database |
Entry ID |
E-value |
Start |
End |
InterPro ID |
Description |
Gene3D | G3DSA:3.30.43.10 | 1.1E-6 | 25 | 105 | IPR016167 | FAD-binding, type 2, subdomain 1 |
SuperFamily | SSF56176 | 1.96E-35 | 28 | 226 | IPR016166 | FAD-binding, type 2 |
PROSITE profile | PS51387 | 13.387 | 46 | 229 | IPR016166 | FAD-binding, type 2 |
PROSITE pattern | PS00862 | 0 | 50 | 85 | IPR006093 | Oxygen oxidoreductase covalent FAD-binding site |
Pfam | PF01565 | 2.0E-16 | 50 | 198 | IPR006094 | FAD linked oxidase, N-terminal |
Gene3D | G3DSA:3.30.465.10 | 1.2E-8 | 142 | 225 | IPR016169 | CO dehydrogenase flavoprotein-like, FAD-binding, subdomain 2 |
Pfam | PF09265 | 2.3E-68 | 230 | 409 | IPR015345 | Cytokinin dehydrogenase 1, FAD/cytokinin binding domain |
SuperFamily | SSF55103 | 6.02E-45 | 230 | 408 | IPR016164 | FAD-linked oxidase-like, C-terminal |
Gene3D | G3DSA:3.40.462.10 | 1.8E-71 | 232 | 411 | IPR016170 | Vanillyl-alcohol oxidase/Cytokinin dehydrogenase C-terminal domain |
PROSITE profile | PS50888 | 14.557 | 532 | 581 | IPR011598 | Myc-type, basic helix-loop-helix (bHLH) domain |
CDD | cd00083 | 8.46E-12 | 532 | 586 | No hit | No description |
SuperFamily | SSF47459 | 1.44E-14 | 534 | 598 | IPR011598 | Myc-type, basic helix-loop-helix (bHLH) domain |
Gene3D | G3DSA:4.10.280.10 | 3.3E-14 | 535 | 598 | IPR011598 | Myc-type, basic helix-loop-helix (bHLH) domain |
Pfam | PF00010 | 1.2E-9 | 536 | 581 | IPR011598 | Myc-type, basic helix-loop-helix (bHLH) domain |
SMART | SM00353 | 9.0E-12 | 538 | 587 | IPR011598 | Myc-type, basic helix-loop-helix (bHLH) domain |
Gene Ontology ? help Back to Top |
GO Term |
GO Category |
GO Description |
GO:0009690 | Biological Process | cytokinin metabolic process |
GO:0055114 | Biological Process | oxidation-reduction process |
GO:0016614 | Molecular Function | oxidoreductase activity, acting on CH-OH group of donors |
GO:0019139 | Molecular Function | cytokinin dehydrogenase activity |
GO:0046983 | Molecular Function | protein dimerization activity |
GO:0050660 | Molecular Function | flavin adenine dinucleotide binding |
Sequence ? help Back to Top |
Protein Sequence Length: 700 aa
Download sequence Send
to blast |
MSNLGKLKSW NPSIPQEIFS LNISSKLSTN SDDIKESSKD FGKIVQKKFP AAVLYPSCVN 60 DIIDLIQFSY DLSVPFQVAA KGHGHSIRGQ AMAQNGVIVE MNSLNNNNNE NCGVRVSWDL 120 DLGFYADVGG EQLWIDVLRS TLEYGLAPVS WTDYLYLTVG GTLSNAGISG QTFRYGPQIS 180 NVHEMDVITG KGELVTCSKD KNSELFFGVL GGLGQFGIII RAKIVLDKAP TRVKWVRMLY 240 DDFPKFTKDQ EYLISIHHNG LDYVEGSLMM EQSSLNNWRS SFFSPSNQAK IVSLLSQNKI 300 MYCLEMVKYY DDHTANTIDE ELKKLVQGLN YLGGFMFKKD VTFVEFLNRV RKGQIELELK 360 GMWDVPHPWL NLFVPKSNIM QFNAAVFEDI ILRQNKPTGP ILVYPTSRKS EYSSLFHNVA 420 KTCYVTQENQ TLTQFPKIEG EDDVIRQAYL AVISSSSPSS SSRGQIQEIL TRDHRLVTRN 480 TTAFTRFRST NYASIGATSS CRQNMLKRSI TFFKNLYTMN RQEGIQVNRA MSTQVHHMIS 540 ERRRREKLNE NFQHLRSLLP PEIKKDKASV LASTTEYLSS LKDQVEKLCK RNEILEATLL 600 SKKEVSQFQQ NGSGRVYIYI TNIEERIVDL QVIAKGKCNT LDLVICLMEF LKMASYVNLM 660 AIDANTTMVQ SCPLTQITLR LRIQVIYVSH SVFDICIGD*
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3D Structure ? help Back to Top |
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PDB ID |
Evalue |
Query Start |
Query End |
Hit Start |
Hit End |
Description |
4o95_A | 1e-138 | 28 | 408 | 27 | 412 | Cytokinin dehydrogenase 4 |
4oal_A | 1e-138 | 28 | 408 | 27 | 412 | Cytokinin dehydrogenase 4 |
4oal_B | 1e-138 | 28 | 408 | 27 | 412 | Cytokinin dehydrogenase 4 |
5hhz_A | 1e-138 | 28 | 408 | 27 | 412 | Cytokinin dehydrogenase 4 |
5hmr_A | 1e-138 | 28 | 408 | 27 | 412 | Cytokinin dehydrogenase 4 |
