PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID Tp57577_TGAC_v2_mRNA38618
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; Trifolieae; Trifolium
Family NAC
Protein Properties Length: 1804aa    MW: 202296 Da    PI: 4.9832
Description NAC family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Tp57577_TGAC_v2_mRNA38618genomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1NAM148.53.5e-46131014372129
                        NAM    2 ppGfrFhPtdeelvveyLkkkvegkkleleevikevdiykvePwdLp.k.kvkaeekewyfFskrdkkyatgkrknratksg 81  
                                  pGfrFhPt  el++++Lk+kv gkk++  +vi+e+diyk+ PwdLp k  +++++ ewyfF++ +kky +g r nrat+ g
  Tp57577_TGAC_v2_mRNA38618 1310 IPGFRFHPTGVELMKYFLKRKVMGKKFHN-NVIAELDIYKYSPWDLPdKsYLQNGDLEWYFFCPIEKKYGSGARMNRATEIG 1390
                                 79************************999.99**************96446667778************************* PP

                        NAM   82 yWkatgkdkevlskkgelvglkktLvfykgrapkgektdWvmheyrle 129 
                                 +Wkatgkd++v   k+++vg+ ktL+f++g+ap+g +tdWvmheyrle
  Tp57577_TGAC_v2_mRNA38618 1391 FWKATGKDRAVQY-KNQTVGMIKTLIFHTGKAPRGDRTDWVMHEYRLE 1437
                                 ************9.8999****************************85 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SuperFamilySSF533835.17E-8104183IPR015424Pyridoxal phosphate-dependent transferase
Gene3DG3DSA:3.40.640.101.2E-10126183IPR015421Pyridoxal phosphate-dependent transferase, major region, subdomain 1
Gene3DG3DSA:3.40.640.101.2E-6208271IPR015421Pyridoxal phosphate-dependent transferase, major region, subdomain 1
SuperFamilySSF483716.33E-7296368IPR016024Armadillo-type fold
Gene3DG3DSA:1.25.40.702.4E-7298370IPR001263Phosphoinositide 3-kinase, accessory (PIK) domain
Gene3DG3DSA:3.30.1010.101.5E-37771865No hitNo description
SuperFamilySSF561128.36E-74796860IPR011009Protein kinase-like domain
CDDcd051681.98E-15810371299No hitNo description
SuperFamilySSF561128.36E-7410591300IPR011009Protein kinase-like domain
Gene3DG3DSA:3.30.1010.101.5E-3710661111No hitNo description
PROSITE profilePS5029055.54710671297IPR000403Phosphatidylinositol 3-/4-kinase, catalytic domain
SMARTSM001464.5E-7310681329IPR000403Phosphatidylinositol 3-/4-kinase, catalytic domain
PfamPF004543.2E-3010681275IPR000403Phosphatidylinositol 3-/4-kinase, catalytic domain
PROSITE patternPS00915010711085IPR018936Phosphatidylinositol 3/4-kinase, conserved site
Gene3DG3DSA:1.10.1070.111.1E-6411121298IPR000403Phosphatidylinositol 3-/4-kinase, catalytic domain
SuperFamilySSF1019416.15E-5613031459IPR003441NAC domain
PROSITE profilePS5100553.28313091459IPR003441NAC domain
PfamPF023652.8E-2213111436IPR003441NAC domain
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0009860Biological Processpollen tube growth
GO:0048768Biological Processroot hair cell tip growth
GO:0005634Cellular Componentnucleus
GO:0005829Cellular Componentcytosol
GO:0005886Cellular Componentplasma membrane
GO:0030659Cellular Componentcytoplasmic vesicle membrane
GO:0035619Cellular Componentroot hair tip
GO:0003677Molecular FunctionDNA binding
GO:0004430Molecular Function1-phosphatidylinositol 4-kinase activity
GO:0017137Molecular FunctionRab GTPase binding
GO:0043424Molecular Functionprotein histidine kinase binding
Sequence ? help Back to Top
