Annotations: 5XOP

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d5xopb1	All alpha proteins	EF Hand-like	EF-hand	Calmodulin-like	automated matches	(Entamoeba histolytica HM-1:IMSS-B ) [TaxId: 885319 ],	SCOPe (2.08)
B	d5xopb2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Entamoeba histolytica HM-1:IMSS-B ) [TaxId: 885319 ],	SCOPe (2.08)
E	d5xope1	All alpha proteins	EF Hand-like	EF-hand	Calmodulin-like	automated matches	(Entamoeba histolytica HM-1:IMSS-B ) [TaxId: 885319 ],	SCOPe (2.08)
E	d5xope2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Entamoeba histolytica HM-1:IMSS-B ) [TaxId: 885319 ],	SCOPe (2.08)
A	d5xopa1	All alpha proteins	EF Hand-like	EF-hand	Calmodulin-like	automated matches	(Entamoeba histolytica HM-1:IMSS-B ) [TaxId: 885319 ],	SCOPe (2.08)
A	d5xopa2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Entamoeba histolytica HM-1:IMSS-B ) [TaxId: 885319 ],	SCOPe (2.08)
C	d5xopc1	All alpha proteins	EF Hand-like	EF-hand	Calmodulin-like	automated matches	(Entamoeba histolytica HM-1:IMSS-B ) [TaxId: 885319 ],	SCOPe (2.08)
C	d5xopc2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Entamoeba histolytica HM-1:IMSS-B ) [TaxId: 885319 ],	SCOPe (2.08)
D	d5xopd1	All alpha proteins	EF Hand-like	EF-hand	Calmodulin-like	automated matches	(Entamoeba histolytica HM-1:IMSS-B ) [TaxId: 885319 ],	SCOPe (2.08)
D	d5xopd2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Entamoeba histolytica HM-1:IMSS-B ) [TaxId: 885319 ],	SCOPe (2.08)
F	d5xopf_	All alpha proteins	EF Hand-like	EF-hand	Calmodulin-like	automated matches	(Entamoeba histolytica HM-1:IMSS-B ) [TaxId: 885319 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	PF13202	e5xopB1	A: alpha arrays	X: EF-hand	H: EF-hand-related	T: EF-hand	F: PF13202	ECOD (1.6)
E	PF13202	e5xopE1	A: alpha arrays	X: EF-hand	H: EF-hand-related	T: EF-hand	F: PF13202	ECOD (1.6)
A	PF13202	e5xopA1	A: alpha arrays	X: EF-hand	H: EF-hand-related	T: EF-hand	F: PF13202	ECOD (1.6)
C	PF13202	e5xopC1	A: alpha arrays	X: EF-hand	H: EF-hand-related	T: EF-hand	F: PF13202	ECOD (1.6)
D	PF13202	e5xopD1	A: alpha arrays	X: EF-hand	H: EF-hand-related	T: EF-hand	F: PF13202	ECOD (1.6)
F	PF13202	e5xopF1	A: alpha arrays	X: EF-hand	H: EF-hand-related	T: EF-hand	F: PF13202	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	1.10.238.10	Mainly Alpha	Orthogonal Bundle	Recoverin	domain 1	CATH (4.3.0)
E	1.10.238.10	Mainly Alpha	Orthogonal Bundle	Recoverin	domain 1	CATH (4.3.0)
A	1.10.238.10	Mainly Alpha	Orthogonal Bundle	Recoverin	domain 1	CATH (4.3.0)
C	1.10.238.10	Mainly Alpha	Orthogonal Bundle	Recoverin	domain 1	CATH (4.3.0)
D	1.10.238.10	Mainly Alpha	Orthogonal Bundle	Recoverin	domain 1	CATH (4.3.0)
F	1.10.238.10	Mainly Alpha	Orthogonal Bundle	Recoverin	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF13499	EF-hand domain pair (EF-hand_7)	EF-hand domain pair	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Calcium-binding protein 1 (EhCBP1), putative	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR018247	EF-Hand 1, calcium-binding site	Binding Site
A, B, C, D, E A, B, C, D, E, F	IPR002048	EF-hand domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR011992	EF-hand domain pair	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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.