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 Pbr011696.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Rosaceae; Maloideae; Maleae; Pyrus
Family bHLH
Protein Properties Length: 2469aa    MW: 273971 Da    PI: 5.3919
Description bHLH family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Pbr011696.1genomeCPETRView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1HLH33.38.8e-11596641555
                  HHHHHHHHHHHHHHHHHHHHCTSCCC...TTS-STCHHHHHHHHHHHHHHH CS
          HLH   5 hnerErrRRdriNsafeeLrellPkaskapskKlsKaeiLekAveYIksLq 55 
                  h+++Er RR++i +++ +L+el+Pk+      + +Ka++L + +eY++ Lq
  Pbr011696.1 596 HSIAERLRREKISDRMKNLQELVPKS-----NRTDKASMLDEIIEYVRFLQ 641
                  99***********************7.....59*****************9 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
Gene3DG3DSA:3.30.40.109.0E-5116184IPR013083Zinc finger, RING/FYVE/PHD-type
SuperFamilySSF578508.12E-14120202No hitNo description
PROSITE profilePS500899.996125171IPR001841Zinc finger, RING-type
PROSITE patternPS005180143152IPR017907Zinc finger, RING-type, conserved site
SMARTSM006471.2E-12193255IPR002867IBR domain
SuperFamilySSF578502.51E-5200260No hitNo description
PfamPF014858.1E-9207255IPR002867IBR domain
SuperFamilySSF578503.35E-6266304No hitNo description
SuperFamilySSF474593.79E-14589646IPR011598Myc-type, basic helix-loop-helix (bHLH) domain
CDDcd000831.01E-11589645No hitNo description
PROSITE profilePS5088816.66591640IPR011598Myc-type, basic helix-loop-helix (bHLH) domain
Gene3DG3DSA:4.10.280.102.6E-14593645IPR011598Myc-type, basic helix-loop-helix (bHLH) domain
PfamPF000104.7E-8596641IPR011598Myc-type, basic helix-loop-helix (bHLH) domain
SMARTSM003532.6E-12597646IPR011598Myc-type, basic helix-loop-helix (bHLH) domain
SMARTSM000641.5E-18675750IPR000306FYVE zinc finger
SuperFamilySSF579031.2E-18678750IPR011011Zinc finger, FYVE/PHD-type
Gene3DG3DSA:3.30.40.106.4E-20679750IPR013083Zinc finger, RING/FYVE/PHD-type
PfamPF013632.2E-16680748IPR000306FYVE zinc finger
PROSITE profilePS5017812.586683749IPR017455Zinc finger, FYVE-related
CDDcd033345.66E-13310341306No hitNo description
PfamPF001189.5E-3110541303IPR002423Chaperonin Cpn60/TCP-1 family
Gene3DG3DSA:3.50.7.107.5E-4810991271IPR027409GroEL-like apical domain
SuperFamilySSF520296.28E-4111001272IPR027409GroEL-like apical domain
PROSITE profilePS5145559.79921142438IPR002498Phosphatidylinositol-4-phosphate 5-kinase, core
SMARTSM003302.6E-13021482439IPR002498Phosphatidylinositol-4-phosphate 5-kinase, core
SuperFamilySSF561044.38E-7921592438No hitNo description
Gene3DG3DSA:3.30.800.102.0E-2721712295IPR027484Phosphatidylinositol-4-phosphate 5-kinase, N-terminal domain
PfamPF015042.2E-4622142436IPR002498Phosphatidylinositol-4-phosphate 5-kinase, core
Gene3DG3DSA:3.30.810.105.4E-2022992378IPR027483Phosphatidylinositol-4-phosphate 5-kinase, C-terminal
Gene3DG3DSA:3.30.810.109.3E-1823792438IPR027483Phosphatidylinositol-4-phosphate 5-kinase, C-terminal
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0046488Biological Processphosphatidylinositol metabolic process
