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Conserved domains on  [gi|2462619690|ref|XP_054216577|]
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regulator of microtubule dynamics protein 1 isoform X23 [Homo sapiens]

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 ...
87-264 8.34e-03

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: 37.67  E-value: 8.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619690  87 QAAVVHATAKVEEILEQADYLYESGEteklyqLLTQYKESEDAELLWRLARASRDVAQLSRTSEEEKKLLVYEALEYakR 166
Cdd:COG3914    18 LAAAAAAELALAAELEAAALAAALGL------ALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLL--Q 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619690 167 ALEKNESSFASHKKAIELNPKDATSIHLMGIWCYtfaempwYQRRiakmlfatppsstYEKALGYFHRAEQVDPNFYSkN 246
Cdd:COG3914    90 ALGRYEEALALYRRALALNPDNAEALFNLGNLLL-------ALGR-------------LEEALAALRRALALNPDFAE-A 148
                         170
                  ....*....|....*...
gi 2462619690 247 LLLLGKTYLKLHNKKLAA 264
Cdd:COG3914   149 YLNLGEALRRLGRLEEAI 166
 
Name Accession Description Interval E-value
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
87-264 8.34e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 37.67  E-value: 8.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619690  87 QAAVVHATAKVEEILEQADYLYESGEteklyqLLTQYKESEDAELLWRLARASRDVAQLSRTSEEEKKLLVYEALEYakR 166
Cdd:COG3914    18 LAAAAAAELALAAELEAAALAAALGL------ALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLL--Q 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619690 167 ALEKNESSFASHKKAIELNPKDATSIHLMGIWCYtfaempwYQRRiakmlfatppsstYEKALGYFHRAEQVDPNFYSkN 246
Cdd:COG3914    90 ALGRYEEALALYRRALALNPDNAEALFNLGNLLL-------ALGR-------------LEEALAALRRALALNPDFAE-A 148
                         170
                  ....*....|....*...
gi 2462619690 247 LLLLGKTYLKLHNKKLAA 264
Cdd:COG3914   149 YLNLGEALRRLGRLEEAI 166
 
Name Accession Description Interval E-value
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
87-264 8.34e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 37.67  E-value: 8.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619690  87 QAAVVHATAKVEEILEQADYLYESGEteklyqLLTQYKESEDAELLWRLARASRDVAQLSRTSEEEKKLLVYEALEYakR 166
Cdd:COG3914    18 LAAAAAAELALAAELEAAALAAALGL------ALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLL--Q 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619690 167 ALEKNESSFASHKKAIELNPKDATSIHLMGIWCYtfaempwYQRRiakmlfatppsstYEKALGYFHRAEQVDPNFYSkN 246
Cdd:COG3914    90 ALGRYEEALALYRRALALNPDNAEALFNLGNLLL-------ALGR-------------LEEALAALRRALALNPDFAE-A 148
                         170
                  ....*....|....*...
gi 2462619690 247 LLLLGKTYLKLHNKKLAA 264
Cdd:COG3914   149 YLNLGEALRRLGRLEEAI 166
 
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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