Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large family of modular RNA-binding proteins which mediate several aspects of gene expression primarily in organelles but also in the nucleus. PPR_long is the region of Arabidopsis protein-only RNase P (PRORP) enzyme that consists of up to eleven alpha-helices. PRORPs are a class of RNA processing enzymes that catalyze maturation of the 5' end of precursor tRNAs in Eukaryotes. All PPR proteins contain tandemly repeated sequence motifs (the PPR motifs) which can vary in number. The series of helix-turn-helix motifs formed by PPR motifs throughout the protein produces a superheros with a central groove that allows the protein to bind RNA. Proteins containing PPR motifs are known to have roles in transcription, RNA processing, splicing, stability, editing, and translation. Over a decade after the discovery of PPR proteins, the super-helical structure was confirmed. The protein-only mitochondrial RNase P crystal structure from Arabidopsis thaliana (PRORP1) confirmed the role of its PPR motifs in pre-tRNA binding and suggest it has evolved independently from other RNase P proteins that rely on catalytic RNA.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390636   162 MKLIGYSPDTGTCNYLVSSLCAVDKLDEAIKVVEEMSAAGCIPDVESYGAVINSLCLARkttDVVKI--VKEMVSKAGIS 239
Cdd:pfam17177  81 MKAQGVSPNEATYTAVARLAAAKGDGDLAFDLVKEMEAAGVSPRLRSYSPALHAYCEAG---DADKAyeVEEHMLAHGVE 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 18390636   240 PRKgmlTKVAAALRANREIWKAIEMIEFVES-RDY--PVEFESYEVVVE 285
Cdd:pfam17177 158 LEE---PELAALLKVSAKAGRADKVYAYLHRlRDAvrQVSESTAGVLEE 203

pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR motif, or pentatricopeptide repeat. Its consensus sequence is 35 positions long and typically is found in four or more tandem copies. This family is strongly represented in plant proteins, particularly those sorted to chloroplasts or mitochondria. The pfam01535, domain of unknown function DUF17, consists of 6 copies of this repeat. This family has a similar consensus to the TPR domain (tetratricopeptide), pfam00515, a 33-residue repeat. It is predicted to form a pair of antiparallel helices similar to that of TPR.

                          10        20        30
                  ....*....|....*....|....*....|....
gi 18390636   173 TCNYLVSSLCAVDKLDEAIKVVEEMSAAGCIPDV 206
Cdd:TIGR00756   2 TYNTLIDGLCKAGRVEEALELFKEMKERGIEPDV 35

Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large family of modular RNA-binding proteins which mediate several aspects of gene expression primarily in organelles but also in the nucleus. PPR_long is the region of Arabidopsis protein-only RNase P (PRORP) enzyme that consists of up to eleven alpha-helices. PRORPs are a class of RNA processing enzymes that catalyze maturation of the 5' end of precursor tRNAs in Eukaryotes. All PPR proteins contain tandemly repeated sequence motifs (the PPR motifs) which can vary in number. The series of helix-turn-helix motifs formed by PPR motifs throughout the protein produces a superheros with a central groove that allows the protein to bind RNA. Proteins containing PPR motifs are known to have roles in transcription, RNA processing, splicing, stability, editing, and translation. Over a decade after the discovery of PPR proteins, the super-helical structure was confirmed. The protein-only mitochondrial RNase P crystal structure from Arabidopsis thaliana (PRORP1) confirmed the role of its PPR motifs in pre-tRNA binding and suggest it has evolved independently from other RNase P proteins that rely on catalytic RNA.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390636   162 MKLIGYSPDTGTCNYLVSSLCAVDKLDEAIKVVEEMSAAGCIPDVESYGAVINSLCLARkttDVVKI--VKEMVSKAGIS 239
Cdd:pfam17177  81 MKAQGVSPNEATYTAVARLAAAKGDGDLAFDLVKEMEAAGVSPRLRSYSPALHAYCEAG---DADKAyeVEEHMLAHGVE 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 18390636   240 PRKgmlTKVAAALRANREIWKAIEMIEFVES-RDY--PVEFESYEVVVE 285
Cdd:pfam17177 158 LEE---PELAALLKVSAKAGRADKVYAYLHRlRDAvrQVSESTAGVLEE 203

pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR motif, or pentatricopeptide repeat. Its consensus sequence is 35 positions long and typically is found in four or more tandem copies. This family is strongly represented in plant proteins, particularly those sorted to chloroplasts or mitochondria. The pfam01535, domain of unknown function DUF17, consists of 6 copies of this repeat. This family has a similar consensus to the TPR domain (tetratricopeptide), pfam00515, a 33-residue repeat. It is predicted to form a pair of antiparallel helices similar to that of TPR.

                          10        20        30
                  ....*....|....*....|....*....|....
gi 18390636   173 TCNYLVSSLCAVDKLDEAIKVVEEMSAAGCIPDV 206
Cdd:TIGR00756   2 TYNTLIDGLCKAGRVEEALELFKEMKERGIEPDV 35

Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat that were not captured by the model for pfam01535. In the case of the Arabidopsis protein UniProtKB:Q66GI4, the repeated helices in this N-terminal region, of protein-only RNase P (PRORP) enzymes, form the pentatricopeptide repeat (PPR) domain which enhances pre-tRNA binding affinity. PROPRP enzymes process precursor tRNAs in human mitochondria and in all tRNA-using compartments of Arabidopsis thaliana.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18390636   158 IINEMKLIGYSPDTGTCNYLVSSLCAVDKLDEAIKVVEEMSAAGCIPDVESYGAVIN 214
Cdd:pfam13812   2 ILREMVRDGIQLNVNTYTHLLHAYANVGNLKLALEIFERMKKKGIKPTLDTYNAILG 58

maturation of RBCL 1; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390636   161 EMKLIGYSPDTGTCNYLVSSLCAVDKLDEAIKVVEEMSAAGCIPDVESYgAVINSLCLARKTTDVVKIVKEMVSKAGISP 240
Cdd:PLN03218  709 DIKSIKLRPTVSTMNALITALCEGNQLPKALEVLSEMKRLGLCPNTITY-SILLVASERKDDADVGLDLLSQAKEDGIKP 787

                  ....
gi 18390636   241 RKGM 244
Cdd:PLN03218  788 NLVM 791

Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large family of modular RNA-binding proteins which mediate several aspects of gene expression primarily in organelles but also in the nucleus. PPR_long is the region of Arabidopsis protein-only RNase P (PRORP) enzyme that consists of up to eleven alpha-helices. PRORPs are a class of RNA processing enzymes that catalyze maturation of the 5' end of precursor tRNAs in Eukaryotes. All PPR proteins contain tandemly repeated sequence motifs (the PPR motifs) which can vary in number. The series of helix-turn-helix motifs formed by PPR motifs throughout the protein produces a superheros with a central groove that allows the protein to bind RNA. Proteins containing PPR motifs are known to have roles in transcription, RNA processing, splicing, stability, editing, and translation. Over a decade after the discovery of PPR proteins, the super-helical structure was confirmed. The protein-only mitochondrial RNase P crystal structure from Arabidopsis thaliana (PRORP1) confirmed the role of its PPR motifs in pre-tRNA binding and suggest it has evolved independently from other RNase P proteins that rely on catalytic RNA.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390636   185 DKLDEAIKVVEEMSAAGCIPDVESYGAVINsLCLARKTTDVV-KIVKEMVsKAGISPRKGMLTKVAAALRANREIWKAIE 263
Cdd:pfam17177  69 LAADRGFEVFEAMKAQGVSPNEATYTAVAR-LAAAKGDGDLAfDLVKEME-AAGVSPRLRSYSPALHAYCEAGDADKAYE 146

                          90       100
                  ....*....|....*....|
gi 18390636   264 MIEFVESRDypVEFESYEVV 283
Cdd:pfam17177 147 VEEHMLAHG--VELEEPELA 164