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Conserved domains on  [gi|148695990|gb|EDL27937|]
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mCG6540 [Mus musculus]

Protein Classification

tetratricopeptide repeat protein( domain architecture ID 708416)

tetratricopeptide repeat (TPR) protein may adopt a right-handed helical structure with an amphipathic channel and may function as an interaction scaffold in the formation of multi-protein complexes

CATH:  1.25.40.10
Gene Ontology:  GO:0005515
PubMed:  10517866|30708253
SCOP:  3001345

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Spy super family cl27809
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
243-448 5.58e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG3914:

Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.29  E-value: 5.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695990 243 LLQADELHQGSKQDKREGFQLLLNNKLAYGSRQDFLWRLARAYSDMSDLTEEESGKKSYAL--NGKEEAEAALKKGDESA 320
Cdd:COG3914   17 LLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLaaLLELAALLLQALGRYEE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695990 321 ACHLW---------YAVLCGQLAEHEGISKRIQSGFsfkEHVDKAIELQPEDPRGHFLLGRwCYQVSHLnwlekktatal 391
Cdd:COG3914   97 ALALYrralalnpdNAEALFNLGNLLLALGRLEEAL---AALRRALALNPDFAEAYLNLGE-ALRRLGR----------- 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148695990 392 fesplsatVQDALQSFLKAEELQPGFSKAgRVYISKCYRELGKNSEARKWMKLAQEL 448
Cdd:COG3914  162 --------LEEAIAALRRALELDPDNAEA-LNNLGNALQDLGRLEEAIAAYRRALEL 209
 
Name Accession Description Interval E-value
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
243-448 5.58e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.29  E-value: 5.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695990 243 LLQADELHQGSKQDKREGFQLLLNNKLAYGSRQDFLWRLARAYSDMSDLTEEESGKKSYAL--NGKEEAEAALKKGDESA 320
Cdd:COG3914   17 LLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLaaLLELAALLLQALGRYEE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695990 321 ACHLW---------YAVLCGQLAEHEGISKRIQSGFsfkEHVDKAIELQPEDPRGHFLLGRwCYQVSHLnwlekktatal 391
Cdd:COG3914   97 ALALYrralalnpdNAEALFNLGNLLLALGRLEEAL---AALRRALALNPDFAEAYLNLGE-ALRRLGR----------- 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148695990 392 fesplsatVQDALQSFLKAEELQPGFSKAgRVYISKCYRELGKNSEARKWMKLAQEL 448
Cdd:COG3914  162 --------LEEAIAALRRALELDPDNAEA-LNNLGNALQDLGRLEEAIAAYRRALEL 209
 
Name Accession Description Interval E-value
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
243-448 5.58e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.29  E-value: 5.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695990 243 LLQADELHQGSKQDKREGFQLLLNNKLAYGSRQDFLWRLARAYSDMSDLTEEESGKKSYAL--NGKEEAEAALKKGDESA 320
Cdd:COG3914   17 LLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLaaLLELAALLLQALGRYEE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695990 321 ACHLW---------YAVLCGQLAEHEGISKRIQSGFsfkEHVDKAIELQPEDPRGHFLLGRwCYQVSHLnwlekktatal 391
Cdd:COG3914   97 ALALYrralalnpdNAEALFNLGNLLLALGRLEEAL---AALRRALALNPDFAEAYLNLGE-ALRRLGR----------- 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148695990 392 fesplsatVQDALQSFLKAEELQPGFSKAgRVYISKCYRELGKNSEARKWMKLAQEL 448
Cdd:COG3914  162 --------LEEAIAALRRALELDPDNAEA-LNNLGNALQDLGRLEEAIAAYRRALEL 209
 
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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