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Conserved domains on  [gi|31621305|ref|NP_573566|]
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leucine-rich PPR motif-containing protein, mitochondrial precursor [Homo sapiens]

Protein Classification

lipopolysaccharide assembly protein LapB( domain architecture ID 11459274)

lipopolysaccharide assembly protein LapB is a tetratricopeptide repeat (TPR) protein that modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03218 super family cl33664
maturation of RBCL 1; Provisional
 144-284 3.93e-07

maturation of RBCL 1; Provisional


The actual alignment was detected with superfamily member PLN03218:

Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 54.88  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305   144 EFAHRIWDTLQKLGAVYDVSHYNALLKVYLQNEYKFSPTDFLAKMEEANIQPNRVTYQRLIASYCNVGDIEGASKILGFM 223
Cdd:PLN03218  631 DFALSIYDDMKKKGVKPDEVFFSALVDVAGHAGDLDKAFEILQDARKQGIKLGTVSYSSLMGACSNAKNWKKALELYEDI 710

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31621305   224 KTKDLPVTEAVFSALVTGHARAGDMENAENILTVMRDAGIEPGPDTYLALLNAYAEKGDID 284
Cdd:PLN03218  711 KSIKLRPTVSTMNALITALCEGNQLPKALEVLSEMKRLGLCPNTITYSILLVASERKDDAD 771
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1046-1311 1.18e-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: 51.65  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305 1046 NQKKGAYDIFLNAKEQNiVFNAETYSNLIKLLMSEDYFTQAMEVkafAETHIKGFTLNDAANSRLIITQVRRDYLKEAVT 1125
Cdd:COG2956   22 GQPDKAIDLLEEALELD-PETVEAHLALGNLYRRRGEYDRAIRI---HQKLLERDPDRAEALLELAQDYLKAGLLDRAEE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305 1126 TLKTVLDQQQTpSRLAVTRVIQALAMKGDVEN-IEVVQKMLNgledsIGLSKMVFINNIALAQIKNNNIDAAIENIENML 1204
Cdd:COG2956   98 LLEKLLELDPD-DAEALRLLAEIYEQEGDWEKaIEVLERLLK-----LGPENAHAYCELAELYLEQGDYDEAIEALEKAL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305 1205 TSENKVIEPqYFGLAYLFRKviEEQLEPAVEKISIMAERLANQFAIYKPVTDFFLQLvdaGKVDDARALLQRCGAIAEQT 1284
Cdd:COG2956  172 KLDPDCARA-LLLLAELYLE--QGDYEEAIAALERALEQDPDYLPALPRLAELYEKL---GDPEEALELLRKALELDPSD 245

                        250       260
                 ....*....|....*....|....*..
gi 31621305 1285 PILLLFLLRNSRKQGKASTVKSVLELI 1311
Cdd:COG2956  246 DLLLALADLLERKEGLEAALALLERQL 272
 
Name Accession Description Interval E-value
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 144-284 3.93e-07

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 54.88  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305   144 EFAHRIWDTLQKLGAVYDVSHYNALLKVYLQNEYKFSPTDFLAKMEEANIQPNRVTYQRLIASYCNVGDIEGASKILGFM 223
Cdd:PLN03218  631 DFALSIYDDMKKKGVKPDEVFFSALVDVAGHAGDLDKAFEILQDARKQGIKLGTVSYSSLMGACSNAKNWKKALELYEDI 710

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31621305   224 KTKDLPVTEAVFSALVTGHARAGDMENAENILTVMRDAGIEPGPDTYLALLNAYAEKGDID 284
Cdd:PLN03218  711 KSIKLRPTVSTMNALITALCEGNQLPKALEVLSEMKRLGLCPNTITYSILLVASERKDDAD 771
PPR_long pfam17177
Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ...
 223-329 4.88e-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: 52.01  E-value: 4.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305    223 MKTKDLPVTEAVFSALVTGHARAGDMENAENILTVMRDAGIEPGPDTYLALLNAYAEKGDIDHVKQTLEKVEKSELHLMD 302
Cdd:pfam17177   81 MKAQGVSPNEATYTAVARLAAAKGDGDLAFDLVKEMEAAGVSPRLRSYSPALHAYCEAGDADKAYEVEEHMLAHGVELEE 160

