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 XP_011077930.1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Lamiales; Pedaliaceae; Sesamum
Family bZIP
Protein Properties Length: 892aa    MW: 95381.3 Da    PI: 8.6279
Description bZIP family protein
Gene Model
Gene Model ID Type Source Coding Sequence
XP_011077930.1genomeNCBIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1bZIP_142.81.1e-13327379557
                     CHHHCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH CS
          bZIP_1   5 krerrkqkNReAArrsRqRKkaeieeLeekvkeLeaeNkaLkkeleelkkeva 57 
                     +r+rr++kNRe+A rsR+RK+a++ eLe +  +L++eN  Lk  l el+ + +
  XP_011077930.1 327 RRQRRMIKNRESAARSRARKQAYTVELEAELNQLKEENAHLKHALAELERKRK 379
                     69*******************************************99997765 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM003385.6E-14323387IPR004827Basic-leucine zipper domain
PROSITE profilePS5021711.611325377IPR004827Basic-leucine zipper domain
SuperFamilySSF579598.75E-11327376No hitNo description
Gene3DG3DSA:1.20.5.1704.8E-14327380No hitNo description
CDDcd147072.76E-25327381No hitNo description
PfamPF001706.9E-12327379IPR004827Basic-leucine zipper domain
PROSITE patternPS000360330345IPR004827Basic-leucine zipper domain
TIGRFAMsTIGR000655.4E-124523847IPR000158Cell division protein FtsZ
HamapMF_0090936.566529873IPR000158Cell division protein FtsZ
SuperFamilySSF524905.1E-66532730IPR003008Tubulin/FtsZ, GTPase domain
Gene3DG3DSA:3.40.50.14409.8E-90532736IPR003008Tubulin/FtsZ, GTPase domain
SMARTSM008645.4E-104533727IPR003008Tubulin/FtsZ, GTPase domain
PfamPF000915.9E-38533694IPR003008Tubulin/FtsZ, GTPase domain
CDDcd022012.61E-143544836No hitNo description
PROSITE patternPS011350619640IPR020805Cell division protein FtsZ, conserved site
PRINTSPR004233.8E-49620640IPR003008Tubulin/FtsZ, GTPase domain
PRINTSPR004233.8E-49648669IPR003008Tubulin/FtsZ, GTPase domain
PRINTSPR004233.8E-49711733IPR003008Tubulin/FtsZ, GTPase domain
SuperFamilySSF553074.81E-39726839IPR008280Tubulin/FtsZ, C-terminal
SMARTSM008657.6E-46729846IPR018316Tubulin/FtsZ, 2-layer sandwich domain
PRINTSPR004233.8E-49734755IPR003008Tubulin/FtsZ, GTPase domain
Gene3DG3DSA:3.30.1330.204.6E-43737840IPR018316Tubulin/FtsZ, 2-layer sandwich domain
PfamPF123271.1E-29744838IPR024757Cell division protein FtsZ, C-terminal
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0005737Cellular Componentcytoplasm
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0003924Molecular FunctionGTPase activity
GO:0005525Molecular FunctionGTP binding
GO:0043565Molecular Functionsequence-specific DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 892 aa     Download sequence    Send to blast
MVATDSDIVS QGDAEPPVQS SQQHTKNLIL QSLGRQSSIY SLTLDEFQHT LCESGKNFGS  60
MNMDEFLNSI WTAEENQAHA TSATATSNNA NAVHFPVQET NTKTDKGIAK QPSLPRQGSL  120
SIPEPLCRKT VDEVWSEIHK KQQHNNDTQG QIQNPNNTQR QPTFGEMTLE DFLIRAGVVR  180
EQNFAPAPPQ QPQFGMFQNS SHPVMGPSFV ARPVMAIGGG VNNVTAQPMP QSAVGEALGY  240
TGGMKRASGY SQPTPTVNYG GRLGNGNGGG FGQVQGLGMG SPVSPVSSDG LGTNHVDSGN  300
QYGLDMGGAR GGRKRIIDGP VXKVVERRQR RMIKNRESAA RSRARKQAYT VELEAELNQL  360
KEENAHLKHA LAELERKRKQ QYYEEARAKA QMQSKAQKAN ETVQAMRRTL SCLYMATCTS  420
QYFTPLDIRS PLGVLTVHGA RVSPLKMVEE RNGFPAAGKK GGSSFPQFKC SANSHSVNQF  480
QSKDPFLNLH PEIALLGGET NSTMINPRQD SSSGSVTESP RDSSTLNNYN EAKIKVIGVG  540
GGGSNAVNRM IESAMKGVEF WIVNTDIQAM KMSPVFPKHR LQIGQELTRG LGAGGNPDVG  600
MNAAKESKEA IEGAVYGADM VFVTAGMGGG TGTGGAPIIA AVAKSMGILT VGIVTTPFSF  660
EGQRRTVQAL EGIAALRENV DTLIVIPNEK LLKAVSSSTP VTEAFNLADD ILRQGVRGIS  720
DIITIPGLVN VDFADVRAIM ANAGSSLMGI GTATGKTRAT DAALNAIQSP LLDIGIERAT  780
GIVWNITGGS DLTLFEVNAA AEVIYDLVDP SANLIFGAVV DPSISGQVSI TLIATGFKRQ  840
GESDGRTLQA NQLPQGDSNI GLNRRPASFL EGGSVEIPEF LRKKGRSRYP RV
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
2vam_A1e-10054984029318CELL DIVISION PROTEIN FTSZ
2vxy_A1e-10054984029318CELL DIVISION PROTEIN FTSZ
Search in ModeBase
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
1880886LRKKGRS
Functional Description ? help Back to Top
Source Description
UniProtExhibits GTPase activity (By similarity). Component of the plastid division machinery that forms a contractile ring at the division site. {ECO:0000250, ECO:0000269|PubMed:18284374, ECO:0000269|PubMed:19995726}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapXP_011077930.1
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_015580584.10.0uncharacterized protein LOC8267156 isoform X3
SwissprotQ9LXJ00.0FTZ22_ARATH; Cell division protein FtsZ homolog 2-2, chloroplastic
TrEMBLA0A103XPN60.0A0A103XPN6_CYNCS; Basic-leucine zipper domain-containing protein
STRINGMigut.L01775.1.p0.0(Erythranthe guttata)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
AsteridsOGEA61552433
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT2G36270.16e-99bZIP family protein
Publications ? help Back to Top
  1. Fujiwara M,Yoshida S
    Chloroplast targeting of chloroplast division FtsZ2 proteins in Arabidopsis.
