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Conserved domains on  [gi|311893396|ref|NP_001185808|]
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ATP5J2-PTCD1 fusion protein [Homo sapiens]

Protein Classification

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 ...
225-268 2.00e-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: 62.00  E-value: 2.00e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 311893396  225 YTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSDATYTALFNVCA 268
Cdd:pfam13041   6 YNTLINGYCKKGKVEEAFKLFNEMKKRGVKPNVYTYTILINGLC 49
PPR_long super family cl38513
Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ...
214-405 2.46e-10

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.


The actual alignment was detected with superfamily member pfam17177:

Pssm-ID: 407303 [Multi-domain]  Cd Length: 212  Bit Score: 60.87  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  214 KEERLQPMESNYTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSDATYTALFNVC-----AESPWKDSALQSALKLRQQLQ 288
Cdd:pfam17177   3 KKKGKQTPESELRFQLDKCSKHADATGALALYDAAKAEGVRLAQYHYNVLLYLCskaadATDLKPQLAADRGFEVFEAMK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  289 AKNFELNLKTYHALLKMAAKCADLRMCLDVFKEIIHKGHVVTEETFSFLLMgCIQDKKTGFRyALQVWRLMLSLGLQPSR 368
Cdd:pfam17177  83 AQGVSPNEATYTAVARLAAAKGDGDLAFDLVKEMEAAGVSPRLRSYSPALH-AYCEAGDADK-AYEVEEHMLAHGVELEE 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 311893396  369 DSYNLLLVAARDCGLGDpQVaSELLLKPREeaTVLQP 405
Cdd:pfam17177 161 PELAALLKVSAKAGRAD-KV-YAYLHRLRD--AVRQV 193
PLN03218 super family cl33664
maturation of RBCL 1; Provisional
179-649 2.72e-10

maturation of RBCL 1; Provisional


The actual alignment was detected with superfamily member PLN03218:

Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 64.13  E-value: 2.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  179 RGRRNTPYwYFLQCKHLIKEGKLVEALDLFErQMLKEERLQPMESNYTVLIGGCGRVGYLKKAFNLYNQMkkrdLEPSDA 258
Cdd:PLN03218  365 SGKRKSPE-YIDAYNRLLRDGRIKDCIDLLE-DMEKRGLLDMDKIYHAKFFKACKKQRAVKEAFRFAKLI----RNPTLS 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  259 TYTALFNVCAESpwKDSAlqSALKLRQQLQAKNFELNLKTYHALLKMAAKCADLRMCLDVFKEIIHKGHVVTEETFSFLL 338
Cdd:PLN03218  439 TFNMLMSVCASS--QDID--GALRVLRLVQEAGLKADCKLYTTLISTCAKSGKVDAMFEVFHEMVNAGVEANVHTFGALI 514
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  339 MGCiqdKKTG-FRYALQVWRLMLSLGLQPSRDSYNLLLVAardCG-LGDPQVASELLLKPREEATVLQPPvsrqrprrta 416
Cdd:PLN03218  515 DGC---ARAGqVAKAFGAYGIMRSKNVKPDRVVFNALISA---CGqSGAVDRAFDVLAEMKAETHPIDPD---------- 578
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  417 QAKAGNLMSAMLHVEALERQlfLEPSQALgppepPEARVpgKAQPEVdtkaepsHTAALTAVALKPppvELEVNL----- 491
Cdd:PLN03218  579 HITVGALMKACANAGQVDRA--KEVYQMI-----HEYNI--KGTPEV-------YTIAVNSCSQKG---DWDFALsiydd 639
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  492 LTPGAVPPTVVSFGtvttpadrlALI------GGLEGFLSKMAEHRQQ-----------------------------PDI 536
Cdd:PLN03218  640 MKKKGVKPDEVFFS---------ALVdvaghaGDLDKAFEILQDARKQgiklgtvsysslmgacsnaknwkkalelyEDI 710
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  537 RTLTLLAEVvesgSPAESLLLALLDEHQVEadltffntlvRKKSKLGDLEGAkallpvlakrGLVPNLQTFCNLAIGCHR 616
Cdd:PLN03218  711 KSIKLRPTV----STMNALITALCEGNQLP----------KALEVLSEMKRL----------GLCPNTITYSILLVASER 766
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 311893396  617 PKD---GLQLLTDMKKSQVTPNTHIYSALINAAIRK 649
Cdd:PLN03218  767 KDDadvGLDLLSQAKEDGIKPNLVMCRCITGLCLRR 802
WRW super family cl10896
Mitochondrial F1F0-ATP synthase, subunit f; This is a family of small proteins of ...
8-41 1.93e-08

Mitochondrial F1F0-ATP synthase, subunit f; This is a family of small proteins of approximately 110 amino acids, which are highly conserved from nematodes to humans. Some members of the family have been annotated in Swiss-Prot as being the f subunit of mitochondrial F1F0-ATP synthase but this could not be confirmed. The sequence has a well-conserved WRW motif. The exact function of the protein is not known.


