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Conserved domains on  [gi|356547476|ref|XP_003542138|]
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pentatricopeptide repeat-containing protein At1g80880, mitochondrial [Glycine max]

Protein Classification

pentatricopeptide repeat-containing protein( domain architecture ID 13329385)

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
PLN03218 super family cl33664
maturation of RBCL 1; Provisional
 160-437 9.28e-20

maturation of RBCL 1; Provisional


The actual alignment was detected with superfamily member PLN03218:

Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 93.02  E-value: 9.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476  160 MIDRYASANNSAKAIQTFNFMDKFRLTPDQEAFHALLTALSKYGNVEEAEEFMLVNK-KLFPLNTESFNI-ILNGWCNIT 237
Cdd:PLN03218  513 LIDGCARAGQVAKAFGAYGIMRSKNVKPDRVVFNALISACGQSGAVDRAFDVLAEMKaETHPIDPDHITVgALMKACANA 592

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476  238 KDVYEAKRVWREMSKYCITPNATSYSYMISCFSNEGNLFDSLRLYDQMKKRGWIPGIEIYNSLVYVLTHENCLKEALRTI 317
Cdd:PLN03218  593 GQVDRAKEVYQMIHEYNIKGTPEVYTIAVNSCSQKGDWDFALSIYDDMKKKGVKPDEVFFSALVDVAGHAGDLDKAFEIL 672

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476  318 DKLKEQGLQPGSATFNSMILPLCEAGKLAGARIIFNTMVEENVSPTTETYHAFF----EGTDYQGTLEFLTRMKDSGLGP 393
Cdd:PLN03218  673 QDARKQGIKLGTVSYSSLMGACSNAKNWKKALELYEDIKSIKLRPTVSTMNALItalcEGNQLPKALEVLSEMKRLGLCP 752

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 356547476  394 NKDSFVIILAKFLKLKQPVNALKFWTEMKTYDVLPSCVHYRIMV 437
Cdd:PLN03218  753 NTITYSILLVASERKDDADVGLDLLSQAKEDGIKPNLVMCRCIT 796
PPR TIGR00756
pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ...
 431-464 4.01e-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: 35.12  E-value: 4.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 356547476  431 VHYRIMVEGLVTCRWFVKARDFYEEMVSNGCSAD 464
Cdd:TIGR00756   1 VTYNTLIDGLCKAGRVEEALELFKEMKERGIEPD 34
 
Name Accession Description Interval E-value
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 160-437 9.28e-20

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 93.02  E-value: 9.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476  160 MIDRYASANNSAKAIQTFNFMDKFRLTPDQEAFHALLTALSKYGNVEEAEEFMLVNK-KLFPLNTESFNI-ILNGWCNIT 237
Cdd:PLN03218  513 LIDGCARAGQVAKAFGAYGIMRSKNVKPDRVVFNALISACGQSGAVDRAFDVLAEMKaETHPIDPDHITVgALMKACANA 592

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476  238 KDVYEAKRVWREMSKYCITPNATSYSYMISCFSNEGNLFDSLRLYDQMKKRGWIPGIEIYNSLVYVLTHENCLKEALRTI 317
Cdd:PLN03218  593 GQVDRAKEVYQMIHEYNIKGTPEVYTIAVNSCSQKGDWDFALSIYDDMKKKGVKPDEVFFSALVDVAGHAGDLDKAFEIL 672

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476  318 DKLKEQGLQPGSATFNSMILPLCEAGKLAGARIIFNTMVEENVSPTTETYHAFF----EGTDYQGTLEFLTRMKDSGLGP 393
Cdd:PLN03218  673 QDARKQGIKLGTVSYSSLMGACSNAKNWKKALELYEDIKSIKLRPTVSTMNALItalcEGNQLPKALEVLSEMKRLGLCP 752

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 356547476  394 NKDSFVIILAKFLKLKQPVNALKFWTEMKTYDVLPSCVHYRIMV 437
Cdd:PLN03218  753 NTITYSILLVASERKDDADVGLDLLSQAKEDGIKPNLVMCRCIT 796
PPR_long pfam17177
Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ...
 256-402 8.15e-09

