Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
C [auth B]SCOP2B SuperfamilyEF-hand8037367 3001983 SCOP2B (2022-06-29)
E [auth D]SCOP2B SuperfamilyEF-hand8037367 3001983 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
B [auth A]Metallophos_2_1e2p6bA1 A: a+b four layersX: Carbon-nitrogen hydrolase-likeH: Metallo-dependent phosphatases (From Topology)T: Metallo-dependent phosphatasesF: Metallophos_2_1ECOD (1.6)
D [auth C]Metallophos_2_1e2p6bC1 A: a+b four layersX: Carbon-nitrogen hydrolase-likeH: Metallo-dependent phosphatases (From Topology)T: Metallo-dependent phosphatasesF: Metallophos_2_1ECOD (1.6)
C [auth B]EF-hand_7_10e2p6bB1 A: alpha arraysX: EF-handH: EF-hand-relatedT: EF-handF: EF-hand_7_10ECOD (1.6)
C [auth B]EF-hand_7_1e2p6bB2 A: alpha arraysX: EF-handH: EF-hand-relatedT: EF-handF: EF-hand_7_1ECOD (1.6)
E [auth D]EF-hand_7_10e2p6bD1 A: alpha arraysX: EF-handH: EF-hand-relatedT: EF-handF: EF-hand_7_10ECOD (1.6)
E [auth D]EF-hand_7_1e2p6bD2 A: alpha arraysX: EF-handH: EF-hand-relatedT: EF-handF: EF-hand_7_1ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B [auth A]3.60.21.10 Alpha Beta 4-Layer Sandwich Purple Acid Phosphatase chain A, domain 2CATH (4.3.0)
D [auth C]3.60.21.10 Alpha Beta 4-Layer Sandwich Purple Acid Phosphatase chain A, domain 2CATH (4.3.0)
C [auth B]1.10.238.10 Mainly Alpha Orthogonal Bundle Recoverin domain 1CATH (4.3.0)
E [auth D]1.10.238.10 Mainly Alpha Orthogonal Bundle Recoverin domain 1CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
B [auth A],
D [auth C]
PF00149Calcineurin-like phosphoesterase (Metallophos)Calcineurin-like phosphoesteraseThis family includes a diverse range of phosphoesterases [1], including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD Swiss:P13457 or ...This family includes a diverse range of phosphoesterases [1], including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD Swiss:P13457 or yeast MRE11 Swiss:P32829. The most conserved regions in this superfamily centre around the metal chelating residues.
Domain
C [auth B],
E [auth D]
PF13499EF-hand domain pair (EF-hand_7)EF-hand domain pair- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A [auth E]PVIVIT 14-mer Peptide---
B [auth A],
D [auth C]
Calmodulin-dependent calcineurin A subunit alpha isoform
C [auth B],
E [auth D]
Calcineurin subunit B isoform 1

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
B [auth A],
D [auth C]
PharosQ08209
C [auth B],
E [auth D]
PharosP63098

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
A [auth E]NH2 RESIDAA0081 , AA0083 , AA0084 , AA0086 , AA0087 , AA0088 , AA0090 , AA0091 , AA0092 , AA0093 , AA0095 , AA0096 , AA0097 , AA0098 , AA0099 , AA0100

PSI-MOD :  L-alanine amide MOD:00090 , L-asparagine amide MOD:00092 , L-aspartic acid 1-amide MOD:00093 , L-glutamine amide MOD:00095 , L-glutamic acid 1-amide MOD:00096 , glycine amide MOD:00097 , L-isoleucine amide MOD:00099 , L-leucine amide MOD:00100 , L-lysine amide MOD:00101 , L-methionine amide MOD:00102 , L-proline amide MOD:00104 , L-serine amide MOD:00105 , L-threonine amide MOD:00106 , L-tryptophan amide MOD:00107 , L-tyrosine amide MOD:00108 , L-valine amide MOD:00109