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 HL.SW.v1.0.G014497.1
Organism
Humulus lupulus
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Cannabaceae; Humulus
Family Trihelix
Protein Properties Length: 785aa    MW: 86577 Da    PI: 8.0986
Description Trihelix family protein
Gene Model
Gene Model ID Type Source Coding Sequence
HL.SW.v1.0.G014497.1genomeHOPBASEView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1Myb_DNA-binding24.56.3e-08690747146
                           TSSS-HHHHHHHHHHHHHTTTT.........-HHHHHHHHT...TTS-HHHHHHHHHH CS
       Myb_DNA-binding   1 rgrWTteEdellvdavkqlGgg.........tWktIartmg...kgRtlkqcksrwqk 46 
                           r++W+ +E ++l+++  ql g+          W+ I++++     +R++ qcksrw +
  HL.SW.v1.0.G014497.1 690 RNKWSNQEVKKLIELRGQLDGRfqvvkgrmaLWEEISKELLsdgMNRSPGQCKSRWTS 747
                           79******************************************9***********76 PP
2trihelix71.51.5e-22692772186
              trihelix   1 rWtkqevlaLiearremeerlrrgklkkplWeevskkmrergferspkqCkekwenlnkrykkikegekkrtsessstcpyfdqle 86 
                           +W++qev++Lie+r +++ r++  k +++lWee+sk + + g++rsp qCk++w +l ++y+ +k g+k++     +++p+f++++
  HL.SW.v1.0.G014497.1 692 KWSNQEVKKLIELRGQLDGRFQVVKGRMALWEEISKELLSDGMNRSPGQCKSRWTSLVQEYEDTKSGKKNN-----KSWPHFEDMD 772
                           7*******************************************************************984.....56*******8 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
Gene3DG3DSA:3.60.15.101.8E-66103353IPR001279Metallo-beta-lactamase
SuperFamilySSF562812.62E-54104369IPR001279Metallo-beta-lactamase
SMARTSM008495.1E-24116313IPR001279Metallo-beta-lactamase
PfamPF127064.7E-10128263IPR001279Metallo-beta-lactamase
PROSITE profilePS500909.477685749IPR017877Myb-like domain
Gene3DG3DSA:1.10.10.601.3E-7686750IPR009057Homeodomain-like
SuperFamilySSF466892.85E-5688750IPR009057Homeodomain-like
SMARTSM007173.2E-7689751IPR001005SANT/Myb domain
PfamPF138379.3E-21690774No hitNo description
CDDcd122037.20E-21691756No hitNo description
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0009658Biological Processchloroplast organization
GO:0009942Biological Processlongitudinal axis specification
GO:0060918Biological Processauxin transport
GO:0009507Cellular Componentchloroplast
GO:0003677Molecular FunctionDNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 785 aa     Download sequence    Send to blast
MKLELLGGFS PSLSSSSSSS SFFSPKMMAL GSLSLCPCSL LWRPNFTRRS VSCSIGSPNA  60
VGASKSNASA RRRPGRKEGP RKSMEDSVQR KMEQFYEGRE GPPIRVLPIG GLGEIGMNCM  120
LVGNYDRYIL IDAGVMFPDY DELGVQKIIP DTTFIKRWSH KIEAVIITHG HEDHIGALPW  180
VIPALDSNTP IFASSFTMEL IRKRLKENGI FVSSRLKVFR TKRKFMAGPF EIEPLRVTHS  240
IPDCCGLVLR CADGTILHTG DWKIDESPLD GKVFDREGLE ELAKEGVTLM MSDSTNVLSP  300
GRTTSESHVA DALLRHISAA KGRVITTQFA SNIHRLGSVK AAADLTGRKL VFVGMSLRTY  360
LDAAFKDGKA PIDPSSLVKV EDIEAYAPKD LLIVTTEPRA ALNLASFGSS HSLKLNEEDL  420
IFHNIFCQYM ENFCSSKSMN CLGNQPVSGT LLMEILRPQN VNGLSENTIK GKIRITTRCL  480
WLDKGKLLDA LHKAAHAALS SCPVNCPLAH MERTVSEVLR KLVRKYSGKR PEVIAIALEN  540
PAAVISDEVS ARLSGKSHVG FETSALNRKI DGHPNKGKSN KVQAEVEKRN SNLDINLQQD  600
LGGDGVEMEL LPEEETTTST SDSDMLSSDS KESDEFWKPF TGSAIPVDNV VEENNGSIPS  660
QEQSLLDKVG KESIETTTDP KPKPSKPVKR NKWSNQEVKK LIELRGQLDG RFQVVKGRMA  720
LWEEISKELL SDGMNRSPGQ CKSRWTSLVQ EYEDTKSGKK NNKSWPHFED MDKILSNSEA  780
IEAK*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
3bk1_A7e-5610442217343Metal dependent hydrolase
3bk2_A7e-5610442217343Metal dependent hydrolase
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtEssential protein required during embryogenesis, especially in initiating and maintaining the organization of shoot apical meristems (SAMs), cotyledons, and hypocotyls (PubMed:15266054, PubMed:25871650). Involved in auxin-mediated pathways during embryogenesis (PubMed:25871650). RNase that has both endonuclease and 5'-3' exonuclease activities. Involved in RNA surveillance to prevent overaccumulation of antisense RNA (PubMed:22033332). Probably involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay (By similarity). {ECO:0000250|UniProtKB:Q72JJ7, ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:22033332, ECO:0000269|PubMed:25871650}.
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By light. {ECO:0000269|PubMed:25871650}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankKP2295890.0KP229589.1 UNVERIFIED: Boehmeria nivea MYB transcription factor-like (MYB33) mRNA, complete sequence.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_015866975.10.0uncharacterized protein LOC107404538
SwissprotQ84W560.0RNJ_ARATH; Ribonuclease J
TrEMBLA0A2P5DVM70.0A0A2P5DVM7_PARAD; Ribonuclease J
STRINGXP_010105237.10.0(Morus notabilis)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF50993450
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT5G63420.10.0Trihelix family protein
Publications ? help Back to Top
  1. Bryant N,Lloyd J,Sweeney C,Myouga F,Meinke D
    Identification of nuclear genes encoding chloroplast-localized proteins required for embryo development in Arabidopsis.
    Plant Physiol., 2011. 155(4): p. 1678-89
    [PMID:21139083]
  2. Halpert M,Liveanu V,Glaser F,Schuster G
    The Arabidopsis chloroplast RNase J displays both exo- and robust endonucleolytic activities.
    Plant Mol. Biol., 2019. 99(1-2): p. 17-29
    [PMID:30511330]