GO:0005524Molecular FunctionATP binding
GO:0008270Molecular Functionzinc ion binding
GO:0016307Molecular Functionphosphatidylinositol phosphate kinase activity
GO:0046983Molecular Functionprotein dimerization activity
Sequence ? help Back to Top
Protein Sequence    Length: 2469 aa     Download sequence    Send to blast
MENPLSSHSH SRINFIDIED DTFRFTPTSR NPSINPINVD DEDRDLRSIT ASLLKSVPTP  60
AEADNFIDLS EETLDFYDGD DELRILRFKP SKTPFGRRGK GLFSDFSVTE SGQSSNSKND  120
PDFVCEICVE PKSGIESFRI ENCSHGYCTE CMVKYVASKL QENITSIRCP VPDCIGLLEP  180
EYCRPILPPK VFDQWGTALC EAVILGSEKF YCPYKDCSAM LIDDGKEVVR QSACPNCWRM  240
FCAQCKAPWH EGIECEEFLK LNKDEREKED IMLKNLAQKQ QWRRCPKCRF YVEKSMGCMF  300
MMCSLSMNVE ESFRAPKGGL NQHKSGLQAF VDKSAKGEDP FLLTMDKYIN QICSSSSWSD  360
VDAKEIPSWA CCESEQPNEA LLGSVVVVDE HENNSSPTYL TYSNSLESLV AQDVSSILQD  420
FEPDAQDGGK NCDVQNIGMH YGVDGNMVRI PLRSIAPENV GCNSFEPLLY QGFNGDFETL  480
SPISQPWPLQ SYEGVSPAPA SGMVQLKMCS FGINGDYGDY VDYVMPSDPN NLAALVTTEK  540
GMQDVQNYPL PSFPIAPRMS GLQSLPQNTS TNPVGECNGN GKPRMRARRG QATDPHSIAE  600
RLRREKISDR MKNLQELVPK SNRTDKASML DEIIEYVRFL QLQLKLSMGT PDNKLSELVD  660
IFKSWIPRRS EPPNVSRDFW MPDQSCRVCY DCDSQFTIFN RRHHCRLCGR VFCAKCTANS  720
IPAASDEPRA GREDWERIRV CYYCFHQWEQ GVAAPNNGAG PAASPGLSPS PSATSLVSTK  780
SSCTCHSSSS TIGSTPYSTG PYQHVPYSSG RSPSQSSSQI DSVPVQQDNV TSQTSISSDV  840
AMAEPSLNQY GFCMNRSDDE DDDYGVYRLD SEPSHLSHGN DYYGAVTIEE FASVYGPQNV  900
HLDGDNTSSL LPGSFDTQDA VGIHKIEEEP YEHDNGDQCG TSPYDLQSTN TEPVDFENNG  960
LLWLPPEPED EEDEREAVLF DDDDYDGGGS GGGAGEWGYL GSSNSFGNGE CHTREKSIEE  1020
HRKAMKNVVE GHFRALVSQL LQVENLPLGD EGNNESWLDI ITSLSWEAAT LLKPDTSKGG  1080
GMDPGGYVKV KCIACGRRTD STVVKGVVCK KNVAHRRMTS KIEKPRFLIL GGALEYQRVS  1140
NLLSSFDTLL QQEMDHLKMA VAKIDSHHPN VLLVEKSVSR YAQDYLLAKD ISLVLNIKRP  1200
LLERIARCTG AQIVPSIDHL TSPKLGFCDM FHVEKFLEVH GSAGQGGKKL TKTLMFFEGC  1260
PKPLGVTVLL YGANGDELKK VKHVVQYGVF AAYHLALETS FLADEGASLP ELTLKSEITV  1320
ALPDKPSSID RSISTIPGFS VPPAGKPQGP DASRELQKSN QGLISDNNSS TTSGPILNMQ  1380
GADSICSSKA CSQAFLIEHA LSSRESRSPF TSLSPPEEDI TECYRKELPS ICASENKIDA  1440
GSKDSCLDNP AQAGEALLNS SLISNSLATS ESLGHGGGAL AANHGETPEL TSIKHHSDYQ  1500
NEEVGSSKEE FPPSPSDHQS ILVSLSTRCV WKGTVCERSH LFRIKYYGSF DKPLGRFLRD  1560
HLFDQNYLCR SCGMPSEAHV HCYTHRQGSL TISVKKLPEI FLPGEREGKI WMWHRCLKCP  1620
RANGFPPATR RVVMSDAAWG LSFGKFLELS FSNHAAANRV ATCGHSLHRD CLRFYGFGRM  1680
VACFRYASIH VHSVYLPPQK LEFNYDNQEW IQKEVEEVGH RAELLFTELH NALNQILEKR  1740
PISGTPDGGK KAPESSHQIV ELEEMLQKER EDFEESLQKA MHREVKCGQP AVDILEINRL  1800
RRQLLFHSYI WDQRLIQAAS LSKNSFQEGL RSSLPKLKEK PISSMEKLVE TNINSKPGKG  1860
FSSCDSSLRE TKPDVSIYQG GDVGGFSQPE GEQKNNEIVQ NPNHSNEAKI STRSSENAMD  1920
KSDPLESGLS ERRALSEGNE SLVVANLSDT LDAAWTGESH PTSMIPKENG YSKPDSTLVN  1980
SPTVMRKVAS NSDLQNCAVD QAGVQTTAST HSLSSTSSLK VFDKSYSLNA QKINIGEYNP  2040
VNVPMFRESE RQSGARLLLP IGINDTVIPV FDDEPTSVIA YALVSPDYHV QISESERPRD  2100
AMDGSVSVPL FDSANLLSLS SFDESFSETY RNIGSSDESM SSVSRSRSSQ ALDSLLSKDI  2160
HARVSFTDDG PLGKVKYTVT CYYATRFEAL RRTCCPSERD FVRSLSRCKK WGAQGGKSNV  2220