                           90       100
                   ....*....|....*....|....*..
gi 31621305    303 RDLLQIIFSFSKAGYPQYVSEILEKVT 329
Cdd:pfam17177  161 PELAALLKVSAKAGRADKVYAYLHRLR 187
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1046-1311 1.18e-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: 51.65  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305 1046 NQKKGAYDIFLNAKEQNiVFNAETYSNLIKLLMSEDYFTQAMEVkafAETHIKGFTLNDAANSRLIITQVRRDYLKEAVT 1125
Cdd:COG2956   22 GQPDKAIDLLEEALELD-PETVEAHLALGNLYRRRGEYDRAIRI---HQKLLERDPDRAEALLELAQDYLKAGLLDRAEE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305 1126 TLKTVLDQQQTpSRLAVTRVIQALAMKGDVEN-IEVVQKMLNgledsIGLSKMVFINNIALAQIKNNNIDAAIENIENML 1204
Cdd:COG2956   98 LLEKLLELDPD-DAEALRLLAEIYEQEGDWEKaIEVLERLLK-----LGPENAHAYCELAELYLEQGDYDEAIEALEKAL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305 1205 TSENKVIEPqYFGLAYLFRKviEEQLEPAVEKISIMAERLANQFAIYKPVTDFFLQLvdaGKVDDARALLQRCGAIAEQT 1284
Cdd:COG2956  172 KLDPDCARA-LLLLAELYLE--QGDYEEAIAALERALEQDPDYLPALPRLAELYEKL---GDPEEALELLRKALELDPSD 245

                        250       260
                 ....*....|....*....|....*..
gi 31621305 1285 PILLLFLLRNSRKQGKASTVKSVLELI 1311
Cdd:COG2956  246 DLLLALADLLERKEGLEAALALLERQL 272
 
Name Accession Description Interval E-value
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 144-284 3.93e-07

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 54.88  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305   144 EFAHRIWDTLQKLGAVYDVSHYNALLKVYLQNEYKFSPTDFLAKMEEANIQPNRVTYQRLIASYCNVGDIEGASKILGFM 223
Cdd:PLN03218  631 DFALSIYDDMKKKGVKPDEVFFSALVDVAGHAGDLDKAFEILQDARKQGIKLGTVSYSSLMGACSNAKNWKKALELYEDI 710

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31621305   224 KTKDLPVTEAVFSALVTGHARAGDMENAENILTVMRDAGIEPGPDTYLALLNAYAEKGDID 284
Cdd:PLN03218  711 KSIKLRPTVSTMNALITALCEGNQLPKALEVLSEMKRLGLCPNTITYSILLVASERKDDAD 771
PPR_long pfam17177
Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ...
 223-329 4.88e-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: 52.01  E-value: 4.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305    223 MKTKDLPVTEAVFSALVTGHARAGDMENAENILTVMRDAGIEPGPDTYLALLNAYAEKGDIDHVKQTLEKVEKSELHLMD 302
Cdd:pfam17177   81 MKAQGVSPNEATYTAVARLAAAKGDGDLAFDLVKEMEAAGVSPRLRSYSPALHAYCEAGDADKAYEVEEHMLAHGVELEE 160

                           90       100
                   ....*....|....*....|....*..
gi 31621305    303 RDLLQIIFSFSKAGYPQYVSEILEKVT 329
Cdd:pfam17177  161 PELAALLKVSAKAGRADKVYAYLHRLR 187
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1046-1311 1.18e-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: 51.65  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305 1046 NQKKGAYDIFLNAKEQNiVFNAETYSNLIKLLMSEDYFTQAMEVkafAETHIKGFTLNDAANSRLIITQVRRDYLKEAVT 1125
Cdd:COG2956   22 GQPDKAIDLLEEALELD-PETVEAHLALGNLYRRRGEYDRAIRI---HQKLLERDPDRAEALLELAQDYLKAGLLDRAEE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305 1126 TLKTVLDQQQTpSRLAVTRVIQALAMKGDVEN-IEVVQKMLNgledsIGLSKMVFINNIALAQIKNNNIDAAIENIENML 1204
Cdd:COG2956   98 LLEKLLELDPD-DAEALRLLAEIYEQEGDWEKaIEVLERLLK-----LGPENAHAYCELAELYLEQGDYDEAIEALEKAL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305 1205 TSENKVIEPqYFGLAYLFRKviEEQLEPAVEKISIMAERLANQFAIYKPVTDFFLQLvdaGKVDDARALLQRCGAIAEQT 1284
Cdd:COG2956  172 KLDPDCARA-LLLLAELYLE--QGDYEEAIAALERALEQDPDYLPALPRLAELYEKL---GDPEEALELLRKALELDPSD 245

                        250       260
                 ....*....|....*....|....*..
gi 31621305 1285 PILLLFLLRNSRKQGKASTVKSVLELI 1311
Cdd:COG2956  246 DLLLALADLLERKEGLEAALALLERQL 272
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 183-300 3.13e-06

