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PX domain superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   Alpha and beta proteins (a+b) [ 53931] (376)
Fold:   PX domain [ 64267]
Superfamily:   PX domain [ 64268]
Families:   PX domain [ 64269] (5)


Superfamily statistics
Genomes (507) Uniprot 2018_03 genome PDB chains (SCOP 1.75)
Domains 11,111 34,954 8
Proteins 11,030 34,697 8


Functional annotation
General category Regulation
Detailed category Signal transduction

Document:
Function annotation of SCOP domain superfamilies

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEO levelAnnotation (direct or inherited)
Enzyme Commission (EC)Acting on ester bonds0.0000005668Least InformativeDirect
Enzyme Commission (EC)Phosphoric diester hydrolases0Moderately InformativeDirect
Enzyme Commission (EC)Protein-serine/threonine kinases0.00009895Moderately InformativeDirect
Enzyme Commission (EC)Phosphotransferases with an alcohol group as accep0.008197Moderately InformativeInherited
Enzyme Commission (EC)Phosphatidylinositol-4-phosphate 3-kinase0Highly InformativeDirect
Enzyme Commission (EC)Phospholipase D0Highly InformativeDirect

Document: EC annotation of SCOP domains

Human Phenotype (HP)

(show details) Document: HP annotation of SCOP domains

Worm Phenotype (WP)

(show details)
WP termFDR (all)SDWP levelAnnotation (direct or inherited)
Worm Phenotype (WP)cell physiology variant0Least InformativeDirect
Worm Phenotype (WP)blast cell physiology variant0Least InformativeDirect
Worm Phenotype (WP)cell development variant0.05503Least InformativeInherited
Worm Phenotype (WP)organism metabolism processing variant0.05577Least InformativeInherited
Worm Phenotype (WP)organ system morphology variant0.1158Least InformativeInherited
Worm Phenotype (WP)organism behavior variant0.5952Least InformativeInherited
Worm Phenotype (WP)apoptosis variant0Moderately InformativeDirect
Worm Phenotype (WP)protein expression variant0.0004111Moderately InformativeDirect
Worm Phenotype (WP)nervous system morphology variant0.02778Moderately InformativeInherited
Worm Phenotype (WP)movement variant0.1014Moderately InformativeInherited
Worm Phenotype (WP)locomotion variant0.3242Moderately InformativeInherited
Worm Phenotype (WP)cell division variant0.9174Moderately InformativeInherited
Worm Phenotype (WP)accumulated germline cell corpses0InformativeDirect
Worm Phenotype (WP)neuron migration variant0.00058InformativeDirect
Worm Phenotype (WP)sensillum morphology variant0.002268InformativeInherited
Worm Phenotype (WP)pattern protein expression variant0.01289InformativeInherited
Worm Phenotype (WP)level of protein expression variant0.3244InformativeInherited
Worm Phenotype (WP)anterior neuron migration defective0.0000003819Highly InformativeDirect
Worm Phenotype (WP)cell division polarity variant0.000004837Highly InformativeDirect
Worm Phenotype (WP)protein expression reduced0.0006388Highly InformativeDirect
Worm Phenotype (WP)amphid phasmid morphology variant0.0006922Highly InformativeDirect

Document: WP annotation of SCOP domains

Yeast Phenotype (YP)

(show details) Document: YP annotation of SCOP domains

Fly Phenotype (FP)

(show details) Document: FP annotation of SCOP domains

Fly Anatomy (FA)

(show details)
FA termFDR (all)SDFA levelAnnotation (direct or inherited)
Fly Anatomy (FA)adult0Least InformativeDirect
Fly Anatomy (FA)organ system subdivision0Least InformativeDirect

Document: FA annotation of SCOP domains

Zebrafish Anatomy (ZA)

(show details) Document: ZA annotation of SCOP domains

Xenopus Anatomy (XA)

(show details) Document: XA annotation of SCOP domains

Arabidopsis Plant Ontology (AP)

