Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyARM repeat-like 8095925 3000116 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyPIN domain-like 8095924 3001041 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APPR_longe4g23A1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PPR_longECOD (1.6)
ARNase_Zc3h12ae4g23A2 A: a/b three-layered sandwichesX: HAD domain-likeH: HAD domain-relatedT: PIN domain-likeF: RNase_Zc3h12aECOD (1.6)
APRORP_C_1e4g23A3 A: few secondary structure elementsX: Protein-only RNase P Zn-binding domain (From Topology)H: Protein-only RNase P Zn-binding domain (From Topology)T: Protein-only RNase P Zn-binding domainF: PRORP_C_1ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A1.25.40.10 Mainly Alpha Alpha Horseshoe Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat Tetratricopeptide repeat domainCATH (4.3.0)
A3.40.50.11980 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF16953Protein-only RNase P (PRORP)Protein-only RNase PPRORPs (protein-only RNase P) are a class of RNA processing enzymes that catalyze maturation of the 5' end of precursor tRNAs in Eukaryotes [1]. Arabidopsis thaliana contains PRORP enzymes (PRORP1, PRORP2 and PRORP3) where PRORP1 localizes to mitocho ...PRORPs (protein-only RNase P) are a class of RNA processing enzymes that catalyze maturation of the 5' end of precursor tRNAs in Eukaryotes [1]. Arabidopsis thaliana contains PRORP enzymes (PRORP1, PRORP2 and PRORP3) where PRORP1 localizes to mitochondria as well as chloroplasts, while PRORP2 and PRORP3 are found in the nucleus. In humans and most other metazoans, mt-RNase P is composed of three protein subunits (mitochondrial RNase P proteins 1-3; MRPP1-3), homologs to the Arabidopsis thaliana PRORP1-3. This domain corresponds to the metallonuclease domain of PRORPs. PRORP1 has 22% sequence identity to the human homologue MRPP3. PRORP1 crystal structure shows a V-shaped tripartite structure with a C-terminal metallonuclease domain of the NYN (N4BL1, YacP-like nuclease) family, with a typical and functional two-metal-ion catalytic site that has conserved aspartate residues [2].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Pentatricopeptide repeat-containing protein At2g32230, mitochondrial