pentatricopeptide repeat-containing protein At3g06920 [Oryza sativa Japonica Group]
List of domain hits
Name | Accession | Description | Interval | E-value | |||||||
PLN03218 super family | cl33664 | maturation of RBCL 1; Provisional |
321-781 | 3.03e-42 | |||||||
maturation of RBCL 1; Provisional The actual alignment was detected with superfamily member PLN03218: Pssm-ID: 215636 [Multi-domain] Cd Length: 1060 Bit Score: 166.98 E-value: 3.03e-42
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
247-296 | 8.28e-14 | |||||||
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. : Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 66.23 E-value: 8.28e-14
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
771-820 | 3.92e-10 | |||||||
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. : Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 55.83 E-value: 3.92e-10
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PPR_2 super family | cl38385 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
806-855 | 1.06e-05 | |||||||
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. The actual alignment was detected with superfamily member pfam13041: Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 43.51 E-value: 1.06e-05
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
285-317 | 2.65e-05 | |||||||
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. : Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 41.67 E-value: 2.65e-05
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PPR_2 super family | cl38385 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
181-226 | 5.66e-05 | |||||||
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. The actual alignment was detected with superfamily member pfam13041: Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 41.19 E-value: 5.66e-05
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DnrI super family | cl34649 | DNA-binding transcriptional regulator DnrI/AfsR/EmbR, SARP family, contains BTAD domain ... |
111-239 | 3.91e-04 | |||||||
DNA-binding transcriptional regulator DnrI/AfsR/EmbR, SARP family, contains BTAD domain [Transcription]; The actual alignment was detected with superfamily member COG3629: Pssm-ID: 442847 [Multi-domain] Cd Length: 244 Bit Score: 42.90 E-value: 3.91e-04
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Name | Accession | Description | Interval | E-value | |||||||
PLN03218 | PLN03218 | maturation of RBCL 1; Provisional |
321-781 | 3.03e-42 | |||||||
maturation of RBCL 1; Provisional Pssm-ID: 215636 [Multi-domain] Cd Length: 1060 Bit Score: 166.98 E-value: 3.03e-42
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
701-750 | 1.24e-17 | |||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 77.02 E-value: 1.24e-17
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
247-296 | 8.28e-14 | |||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 66.23 E-value: 8.28e-14
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
771-820 | 3.92e-10 | |||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 55.83 E-value: 3.92e-10
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
739-773 | 2.54e-07 | |||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 47.45 E-value: 2.54e-07
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
250-284 | 4.23e-07 | |||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 46.68 E-value: 4.23e-07
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LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
177-452 | 7.36e-06 | |||||||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 48.57 E-value: 7.36e-06
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
806-855 | 1.06e-05 | |||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 43.51 E-value: 1.06e-05
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
285-317 | 2.65e-05 | |||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 41.67 E-value: 2.65e-05
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
774-808 | 3.49e-05 | |||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 41.29 E-value: 3.49e-05
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
181-226 | 5.66e-05 | |||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 41.19 E-value: 5.66e-05
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PPR | pfam01535 | PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ... |
285-311 | 6.09e-05 | |||||||
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. Pssm-ID: 366695 [Multi-domain] Cd Length: 31 Bit Score: 40.53 E-value: 6.09e-05
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DnrI | COG3629 | DNA-binding transcriptional regulator DnrI/AfsR/EmbR, SARP family, contains BTAD domain ... |
111-239 | 3.91e-04 | |||||||
DNA-binding transcriptional regulator DnrI/AfsR/EmbR, SARP family, contains BTAD domain [Transcription]; Pssm-ID: 442847 [Multi-domain] Cd Length: 244 Bit Score: 42.90 E-value: 3.91e-04
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
213-261 | 7.60e-04 | |||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 38.11 E-value: 7.60e-04
