2FBN

Plasmodium falciparum putative FK506-binding protein PFL2275c, C-terminal TPR-containing domain

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2fbna1	All alpha proteins	alpha-alpha superhelix	TPR-like	Tetratricopeptide repeat (TPR)	Putative 70 kda peptidylprolyl isomerase PFL2275c	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)
B	d2fbnb_	All alpha proteins	alpha-alpha superhelix	TPR-like	Tetratricopeptide repeat (TPR)	Putative 70 kda peptidylprolyl isomerase PFL2275c	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Tetratricopeptide repeat (TPR)	8028371	4001344	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	TPR-like	8040750	3001345	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	TPR-like	8040750	3001345	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	TPR_11_8	e2fbnA1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: TPR_11_8	ECOD (1.6)
B	TPR_11_8	e2fbnB1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: TPR_11_8	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)
B	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	70 kDa peptidylprolyl isomerase, putative	isomerase activity catalytic activity, acting on a protein peptidyl-prolyl cis-trans isomerase activity catalytic activity cis-trans isomerase activity FK506 binding amide binding binding organic cyclic compound binding macrolide binding protein binding protein dimerization activity	protein dephosphorylation regulation of cellular process regulation of phosphatase activity regulation of catalytic activity negative regulation of biological process negative regulation of catalytic activity negative regulation of cellular metabolic process regulation of primary metabolic process regulation of phosphate metabolic process phosphate-containing compound metabolic process negative regulation of protein modification process negative regulation of dephosphorylation phosphorus metabolic process protein modification process protein dephosphorylation regulation of cellular process regulation of phosphatase activity regulation of catalytic activity negative regulation of biological process negative regulation of catalytic activity negative regulation of cellular metabolic process regulation of primary metabolic process regulation of phosphate metabolic process phosphate-containing compound metabolic process negative regulation of protein modification process negative regulation of dephosphorylation phosphorus metabolic process protein modification process negative regulation of protein metabolic process regulation of biological process regulation of dephosphorylation cellular metabolic process negative regulation of metabolic process dephosphorylation regulation of protein metabolic process regulation of cellular metabolic process primary metabolic process regulation of molecular function regulation of hydrolase activity macromolecule modification regulation of phosphorus metabolic process metabolic process macromolecule metabolic process regulation of metabolic process negative regulation of hydrolase activity negative regulation of phosphoprotein phosphatase activity negative regulation of protein dephosphorylation regulation of protein modification process negative regulation of phosphate metabolic process regulation of phosphoprotein phosphatase activity organic substance metabolic process negative regulation of phosphatase activity negative regulation of cellular process protein metabolic process negative regulation of macromolecule metabolic process organonitrogen compound metabolic process regulation of protein dephosphorylation biological regulation negative regulation of molecular function regulation of macromolecule metabolic process negative regulation of phosphorus metabolic process cellular process cellular biosynthetic process gene expression macromolecule biosynthetic process protein maturation protein folding biosynthetic process organic substance biosynthetic process chaperone-mediated protein folding peptidyl-amino acid modification peptidyl-proline modification protein peptidyl-prolyl isomerization	intracellular anatomical structure cytoplasm cellular anatomical entity membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR046357	Peptidyl-prolyl cis-trans isomerase domain superfamily	Homologous Superfamily
A, B	IPR011990	Tetratricopeptide-like helical domain superfamily	Homologous Superfamily
A, B	IPR001179	FKBP-type peptidyl-prolyl cis-trans isomerase domain	Domain
A, B	IPR019734	Tetratricopeptide repeat	Repeat

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.