(show details)
AP termFDR (all)SDAP levelAnnotation (direct or inherited)
Plant ANatomical entity (PAN)guard cell0Least InformativeDirect
Plant structure DEvelopment stage (PDE)4 leaf senescence stage0Least InformativeDirect
Plant structure DEvelopment stage (PDE)E expanded cotyledon stage0Least InformativeDirect
Plant structure DEvelopment stage (PDE)F mature embryo stage0Least InformativeDirect
Plant structure DEvelopment stage (PDE)D bilateral stage0Least InformativeDirect
Plant structure DEvelopment stage (PDE)LP.08 eight leaves visible stage0Least InformativeDirect
Plant structure DEvelopment stage (PDE)LP.02 two leaves visible stage0Least InformativeDirect
Plant structure DEvelopment stage (PDE)LP.10 ten leaves visible stage0Least InformativeDirect
Plant structure DEvelopment stage (PDE)LP.04 four leaves visible stage0Least InformativeDirect
Plant structure DEvelopment stage (PDE)LP.06 six leaves visible stage0Least InformativeDirect

Document: AP annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEC levelAnnotation (direct or inherited)
Enzyme Commission (EC)Transferring phosphorus-containing groups0.00000005435Least InformativeDirect
Enzyme Commission (EC)Hydrolases0.007564Least InformativeInherited
Enzyme Commission (EC)Protein-serine/threonine kinases0.00028Moderately InformativeDirect
Enzyme Commission (EC)Phosphotransferases with an alcohol group as acceptor0.003588Moderately InformativeInherited
Enzyme Commission (EC)Phosphoric diester hydrolases0InformativeDirect
Enzyme Commission (EC)Non-specific serine/threonine protein kinase0.00000000189InformativeDirect

Document: EC annotation of SCOP domains

InterPro annotation
Cross references IPR001683 SSF64268 Protein matches
Abstract

The PX (phox) domain [PubMed8931154] occurs in a variety of eukaryotic proteins and have been implicated in highly diverse functions such as cell signalling, vesicular trafficking, protein sorting and lipid modification [PubMed10782093, PubMed11736640, PubMed12461558]. PX domains are important phosphoinositide-binding modules that have varying lipid-binding specificities [PubMed11884510]. The PX domain is approximately 120 residues long [PubMed11373621], and folds into a three-stranded beta-sheet followed by three -helices and a proline-rich region that immediately preceeds a membrane-interaction loop and spans approximately eight hydrophobic and polar residues. The PX domain of p47phox binds to the SH3 domain in the same protein [PubMed11373621]. Phosphorylation of p47(phox), a cytoplasmic activator of the microbicidal phagocyte oxidase (phox), elicits interaction of p47(phox) with phoinositides. The protein phosphorylation-driven conformational change of p47(phox) enables its PX domain to bind to phosphoinositides, the interaction of which plays a crucial role in recruitment of p47(phox) from the cytoplasm to membranes and subsequent activation of the phagocyte oxidase. The lipid-binding activity of this protein is normally suppressed by intramolecular interaction of the PX domain with the C-terminal Src homology 3 (SH3) domain [PubMed12356722].

The PX domain is conserved from yeast to human. A recent multiple alignment of representative PX domain sequences can be found in [PubMed9687503], although showing relatively little sequence conservation, their structure appears to be highly conserved. Although phosphatidylinositol-3-phosphate (PtdIns(3)P) is the primary target of PX domains, binding to phosphatidic acid, phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4)P2), phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2), phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2), and phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) has been reported as well. The PX-domain is also a protein-protein interaction domain [PubMed15263065].


InterPro database


PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Human Phenotype (HP) · Worm Phenotype (WP) · Yeast Phenotype (YP) · Fly Phenotype (FP) · Fly Anatomy (FA) · Zebrafish Anatomy (ZA) · Xenopus Anatomy (XA) · Arabidopsis Plant Ontology (AP) · Enzyme Commission (EC) ]

Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.


Alignments of sequences to 16 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.


Browse and view proteins in genomes which have different domain combinations including a PX domain domain.


Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 16 hidden Markov models representing the PX domain superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Human Phenotype (HP) · Worm Phenotype (WP) · Yeast Phenotype (YP) · Fly Phenotype (FP) · Fly Anatomy (FA) · Zebrafish Anatomy (ZA) · Xenopus Anatomy (XA) · Arabidopsis Plant Ontology (AP) · Enzyme Commission (EC) · Internal database links ]