Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyPLC-like phosphodiesterases 8043839 3000615 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyC2 domain (calcium/lipid-binding domain, calb) 8040702 3000965 SCOP2B (2022-06-29)
BSCOP2 FamilyEF-hand modules in multidomain proteins 8024997 4000949 SCOP2 (2022-06-29)
BSCOP2 FamilyPLC-like (P variant) 8028323 4002218 SCOP2 (2022-06-29)
BSCOP2 FamilyMammalian PLC 8031461 4003332 SCOP2 (2022-06-29)
BSCOP2 SuperfamilyEF-hand 8037376 3001983 SCOP2 (2022-06-29)
BSCOP2 SuperfamilyC2 domain (calcium/lipid-binding domain, calb) 8040702 3000965 SCOP2 (2022-06-29)
BSCOP2 SuperfamilyPLC-like phosphodiesterases 8043839 3000615 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AC2e1djxA3 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: C2 domain (From Topology)T: C2 domainF: C2ECOD (1.6)
AEF-hand_likee1djxA1 A: alpha arraysX: EF-handH: EF-hand-relatedT: EF-handF: EF-hand_likeECOD (1.6)
API-PLC-Xe1djxA2 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PI-PLC-XECOD (1.6)
BC2e1djxB4 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: C2 domain (From Topology)T: C2 domainF: C2ECOD (1.6)
BEF-hand_10e1djxB1 A: alpha arraysX: EF-handH: EF-hand-relatedT: EF-handF: EF-hand_10ECOD (1.6)
BEF-hand_likee1djxB2 A: alpha arraysX: EF-handH: EF-hand-relatedT: EF-handF: EF-hand_likeECOD (1.6)
BPI-PLC-Xe1djxB3 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PI-PLC-XECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A1.10.238.10 Mainly Alpha Orthogonal Bundle Recoverin domain 1CATH (4.3.0)
A3.20.20.190 Alpha Beta Alpha-Beta Barrel TIM Barrel Phosphatidylinositol (PI) phosphodiesteraseCATH (4.3.0)
A2.60.40.150 Mainly Beta Sandwich Immunoglobulin-like C2 domainCATH (4.3.0)
B1.10.238.10 Mainly Alpha Orthogonal Bundle Recoverin domain 1CATH (4.3.0)
B3.20.20.190 Alpha Beta Alpha-Beta Barrel TIM Barrel Phosphatidylinositol (PI) phosphodiesteraseCATH (4.3.0)
B2.60.40.150 Mainly Beta Sandwich Immunoglobulin-like C2 domainCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF09279Phosphoinositide-specific phospholipase C, efhand-like (EF-hand_like)Phosphoinositide-specific phospholipase C, efhand-likeMembers of this family are predominantly found in phosphoinositide-specific phospholipase C. They adopt a structure consisting of a core of four alpha helices, in an EF like fold, and are required for functioning of the enzyme [1].Domain
A, B
PF00387Phosphatidylinositol-specific phospholipase C, Y domain (PI-PLC-Y)Phosphatidylinositol-specific phospholipase C, Y domain- Family
A, B
PF00168C2 domain (C2)C2 domain- Domain
A, B
PF00388Phosphatidylinositol-specific phospholipase C, X domain (PI-PLC-X)Phosphatidylinositol-specific phospholipase C, X domain- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
phosphoinositide phospholipase C  M-CSA #28

Mammalian phospholipase C catalyses the hydrolysis of inositol lipid to inositol 1,4,5 trisphosphate and diacyl glycerol, both of which are important second messengers in Ca(II) signalling pathways. It possesses a Triose phosphate isomerase-like catalytic domain, indicating some homology with triosephosphate isomerase, but catalyses a different reaction by a mechanism more similar to the T1 RNAases.

Defined by 6 residues: HIS:A-179 [auth A-311]ASN:A-180 [auth A-312]GLU:A-209 [auth A-341]ASP:A-211 [auth A-343]HIS:A-224 [auth A-356]GLU:A-258 [auth A-390]
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