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Conserved domains on  [gi|755515038|ref|XP_011239315|]
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pentatricopeptide repeat-containing protein 1, mitochondrial isoform X1 [Mus musculus]

Protein Classification

pentatricopeptide repeat-containing protein( domain architecture ID 12127860)

pentatricopeptide repeat (PPR)-containing protein may form anti-parallel alpha helices and bind single-stranded RNA in a sequence-specific and modular manner

CATH:  1.25.40.10
Gene Ontology:  GO:0003723
PubMed:  19004664|23635770|25882680|34065603|18031283|30809817
SCOP:  4001344

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PPR_2 pfam13041
PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ...
 174-217 1.13e-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: 64.69  E-value: 1.13e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 755515038  174 YTVLIGGCGRVGYLKKAFRLFNDMKKRDLEPSDATYTALFNVCA 217
Cdd:pfam13041   6 YNTLINGYCKKGKVEEAFKLFNEMKKRGVKPNVYTYTILINGLC 49
PLN03218 super family cl33664
maturation of RBCL 1; Provisional
 125-331 1.18e-11

maturation of RBCL 1; Provisional


The actual alignment was detected with superfamily member PLN03218:

Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 66.05  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  125 RPWRGRRNTQYwYFFQCKRLIKEGKLAEALDLFErQMLKEERLQPLECNYTVLIGGCGRVGYLKKAFRLfndmKKRDLEP 204
Cdd:PLN03218  362 GGVSGKRKSPE-YIDAYNRLLRDGRIKDCIDLLE-DMEKRGLLDMDKIYHAKFFKACKKQRAVKEAFRF----AKLIRNP 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  205 SDATYTALFNVCAESpwKDSAlqSALKLRQQLQARNFQLNLKTYHALLKVAAKCADLRLCLDVFKEIIQRGHAVTEETFC 284
Cdd:PLN03218  436 TLSTFNMLMSVCASS--QDID--GALRVLRLVQEAGLKADCKLYTTLISTCAKSGKVDAMFEVFHEMVNAGVEANVHTFG 511

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 755515038  285 FLLVGCiqdKKTG-FRQAMQVWRQMLSLGIKPSRHGYNLLLEAardCG 331
Cdd:PLN03218  512 ALIDGC---ARAGqVAKAFGAYGIMRSKNVKPDRVVFNALISA---CG 553
 
Name Accession Description Interval E-value
PPR_2 pfam13041
PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ...
 174-217 1.13e-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: 64.69  E-value: 1.13e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 755515038  174 YTVLIGGCGRVGYLKKAFRLFNDMKKRDLEPSDATYTALFNVCA 217
Cdd:pfam13041   6 YNTLINGYCKKGKVEEAFKLFNEMKKRGVKPNVYTYTILINGLC 49
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 125-331 1.18e-11

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 66.05  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  125 RPWRGRRNTQYwYFFQCKRLIKEGKLAEALDLFErQMLKEERLQPLECNYTVLIGGCGRVGYLKKAFRLfndmKKRDLEP 204
Cdd:PLN03218  362 GGVSGKRKSPE-YIDAYNRLLRDGRIKDCIDLLE-DMEKRGLLDMDKIYHAKFFKACKKQRAVKEAFRF----AKLIRNP 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  205 SDATYTALFNVCAESpwKDSAlqSALKLRQQLQARNFQLNLKTYHALLKVAAKCADLRLCLDVFKEIIQRGHAVTEETFC 284
Cdd:PLN03218  436 TLSTFNMLMSVCASS--QDID--GALRVLRLVQEAGLKADCKLYTTLISTCAKSGKVDAMFEVFHEMVNAGVEANVHTFG 511