    Biochem. Biophys. Res. Commun., 2001. 287(2): p. 462-7
    [PMID:11554751]
  2. McAndrew RS,Froehlich JE,Vitha S,Stokes KD,Osteryoung KW
    Colocalization of plastid division proteins in the chloroplast stromal compartment establishes a new functional relationship between FtsZ1 and FtsZ2 in higher plants.
    Plant Physiol., 2001. 127(4): p. 1656-66
    [PMID:11743110]
  3. Reumann S,Ma C,Lemke S,Babujee L
    AraPerox. A database of putative Arabidopsis proteins from plant peroxisomes.
    Plant Physiol., 2004. 136(1): p. 2587-608
    [PMID:15333753]
  4. Maple J,Aldridge C,Møller SG
    Plastid division is mediated by combinatorial assembly of plastid division proteins.
    Plant J., 2005. 43(6): p. 811-23
    [PMID:16146521]
  5. McAndrew RS, et al.
    In vivo quantitative relationship between plastid division proteins FtsZ1 and FtsZ2 and identification of ARC6 and ARC3 in a native FtsZ complex.
    Biochem. J., 2008. 412(2): p. 367-78
    [PMID:18284374]
  6. Schmitz AJ,Glynn JM,Olson BJ,Stokes KD,Osteryoung KW
    Arabidopsis FtsZ2-1 and FtsZ2-2 are functionally redundant, but FtsZ-based plastid division is not essential for chloroplast partitioning or plant growth and development.
    Mol Plant, 2009. 2(6): p. 1211-22
    [PMID:19995726]
  7. Olson BJ,Wang Q,Osteryoung KW
    GTP-dependent heteropolymer formation and bundling of chloroplast FtsZ1 and FtsZ2.
    J. Biol. Chem., 2010. 285(27): p. 20634-43
    [PMID:20421292]
  8. Karamoko M,El-Kafafi el-S,Mandaron P,Lerbs-Mache S,Falconet D
    Multiple FtsZ2 isoforms involved in chloroplast division and biogenesis are developmentally associated with thylakoid membranes in Arabidopsis.
    FEBS Lett., 2011. 585(8): p. 1203-8
    [PMID:21439281]
  9. Gargano D,Maple-Grødem J,Møller SG
    In vivo phosphorylation of FtsZ2 in Arabidopsis thaliana.
    Biochem. J., 2012. 446(3): p. 517-21
    [PMID:22823492]
  10. Gargano D,Maple-Grødem J,Reisinger V,Eichacker LA,Møller SG
    Analysis of the chloroplast proteome in arc mutants and identification of novel protein components associated with FtsZ2.
    Plant Mol. Biol., 2013. 81(3): p. 235-44
    [PMID:23225155]
  11. Zhang M,Schmitz AJ,Kadirjan-Kalbach DK,Terbush AD,Osteryoung KW
    Chloroplast division protein ARC3 regulates chloroplast FtsZ-ring assembly and positioning in arabidopsis through interaction with FtsZ2.
    Plant Cell, 2013. 25(5): p. 1787-802
    [PMID:23715471]
  12. Liu Z,Li Y,Cao H,Ren D
    Comparative phospho-proteomics analysis of salt-responsive phosphoproteins regulated by the MKK9-MPK6 cascade in Arabidopsis.
    Plant Sci., 2015. 241: p. 138-50
    [PMID:26706066]
  13. Dutta S, et al.
    Variations in chloroplast movement and chlorophyll fluorescence among chloroplast division mutants under light stress.
    J. Exp. Bot., 2017. 68(13): p. 3541-3555
    [PMID:28645163]