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 Kalax.0508s0018.1.p
Organism
Kalanchoe marnieriana
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; Saxifragales; Crassulaceae; Kalanchoe
Family C2H2
Protein Properties Length: 612aa    MW: 68193.7 Da    PI: 4.1916
Description C2H2 family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Kalax.0508s0018.1.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1zf-C2H212.30.00051115133220
                          EETTTTEEESSHHHHHHHH CS
              zf-C2H2   2 kCpdCgksFsrksnLkrHi 20 
                          kC +C+ sF+++ +L+ H+
  Kalax.0508s0018.1.p 115 KCWICNLSFPSSQELQAHL 133
                          7*****************7 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SuperFamilySSF576677.02E-3244173No hitNo description
PfamPF127564.5E-861134IPR015880Zinc finger, C2H2-like
PROSITE profilePS5167874.264253568IPR025799Protein arginine N-methyltransferase
Gene3DG3DSA:3.40.50.1501.5E-32254412IPR029063S-adenosyl-L-methionine-dependent methyltransferase
SuperFamilySSF533357.19E-59260555IPR029063S-adenosyl-L-methionine-dependent methyltransferase
PfamPF136497.1E-8296409No hitNo description
CDDcd024404.19E-9297412No hitNo description
Gene3DG3DSA:2.70.160.111.9E-43416594No hitNo description
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006479Biological Processprotein methylation
GO:0005829Cellular Componentcytosol
GO:0008168Molecular Functionmethyltransferase activity
Sequence ? help Back to Top
Protein Sequence    Length: 612 aa     Download sequence    Send to blast
MEFQMLVPAE MEHVPNLVAP EEEDNDEIDD DVEEQGWDDW RAGSDGGAED EEGDPEPDML  60
CLFCDSVFTS RDDIFGHCAG AHRFDFSELR KKLGLDFYAC FKLLNYIRIQ VAERKCWICN  120
LSFPSSQELQ AHLHPTVDFN RSNLPWEDDK YLSPFIQDDP LLYIFGEDED DVDYPNEEDR  180
EELIKEIELL KVDDIINELS IRNDNLKTCT VNGLTDRPST SDGSFKPYNE TAEDRDSKIP  240
LSNAVTVQIK NANRSYFGGY SSFVIHREMI SDKVRTDAYR DAILGNPCLF NGAILMDVGC  300
GTGILSLFAV QAGASRVIAV EASEKMASVA TQIAKDNALL WEKSPGLNSK GNGGIQVVQG  360
MIEEINDFDG ILPNSVDVLI SEWMGYCLLY ETMLNSVLFA RDRWLKPGGA VLPDTATMFV  420
AGFGKGATSI PFWDNVYGFN MSCIGTEVVE HASKNPIVDV VDSEDIVTNS VVLKAFDLAT  480
VTPEELDFTT SVALEPKSND VTWCYGLVLW FDTNFTSRFC KEKQTVLSTS PFTQKTHWSQ  540
TILTFREPVA LFSGEPSAKL MSDGVTPWAK MLARISIARA AQHRSIDISL EVTATSLDGR  600
KNRLPAQLFT L*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
6nt2_A6e-7025655553329Protein arginine N-methyltransferase 1
6nt2_B6e-7025655553329Protein arginine N-methyltransferase 1
6nt2_C6e-7025655553329Protein arginine N-methyltransferase 1
6nt2_D6e-7025655553329Protein arginine N-methyltransferase 1
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtMethylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins. {ECO:0000250}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_010659086.10.0PREDICTED: probable protein arginine N-methyltransferase 3
SwissprotQ0WVD60.0ANM3_ARATH; Probable protein arginine N-methyltransferase 3
TrEMBLF6HVC80.0F6HVC8_VITVI; Uncharacterized protein
STRINGVIT_13s0084g00650.t010.0(Vitis vinifera)
Publications ? help Back to Top
  1. Krause CD, et al.
    Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential.
    Pharmacol. Ther., 2007. 113(1): p. 50-87
    [PMID:17005254]
  2. Hang R, et al.
    Arabidopsis protein arginine methyltransferase 3 is required for ribosome biogenesis by affecting precursor ribosomal RNA processing.
    Proc. Natl. Acad. Sci. U.S.A., 2014. 111(45): p. 16190-5
    [PMID:25352672]