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 63054641    888 ASTFAHLINNSTRRGDtddATTALNIFEETKRHNVKPSVFLYNAVLSKLGRARRTTECWK---------LFQEMKESGLL 958
Cdd:pfam17177   11 ESELRFQLDKCSKHAD---ATGALALYDAAKAEGVRLAQYHYNVLLYLCSKAADATDLKPqlaadrgfeVFEAMKAQGVS 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054641    959 PTSVTYGTVINAACRIGDESLAEKLFAEMENQpNYQPRVAPYNTMIqFEVQTMFNREKALFYYNRLCATDIEPSSHTYKL 1038
Cdd:pfam17177   88 PNEATYTAVARLAAAKGDGDLAFDLVKEMEAA-GVSPRLRSYSPAL-HAYCEAGDADKAYEVEEHMLAHGVELEEPELAA 165

                          170       180
                   ....*....|....*....|....*.
gi 63054641   1039 LMDAygtlkPVNVGSVKAVLELMERT 1064
Cdd:pfam17177  166 LLKV-----SAKAGRADKVYAYLHRL 186

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 63054641    888 ASTFAHLINNSTRRGDtddATTALNIFEETKRHNVKPSVFLYNAVLSKLGRARRTTECWK---------LFQEMKESGLL 958
Cdd:pfam17177   11 ESELRFQLDKCSKHAD---ATGALALYDAAKAEGVRLAQYHYNVLLYLCSKAADATDLKPqlaadrgfeVFEAMKAQGVS 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054641    959 PTSVTYGTVINAACRIGDESLAEKLFAEMENQpNYQPRVAPYNTMIqFEVQTMFNREKALFYYNRLCATDIEPSSHTYKL 1038
Cdd:pfam17177   88 PNEATYTAVARLAAAKGDGDLAFDLVKEMEAA-GVSPRLRSYSPAL-HAYCEAGDADKAYEVEEHMLAHGVELEEPELAA 165

                          170       180
                   ....*....|....*....|....*.
gi 63054641   1039 LMDAygtlkPVNVGSVKAVLELMERT 1064
Cdd:pfam17177  166 LLKV-----SAKAGRADKVYAYLHRL 186

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 63054641    927 FLYNAVLSKLGRARRTTECWKLFQEMKESGLLPTS 961
Cdd:TIGR00756    1 VTYNTLIDGLCKAGRVEEALELFKEMKERGIEPDV 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 63054641    888 ASTFAHLINNSTRRGDtddATTALNIFEETKRHNVKPSVFLYNAVLSKLGRARRTTECWK---------LFQEMKESGLL 958
Cdd:pfam17177   11 ESELRFQLDKCSKHAD---ATGALALYDAAKAEGVRLAQYHYNVLLYLCSKAADATDLKPqlaadrgfeVFEAMKAQGVS 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054641    959 PTSVTYGTVINAACRIGDESLAEKLFAEMENQpNYQPRVAPYNTMIqFEVQTMFNREKALFYYNRLCATDIEPSSHTYKL 1038
Cdd:pfam17177   88 PNEATYTAVARLAAAKGDGDLAFDLVKEMEAA-GVSPRLRSYSPAL-HAYCEAGDADKAYEVEEHMLAHGVELEEPELAA 165

                          170       180
                   ....*....|....*....|....*.
gi 63054641   1039 LMDAygtlkPVNVGSVKAVLELMERT 1064
Cdd:pfam17177  166 LLKV-----SAKAGRADKVYAYLHRL 186

PPR repeat; This family matches additional variants of the PPR repeat that were not captured by the model for pfam01535. The exact function is not known.

                           10        20        30
                   ....*....|....*....|....*....|...
gi 63054641    956 GLLPTSVTYGTVINAACRIGDESLAEKLFAEME 988
Cdd:pfam12854    2 GLKPDVVTYNTLINGLCRAGRVDEAFELLDEME 34

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 63054641    913 IFEETKRHNVKPSVFLYNAVLSKLGRARRTTECWKLFQEMKESGLLPTSVTYGTVINA 970
Cdd:pfam13812    2 ILREMVRDGIQLNVNTYTHLLHAYANVGNLKLALEIFERMKKKGIKPTLDTYNAILGV 59

PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is found in up to 18 copies in some proteins. The family appears to be greatly expanded in plants and fungi. The repeat has been called PPR.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 63054641    959 PTSVTYGTVINAACRIGDESLAEKLFAEMENQpNYQPRVAPYNTMIQ 1005
Cdd:pfam13041    1 PDVVTYNTLINGYCKKGKVEEAFKLFNEMKKR-GVKPNVYTYTILIN 46

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 63054641    947 KLFQEMKESGLLPTSVTYGTVINAACRIGDESLAEKLFAEMEnQPNYQPRVAPYNTMI 1004
Cdd:pfam13812    1 SILREMVRDGIQLNVNTYTHLLHAYANVGNLKLALEIFERMK-KKGIKPTLDTYNAIL 57

PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up to 18 copies in some proteins. This family appears to be greatly expanded in plants. This repeat occurs in PET309 that may be involved in RNA stabilization. This domain occurs in crp1 that is involved in RNA processing. This repeat is associated with a predicted plant protein Swiss:O49549 that has a domain organization similar to the human BRCA1 protein. The repeat has been called PPR.

                           10        20        30
                   ....*....|....*....|....*....|.
gi 63054641    927 FLYNAVLSKLGRARRTTECWKLFQEMKESGL 957
Cdd:pfam01535    1 VTYNSLISGYCKNGKLEEALELFKEMKEKGI 31

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        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054641    877 DNMKMLGYIPRASTFAHLINNSTRRGDTDDAttaLNIFEETKRHNVKPSVFLYNAVLSKLG 937
Cdd:pfam13812    4 REMVRDGIQLNVNTYTHLLHAYANVGNLKLA---LEIFERMKKKGIKPTLDTYNAILGVIG 61