The actual alignment was detected with superfamily member pfam10206:

Pssm-ID: 431134  Cd Length: 102  Bit Score: 52.68  E-value: 1.93e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 311893396    8 KDKKLLEVKLGELPSWILMRDFSPSGIFGAFQRG 41
Cdd:pfam10206  26 PDTPFGDVKLGELPSWLGRRNKTPSAFAGAFSRA 59
 
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 ...
225-268 2.00e-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: 62.00  E-value: 2.00e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 311893396  225 YTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSDATYTALFNVCA 268
Cdd:pfam13041   6 YNTLINGYCKKGKVEEAFKLFNEMKKRGVKPNVYTYTILINGLC 49
PPR_long pfam17177
Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ...
214-405 2.46e-10

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: 60.87  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  214 KEERLQPMESNYTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSDATYTALFNVC-----AESPWKDSALQSALKLRQQLQ 288
Cdd:pfam17177   3 KKKGKQTPESELRFQLDKCSKHADATGALALYDAAKAEGVRLAQYHYNVLLYLCskaadATDLKPQLAADRGFEVFEAMK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  289 AKNFELNLKTYHALLKMAAKCADLRMCLDVFKEIIHKGHVVTEETFSFLLMgCIQDKKTGFRyALQVWRLMLSLGLQPSR 368
Cdd:pfam17177  83 AQGVSPNEATYTAVARLAAAKGDGDLAFDLVKEMEAAGVSPRLRSYSPALH-AYCEAGDADK-AYEVEEHMLAHGVELEE 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 311893396  369 DSYNLLLVAARDCGLGDpQVaSELLLKPREeaTVLQP 405
Cdd:pfam17177 161 PELAALLKVSAKAGRAD-KV-YAYLHRLRD--AVRQV 193
PLN03218 PLN03218
maturation of RBCL 1; Provisional
179-649 2.72e-10

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 64.13  E-value: 2.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  179 RGRRNTPYwYFLQCKHLIKEGKLVEALDLFErQMLKEERLQPMESNYTVLIGGCGRVGYLKKAFNLYNQMkkrdLEPSDA 258
Cdd:PLN03218  365 SGKRKSPE-YIDAYNRLLRDGRIKDCIDLLE-DMEKRGLLDMDKIYHAKFFKACKKQRAVKEAFRFAKLI----RNPTLS 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  259 TYTALFNVCAESpwKDSAlqSALKLRQQLQAKNFELNLKTYHALLKMAAKCADLRMCLDVFKEIIHKGHVVTEETFSFLL 338
Cdd:PLN03218  439 TFNMLMSVCASS--QDID--GALRVLRLVQEAGLKADCKLYTTLISTCAKSGKVDAMFEVFHEMVNAGVEANVHTFGALI 514
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  339 MGCiqdKKTG-FRYALQVWRLMLSLGLQPSRDSYNLLLVAardCG-LGDPQVASELLLKPREEATVLQPPvsrqrprrta 416
Cdd:PLN03218  515 DGC---ARAGqVAKAFGAYGIMRSKNVKPDRVVFNALISA---CGqSGAVDRAFDVLAEMKAETHPIDPD---------- 578
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  417 QAKAGNLMSAMLHVEALERQlfLEPSQALgppepPEARVpgKAQPEVdtkaepsHTAALTAVALKPppvELEVNL----- 491
Cdd:PLN03218  579 HITVGALMKACANAGQVDRA--KEVYQMI-----HEYNI--KGTPEV-------YTIAVNSCSQKG---DWDFALsiydd 639
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  492 LTPGAVPPTVVSFGtvttpadrlALI------GGLEGFLSKMAEHRQQ-----------------------------PDI 536
Cdd:PLN03218  640 MKKKGVKPDEVFFS---------ALVdvaghaGDLDKAFEILQDARKQgiklgtvsysslmgacsnaknwkkalelyEDI 710
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  537 RTLTLLAEVvesgSPAESLLLALLDEHQVEadltffntlvRKKSKLGDLEGAkallpvlakrGLVPNLQTFCNLAIGCHR 616
Cdd:PLN03218  711 KSIKLRPTV----STMNALITALCEGNQLP----------KALEVLSEMKRL----------GLCPNTITYSILLVASER 766
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 311893396  617 PKD---GLQLLTDMKKSQVTPNTHIYSALINAAIRK 649
Cdd:PLN03218  767 KDDadvGLDLLSQAKEDGIKPNLVMCRCITGLCLRR 802
WRW pfam10206
Mitochondrial F1F0-ATP synthase, subunit f; This is a family of small proteins of ...
8-41 1.93e-08