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BTAD | smart01043 | Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. ... |
124-235 | 9.16e-04 | |||||||
Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. This region of AFSR along with the C terminal region is capable of independently directing actinorhodin production. This family contains TPR repeats. Pssm-ID: 198111 [Multi-domain] Cd Length: 145 Bit Score: 40.36 E-value: 9.16e-04
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Name | Accession | Description | Interval | E-value | ||||||||||
PLN03218 | PLN03218 | maturation of RBCL 1; Provisional |
321-781 | 3.03e-42 | ||||||||||
maturation of RBCL 1; Provisional Pssm-ID: 215636 [Multi-domain] Cd Length: 1060 Bit Score: 166.98 E-value: 3.03e-42
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PLN03077 | PLN03077 | Protein ECB2; Provisional |
221-862 | 4.35e-31 | ||||||||||
Protein ECB2; Provisional Pssm-ID: 215561 [Multi-domain] Cd Length: 857 Bit Score: 131.13 E-value: 4.35e-31
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PLN03218 | PLN03218 | maturation of RBCL 1; Provisional |
227-675 | 9.27e-31 | ||||||||||
maturation of RBCL 1; Provisional Pssm-ID: 215636 [Multi-domain] Cd Length: 1060 Bit Score: 130.77 E-value: 9.27e-31
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PLN03218 | PLN03218 | maturation of RBCL 1; Provisional |
589-862 | 1.17e-25 | ||||||||||
maturation of RBCL 1; Provisional Pssm-ID: 215636 [Multi-domain] Cd Length: 1060 Bit Score: 114.20 E-value: 1.17e-25
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PLN03081 | PLN03081 | pentatricopeptide (PPR) repeat-containing protein; Provisional |
168-664 | 2.51e-24 | ||||||||||
pentatricopeptide (PPR) repeat-containing protein; Provisional Pssm-ID: 215563 [Multi-domain] Cd Length: 697 Bit Score: 109.19 E-value: 2.51e-24
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PLN03218 | PLN03218 | maturation of RBCL 1; Provisional |
127-553 | 2.33e-21 | ||||||||||
maturation of RBCL 1; Provisional Pssm-ID: 215636 [Multi-domain] Cd Length: 1060 Bit Score: 100.34 E-value: 2.33e-21
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PLN03081 | PLN03081 | pentatricopeptide (PPR) repeat-containing protein; Provisional |
371-841 | 6.16e-20 | ||||||||||
pentatricopeptide (PPR) repeat-containing protein; Provisional Pssm-ID: 215563 [Multi-domain] Cd Length: 697 Bit Score: 95.32 E-value: 6.16e-20
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PLN03081 | PLN03081 | pentatricopeptide (PPR) repeat-containing protein; Provisional |
507-861 | 6.22e-18 | ||||||||||
pentatricopeptide (PPR) repeat-containing protein; Provisional Pssm-ID: 215563 [Multi-domain] Cd Length: 697 Bit Score: 88.77 E-value: 6.22e-18
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
701-750 | 1.24e-17 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 77.02 E-value: 1.24e-17
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
736-785 | 1.39e-16 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 74.32 E-value: 1.39e-16
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
247-296 | 8.28e-14 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 66.23 E-value: 8.28e-14
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
352-399 | 8.45e-14 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 66.23 E-value: 8.45e-14
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
667-715 | 1.14e-13 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 65.85 E-value: 1.14e-13
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
597-645 | 3.26e-12 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 61.61 E-value: 3.26e-12
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PLN03077 | PLN03077 | Protein ECB2; Provisional |
170-598 | 4.92e-12 | ||||||||||
Protein ECB2; Provisional Pssm-ID: 215561 [Multi-domain] Cd Length: 857 Bit Score: 69.88 E-value: 4.92e-12
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PPR_1 | pfam12854 | PPR repeat; This family matches additional variants of the PPR repeat that were not captured ... |
452-484 | 1.33e-11 | ||||||||||
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. Pssm-ID: 403914 [Multi-domain] Cd Length: 34 Bit Score: 59.67 E-value: 1.33e-11
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
386-435 | 2.15e-11 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 59.30 E-value: 2.15e-11
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
421-470 | 5.18e-11 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 58.53 E-value: 5.18e-11
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
317-366 | 5.44e-11 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 58.14 E-value: 5.44e-11
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
631-680 | 1.86e-10 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 56.60 E-value: 1.86e-10
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
655-715 | 1.96e-10 | ||||||||||
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. Pssm-ID: 316342 [Multi-domain] Cd Length: 63 Bit Score: 56.98 E-value: 1.96e-10
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
