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Conserved domains on  [gi|124486791|ref|NP_001074812|]
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guanine nucleotide exchange factor C9orf72 homolog isoform 1 [Mus musculus]

Protein Classification

C9orf72-like domain-containing protein( domain architecture ID 10633239)

C9orf72-like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
C9orf72-like pfam15019
C9orf72-like protein family; The precise function of this family is unknown but members have ...
61-324 1.88e-82

C9orf72-like protein family; The precise function of this family is unknown but members have been found to be localized in the cytoplasm of brain tissue. Defects in the gene, C9orf72, are the cause of frontotemporal dementia and/or amyotrophic lateral sclerosis (FTDALS) which is an autosomal dominant neurodegenerative disorder. The disorder is caused by a large expansion of a GGGGCC hexa-nucleotide within the first C9orf72 intron located between the first and the second non-coding exons. The expansion leads to the loss of transcription of one of the two transcripts encoding isoform 1 and to the formation of nuclear RNA foci. This domain family is found in eukaryotes, and is typically between 230 and 250 amino acids in length. There is a single completely conserved residue F that may be functionally important.


:

Pssm-ID: 464450  Cd Length: 230  Bit Score: 254.51  E-value: 1.88e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486791   61 FLANHTLNGEIL-RNAESGAIDVKFFVLSEKGVIIVSLIFDGNWNGDRSTYGLSIILPQTELSFYLPLHRVCVDRLTHII 139
Cdd:pfam15019   1 SLAKLTLSNEIRqRDEAFNKIPTKFFVLPSKNLIVVAFIFSIPTNGGKTYYALSLILPHTEISNYLPLHSVLEDRLKIIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486791  140 RKGRIWMHKERQENVqkivlegtermedqgqsiipmLTGEVIPVMELLASMKSHSVPEDIDIADTVlnDDDIgdscheGF 219
Cdd:pfam15019  81 AKAKISLKKNKPLEK---------------------LTPEIQRFLELISALLSSGIPLPPDFPIDP--ADDI------PF 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486791  220 LLNAISSHLQTCGCSVVVGSSAEKVNKIVRTLCLFLTPAERKCSRLCEAEssfKYESGLFVQGLLKDATGSFVLpfrQVM 299
Cdd:pfam15019 132 LAKAITSHLQTQMTTIIEGSDFEEANKLFNFLALFLLPYQLSLSSLEYRD---RYIPGLFLQGVSKQATGSPED---ILL 205
                         250       260
                  ....*....|....*....|....*
gi 124486791  300 YAPYPTTHIDVDVNTVKQMPPCHEH 324
Cdd:pfam15019 206 TSKRPTTWIDLDEKIVKQTPPIDEQ 230
 
Name Accession Description Interval E-value
C9orf72-like pfam15019
C9orf72-like protein family; The precise function of this family is unknown but members have ...
61-324 1.88e-82

C9orf72-like protein family; The precise function of this family is unknown but members have been found to be localized in the cytoplasm of brain tissue. Defects in the gene, C9orf72, are the cause of frontotemporal dementia and/or amyotrophic lateral sclerosis (FTDALS) which is an autosomal dominant neurodegenerative disorder. The disorder is caused by a large expansion of a GGGGCC hexa-nucleotide within the first C9orf72 intron located between the first and the second non-coding exons. The expansion leads to the loss of transcription of one of the two transcripts encoding isoform 1 and to the formation of nuclear RNA foci. This domain family is found in eukaryotes, and is typically between 230 and 250 amino acids in length. There is a single completely conserved residue F that may be functionally important.


Pssm-ID: 464450  Cd Length: 230  Bit Score: 254.51  E-value: 1.88e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486791   61 FLANHTLNGEIL-RNAESGAIDVKFFVLSEKGVIIVSLIFDGNWNGDRSTYGLSIILPQTELSFYLPLHRVCVDRLTHII 139
Cdd:pfam15019   1 SLAKLTLSNEIRqRDEAFNKIPTKFFVLPSKNLIVVAFIFSIPTNGGKTYYALSLILPHTEISNYLPLHSVLEDRLKIIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486791  140 RKGRIWMHKERQENVqkivlegtermedqgqsiipmLTGEVIPVMELLASMKSHSVPEDIDIADTVlnDDDIgdscheGF 219
Cdd:pfam15019  81 AKAKISLKKNKPLEK---------------------LTPEIQRFLELISALLSSGIPLPPDFPIDP--ADDI------PF 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486791  220 LLNAISSHLQTCGCSVVVGSSAEKVNKIVRTLCLFLTPAERKCSRLCEAEssfKYESGLFVQGLLKDATGSFVLpfrQVM 299
Cdd:pfam15019 132 LAKAITSHLQTQMTTIIEGSDFEEANKLFNFLALFLLPYQLSLSSLEYRD---RYIPGLFLQGVSKQATGSPED---ILL 205
                         250       260
                  ....*....|....*....|....*
gi 124486791  300 YAPYPTTHIDVDVNTVKQMPPCHEH 324
Cdd:pfam15019 206 TSKRPTTWIDLDEKIVKQTPPIDEQ 230
 
Name Accession Description Interval E-value
C9orf72-like pfam15019
C9orf72-like protein family; The precise function of this family is unknown but members have ...
61-324 1.88e-82

C9orf72-like protein family; The precise function of this family is unknown but members have been found to be localized in the cytoplasm of brain tissue. Defects in the gene, C9orf72, are the cause of frontotemporal dementia and/or amyotrophic lateral sclerosis (FTDALS) which is an autosomal dominant neurodegenerative disorder. The disorder is caused by a large expansion of a GGGGCC hexa-nucleotide within the first C9orf72 intron located between the first and the second non-coding exons. The expansion leads to the loss of transcription of one of the two transcripts encoding isoform 1 and to the formation of nuclear RNA foci. This domain family is found in eukaryotes, and is typically between 230 and 250 amino acids in length. There is a single completely conserved residue F that may be functionally important.


Pssm-ID: 464450  Cd Length: 230  Bit Score: 254.51  E-value: 1.88e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486791   61 FLANHTLNGEIL-RNAESGAIDVKFFVLSEKGVIIVSLIFDGNWNGDRSTYGLSIILPQTELSFYLPLHRVCVDRLTHII 139
Cdd:pfam15019   1 SLAKLTLSNEIRqRDEAFNKIPTKFFVLPSKNLIVVAFIFSIPTNGGKTYYALSLILPHTEISNYLPLHSVLEDRLKIIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486791  140 RKGRIWMHKERQENVqkivlegtermedqgqsiipmLTGEVIPVMELLASMKSHSVPEDIDIADTVlnDDDIgdscheGF 219
Cdd:pfam15019  81 AKAKISLKKNKPLEK---------------------LTPEIQRFLELISALLSSGIPLPPDFPIDP--ADDI------PF 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486791  220 LLNAISSHLQTCGCSVVVGSSAEKVNKIVRTLCLFLTPAERKCSRLCEAEssfKYESGLFVQGLLKDATGSFVLpfrQVM 299
Cdd:pfam15019 132 LAKAITSHLQTQMTTIIEGSDFEEANKLFNFLALFLLPYQLSLSSLEYRD---RYIPGLFLQGVSKQATGSPED---ILL 205
                         250       260
                  ....*....|....*....|....*
gi 124486791  300 YAPYPTTHIDVDVNTVKQMPPCHEH 324
Cdd:pfam15019 206 TSKRPTTWIDLDEKIVKQTPPIDEQ 230
 
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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