Mitochondrial F1F0-ATP synthase, subunit f; This is a family of small proteins of approximately 110 amino acids, which are highly conserved from nematodes to humans. Some members of the family have been annotated in Swiss-Prot as being the f subunit of mitochondrial F1F0-ATP synthase but this could not be confirmed. The sequence has a well-conserved WRW motif. The exact function of the protein is not known.


Pssm-ID: 431134  Cd Length: 102  Bit Score: 52.68  E-value: 1.93e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 311893396    8 KDKKLLEVKLGELPSWILMRDFSPSGIFGAFQRG 41
Cdd:pfam10206  26 PDTPFGDVKLGELPSWLGRRNKTPSAFAGAFSRA 59
PPR TIGR00756
pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ...
225-257 1.51e-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: 42.44  E-value: 1.51e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 311893396  225 YTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSD 257
Cdd:TIGR00756   3 YNTLIDGLCKAGRVEEALELFKEMKERGIEPDV 35
PLN03077 PLN03077
Protein ECB2; Provisional
195-319 5.65e-05

Protein ECB2; Provisional


Pssm-ID: 215561 [Multi-domain]  Cd Length: 857  Bit Score: 46.77  E-value: 5.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396 195 LIKEGKLVEALDLFERqmLKEERLqpmeSNYTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSDATYTALFNVCAESP-WK 273
Cdd:PLN03077 131 FVRFGELVHAWYVFGK--MPERDL----FSWNVLVGGYAKAGYFDEALCLYHRMLWAGVRPDVYTFPCVLRTCGGIPdLA 204
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 311893396 274 DSALQSALKLRQqlqakNFELNLKTYHALLKMAAKCADLRMCLDVF 319
Cdd:PLN03077 205 RGREVHAHVVRF-----GFELDVDVVNALITMYVKCGDVVSARLVF 245
PPR_2 pfam13041
PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ...
616-645 6.99e-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: 35.03  E-value: 6.99e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 311893396  616 RPKDGLQLLTDMKKSQVTPNTHIYSALINA 645
Cdd:pfam13041  18 KVEEAFKLFNEMKKRGVKPNVYTYTILING 47
 
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 ...
225-268 2.00e-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: 62.00  E-value: 2.00e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 311893396  225 YTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSDATYTALFNVCA 268
Cdd:pfam13041   6 YNTLINGYCKKGKVEEAFKLFNEMKKRGVKPNVYTYTILINGLC 49
PPR_long pfam17177
Pentacotripeptide-repeat region of PRORP; Pentatricopeptide repeat (PPR) proteins are a large ...
214-405 2.46e-10

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: 60.87  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  214 KEERLQPMESNYTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSDATYTALFNVC-----AESPWKDSALQSALKLRQQLQ 288
Cdd:pfam17177   3 KKKGKQTPESELRFQLDKCSKHADATGALALYDAAKAEGVRLAQYHYNVLLYLCskaadATDLKPQLAADRGFEVFEAMK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  289 AKNFELNLKTYHALLKMAAKCADLRMCLDVFKEIIHKGHVVTEETFSFLLMgCIQDKKTGFRyALQVWRLMLSLGLQPSR 368
Cdd:pfam17177  83 AQGVSPNEATYTAVARLAAAKGDGDLAFDLVKEMEAAGVSPRLRSYSPALH-AYCEAGDADK-AYEVEEHMLAHGVELEE 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 311893396  369 DSYNLLLVAARDCGLGDpQVaSELLLKPREeaTVLQP 405
Cdd:pfam17177 161 PELAALLKVSAKAGRAD-KV-YAYLHRLRD--AVRQV 193
PLN03218 PLN03218
maturation of RBCL 1; Provisional
179-649 2.72e-10