771-820 | 3.92e-10 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 55.83 E-value: 3.92e-10
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PLN03077 | PLN03077 | Protein ECB2; Provisional |
146-414 | 6.28e-10 | ||||||||||
Protein ECB2; Provisional Pssm-ID: 215561 [Multi-domain] Cd Length: 857 Bit Score: 62.94 E-value: 6.28e-10
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PPR_1 | pfam12854 | PPR repeat; This family matches additional variants of the PPR repeat that were not captured ... |
382-415 | 1.52e-09 | ||||||||||
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. Pssm-ID: 403914 [Multi-domain] Cd Length: 34 Bit Score: 53.89 E-value: 1.52e-09
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
456-503 | 1.63e-09 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 53.91 E-value: 1.63e-09
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PPR_1 | pfam12854 | PPR repeat; This family matches additional variants of the PPR repeat that were not captured ... |
279-311 | 1.68e-08 | ||||||||||
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. Pssm-ID: 403914 [Multi-domain] Cd Length: 34 Bit Score: 50.81 E-value: 1.68e-08
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PPR_1 | pfam12854 | PPR repeat; This family matches additional variants of the PPR repeat that were not captured ... |
662-694 | 2.49e-08 | ||||||||||
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. Pssm-ID: 403914 [Multi-domain] Cd Length: 34 Bit Score: 50.42 E-value: 2.49e-08
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
561-610 | 2.51e-08 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 50.82 E-value: 2.51e-08
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
585-640 | 4.10e-08 | ||||||||||
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. Pssm-ID: 316342 [Multi-domain] Cd Length: 63 Bit Score: 50.43 E-value: 4.10e-08
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PPR_1 | pfam12854 | PPR repeat; This family matches additional variants of the PPR repeat that were not captured ... |
593-625 | 6.13e-08 | ||||||||||
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. Pssm-ID: 403914 [Multi-domain] Cd Length: 34 Bit Score: 49.27 E-value: 6.13e-08
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PPR_1 | pfam12854 | PPR repeat; This family matches additional variants of the PPR repeat that were not captured ... |
768-798 | 7.53e-08 | ||||||||||
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. Pssm-ID: 403914 [Multi-domain] Cd Length: 34 Bit Score: 48.88 E-value: 7.53e-08
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
762-815 | 8.38e-08 | ||||||||||
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. Pssm-ID: 316342 [Multi-domain] Cd Length: 63 Bit Score: 49.66 E-value: 8.38e-08
|
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
282-329 | 8.80e-08 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 49.28 E-value: 8.80e-08
|
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
689-746 | 9.33e-08 | ||||||||||
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. Pssm-ID: 316342 [Multi-domain] Cd Length: 63 Bit Score: 49.66 E-value: 9.33e-08
|
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
739-773 | 2.54e-07 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 47.45 E-value: 2.54e-07
|
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
526-575 | 3.08e-07 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 47.74 E-value: 3.08e-07
|
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
669-703 | 3.61e-07 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 47.06 E-value: 3.61e-07
|
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
250-284 | 4.23e-07 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 46.68 E-value: 4.23e-07
|
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
320-354 | 4.80e-07 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 46.68 E-value: 4.80e-07
|
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PPR_long | pfam17177 | Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ... |
574-716 | 5.54e-07 | ||||||||||
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. Pssm-ID: 407303 [Multi-domain] Cd Length: 212 Bit Score: 51.24 E-value: 5.54e-07
|
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PPR_1 | pfam12854 | PPR repeat; This family matches additional variants of the PPR repeat that were not captured ... |
734-764 | 1.25e-06 | ||||||||||
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. Pssm-ID: 403914 [Multi-domain] Cd Length: 34 Bit Score: 45.41 E-value: 1.25e-06
|
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
599-633 | 1.56e-06 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 45.14 E-value: 1.56e-06
|
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PPR | pfam01535 | PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ... |
459-489 | 1.68e-06 | ||||||||||
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. Pssm-ID: 366695 [Multi-domain] Cd Length: 31 Bit Score: 45.15 E-value: 1.68e-06
|