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 51.80  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305   183 DFLAKM--EEANIQPNRVTYQRLIASYCNVGDIEGASKILGFMKTKDLPVTEAVFSALVTGHARAGDMENAENILTVMRD 260
Cdd:PLN03218  563 DVLAEMkaETHPIDPDHITVGALMKACANAGQVDRAKEVYQMIHEYNIKGTPEVYTIAVNSCSQKGDWDFALSIYDDMKK 642

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 31621305   261 AGIEPGPDTYLALLNAYAEKGDIDHVKQTLEKVEKSELHL 300
Cdd:PLN03218  643 KGVKPDEVFFSALVDVAGHAGDLDKAFEILQDARKQGIKL 682
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 188-298 1.22e-05

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 49.88  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305   188 MEEANIQPNRVTYQRLIASYCNVGDIEGASKILGFMKTKDLPVTEAVFSALVTGHARAGDMENAENILTVMRDAGIEPGP 267
Cdd:PLN03218  605 IHEYNIKGTPEVYTIAVNSCSQKGDWDFALSIYDDMKKKGVKPDEVFFSALVDVAGHAGDLDKAFEILQDARKQGIKLGT 684

                          90       100       110
                  ....*....|....*....|....*....|.
gi 31621305   268 DTYLALLNAYAEKGDIDHVKQTLEKVEKSEL 298
Cdd:PLN03218  685 VSYSSLMGACSNAKNWKKALELYEDIKSIKL 715
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 187-296 1.40e-05

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 49.88  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305   187 KMEEANIQPNRVTYQRLIASYCNVGDIEGASKILGFMKTKDLPVTEAVFSALVTGHARAGDMENAENILTVMRDAG--IE 264
Cdd:PLN03218  497 EMVNAGVEANVHTFGALIDGCARAGQVAKAFGAYGIMRSKNVKPDRVVFNALISACGQSGAVDRAFDVLAEMKAEThpID 576

                          90       100       110
                  ....*....|....*....|....*....|..
gi 31621305   265 PGPDTYLALLNAYAEKGDIDHVKQTLEKVEKS 296
Cdd:PLN03218  577 PDHITVGALMKACANAGQVDRAKEVYQMIHEY 608
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1184-1348 4.75e-05

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: 46.65  E-value: 4.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305 1184 ALAQIKNNNIDAAIENIENMLTSENKVIEPqYFGLAYLFRKviEEQLEPAVEK----ISIMAERLANQFAIYKpvtDFFl 1259
Cdd:COG2956   15 GLNYLLNGQPDKAIDLLEEALELDPETVEA-HLALGNLYRR--RGEYDRAIRIhqklLERDPDRAEALLELAQ---DYL- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305 1260 qlvDAGKVDDARALLQRCGAIAEQTPILLLFLLRNSRKQGKASTVKSVLELIPELN-EKEEAYNSLMKSYVSEKDVTSAK 1338
Cdd:COG2956   88 ---KAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGpENAHAYCELAELYLEQGDYDEAI 164

                        170
                 ....*....|
gi 31621305 1339 ALYEHLTAKN 1348
Cdd:COG2956  165 EALEKALKLD 174
PPR_2 pfam13041
PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ...
 195-244 1.75e-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: 40.42  E-value: 1.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 31621305    195 PNRVTYQRLIASYCNVGDIEGASKILGFMKTKDLPVTEAVFSALVTGHAR 244
Cdd:pfam13041    1 PDVVTYNTLINGYCKKGKVEEAFKLFNEMKKRGVKPNVYTYTILINGLCK 50
PPR_long pfam17177
Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ...
 183-269 2.20e-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: 43.92  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305    183 DFLAKMEEANIQPNRVTYQRLIASYCNVGDIEGASKILGFMKTKDLPVTEAVFSALVTGHARAGDMENAENILTVMRDAG 262
Cdd:pfam17177  111 DLVKEMEAAGVSPRLRSYSPALHAYCEAGDADKAYEVEEHMLAHGVELEEPELAALLKVSAKAGRADKVYAYLHRLRDAV 190


                   ....*..
gi 31621305    263 IEPGPDT 269
Cdd:pfam17177  191 RQVSEST 197
PPR_long pfam17177
Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ...
 135-292 3.55e-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: 3.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305    135 PELKLEERTEFAHRIWDTLQKLgAVYDVS----------HYNALLKVYLQNEYKFSPTDFLA---------KMEEANIQP 195
Cdd:pfam17177   10 PESELRFQLDKCSKHADATGAL-ALYDAAkaegvrlaqyHYNVLLYLCSKAADATDLKPQLAadrgfevfeAMKAQGVSP 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305    196 NRVTYQRLIASYCNVGDIEGASKILGFMKTKDLPVTEAVFSALVTGHARAGDMENAENILTVMRDAGIEPGPDTYLALLN 275
Cdd:pfam17177   89 NEATYTAVARLAAAKGDGDLAFDLVKEMEAAGVSPRLRSYSPALHAYCEAGDADKAYEVEEHMLAHGVELEEPELAALLK 168

