PENTATRICOPEPTIDE REPEAT 596 [Arabidopsis thaliana]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
340-501 | 1.50e-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: 50.11 E-value: 1.50e-06
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PPR_3 super family | cl37870 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
250-309 | 1.04e-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. The actual alignment was detected with superfamily member pfam13812: Pssm-ID: 316342 [Multi-domain] Cd Length: 63 Bit Score: 40.42 E-value: 1.04e-04
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Name | Accession | Description | Interval | E-value | ||||
LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
340-501 | 1.50e-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: 50.11 E-value: 1.50e-06
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
250-309 | 1.04e-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: 1.04e-04
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
437-468 | 9.81e-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: 33.97 E-value: 9.81e-03
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Name | Accession | Description | Interval | E-value | ||||
LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
340-501 | 1.50e-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: 50.11 E-value: 1.50e-06
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PPR_3 | pfam13812 | Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ... |
250-309 | 1.04e-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: 1.04e-04
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PPR | TIGR00756 | pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ... |
437-468 | 9.81e-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: 33.97 E-value: 9.81e-03
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Blast search parameters | ||||
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