5hqx_A | 1e-138 | 28 | 408 | 27 | 412 | Cytokinin dehydrogenase 4 |
Search in ModeBase |
Nucleic Localization
Signal ? help
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 |
No. |
Start |
End |
Sequence |
1 | 540 | 545 | ERRRRE |
2 | 541 | 546 | RRRREK |
Functional Description ? help
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Source |
Description |
UniProt | Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group. {ECO:0000269|PubMed:14555694}. |
Regulation -- Description ? help
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Source |
Description |
UniProt | INDUCTION: Regulated by GATA18/HAN. {ECO:0000269|PubMed:26390296}. |
Annotation --
Nucleotide ? help
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Source |
Hit ID |
E-value |
Description |
GenBank | FJ751239 | 0.0 | FJ751239.1 Solanum tuberosum cytokinin oxidase/dehydrogenase 2 mRNA, complete cds. |
Publications
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- Bilyeu KD, et al.
Molecular and biochemical characterization of a cytokinin oxidase from maize. Plant Physiol., 2001. 125(1): p. 378-86 [PMID:11154345] - Werner T,Motyka V,Strnad M,Schmülling T
Regulation of plant growth by cytokinin. Proc. Natl. Acad. Sci. U.S.A., 2001. 98(18): p. 10487-92 [PMID:11504909] - Schmülling T,Werner T,Riefler M,Krupková E,Bartrina y Manns I
Structure and function of cytokinin oxidase/dehydrogenase genes of maize, rice, Arabidopsis and other species. J. Plant Res., 2003. 116(3): p. 241-52 [PMID:12721786] - Werner T, et al.
Cytokinin-deficient transgenic Arabidopsis plants show multiple developmental alterations indicating opposite functions of cytokinins in the regulation of shoot and root meristem activity. Plant Cell, 2003. 15(11): p. 2532-50 [PMID:14555694] - Lohar DP, et al.
Cytokinins play opposite roles in lateral root formation, and nematode and Rhizobial symbioses. Plant J., 2004. 38(2): p. 203-14 [PMID:15078325] - Deeken R, et al.
An integrated view of gene expression and solute profiles of Arabidopsis tumors: a genome-wide approach. Plant Cell, 2006. 18(12): p. 3617-34 [PMID:17172353] - Kowalska M, et al.
Vacuolar and cytosolic cytokinin dehydrogenases of Arabidopsis thaliana: heterologous expression, purification and properties. Phytochemistry, 2010. 71(17-18): p. 1970-8 [PMID:20825956] - Gajdosová S, et al.
Distribution, biological activities, metabolism, and the conceivable function of cis-zeatin-type cytokinins in plants. J. Exp. Bot., 2011. 62(8): p. 2827-40 [PMID:21282330] - Xu X, et al.
Genome sequence and analysis of the tuber crop potato. Nature, 2011. 475(7355): p. 189-95 [PMID:21743474] - Xiao D, et al.
SENESCENCE-SUPPRESSED PROTEIN PHOSPHATASE Directly Interacts with the Cytoplasmic Domain of SENESCENCE-ASSOCIATED RECEPTOR-LIKE KINASE and Negatively Regulates Leaf Senescence in Arabidopsis. Plant Physiol., 2015. 169(2): p. 1275-91 [PMID:26304848] - Han Y,Jiao Y
APETALA1 establishes determinate floral meristem through regulating cytokinins homeostasis in Arabidopsis. Plant Signal Behav, 2015. 10(11): p. e989039 [PMID:26359644] - Pernisova M, et al.
Cytokinins influence root gravitropism via differential regulation of auxin transporter expression and localization in Arabidopsis. New Phytol., 2016. 212(2): p. 497-509 [PMID:27322763] - Farber M,Attia Z,Weiss D
Cytokinin activity increases stomatal density and transpiration rate in tomato. J. Exp. Bot., 2016. 67(22): p. 6351-6362 [PMID:27811005]
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