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: 55.87  E-value: 8.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476  256 TPNAtSYSYMISCFSNEGNLFDSLRLYDQMKKRGWIPGIEIYNSLVYVLT---------HENCLKEALRTIDKLKEQGLQ 326
Cdd:pfam17177   9 TPES-ELRFQLDKCSKHADATGALALYDAAKAEGVRLAQYHYNVLLYLCSkaadatdlkPQLAADRGFEVFEAMKAQGVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476  327 PGSATFNSMILPLCEAGKLAGARIIFNTMVEENVSPTTETY----HAFFEGTDYQGTLEFLTRMKDSGLGPNKDSFVIIL 402
Cdd:pfam17177  88 PNEATYTAVARLAAAKGDGDLAFDLVKEMEAAGVSPRLRSYspalHAYCEAGDADKAYEVEEHMLAHGVELEEPELAALL 167
PPR TIGR00756
pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ...
 261-294 2.10e-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: 38.59  E-value: 2.10e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 356547476  261 SYSYMISCFSNEGNLFDSLRLYDQMKKRGWIPGI 294
Cdd:TIGR00756   2 TYNTLIDGLCKAGRVEEALELFKEMKERGIEPDV 35
PPR TIGR00756
pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ...
 431-464 4.01e-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: 35.12  E-value: 4.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 356547476  431 VHYRIMVEGLVTCRWFVKARDFYEEMVSNGCSAD 464
Cdd:TIGR00756   1 VTYNTLIDGLCKAGRVEEALELFKEMKERGIEPD 34
 
Name Accession Description Interval E-value
PLN03218 PLN03218
maturation of RBCL 1; Provisional
 160-437 9.28e-20

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 93.02  E-value: 9.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476  160 MIDRYASANNSAKAIQTFNFMDKFRLTPDQEAFHALLTALSKYGNVEEAEEFMLVNK-KLFPLNTESFNI-ILNGWCNIT 237
Cdd:PLN03218  513 LIDGCARAGQVAKAFGAYGIMRSKNVKPDRVVFNALISACGQSGAVDRAFDVLAEMKaETHPIDPDHITVgALMKACANA 592

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476  238 KDVYEAKRVWREMSKYCITPNATSYSYMISCFSNEGNLFDSLRLYDQMKKRGWIPGIEIYNSLVYVLTHENCLKEALRTI 317
Cdd:PLN03218  593 GQVDRAKEVYQMIHEYNIKGTPEVYTIAVNSCSQKGDWDFALSIYDDMKKKGVKPDEVFFSALVDVAGHAGDLDKAFEIL 672

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476  318 DKLKEQGLQPGSATFNSMILPLCEAGKLAGARIIFNTMVEENVSPTTETYHAFF----EGTDYQGTLEFLTRMKDSGLGP 393
Cdd:PLN03218  673 QDARKQGIKLGTVSYSSLMGACSNAKNWKKALELYEDIKSIKLRPTVSTMNALItalcEGNQLPKALEVLSEMKRLGLCP 752

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 356547476  394 NKDSFVIILAKFLKLKQPVNALKFWTEMKTYDVLPSCVHYRIMV 437
Cdd:PLN03218  753 NTITYSILLVASERKDDADVGLDLLSQAKEDGIKPNLVMCRCIT 796
PPR_long pfam17177
Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ...
 256-402 8.15e-09

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: 55.87  E-value: 8.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476  256 TPNAtSYSYMISCFSNEGNLFDSLRLYDQMKKRGWIPGIEIYNSLVYVLT---------HENCLKEALRTIDKLKEQGLQ 326
Cdd:pfam17177   9 TPES-ELRFQLDKCSKHADATGALALYDAAKAEGVRLAQYHYNVLLYLCSkaadatdlkPQLAADRGFEVFEAMKAQGVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476  327 PGSATFNSMILPLCEAGKLAGARIIFNTMVEENVSPTTETY----HAFFEGTDYQGTLEFLTRMKDSGLGPNKDSFVIIL 402
Cdd:pfam17177  88 PNEATYTAVARLAAAKGDGDLAFDLVKEMEAAGVSPRLRSYspalHAYCEAGDADKAYEVEEHMLAHGVELEEPELAALL 167
PPR_2 pfam13041
PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ...
 222-271 6.75e-06