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 755515038  285 FLLVGCiqdKKTG-FRQAMQVWRQMLSLGIKPSRHGYNLLLEAardCG 331
Cdd:PLN03218  512 ALIDGC---ARAGqVAKAFGAYGIMRSKNVKPDRVVFNALISA---CG 553
PPR_long pfam17177
Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ...
 163-334 2.57e-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: 50.86  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  163 KEERLQPLECNYTVLIGGCGRVGYLKKAFRLFNDMKKRDLEPSDATYTALFNVC-----AESPWKDSALQSALKLRQQLQ 237
Cdd:pfam17177   3 KKKGKQTPESELRFQLDKCSKHADATGALALYDAAKAEGVRLAQYHYNVLLYLCskaadATDLKPQLAADRGFEVFEAMK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  238 ARNFQLNLKTYHALLKVAAKCADLRLCLDVFKEIIQRGHAVTEETFCFLLVgCIQDKKTgFRQAMQVWRQMLSLGIKPSR 317
Cdd:pfam17177  83 AQGVSPNEATYTAVARLAAAKGDGDLAFDLVKEMEAAGVSPRLRSYSPALH-AYCEAGD-ADKAYEVEEHMLAHGVELEE 160

                         170
                  ....*....|....*..
gi 755515038  318 HGYNLLLEAARDCGLGD 334
Cdd:pfam17177 161 PELAALLKVSAKAGRAD 177
PPR TIGR00756
pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ...
 174-206 1.18e-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: 1.18e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 755515038  174 YTVLIGGCGRVGYLKKAFRLFNDMKKRDLEPSD 206
Cdd:TIGR00756   3 YNTLIDGLCKAGRVEEALELFKEMKERGIEPDV 35
 
Name Accession Description Interval E-value
PPR_2 pfam13041
PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ...
 174-217 1.13e-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: 64.69  E-value: 1.13e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 755515038  174 YTVLIGGCGRVGYLKKAFRLFNDMKKRDLEPSDATYTALFNVCA 217
Cdd:pfam13041   6 YNTLINGYCKKGKVEEAFKLFNEMKKRGVKPNVYTYTILINGLC 49
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 125-331 1.18e-11

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 66.05  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  125 RPWRGRRNTQYwYFFQCKRLIKEGKLAEALDLFErQMLKEERLQPLECNYTVLIGGCGRVGYLKKAFRLfndmKKRDLEP 204
Cdd:PLN03218  362 GGVSGKRKSPE-YIDAYNRLLRDGRIKDCIDLLE-DMEKRGLLDMDKIYHAKFFKACKKQRAVKEAFRF----AKLIRNP 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  205 SDATYTALFNVCAESpwKDSAlqSALKLRQQLQARNFQLNLKTYHALLKVAAKCADLRLCLDVFKEIIQRGHAVTEETFC 284
Cdd:PLN03218  436 TLSTFNMLMSVCASS--QDID--GALRVLRLVQEAGLKADCKLYTTLISTCAKSGKVDAMFEVFHEMVNAGVEANVHTFG 511

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 755515038  285 FLLVGCiqdKKTG-FRQAMQVWRQMLSLGIKPSRHGYNLLLEAardCG 331
Cdd:PLN03218  512 ALIDGC---ARAGqVAKAFGAYGIMRSKNVKPDRVVFNALISA---CG 553
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 142-350 1.10e-09

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 59.89  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  142 KRLIKEGKLAEALDLFerQMLKEERLQ-PLECnYTVLIGGCGRVGYLKKAFRLFNDMKKRDLEPSDATYTALFNVCAESp 220
Cdd:PLN03218  587 KACANAGQVDRAKEVY--QMIHEYNIKgTPEV-YTIAVNSCSQKGDWDFALSIYDDMKKKGVKPDEVFFSALVDVAGHA- 662

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  221 wkdSALQSALKLRQQLQARNFQLNLKTYHALLKVAAKCADLRLCLDVFKEIIQRGHAVTEETFCFLLVGCIQDKKtgFRQ 300
Cdd:PLN03218  663 ---GDLDKAFEILQDARKQGIKLGTVSYSSLMGACSNAKNWKKALELYEDIKSIKLRPTVSTMNALITALCEGNQ--LPK 737

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755515038  301 AMQVWRQMLSLGIKPSRHGYNLLLEAA-RDcglGDPEVASRLLLTSQEETI 350
Cdd:PLN03218  738 ALEVLSEMKRLGLCPNTITYSILLVASeRK---DDADVGLDLLSQAKEDGI 785
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 174-334 1.86e-08