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PPR | pfam01535 | PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ... |
320-350 | 1.84e-06 | ||||||||||
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. Pssm-ID: 366695 [Multi-domain] Cd Length: 31 Bit Score: 45.15 E-value: 1.84e-06
|
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
459-492 | 2.03e-06 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 44.75 E-value: 2.03e-06
|
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PPR_long | pfam17177 | Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ... |
652-800 | 2.36e-06 | ||||||||||
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. Pssm-ID: 407303 [Multi-domain] Cd Length: 212 Bit Score: 49.32 E-value: 2.36e-06
|
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
704-738 | 2.78e-06 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 44.37 E-value: 2.78e-06
|
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
390-422 | 5.62e-06 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 43.60 E-value: 5.62e-06
|
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LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
177-452 | 7.36e-06 | ||||||||||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 48.57 E-value: 7.36e-06
|
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PPR | pfam01535 | PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ... |
600-629 | 7.53e-06 | ||||||||||
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. Pssm-ID: 366695 [Multi-domain] Cd Length: 31 Bit Score: 43.22 E-value: 7.53e-06
|
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PPR_1 | pfam12854 | PPR repeat; This family matches additional variants of the PPR repeat that were not captured ... |
348-381 | 7.75e-06 | ||||||||||
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. Pssm-ID: 403914 [Multi-domain] Cd Length: 34 Bit Score: 43.10 E-value: 7.75e-06
|
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
806-855 | 1.06e-05 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 43.51 E-value: 1.06e-05
|
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PPR | pfam01535 | PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ... |
669-699 | 1.16e-05 | ||||||||||
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. Pssm-ID: 366695 [Multi-domain] Cd Length: 31 Bit Score: 42.84 E-value: 1.16e-05
|
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PPR_long | pfam17177 | Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ... |
690-835 | 1.40e-05 | ||||||||||
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. Pssm-ID: 407303 [Multi-domain] Cd Length: 212 Bit Score: 47.01 E-value: 1.40e-05
|
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
306-366 | 1.70e-05 | ||||||||||
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. Pssm-ID: 316342 [Multi-domain] Cd Length: 63 Bit Score: 43.12 E-value: 1.70e-05
|
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
285-317 | 2.65e-05 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 41.67 E-value: 2.65e-05
|
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
620-680 | 3.22e-05 | ||||||||||
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. Pssm-ID: 316342 [Multi-domain] Cd Length: 63 Bit Score: 42.35 E-value: 3.22e-05
|
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PPR_long | pfam17177 | Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ... |
296-487 | 3.47e-05 | ||||||||||
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. Pssm-ID: 407303 [Multi-domain] Cd Length: 212 Bit Score: 45.85 E-value: 3.47e-05
|
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
774-808 | 3.49e-05 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 41.29 E-value: 3.49e-05
|
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PPR_long | pfam17177 | Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ... |
539-653 | 4.66e-05 | ||||||||||
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. Pssm-ID: 407303 [Multi-domain] Cd Length: 212 Bit Score: 45.47 E-value: 4.66e-05
|
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
181-226 | 5.66e-05 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 41.19 E-value: 5.66e-05
|
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PPR | pfam01535 | PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ... |
285-311 | 6.09e-05 | ||||||||||
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. Pssm-ID: 366695 [Multi-domain] Cd Length: 31 Bit Score: 40.53 E-value: 6.09e-05
|
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
425-458 | 9.59e-05 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 40.13 E-value: 9.59e-05
|
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PPR_1 | pfam12854 | PPR repeat; This family matches additional variants of the PPR repeat that were not captured ... |
419-447 | 1.14e-04 | ||||||||||
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. Pssm-ID: 403914 [Multi-domain] Cd Length: 34 Bit Score: 40.02 E-value: 1.14e-04
|
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Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
