Gene: Peaxi162Scf00132g00233

General Information

Structural Information

  • Species Petunia axillaris
  • Gene Identifier Peaxi162Scf00132g00233
  • Transcript Identifier Peaxi162Scf00132g00233.1
  • Gene Type Coding gene
  • Location Peaxi162Scf00132 : 183508-190444 : positive

Gene Family Information

  • ID HOM05D001229
  • #Genes/#Species 505/100
  • Phylogenetic origin

Gene Duplication Information

Labels

Identifiers

  • GenePreviousVersionID Peaxi162Scf00132g02031

Descriptions

  • Description Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
  • Loading (ortholog descriptions from ath)...

Functional Annotation

Biological Process

GO termEvidence(s)Provider(s)DescriptionSource(s)
GO:0009231
ISO
PLAZA Integrative Orthologyriboflavin biosynthetic process AT2G20690

Molecular Function

GO termEvidence(s)Provider(s)DescriptionSource(s)
GO:0005515
IEA
InterProprotein binding
GO:0019888
IEA
InterProprotein phosphatase regulator activity
GO:0004746
ISO
PLAZA Integrative Orthologyriboflavin synthase activity AT2G20690

Cellular Component

GO termEvidence(s)Provider(s)DescriptionSource(s)
GO:0000159
IEA
InterProprotein phosphatase type 2A complex
GO:0009507
ISO
PLAZA Integrative Orthologychloroplast AT2G20690

Color Legend

Experimental Evidence
Computational Reviewed Evidence
Electronic Evidence
GO Sources: Primary Orthology Homology
Show redundant parents:
InterPro Description
IPR026017 Lumazine-binding domain
IPR015943 WD40/YVTN repeat-like-containing domain superfamily
IPR017938 Riboflavin synthase-like beta-barrel
IPR001783 Lumazine-binding protein
IPR000009 Protein phosphatase 2A regulatory subunit PR55
IPR036322 WD40-repeat-containing domain superfamily
IPR023366 ATP synthase subunit alpha, N-terminal domain-like superfamily
Mapman id Description
18.4.25.1.2.2 Protein modification.phosphorylation.protein serine/threonine phosphatase superfamily.PPP Fe-Zn-dependent phosphatase families.PP2A-class phosphatase complexes.regulatory component B
7.10.8 Coenzyme metabolism.FMN/FAD biosynthesis.riboflavin synthase (RibC)