Protein Sequence    Length: 1804 aa     Download sequence    Send to blast
MFHYINNIIH HYIQFFIMEL EQPLLVDIIH MLAQSQNIKA KNEVSVPLSK TNSILETSHD  60
FCYHPESFKK LVEMDLPCNE SVEEKLSWLR SQIVGNDEEF DSSFGRRKLV YADHTASGRS  120
LRYNENFIIN HLLPFYGNTH TCDSYVGSRT TKMLHEATEY IKKCLGGGED DAIIFCGSGT  180
TAAIKRLQEV MGIAVPSILR XXLEADGPYV EIDMRSGDID GYDAVFLSPH KFLGGPDSPG  240
VLLMNMALYR LGSSPPSTCG GGTVTYVNAF NEKVNLILFF DSSFFCEWIA VSYLYKHDHA  300
GVRDYLCNRM YTLPLQGLES YLFQICYMTI HKPSPSLDKF VIDMCSKSLK IALKVHWFLM  360
AELEDSDDND GISRIQEKCQ MAATLMGEWP PLIRPHTEPP SPGGKSQVLN RLLSSKNRLL  420
SLTTSPPKSL SFSSSPGNNL QDDGNPLSPD ENRIFKKFMP SPKVRDALLF RKSADKDDGD  480
SEKDGFFKRL LRDSKGDDEL GQKIRDAFHF RKSSEKDALD SEKENFFKRF LRDSKDSTRG  540
DDDDSEKDGF FQRILRDSRS EDEDVTSSSE GFFKKLFRDS KNDPEDRIST KTVEDEEKNG  600
LFRKFFREKF EDRKDGRDRN DNRNVANSEE NCSKPDEEDE KDGFFRKFFK DKFEDKKDTK  660
DKIEEGTANG EEEEPSEVSL FKRLFRVHPE DDQSSPANEN SNNGGLFQSS PGTENFFRKL  720
FKDRDRSIED SELLGSKRQK EKHPGTPKQH SEKSSTKPPL PINPTQFRKG AYHDSLEFVQ  780
SLCDTSYGLV DVFPIEDRKS ALQESLREIN IHVKEVQNTG GVCFPLGKGM YRVLHMPVDE  840
AILLNSREKA PYMICIEVLR CEMPSNFKEA SSSQKLSQGG IPLANGDAFL QKPPPWAYPL  900
WSAQEVYRNS NDRMSRSTAQ AIDQAMTHVS EPKIKLVSLN LSVETRYNGQ EGAEHDSDLE  960
WVRVVLTADP GVRLEDIEDQ APPRKKEHRR VPSTVAMEEV KAAAAKGEAP LGLPLKGAGQ  1020
DSSDAQPRAN GITPKASDAL SGELWEAKKD RVCKASIYGK LPGWDLRSII VKSGDDCRQE  1080
HLAVQLISHF YDIFQEAGLP LWLRPYEVLC TSSYTALIET IPDTASLHSI KSRYPNISSL  1140
REFFNAKYEE NSPSFKLAQR NFVESMAGYS LVCYFLQVKD RHNGNLLLDE EGHIIHIDFG  1200
FMLSNSPGGV NFESAPFKLT RELLEVMDSD AEGLPSEFFD YFKVLCIQGF LTCRKHAERI  1260
ILLVEMLQDS GFPCFKGGVR TIQNLRKRFH LNLTEENLVL ISSMAMANMI PGFRFHPTGV  1320
ELMKYFLKRK VMGKKFHNNV IAELDIYKYS PWDLPDKSYL QNGDLEWYFF CPIEKKYGSG  1380
ARMNRATEIG FWKATGKDRA VQYKNQTVGM IKTLIFHTGK APRGDRTDWV MHEYRLEDKD  1440
LADKGIVQDS YVICKVFQKE GPGPRNGAQY GRPFNEEDWS DDEVGLPLVA ESAALVPSSA  1500
LTTNSSVLND QNLHASEYGS TSMPCQLRLT PSPYPTNSCQ TGLPLSPGVV YSCQTGLMSS  1560
DTVRSCETGL LPSPDPANSC QIGLIPSPDP ASSCQMGSML PFPDPANSCQ IGSMPSLYPA  1620
NSCQTGLMPF PDPANSCQIG SMPSLYPANS CQTGLMPSPD PAYSCQTEPE NSCQTGSMPS  1680
HDPANSCQTG SMPYSDPANH SYPDNQAVNN DDILSMLDIF EDNDIFPEEN IAEGALLGDF  1740
FEGLGDLDCS ALGSFGQNAE FSTNGVATMG DVGGDDLDFV QLTDLDSELF WQSTTPGSWN  1800
QNK*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
6gl3_A1e-74990130965385Phosphatidylinositol 4-kinase beta,Phosphatidylinositol 4-kinase beta
6gl3_B1e-74990130965385Phosphatidylinositol 4-kinase beta,Phosphatidylinositol 4-kinase beta
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtActs on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5-trisphosphate. Necessary for proper organization of the trans-Golgi network (TGN) and post-Golgi secretion in root hairs. Together with PI4KB2, required during polarized root hair expansion and pollen tube elongation. Functions redundantly with PI4KB2 upstream of the cold response phosphoinositide-dependent phospholipase C (PI-PLC) pathway. {ECO:0000269|PubMed:10026194, ECO:0000269|PubMed:16567499, ECO:0000269|PubMed:19208902, ECO:0000269|PubMed:20603382, ECO:0000269|PubMed:21134079, ECO:0000269|PubMed:22318862}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapTp57577_TGAC_v2_mRNA38618
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankAC1582090.0AC158209.13 Medicago truncatula clone mth2-154h5, complete sequence.
