PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
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(e.g., LFY)
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID Migut.H00513.1.p
Common NameMIMGU_mgv1a000212mg
Organism
Mimulus guttatus
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Lamiales; Phrymaceae; Erythranthe
Family C2H2
Protein Properties Length: 1427aa    MW: 161378 Da    PI: 6.8374
Description C2H2 family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Migut.H00513.1.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1zf-C2H213.90.00016799822123
                       EEETTTTEEESSHHHHHHHHHH.T CS
           zf-C2H2   1 ykCpdCgksFsrksnLkrHirt.H 23 
                       y+C +C +sF++k  L+ H +  H
  Migut.H00513.1.p 799 YVCAICLESFTNKKVLEAHVQErH 822
                       9******************99886 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM003555.3765788IPR015880Zinc finger, C2H2-like
PROSITE profilePS501578.6765793IPR007087Zinc finger, C2H2
PROSITE patternPS000280767788IPR007087Zinc finger, C2H2
SMARTSM003550.025799822IPR015880Zinc finger, C2H2-like
PROSITE profilePS501578.85799822IPR007087Zinc finger, C2H2
PROSITE patternPS000280801823IPR007087Zinc finger, C2H2
SMARTSM003550.88833856IPR015880Zinc finger, C2H2-like
PROSITE patternPS000280835856IPR007087Zinc finger, C2H2
SMARTSM003551.7886909IPR015880Zinc finger, C2H2-like
PROSITE profilePS501579.619886914IPR007087Zinc finger, C2H2
PROSITE patternPS000280888909IPR007087Zinc finger, C2H2
SuperFamilySSF821991.44E-7411291416No hitNo description
Gene3DG3DSA:2.170.270.102.5E-8011301425No hitNo description
SMARTSM004688.3E-511361255IPR007728Pre-SET domain
PfamPF050332.3E-1211391263IPR007728Pre-SET domain
PROSITE profilePS508679.16911921268IPR007728Pre-SET domain
PROSITE profilePS5028019.36712711403IPR001214SET domain
SMARTSM003171.1E-4012711409IPR001214SET domain
PfamPF008561.2E-2012821401IPR001214SET domain
PROSITE profilePS508689.69114101426IPR003616Post-SET domain
SMARTSM005080.003514101426IPR003616Post-SET domain
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006342Biological Processchromatin silencing
GO:1900109Biological Processregulation of histone H3-K9 dimethylation
GO:0005634Cellular Componentnucleus
GO:0005694Cellular Componentchromosome
GO:0005515Molecular Functionprotein binding
GO:0008270Molecular Functionzinc ion binding
GO:0018024Molecular Functionhistone-lysine N-methyltransferase activity
GO:0043565Molecular Functionsequence-specific DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 1427 aa     Download sequence    Send to blast
MMETLPCSGA RRIEESDAEP VRSDLKVDDL ITIDVGESHD VREGEGHLIF EGFPALEENS  60
NVDAYDEFEV DGQNLSCYSH DSGDDNLDKN DDFAGPELTL ESSHLVLETI ESELLNNNQE  120
GSSHPEIKSL ERDEPQAVWV KWRGKWQSGI RCARADWPLA TLKAKPTHDR KQYLVIFFPR  180
TRNYSWADVL LVRPINEYPH PIAYKTHKVG AKMVNDLTLA RRFIMQKLAV SMLNILDQLN  240
REALEEMSRN VMVLKDFAME ASRCKDYSDL GRMLSKLQNM ILQRCITSDW IHQSMQSWKQ  300
RCQDANSAEC IELLKEELTD SILWNEVNLP SGESAQADLG SDWKSWKHEV MKWFSVSHPI  360
STAVDSDQPK NDSPLTTGLQ LTRKRPKLEV RRPDAHASSS HQSVSVETDS AYFNGYSQNL  420
KSNPIEDTVV GPSPSGVVSK LSDIFVAAGN SELTPRTVVT QSHNRQCVAF IESKGRQCVR  480
YASEGDVYCC VHLSSRFVAS SVKVEATSSV DSPMCGGTTV LGTKCKHRAL VGGSFCKKHR  540
PHDGKNTISP VNKLKRKIEE NLMYTGTRID ESPVHIDPLL DVREYSIQEN SMSEPPQQVR  600
SGAEVAQCIG SWPHGGGVEE PCLESPKRHS LYCEKHIPNW LKRARNGKSR IISKEVFIEI  660
LKNCHSRERK LQLHQACELF YRLFKSVLSL RNPVPKDVQF QWAITEASKD ARVGDFLMKL  720
VSSEKERLKK LWEIEDGQAK STVEELVPIP VQTTNDISDN QENDIKCKIC SEEFLDDQAL  780
GTHWMNSHKK EAQWLFRGYV CAICLESFTN KKVLEAHVQE RHHSQFVEQC MLLQCIPCGS  840
HFGNPDELWL HVQSIHPRNL RLSEQKEEIL AEQTKPENQN SVNRRFICRF CGLKFDLLPD  900
LGRHHQAAHM GAQNSTGPRL TKKGIQFYAR KLKSGRLTRP RFKKGLNSAA SYKIRNRSVQ  960
NLKKRIQASN SIGSPIEIAV QSAIPETSTL GRLADSQCSA IAKILISEIK KTKPRPSSSE  1020