111-344 | 1.22e-04 | ||||||||||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 45.75 E-value: 1.22e-04
|
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
201-261 | 1.23e-04 | ||||||||||
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. Pssm-ID: 316342 [Multi-domain] Cd Length: 63 Bit Score: 40.80 E-value: 1.23e-04
|
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PPR | pfam01535 | PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ... |
774-803 | 1.23e-04 | ||||||||||
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. Pssm-ID: 366695 [Multi-domain] Cd Length: 31 Bit Score: 39.76 E-value: 1.23e-04
|
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
494-527 | 1.37e-04 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 39.75 E-value: 1.37e-04
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PPR_1 | pfam12854 | PPR repeat; This family matches additional variants of the PPR repeat that were not captured ... |
627-658 | 1.42e-04 | ||||||||||
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. Pssm-ID: 403914 [Multi-domain] Cd Length: 34 Bit Score: 39.64 E-value: 1.42e-04
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
270-330 | 1.60e-04 | ||||||||||
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. Pssm-ID: 316342 [Multi-domain] Cd Length: 63 Bit Score: 40.42 E-value: 1.60e-04
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TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
181-348 | 2.01e-04 | ||||||||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 43.84 E-value: 2.01e-04
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PPR_long | pfam17177 | Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ... |
565-692 | 2.09e-04 | ||||||||||
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. Pssm-ID: 407303 [Multi-domain] Cd Length: 212 Bit Score: 43.54 E-value: 2.09e-04
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PPR_long | pfam17177 | Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ... |
225-412 | 2.78e-04 | ||||||||||
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. Pssm-ID: 407303 [Multi-domain] Cd Length: 212 Bit Score: 43.15 E-value: 2.78e-04
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
340-397 | 2.80e-04 | ||||||||||
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. Pssm-ID: 316342 [Multi-domain] Cd Length: 63 Bit Score: 39.65 E-value: 2.80e-04
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PPR | pfam01535 | PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ... |
355-383 | 2.99e-04 | ||||||||||
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. Pssm-ID: 366695 [Multi-domain] Cd Length: 31 Bit Score: 38.60 E-value: 2.99e-04
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
635-668 | 3.03e-04 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 38.98 E-value: 3.03e-04
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PPR_1 | pfam12854 | PPR repeat; This family matches additional variants of the PPR repeat that were not captured ... |
697-730 | 3.14e-04 | ||||||||||
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. Pssm-ID: 403914 [Multi-domain] Cd Length: 34 Bit Score: 38.87 E-value: 3.14e-04
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LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
297-554 | 3.78e-04 | ||||||||||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 43.18 E-value: 3.78e-04
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DnrI | COG3629 | DNA-binding transcriptional regulator DnrI/AfsR/EmbR, SARP family, contains BTAD domain ... |
111-239 | 3.91e-04 | ||||||||||
DNA-binding transcriptional regulator DnrI/AfsR/EmbR, SARP family, contains BTAD domain [Transcription]; Pssm-ID: 442847 [Multi-domain] Cd Length: 244 Bit Score: 42.90 E-value: 3.91e-04
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PPR_1 | pfam12854 | PPR repeat; This family matches additional variants of the PPR repeat that were not captured ... |
244-276 | 5.29e-04 | ||||||||||
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. Pssm-ID: 403914 [Multi-domain] Cd Length: 34 Bit Score: 38.10 E-value: 5.29e-04
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PPR | pfam01535 | PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ... |
389-415 | 5.33e-04 | ||||||||||
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. Pssm-ID: 366695 [Multi-domain] Cd Length: 31 Bit Score: 37.83 E-value: 5.33e-04
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LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
296-522 | 5.65e-04 | ||||||||||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 42.79 E-value: 5.65e-04
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PPR | pfam01535 | PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ... |
704-734 | 6.62e-04 | ||||||||||
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. Pssm-ID: 366695 [Multi-domain] Cd Length: 31 Bit Score: 37.83 E-value: 6.62e-04
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PPR_long | pfam17177 | Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ... |
475-587 | 7.08e-04 | ||||||||||