GenBankAC1743080.0AC174308.7 Medicago truncatula clone mth2-139i23, complete sequence.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_024628995.10.0phosphatidylinositol 4-kinase beta 1 isoform X1
SwissprotQ9FMJ00.0P4KB1_ARATH; Phosphatidylinositol 4-kinase beta 1
TrEMBLA0A2K3NSZ90.0A0A2K3NSZ9_TRIPR; Phosphatidylinositol 4-kinase beta 1-like protein (Fragment)
STRINGAET047350.0(Medicago truncatula)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT5G64060.14e-81NAC domain containing protein 103
Publications ? help Back to Top
  1. Xue HW,Pical C,Brearley C,Elge S,Müller-Röber B
    A plant 126-kDa phosphatidylinositol 4-kinase with a novel repeat structure. Cloning and functional expression in baculovirus-infected insect cells.
    J. Biol. Chem., 1999. 274(9): p. 5738-45
    [PMID:10026194]
  2. Mueller-Roeber B,Pical C
    Inositol phospholipid metabolism in Arabidopsis. Characterized and putative isoforms of inositol phospholipid kinase and phosphoinositide-specific phospholipase C.
    Plant Physiol., 2002. 130(1): p. 22-46
    [PMID:12226484]
  3. Stevenson-Paulik J,Love J,Boss WF
    Differential regulation of two Arabidopsis type III phosphatidylinositol 4-kinase isoforms. A regulatory role for the pleckstrin homology domain.
    Plant Physiol., 2003. 132(2): p. 1053-64
    [PMID:12805633]
  4. Lin WH,Ye R,Ma H,Xu ZH,Xue HW
    DNA chip-based expression profile analysis indicates involvement of the phosphatidylinositol signaling pathway in multiple plant responses to hormone and abiotic treatments.
    Cell Res., 2004. 14(1): p. 34-45
    [PMID:15040888]
  5. van Leeuwen W,Okrész L,Bögre L,Munnik T
    Learning the lipid language of plant signalling.
    Trends Plant Sci., 2004. 9(8): p. 378-84
    [PMID:15358268]
  6. Preuss ML, et al.
    A role for the RabA4b effector protein PI-4Kbeta1 in polarized expansion of root hair cells in Arabidopsis thaliana.
    J. Cell Biol., 2006. 172(7): p. 991-8
    [PMID:16567499]
  7. Lou Y, et al.
    The highly charged region of plant beta-type phosphatidylinositol 4-kinase is involved in membrane targeting and phospholipid binding.
    Plant Mol. Biol., 2006. 60(5): p. 729-46
    [PMID:16649109]
  8. Davis AJ,Im YJ,Dubin JS,Tomer KB,Boss WF
    Arabidopsis phosphatidylinositol phosphate kinase 1 binds F-actin and recruits phosphatidylinositol 4-kinase beta1 to the actin cytoskeleton.
    J. Biol. Chem., 2007. 282(19): p. 14121-31
    [PMID:17379598]
  9. Szumlanski AL,Nielsen E
    The Rab GTPase RabA4d regulates pollen tube tip growth in Arabidopsis thaliana.
    Plant Cell, 2009. 21(2): p. 526-44
    [PMID:19208902]
  10. Ischebeck T, et al.
    Functional cooperativity of enzymes of phosphoinositide conversion according to synergistic effects on pectin secretion in tobacco pollen tubes.
    Mol Plant, 2010. 3(5): p. 870-81
    [PMID:20603382]
  11. Kang BH,Nielsen E,Preuss ML,Mastronarde D,Staehelin LA
    Electron tomography of RabA4b- and PI-4Kβ1-labeled trans Golgi network compartments in Arabidopsis.
    Traffic, 2011. 12(3): p. 313-29
    [PMID:21134079]
  12. Delage E,Ruelland E,Zachowski A,Puyaubert J
    Eat in or take away? How phosphatidylinositol 4-kinases feed the phospholipase C pathway with substrate.
    Plant Signal Behav, 2012. 7(9): p. 1197-9
    [PMID:22899063]
  13. Sašek V, et al.
    Constitutive salicylic acid accumulation in pi4kIIIβ1β2 Arabidopsis plants stunts rosette but not root growth.
    New Phytol., 2014. 203(3): p. 805-16
    [PMID:24758581]
  14. Janda M,Šašek V,Ruelland E
    The Arabidopsis pi4kIIIβ1β2 double mutant is salicylic acid-overaccumulating: a new example of salicylic acid influence on plant stature.
    Plant Signal Behav, 2014. 9(12): p. e977210
    [PMID:25482755]
  15. Antignani V, et al.
    Recruitment of PLANT U-BOX13 and the PI4Kβ1/β2 phosphatidylinositol-4 kinases by the small GTPase RabA4B plays important roles during salicylic acid-mediated plant defense signaling in Arabidopsis.
    Plant Cell, 2015. 27(1): p. 243-61
    [PMID:25634989]