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 56.04  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  174 YTVLIGGCGRVGYLKKAFRLFNDMKKRDLEPSDATYTALFNVCAESpwkdSALQSALKLRQQLQARNFQLNLK--TYHAL 251
Cdd:PLN03218  510 FGALIDGCARAGQVAKAFGAYGIMRSKNVKPDRVVFNALISACGQS----GAVDRAFDVLAEMKAETHPIDPDhiTVGAL 585

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  252 LKVAAKCADLRLCLDVFKEIIQRGHAVTEETFCFLLVGCIQDKKTGFrqAMQVWRQMLSLGIKPSRHGYNLLLEAARDCG 331
Cdd:PLN03218  586 MKACANAGQVDRAKEVYQMIHEYNIKGTPEVYTIAVNSCSQKGDWDF--ALSIYDDMKKKGVKPDEVFFSALVDVAGHAG 663


                  ...
gi 755515038  332 LGD 334
Cdd:PLN03218  664 DLD 666
PPR_long pfam17177
Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ...
 163-334 2.57e-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: 50.86  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  163 KEERLQPLECNYTVLIGGCGRVGYLKKAFRLFNDMKKRDLEPSDATYTALFNVC-----AESPWKDSALQSALKLRQQLQ 237
Cdd:pfam17177   3 KKKGKQTPESELRFQLDKCSKHADATGALALYDAAKAEGVRLAQYHYNVLLYLCskaadATDLKPQLAADRGFEVFEAMK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  238 ARNFQLNLKTYHALLKVAAKCADLRLCLDVFKEIIQRGHAVTEETFCFLLVgCIQDKKTgFRQAMQVWRQMLSLGIKPSR 317
Cdd:pfam17177  83 AQGVSPNEATYTAVARLAAAKGDGDLAFDLVKEMEAAGVSPRLRSYSPALH-AYCEAGD-ADKAYEVEEHMLAHGVELEE 160

                         170
                  ....*....|....*..
gi 755515038  318 HGYNLLLEAARDCGLGD 334
Cdd:pfam17177 161 PELAALLKVSAKAGRAD 177
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 146-315 4.23e-07

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 51.80  E-value: 4.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  146 KEGKLAEALDLFERqmLKEERLQPLECNYTVLIGGCGRVGYLKKAFRLFNDMKKRDLEPSDATYTALFNVCAESP-Wkds 224
Cdd:PLN03218  626 QKGDWDFALSIYDD--MKKKGVKPDEVFFSALVDVAGHAGDLDKAFEILQDARKQGIKLGTVSYSSLMGACSNAKnW--- 700

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  225 alQSALKLRQQLQARNFQLNLKTYHALLKVAAKCADLRLCLDVFKEIIQRGHAVTEETFCFLLVGCiqDKKTGFRQAMQV 304
Cdd:PLN03218  701 --KKALELYEDIKSIKLRPTVSTMNALITALCEGNQLPKALEVLSEMKRLGLCPNTITYSILLVAS--ERKDDADVGLDL 776

                         170
                  ....*....|.
gi 755515038  305 WRQMLSLGIKP 315
Cdd:PLN03218  777 LSQAKEDGIKP 787
PPR TIGR00756
pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ...
 174-206 1.18e-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: 1.18e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 755515038  174 YTVLIGGCGRVGYLKKAFRLFNDMKKRDLEPSD 206
Cdd:TIGR00756   3 YNTLIDGLCKAGRVEEALELFKEMKERGIEPDV 35
PPR_long pfam17177
Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ...
 124-311 2.73e-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: 47.78  E-value: 2.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  124 PRPWRGRRNTQYWYFFQCKRLIKEGKLAEALDLFErQMLKEE-RLQPLecNYTVLIGGCGRVG---------YLKKAFRL 193
Cdd:pfam17177   1 QRKKKGKQTPESELRFQLDKCSKHADATGALALYD-AAKAEGvRLAQY--HYNVLLYLCSKAAdatdlkpqlAADRGFEV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  194 FNDMKKRDLEPSDATYTALFNVCAespwKDSALQSALKLRQQLQARNFQLNLKTYHALLKVAAKCADLRLCLDVFKEIIQ 273
Cdd:pfam17177  78 FEAMKAQGVSPNEATYTAVARLAA----AKGDGDLAFDLVKEMEAAGVSPRLRSYSPALHAYCEAGDADKAYEVEEHMLA 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 755515038  274 RGHAVTEETFCFLLVGCIqdkKTGfrQAMQVWRQMLSL 311
Cdd:pfam17177 154 HGVELEEPELAALLKVSA---KAG--RADKVYAYLHRL 186
PPR pfam01535
PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ...
 174-202 1.27e-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: 41.68  E-value: 1.27e-05
                          10        20
                  ....*....|....*....|....*....
gi 755515038  174 YTVLIGGCGRVGYLKKAFRLFNDMKKRDL 202
Cdd:pfam01535   3 YNSLISGYCKNGKLEEALELFKEMKEKGI 31
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 148-316 1.84e-05