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. Pssm-ID: 407303 [Multi-domain] Cd Length: 212 Bit Score: 42.00 E-value: 7.08e-04
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PPR_2 | pfam13041 | PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ... |
213-261 | 7.60e-04 | ||||||||||
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. Pssm-ID: 463778 [Multi-domain] Cd Length: 50 Bit Score: 38.11 E-value: 7.60e-04
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PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
258-348 | 7.63e-04 | ||||||||||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 39.38 E-value: 7.63e-04
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PPR | pfam01535 | PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ... |
250-280 | 8.14e-04 | ||||||||||
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. Pssm-ID: 366695 [Multi-domain] Cd Length: 31 Bit Score: 37.44 E-value: 8.14e-04
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BTAD | smart01043 | Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. ... |
124-235 | 9.16e-04 | ||||||||||
Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. This region of AFSR along with the C terminal region is capable of independently directing actinorhodin production. This family contains TPR repeats. Pssm-ID: 198111 [Multi-domain] Cd Length: 145 Bit Score: 40.36 E-value: 9.16e-04
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PPR_1 | pfam12854 | PPR repeat; This family matches additional variants of the PPR repeat that were not captured ... |
322-346 | 1.58e-03 | ||||||||||
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. Pssm-ID: 403914 [Multi-domain] Cd Length: 34 Bit Score: 36.55 E-value: 1.58e-03
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
355-383 | 1.76e-03 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 36.66 E-value: 1.76e-03
|
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
236-291 | 2.06e-03 | ||||||||||
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. Pssm-ID: 316342 [Multi-domain] Cd Length: 63 Bit Score: 37.34 E-value: 2.06e-03
|
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
479-535 | 3.48e-03 | ||||||||||
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. Pssm-ID: 316342 [Multi-domain] Cd Length: 63 Bit Score: 36.57 E-value: 3.48e-03
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BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
222-348 | 4.14e-03 | ||||||||||
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 38.63 E-value: 4.14e-03
|
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
564-598 | 4.76e-03 | ||||||||||
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. Pssm-ID: 273253 [Multi-domain] Cd Length: 35 Bit Score: 35.51 E-value: 4.76e-03
|
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PPR | pfam01535 | PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ... |
739-769 | 4.87e-03 | ||||||||||
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. Pssm-ID: 366695 [Multi-domain] Cd Length: 31 Bit Score: 35.13 E-value: 4.87e-03
|
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PPR | pfam01535 | PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ... |
635-664 | 5.22e-03 | ||||||||||
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. Pssm-ID: 366695 [Multi-domain] Cd Length: 31 Bit Score: 35.13 E-value: 5.22e-03
|
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
409-470 | 5.42e-03 | ||||||||||
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. Pssm-ID: 316342 [Multi-domain] Cd Length: 63 Bit Score: 36.18 E-value: 5.42e-03
|
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PPR | pfam01535 | PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ... |
180-209 | 5.59e-03 | ||||||||||
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. Pssm-ID: 366695 [Multi-domain] Cd Length: 31 Bit Score: 35.13 E-value: 5.59e-03
|
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
726-781 | 7.80e-03 | ||||||||||
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. Pssm-ID: 316342 [Multi-domain] Cd Length: 63 Bit Score: 35.80 E-value: 7.80e-03
|
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PPR_1 | pfam12854 | PPR repeat; This family matches additional variants of the PPR repeat that were not captured ... |
802-833 | 8.56e-03 | ||||||||||
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. Pssm-ID: 403914 [Multi-domain] Cd Length: 34 Bit Score: 34.63 E-value: 8.56e-03
|
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TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
196-348 | 8.80e-03 | ||||||||||
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 38.02 E-value: 8.80e-03
|
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PPR_long | pfam17177 | Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ... |
373-488 | 9.30e-03 | ||||||||||
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. Pssm-ID: 407303 [Multi-domain] Cd Length: 212 Bit Score: 38.53 E-value: 9.30e-03
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Blast search parameters | ||||
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