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 64.13  E-value: 2.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  179 RGRRNTPYwYFLQCKHLIKEGKLVEALDLFErQMLKEERLQPMESNYTVLIGGCGRVGYLKKAFNLYNQMkkrdLEPSDA 258
Cdd:PLN03218  365 SGKRKSPE-YIDAYNRLLRDGRIKDCIDLLE-DMEKRGLLDMDKIYHAKFFKACKKQRAVKEAFRFAKLI----RNPTLS 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  259 TYTALFNVCAESpwKDSAlqSALKLRQQLQAKNFELNLKTYHALLKMAAKCADLRMCLDVFKEIIHKGHVVTEETFSFLL 338
Cdd:PLN03218  439 TFNMLMSVCASS--QDID--GALRVLRLVQEAGLKADCKLYTTLISTCAKSGKVDAMFEVFHEMVNAGVEANVHTFGALI 514
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  339 MGCiqdKKTG-FRYALQVWRLMLSLGLQPSRDSYNLLLVAardCG-LGDPQVASELLLKPREEATVLQPPvsrqrprrta 416
Cdd:PLN03218  515 DGC---ARAGqVAKAFGAYGIMRSKNVKPDRVVFNALISA---CGqSGAVDRAFDVLAEMKAETHPIDPD---------- 578
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  417 QAKAGNLMSAMLHVEALERQlfLEPSQALgppepPEARVpgKAQPEVdtkaepsHTAALTAVALKPppvELEVNL----- 491
Cdd:PLN03218  579 HITVGALMKACANAGQVDRA--KEVYQMI-----HEYNI--KGTPEV-------YTIAVNSCSQKG---DWDFALsiydd 639
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  492 LTPGAVPPTVVSFGtvttpadrlALI------GGLEGFLSKMAEHRQQ-----------------------------PDI 536
Cdd:PLN03218  640 MKKKGVKPDEVFFS---------ALVdvaghaGDLDKAFEILQDARKQgiklgtvsysslmgacsnaknwkkalelyEDI 710
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  537 RTLTLLAEVvesgSPAESLLLALLDEHQVEadltffntlvRKKSKLGDLEGAkallpvlakrGLVPNLQTFCNLAIGCHR 616
Cdd:PLN03218  711 KSIKLRPTV----STMNALITALCEGNQLP----------KALEVLSEMKRL----------GLCPNTITYSILLVASER 766
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 311893396  617 PKD---GLQLLTDMKKSQVTPNTHIYSALINAAIRK 649
Cdd:PLN03218  767 KDDadvGLDLLSQAKEDGIKPNLVMCRCITGLCLRR 802
WRW pfam10206
Mitochondrial F1F0-ATP synthase, subunit f; This is a family of small proteins of ...
8-41 1.93e-08

Mitochondrial F1F0-ATP synthase, subunit f; This is a family of small proteins of approximately 110 amino acids, which are highly conserved from nematodes to humans. Some members of the family have been annotated in Swiss-Prot as being the f subunit of mitochondrial F1F0-ATP synthase but this could not be confirmed. The sequence has a well-conserved WRW motif. The exact function of the protein is not known.


Pssm-ID: 431134  Cd Length: 102  Bit Score: 52.68  E-value: 1.93e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 311893396    8 KDKKLLEVKLGELPSWILMRDFSPSGIFGAFQRG 41
Cdd:pfam10206  26 PDTPFGDVKLGELPSWLGRRNKTPSAFAGAFSRA 59
PPR TIGR00756
pentatricopeptide repeat domain (PPR motif); This model describes a domain called the PPR ...
225-257 1.51e-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: 42.44  E-value: 1.51e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 311893396  225 YTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSD 257
Cdd:TIGR00756   3 YNTLIDGLCKAGRVEEALELFKEMKERGIEPDV 35
PLN03077 PLN03077
Protein ECB2; Provisional
195-319 5.65e-05

Protein ECB2; Provisional


Pssm-ID: 215561 [Multi-domain]  Cd Length: 857  Bit Score: 46.77  E-value: 5.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396 195 LIKEGKLVEALDLFERqmLKEERLqpmeSNYTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSDATYTALFNVCAESP-WK 273
Cdd:PLN03077 131 FVRFGELVHAWYVFGK--MPERDL----FSWNVLVGGYAKAGYFDEALCLYHRMLWAGVRPDVYTFPCVLRTCGGIPdLA 204
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 311893396 274 DSALQSALKLRQqlqakNFELNLKTYHALLKMAAKCADLRMCLDVF 319
Cdd:PLN03077 205 RGREVHAHVVRF-----GFELDVDVVNALITMYVKCGDVVSARLVF 245
PLN03077 PLN03077
Protein ECB2; Provisional
199-325 1.38e-04