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 46.79  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  148 GKLAEALDLFerQMLKEERLQPLECNYTVLIGGCGRVGYLKKAFRLFNDMKKRDLEPSDATYTALFNVCAESpwkdSALQ 227
Cdd:PLN03218  663 GDLDKAFEIL--QDARKQGIKLGTVSYSSLMGACSNAKNWKKALELYEDIKSIKLRPTVSTMNALITALCEG----NQLP 736

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038  228 SALKLRQQLQARNFQLNLKTYHALLKVAAKCADLRLCLDVFKEIIQRGHAVTeetfcFLLVGCI---------------- 291
Cdd:PLN03218  737 KALEVLSEMKRLGLCPNTITYSILLVASERKDDADVGLDLLSQAKEDGIKPN-----LVMCRCItglclrrfekacalge 811

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 755515038  292 ------------QDKKTGfrQAMQVWRQMLSLGIKPS 316
Cdd:PLN03218  812 pvvsfdsgrpqiENKWTS--WALMVYRETISAGTLPT 846
PPR_3 pfam13812
Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ...
 174-216 4.92e-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: 40.80  E-value: 4.92e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 755515038  174 YTVLIGGCGRVGYLKKAFRLFNDMKKRDLEPSDATYTALFNVC 216
Cdd:pfam13812  18 YTHLLHAYANVGNLKLALEIFERMKKKGIKPTLDTYNAILGVI 60
PPR_3 pfam13812
Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ...
 231-287 1.51e-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: 39.26  E-value: 1.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755515038  231 KLRQQLQARNFQLNLKTYHALLKVAAKCADLRLCLDVFKEIIQRGHAVTEETFCFLL 287
Cdd:pfam13812   1 SILREMVRDGIQLNVNTYTHLLHAYANVGNLKLALEIFERMKKKGIKPTLDTYNAIL 57
PPR_1 pfam12854
PPR repeat; This family matches additional variants of the PPR repeat that were not captured ...
 174-198 1.49e-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: 35.78  E-value: 1.49e-03
                          10        20
                  ....*....|....*....|....*
gi 755515038  174 YTVLIGGCGRVGYLKKAFRLFNDMK 198
Cdd:pfam12854  10 YNTLINGLCRAGRVDEAFELLDEME 34
PLN03077 PLN03077
Protein ECB2; Provisional
 185-338 1.57e-03

Protein ECB2; Provisional


Pssm-ID: 215561 [Multi-domain]  Cd Length: 857  Bit Score: 40.60  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515038 185 GYLKKAFRLFNDMKKRDLEPSDATYTALFNVCAespWKdSALQSALKLRQQLQARNFQLNLKTYHALLKVAAKCADLRLC 264
Cdd:PLN03077  65 GQLEQALKLLESMQELRVPVDEDAYVALFRLCE---WK-RAVEEGSRVCSRALSSHPSLGVRLGNAMLSMFVRFGELVHA 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755515038 265 LDVFKEIIQRghavteETFCF-LLVGCIQdKKTGFRQAMQVWRQMLSLGIKPSRHGYNLLLeaaRDCGlGDPEVA 338
Cdd:PLN03077 141 WYVFGKMPER------DLFSWnVLVGGYA-KAGYFDEALCLYHRMLWAGVRPDVYTFPCVL---RTCG-GIPDLA 204
 
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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