FFAKTLDDRF IIKQVTKTEL ESFIKFAPSY FKYLSESISF RSPTCLAKIL GIYQVSSKHG  2280
KAGKESKMDV LVMENLLFRR NVTRLYDLKG SSRSRYNPDT SGSNKVLLDQ NLIEAMPTSP  2340
IFVGSKAKRR LERAVWNDTA FLASIDVMDY SLLVGVDEEK DELVVGIIDF MRQYTWDKHL  2400
ETWVKTSGIL GGPKNTSPTV ISPQQYKKRF RKAMTTYFLM VPDQWSPLTI VPSGSQSDLG  2460
EETAQDPS*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
5gw4_G5e-2010571315167426T-complex protein 1 subunit gamma
5gw5_G5e-2010571315167426T-complex protein 1 subunit gamma
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtThe PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate (By similarity). Plays an important role in maintenance of endomembrane homeostasis including endocytosis, vacuole formation, and vacuolar acidification processes. Required for development of viable pollen. Might mediate recycling of auxin transporters. {ECO:0000250, ECO:0000269|PubMed:19846542, ECO:0000269|PubMed:21173023, ECO:0000269|PubMed:21412048}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapPbr011696.1
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_009369728.10.0PREDICTED: 1-phosphatidylinositol-3-phosphate 5-kinase FAB1A
SwissprotQ9LUM00.0FAB1B_ARATH; 1-phosphatidylinositol-3-phosphate 5-kinase FAB1B
TrEMBLA0A498KFS50.0A0A498KFS5_MALDO; Uncharacterized protein
STRINGXP_009369728.10.0(Pyrus x bretschneideri)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF253122
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT5G58010.12e-31LJRHL1-like 3
Publications ? help Back to Top
  1. 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]
  2. 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]
  3. Lee Y, et al.
    The Arabidopsis phosphatidylinositol 3-kinase is important for pollen development.
    Plant Physiol., 2008. 147(4): p. 1886-97
    [PMID:18515640]
  4. Whitley P,Hinz S,Doughty J
    Arabidopsis FAB1/PIKfyve proteins are essential for development of viable pollen.
    Plant Physiol., 2009. 151(4): p. 1812-22
    [PMID:19846542]
  5. Wywial E,Singh SM
    Identification and structural characterization of FYVE domain-containing proteins of Arabidopsis thaliana.
    BMC Plant Biol., 2010. 10: p. 157
    [PMID:20678208]
  6. Hirano T,Matsuzawa T,Takegawa K,Sato MH
    Loss-of-function and gain-of-function mutations in FAB1A/B impair endomembrane homeostasis, conferring pleiotropic developmental abnormalities in Arabidopsis.
    Plant Physiol., 2011. 155(2): p. 797-807
    [PMID:21173023]
  7. Hirano T,Sato MH
    Arabidopsis FAB1A/B is possibly involved in the recycling of auxin transporters.
    Plant Signal Behav, 2011. 6(4): p. 583-5
    [PMID:21412048]
  8. Bak G, et al.
    Rapid structural changes and acidification of guard cell vacuoles during stomatal closure require phosphatidylinositol 3,5-bisphosphate.
    Plant Cell, 2013. 25(6): p. 2202-16
    [PMID:23757398]
  9. Serrazina S,Dias FV,Malhó R
    Characterization of FAB1 phosphatidylinositol kinases in Arabidopsis pollen tube growth and fertilization.
    New Phytol., 2014. 203(3): p. 784-93
    [PMID:24807078]