Protein ECB2; Provisional


Pssm-ID: 215561 [Multi-domain]  Cd Length: 857  Bit Score: 45.23  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396 199 GKLVEALDLFERQMLKEErlqpmeSNYTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSDATYTALFNVCAESpwkdSALQ 278
Cdd:PLN03077 337 GSWGEAEKVFSRMETKDA------VSWTAMISGYEKNGLPDKALETYALMEQDNVSPDEITIASVLSACACL----GDLD 406
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 311893396 279 SALKLRQQLQAKNFELNLKTYHALLKMAAKCADLRMCLDVFKEIIHK 325
Cdd:PLN03077 407 VGVKLHELAERKGLISYVVVANALIEMYSKCKCIDKALEVFHNIPEK 453
PPR pfam01535
PPR repeat; This repeat has no known function. It is about 35 amino acids long and found in up ...
225-253 1.48e-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: 39.37  E-value: 1.48e-04
                          10        20
                  ....*....|....*....|....*....
gi 311893396  225 YTVLIGGCGRVGYLKKAFNLYNQMKKRDL 253
Cdd:pfam01535   3 YNSLISGYCKNGKLEEALELFKEMKEKGI 31
PLN03218 PLN03218
maturation of RBCL 1; Provisional
534-669 7.80e-04

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 42.94  E-value: 7.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  534 PDIRTLTLLAEVVESGSPAESLL--LALLDEHQVEADLTFFNTLVRKKSKLGDLEGAKALLPVLAKRGLVPNLQTFCNLA 611
Cdd:PLN03218  435 PTLSTFNMLMSVCASSQDIDGALrvLRLVQEAGLKADCKLYTTLISTCAKSGKVDAMFEVFHEMVNAGVEANVHTFGALI 514
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311893396  612 IGCHR----PKD----GLqlltdMKKSQVTPNTHIYSALINAAIRKLNYTYLISILKDMKQNRVPV 669
Cdd:PLN03218  515 DGCARagqvAKAfgayGI-----MRSKNVKPDRVVFNALISACGQSGAVDRAFDVLAEMKAETHPI 575
PLN03218 PLN03218
maturation of RBCL 1; Provisional
569-670 8.71e-04

maturation of RBCL 1; Provisional


Pssm-ID: 215636 [Multi-domain]  Cd Length: 1060  Bit Score: 42.94  E-value: 8.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  569 LTFFNTLVRKKSKLGDLEGAKALLPVLAKRGLVPNLQTFCNLAIGChrPKDG-----LQLLTDMKKSQVTPNTHIYSALI 643
Cdd:PLN03218  437 LSTFNMLMSVCASSQDIDGALRVLRLVQEAGLKADCKLYTTLISTC--AKSGkvdamFEVFHEMVNAGVEANVHTFGALI 514
                          90       100       110
                  ....*....|....*....|....*....|..
gi 311893396  644 NAAIR-----KLNYTYLISILKDMKQNRVPVN 670
Cdd:PLN03218  515 DGCARagqvaKAFGAYGIMRSKNVKPDRVVFN 546
PPR_3 pfam13812
Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ...
218-267 1.37e-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: 37.72  E-value: 1.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 311893396  218 LQPMESNYTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSDATYTALFNVC 267
Cdd:pfam13812  11 IQLNVNTYTHLLHAYANVGNLKLALEIFERMKKKGIKPTLDTYNAILGVI 60
PPR_3 pfam13812
Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ...
282-341 1.70e-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: 1.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396  282 KLRQQLQAKNFELNLKTYHALLKMAAKCADLRMCLDVFKEIIHKGHVVTEETFSFLLMGC 341
Cdd:pfam13812   1 SILREMVRDGIQLNVNTYTHLLHAYANVGNLKLALEIFERMKKKGIKPTLDTYNAILGVI 60
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
362-512 1.73e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.62  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893396 362 LGLQPsrDSYN------LLLVAARdcglgdPQVASELLlKPREEATVLQPPVSRQRPRRTAQAKAGNLMSAMlhvealer 435
Cdd:PRK14951 344 LGLAP--DEYAaltmvlLRLLAFK------PAAAAEAA-APAEKKTPARPEAAAPAAAPVAQAAAAPAPAAA-------- 406
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311893396 436 qlflEPSQALGPPEPPEARVPGKAQPEVDTKAEPSHTAALTAVAlkPPPVELEVNLLTPGAVPPTVVSFGTVTTPAD 512
Cdd:PRK14951 407 ----PAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVA--LAPAPPAQAAPETVAIPVRVAPEPAVASAAP 477
PPR_2 pfam13041
PPR repeat family; This repeat has no known function. It is about 35 amino acids long and is ...
616-645 6.99e-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: 35.03  E-value: 6.99e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 311893396  616 RPKDGLQLLTDMKKSQVTPNTHIYSALINA 645
Cdd:pfam13041  18 KVEEAFKLFNEMKKRGVKPNVYTYTILING 47
 
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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