ILSVATSACC RVSLKASLEV KYGTLPESLY LKAAKLCSEH NILVQWHREG YICPKGCTSS  1080
LMSTILSPLS ENPFKARSSV QTSYPMNSEW TMDECHIVID SRHFSMDLSE KNIVLCDDIS  1140
FGKESVPIAC VVDENFLNGQ ISEYSFPWES FTYVTKPLLD QSLVLETESL QLGCACANST  1200
CSAETCDHVY LFDNDYEDAK DIYGKPMNGR FPYDERGRII LEEGYLVYEC NQRCCCGKAC  1260
RNRVLQNGVK VKLEIFKTDK KGWAVRARQA IPRGTFVCEY IGEVIDETEA NERRNRYDKE  1320
GCRYFYEIDA HINDMSRLIE GQVPYVIDAT NYGNVSRYVN HSCSPNLVNH QVLVESMDSQ  1380
LAHIGFYASR DIALGEELTY DFRYKLLTGE GSPCLCGASN CRGRLY*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2o8j_A2e-46113414229264Histone-lysine N-methyltransferase, H3 lysine-9 specific 3
2o8j_B2e-46113414229264Histone-lysine N-methyltransferase, H3 lysine-9 specific 3
2o8j_C2e-46113414229264Histone-lysine N-methyltransferase, H3 lysine-9 specific 3
2o8j_D2e-46113414229264Histone-lysine N-methyltransferase, H3 lysine-9 specific 3
4nvq_A3e-461134142213268Histone-lysine N-methyltransferase EHMT2
4nvq_B3e-461134142213268Histone-lysine N-methyltransferase EHMT2
5t0k_A2e-46113414229264Histone-lysine N-methyltransferase EHMT2
5t0k_B2e-46113414229264Histone-lysine N-methyltransferase EHMT2
5t0m_A2e-46113414229264Histone-lysine N-methyltransferase EHMT2
5t0m_B2e-46113414229264Histone-lysine N-methyltransferase EHMT2
5tuy_A2e-46113414221256Histone-lysine N-methyltransferase EHMT2
5tuy_B2e-46113414221256Histone-lysine N-methyltransferase EHMT2
5v9i_A3e-461134142211266Histone-lysine N-methyltransferase EHMT2
5v9i_B3e-461134142211266Histone-lysine N-methyltransferase EHMT2
5v9i_C3e-461134142211266Histone-lysine N-methyltransferase EHMT2
5v9i_D3e-461134142211266Histone-lysine N-methyltransferase EHMT2
5vsc_A2e-46113414226261Histone-lysine N-methyltransferase EHMT2
5vsc_B2e-46113414226261Histone-lysine N-methyltransferase EHMT2
5vse_A2e-46113414226261Histone-lysine N-methyltransferase EHMT2
5vse_B2e-46113414226261Histone-lysine N-methyltransferase EHMT2
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtHistone methyltransferase that functions together with its binding partner LDL1/SWP1 as one of the regulators of flower timing in Arabidopsis (PubMed:17224141). Mediates H3K9me2 deposition and regulates gene expression in a DNA methylation-independent manner. Binds DNA through its zinc fingers and represses the expression of a subset of stimulus response genes. May represent a novel mechanism for plants to regulate their chromatin and transcriptional state, which may allow for the adaptability and modulation necessary to rapidly respond to environment or developmental cues (PubMed:23071452). {ECO:0000269|PubMed:17224141, ECO:0000269|PubMed:23071452}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapMigut.H00513.1.p
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankAC1825700.0AC182570.2 Erythranthe guttata clone MGBa-64L10, complete sequence.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_012852709.10.0PREDICTED: histone-lysine N-methyltransferase SUVR5
RefseqXP_012852716.10.0PREDICTED: histone-lysine N-methyltransferase SUVR5
RefseqXP_012852725.10.0PREDICTED: histone-lysine N-methyltransferase SUVR5
SwissprotO648270.0SUVR5_ARATH; Histone-lysine N-methyltransferase SUVR5
TrEMBLA0A022RX440.0A0A022RX44_ERYGU; Uncharacterized protein
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
AsteridsOGEA932334
Publications ? help Back to Top
  1. Baumbusch LO, et al.
    The Arabidopsis thaliana genome contains at least 29 active genes encoding SET domain proteins that can be assigned to four evolutionarily conserved classes.
    Nucleic Acids Res., 2001. 29(21): p. 4319-33
    [PMID:11691919]
  2. Caro E, et al.
    The SET-domain protein SUVR5 mediates H3K9me2 deposition and silencing at stimulus response genes in a DNA methylation-independent manner.
    PLoS Genet., 2012. 8(10): p. e1002995
    [PMID:23071452]