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: 43.12  E-value: 6.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 356547476  222 NTESFNIILNGWCNiTKDVYEAKRVWREMSKYCITPNATSYSYMISCFSN 271
Cdd:pfam13041   2 DVVTYNTLINGYCK-KGKVEEAFKLFNEMKKRGVKPNVYTYTILINGLCK 50
PPR_2 pfam13041
PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ...
 327-367 5.16e-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: 40.81  E-value: 5.16e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 356547476  327 PGSATFNSMILPLCEAGKLAGARIIFNTMVEENVSPTTETY 367
Cdd:pfam13041   1 PDVVTYNTLINGYCKKGKVEEAFKLFNEMKKRGVKPNVYTY 41
PPR TIGR00756
pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ...
 261-294 2.10e-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: 38.59  E-value: 2.10e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 356547476  261 SYSYMISCFSNEGNLFDSLRLYDQMKKRGWIPGI 294
Cdd:TIGR00756   2 TYNTLIDGLCKAGRVEEALELFKEMKERGIEPDV 35
PPR_2 pfam13041
PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ...
 292-340 3.41e-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: 38.50  E-value: 3.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 356547476  292 PGIEIYNSLVYVLTHENCLKEALRTIDKLKEQGLQPGSATFNSMILPLC 340
Cdd:pfam13041   1 PDVVTYNTLINGYCKKGKVEEAFKLFNEMKKRGVKPNVYTYTILINGLC 49
PPR_2 pfam13041
PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ...
 257-301 7.42e-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: 37.34  E-value: 7.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 356547476  257 PNATSYSYMISCFSNEGNLFDSLRLYDQMKKRGWIPGIEIYNSLV 301
Cdd:pfam13041   1 PDVVTYNTLINGYCKKGKVEEAFKLFNEMKKRGVKPNVYTYTILI 45
PPR_3 pfam13812
Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ...
 245-301 8.90e-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: 37.72  E-value: 8.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 356547476  245 RVWREMSKYCITPNATSYSYMISCFSNEGNLFDSLRLYDQMKKRGWIPGIEIYNSLV 301
Cdd:pfam13812   1 SILREMVRDGIQLNVNTYTHLLHAYANVGNLKLALEIFERMKKKGIKPTLDTYNAIL 57
PPR_3 pfam13812
Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ...
 280-336 1.17e-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: 1.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 356547476  280 RLYDQMKKRGWIPGIEIYNSLVYVLTHENCLKEALRTIDKLKEQGLQPGSATFNSMI 336
Cdd:pfam13812   1 SILREMVRDGIQLNVNTYTHLLHAYANVGNLKLALEIFERMKKKGIKPTLDTYNAIL 57
PLN03077 PLN03077
Protein ECB2; Provisional
 159-397 2.37e-03

Protein ECB2; Provisional


Pssm-ID: 215561 [Multi-domain]  Cd Length: 857  Bit Score: 40.60  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476 159 IMIDRYASANNSAKAIQTFNFMDKFRLTPDQEAFHALLTALSKYGNVEEAEEfmlvnkkLFPLNTEsfniilngwcnitk 238
Cdd:PLN03077 559 ILLTGYVAHGKGSMAVELFNRMVESGVNPDEVTFISLLCACSRSGMVTQGLE-------YFHSMEE-------------- 617

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476 239 dvyeakrvwremsKYCITPNATSYSYMISCFSNEGNLFDSLRLYDQMKKRgwiPGIEIYNSLVYVL-THENCLKEALRTI 317
Cdd:PLN03077 618 -------------KYSITPNLKHYACVVDLLGRAGKLTEAYNFINKMPIT---PDPAVWGALLNACrIHRHVELGELAAQ 681

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356547476 318 DKLKeqgLQPGSATFNSMILPL-CEAGKLAGARIIFNTMVEENVS--------PTTETYHAFFEGTDYQGTLE------- 381
Cdd:PLN03077 682 HIFE---LDPNSVGYYILLCNLyADAGKWDEVARVRKTMRENGLTvdpgcswvEVKGKVHAFLTDDESHPQIKeintvle 758

                        250
                 ....*....|....*..
gi 356547476 382 -FLTRMKDSGLGPNKDS 397
Cdd:PLN03077 759 gFYEKMKASGLAGSESS 775
PPR pfam01535
PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ...
 261-289 2.46e-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: 35.52  E-value: 2.46e-03
                          10        20
                  ....*....|....*....|....*....
gi 356547476  261 SYSYMISCFSNEGNLFDSLRLYDQMKKRG 289
Cdd:pfam01535   2 TYNSLISGYCKNGKLEEALELFKEMKEKG 30
PPR TIGR00756
pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ...
 431-464 4.01e-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: 35.12  E-value: 4.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 356547476  431 VHYRIMVEGLVTCRWFVKARDFYEEMVSNGCSAD 464
Cdd:TIGR00756   1 VTYNTLIDGLCKAGRVEEALELFKEMKERGIEPD 34
 
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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