                          170
                   ....*....|....*..
gi 31621305    276 AYAEKGDIDHVKQTLEK 292
Cdd:pfam17177  169 VSAKAGRADKVYAYLHR 185
PPR_3 pfam13812
Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ...
 218-277 3.66e-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: 40.03  E-value: 3.66e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305    218 KILGFMKTKDLPVTEAVFSALVTGHARAGDMENAENILTVMRDAGIEPGPDTYLALLNAY 277
Cdd:pfam13812    1 SILREMVRDGIQLNVNTYTHLLHAYANVGNLKLALEIFERMKKKGIKPTLDTYNAILGVI 60
PPR_3 pfam13812
Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ...
 148-209 1.02e-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: 38.88  E-value: 1.02e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31621305    148 RIWDTLQKLGAVYDVSHYNALLKVYLQNEYKFSPTDFLAKMEEANIQPNRVTYQRLIASYCN 209
Cdd:pfam13812    1 SILREMVRDGIQLNVNTYTHLLHAYANVGNLKLALEIFERMKKKGIKPTLDTYNAILGVIGG 62
PPR_3 pfam13812
Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ...
 185-239 1.02e-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: 38.88  E-value: 1.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 31621305    185 LAKMEEANIQPNRVTYQRLIASYCNVGDIEGASKILGFMKTKDLPVTEAVFSALV 239
Cdd:pfam13812    3 LREMVRDGIQLNVNTYTHLLHAYANVGNLKLALEIFERMKKKGIKPTLDTYNAIL 57
PPR_2 pfam13041
PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ...
 235-278 1.68e-03

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: 37.73  E-value: 1.68e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 31621305    235 FSALVTGHARAGDMENAENILTVMRDAGIEPGPDTYLALLNAYA 278
Cdd:pfam13041    6 YNTLINGYCKKGKVEEAFKLFNEMKKRGVKPNVYTYTILINGLC 49
PPR_1 pfam12854
PPR repeat; This family matches additional variants of the PPR repeat that were not captured ...
 192-224 6.52e-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: 35.40  E-value: 6.52e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 31621305    192 NIQPNRVTYQRLIASYCNVGDIEGASKILGFMK 224
Cdd:pfam12854    2 GLKPDVVTYNTLINGLCRAGRVDEAFELLDEME 34
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 195-283 8.02e-03

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 40.63  E-value: 8.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305   195 PNRVTYQRLIASYCNVGDIEGASKILGFMKTKDLPVTEAVFSALVTGHARAGDMENAENILTVMRDAGIEPGPDTYLALL 274
Cdd:PLN03218  435 PTLSTFNMLMSVCASSQDIDGALRVLRLVQEAGLKADCKLYTTLISTCAKSGKVDAMFEVFHEMVNAGVEANVHTFGALI 514


                  ....*....
gi 31621305   275 NAYAEKGDI 283
Cdd:PLN03218  515 DGCARAGQV 523
PPR_2 pfam13041
PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ...
 161-209 8.07e-03

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: 35.80  E-value: 8.07e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 31621305    161 DVSHYNALLKVYLQNEyKFSPT-DFLAKMEEANIQPNRVTYQRLIASYCN 209
Cdd:pfam13041    2 DVVTYNTLINGYCKKG-KVEEAfKLFNEMKKRGVKPNVYTYTILINGLCK 50
PLN03077 PLN03077
Protein ECB2; Provisional
 158-261 9.71e-03

Protein ECB2; Provisional


Pssm-ID: 215561 [Multi-domain]  Cd Length: 857  Bit Score: 40.60  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31621305   158 AVYDVSHYNALLKVYLQNEYKFSPTDFLAKMEEANIQPNRVTYQRLIASYCNVGDIEGASKILGFMKTKDLPVTEAVFSA 237
Cdd:PLN03077  249 PRRDCISWNAMISGYFENGECLEGLELFFTMRELSVDPDLMTITSVISACELLGDERLGREMHGYVVKTGFAVDVSVCNS 328

                          90       100
                  ....*....|....*....|....*.
gi 31621305   238 LVTGHARAGDMENAENILTVM--RDA 261
Cdd:PLN03077  329 LIQMYLSLGSWGEAEKVFSRMetKDA 354
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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