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 678463104
Organism
Utricularia gibba
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Lamiales; Lentibulariaceae; Utricularia
Family MYB_related
Protein Properties Length: 368aa    MW: 40913.2 Da    PI: 8.217
Description MYB_related family protein
Gene Model
Gene Model ID Type Source Coding Sequence
678463104genomeUGSPView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1Myb_DNA-binding24.66e-081750135
                     TSSS-HHHHHHHHHHHHHTTTT-HHHHHHHHTTTS CS
  Myb_DNA-binding  1 rgrWTteEdellvdavkqlGggtWktIartmgkgR 35
                     +g+WT+eEd  lv +v+++G+g+ +++ r  g + 
        678463104 17 KGPWTPEEDIVLVSYVQEHGPGNCRAVRRNTG-RQ 50
                     79********************9888888777.55 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SuperFamilySSF466891.72E-51146IPR009057Homeodomain-like
Gene3DG3DSA:1.10.10.601.4E-71649IPR009057Homeodomain-like
PfamPF002491.5E-51755IPR001005SANT/Myb domain
CDDcd001670.003041956No hitNo description
Gene3DG3DSA:3.60.15.103.3E-40103344IPR001279Metallo-beta-lactamase
SuperFamilySSF562812.71E-34119344IPR001279Metallo-beta-lactamase
PfamPF127069.8E-13135337IPR001279Metallo-beta-lactamase
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0034414Biological ProcesstRNA 3'-trailer cleavage, endonucleolytic
GO:0003677Molecular FunctionDNA binding
GO:0042781Molecular Function3'-tRNA processing endoribonuclease activity
Sequence ? help Back to Top
Protein Sequence    Length: 368 aa     Download sequence    Send to blast
MAPMGRVRGL IKVESKKGPW TPEEDIVLVS YVQEHGPGNC RAVRRNTGRQ AGENCIIGLM  60
DTLKGGDQNS HESTDGKLEK HRKKKKKANA TEGALTLEGY SICGLSIAGQ ETCVILPNLK  120
LAFDIGKCPQ RAVSQQFLFI SHGHMDHIGG LPMYVATRGL CKMVPPSVFV PKTIKGSVEK  180
IFEAHRAMDQ SELNHTLIGL DAGEEFYIRR DIKVKAFRTY HTIPSQGYII YSVKQKLKPV  240
YSMLPETDIK SMRLSGVEVT DTQVSPEVAF TGDTMSDFIT DPNNADVLRA KILIMESTFI  300
DDCCTVEDAR EYGHTHLSEI IKYADRFQNK AIVLIHFSAR YDIHTIEKAI TTLPLPLAGR  360
VFALTNGF
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
1ww1_A3e-121013412249tRNase Z
1ww1_B3e-121013412249tRNase Z
2e7y_A3e-121013412249tRNase Z
2e7y_B3e-121013412249tRNase Z
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtZinc phosphodiesterase, which displays tRNA 3'-processing endonuclease activity (PubMed:12032089, PubMed:16118225, PubMed:18052196, PubMed:19411372). Involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA (PubMed:12032089, PubMed:18052196, PubMed:19411372). Can use bis-(p-nitophenyl) phosphate (bpNPP) as substrate (PubMed:18052196). Involved in the processing of small nucleolar RNAs (snoRNAs) (PubMed:19420328). {ECO:0000269|PubMed:12032089, ECO:0000269|PubMed:16118225, ECO:0000269|PubMed:18052196, ECO:0000269|PubMed:19411372, ECO:0000269|PubMed:19420328}.
Cis-element ? help Back to Top
SourceLink
PlantRegMap678463104
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_012839402.11e-162PREDICTED: nuclear ribonuclease Z
SwissprotQ8LGU71e-136RNZ1_ARATH; tRNase Z TRZ1
TrEMBLS8DE181e-165S8DE18_9LAMI; Uncharacterized protein
STRINGMigut.I00132.1.p1e-161(Erythranthe guttata)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT5G62470.12e-15myb domain protein 96
Publications ? help Back to Top
  1. Schiffer S,Rösch S,Marchfelder A
    Assigning a function to a conserved group of proteins: the tRNA 3'-processing enzymes.
    EMBO J., 2002. 21(11): p. 2769-77
    [PMID:12032089]
  2. Späth B, et al.
    Analysis of the functional modules of the tRNA 3' endonuclease (tRNase Z).
    J. Biol. Chem., 2005. 280(42): p. 35440-7
    [PMID:16118225]
  3. Vogel A,Schilling O,Späth B,Marchfelder A
    The tRNase Z family of proteins: physiological functions, substrate specificity and structural properties.
    Biol. Chem., 2005. 386(12): p. 1253-64
    [PMID:16336119]
  4. Späth B, et al.
    Metal requirements and phosphodiesterase activity of tRNase Z enzymes.
    Biochemistry, 2007. 46(51): p. 14742-50
    [PMID:18052196]
  5. Canino G, et al.
    Arabidopsis encodes four tRNase Z enzymes.
    Plant Physiol., 2009. 150(3): p. 1494-502
    [PMID:19411372]
  6. Barbezier N, et al.
    Processing of a dicistronic tRNA-snoRNA precursor: combined analysis in vitro and in vivo reveals alternate pathways and coupling to assembly of snoRNP.
    Plant Physiol., 2009. 150(3): p. 1598-610
    [PMID:19420328]
  7. Fan L, et al.
    A survey of green plant tRNA 3'-end processing enzyme tRNase Zs, homologs of the candidate prostate cancer susceptibility protein ELAC2.
    BMC Evol. Biol., 2011. 11: p. 219
    [PMID:21781332]