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Conserved domains on  [gi|2462619694|ref|XP_054216579|]
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regulator of microtubule dynamics protein 1 isoform X25 [Homo sapiens]

Protein Classification

tetratricopeptide repeat protein( domain architecture ID 11469162)

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
ACL4-like super family cl23710
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 159-221 8.10e-04

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


The actual alignment was detected with superfamily member cd24142:

Pssm-ID: 474029 [Multi-domain]  Cd Length: 306  Bit Score: 40.30  E-value: 8.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619694 159 EALEYAKRALEKNESSFASHKWYAICLSDVGDYEgikakiaNAYiikEHFEKAIELNPKDATS 221
Cdd:cd24142    18 LALKFLQRALELEPNNVEALELLGEILLELGDVE-------EAR---EVLLRAIELDPDGGYE 70
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 94-226 9.72e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 38.63  E-value: 9.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619694  94 TAKVEEILEQADYLYESGETEKLYQLLTQY--KESEDAELLWRLARASRDVAQLSrtseeekkllvyEALEYAKRALEKN 171
Cdd:COG4783     1 AACAEALYALAQALLLAGDYDEAEALLEKAleLDPDNPEAFALLGEILLQLGDLD------------EAIVLLHEALELD 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462619694 172 ESSFASHKWYAICLSDVGDYEgiKAkianayiiKEHFEKAIELNPKDATSIHLMG 226
Cdd:COG4783    69 PDEPEARLNLGLALLKAGDYD--EA--------LALLEKALKLDPEHPEAYLRLA 113
 
Name Accession Description Interval E-value
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 159-221 8.10e-04

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 40.30  E-value: 8.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619694 159 EALEYAKRALEKNESSFASHKWYAICLSDVGDYEgikakiaNAYiikEHFEKAIELNPKDATS 221
Cdd:cd24142    18 LALKFLQRALELEPNNVEALELLGEILLELGDVE-------EAR---EVLLRAIELDPDGGYE 70
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 94-226 9.72e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 38.63  E-value: 9.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619694  94 TAKVEEILEQADYLYESGETEKLYQLLTQY--KESEDAELLWRLARASRDVAQLSrtseeekkllvyEALEYAKRALEKN 171
Cdd:COG4783     1 AACAEALYALAQALLLAGDYDEAEALLEKAleLDPDNPEAFALLGEILLQLGDLD------------EAIVLLHEALELD 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462619694 172 ESSFASHKWYAICLSDVGDYEgiKAkianayiiKEHFEKAIELNPKDATSIHLMG 226
Cdd:COG4783    69 PDEPEARLNLGLALLKAGDYD--EA--------LALLEKALKLDPEHPEAYLRLA 113
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
159-227 1.65e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.22  E-value: 1.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619694 159 EALEYAKRALEKNESSFASHKWYAICLSDVGDYEgiKAkianayiiKEHFEKAIELNPKDATSIHLMGI 227
Cdd:COG0457    26 EAIEDYEKALELDPDDAEALYNLGLAYLRLGRYE--EA--------LADYEQALELDPDDAEALNNLGL 84
 
Name Accession Description Interval E-value
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 159-221 8.10e-04

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 40.30  E-value: 8.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619694 159 EALEYAKRALEKNESSFASHKWYAICLSDVGDYEgikakiaNAYiikEHFEKAIELNPKDATS 221
Cdd:cd24142    18 LALKFLQRALELEPNNVEALELLGEILLELGDVE-------EAR---EVLLRAIELDPDGGYE 70
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 94-226 9.72e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 38.63  E-value: 9.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619694  94 TAKVEEILEQADYLYESGETEKLYQLLTQY--KESEDAELLWRLARASRDVAQLSrtseeekkllvyEALEYAKRALEKN 171
Cdd:COG4783     1 AACAEALYALAQALLLAGDYDEAEALLEKAleLDPDNPEAFALLGEILLQLGDLD------------EAIVLLHEALELD 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462619694 172 ESSFASHKWYAICLSDVGDYEgiKAkianayiiKEHFEKAIELNPKDATSIHLMG 226
Cdd:COG4783    69 PDEPEARLNLGLALLKAGDYD--EA--------LALLEKALKLDPEHPEAYLRLA 113
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
159-227 1.65e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.22  E-value: 1.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619694 159 EALEYAKRALEKNESSFASHKWYAICLSDVGDYEgiKAkianayiiKEHFEKAIELNPKDATSIHLMGI 227
Cdd:COG0457    26 EAIEDYEKALELDPDDAEALYNLGLAYLRLGRYE--EA--------LADYEQALELDPDDAEALNNLGL 84
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 111-225 1.74e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.59  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619694 111 GETEKLYQLLTQYKeSEDAELLWRLARASRDVAQLSrtseeekkllvyEALEYAKRALEKNESSFASHKWYAICLSDVGD 190
Cdd:COG3914   129 EEALAALRRALALN-PDFAEAYLNLGEALRRLGRLE------------EAIAALRRALELDPDNAEALNNLGNALQDLGR 195

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462619694 191 Y-EGIkakianayiikEHFEKAIELNPKDATSIHLM 225
Cdd:COG3914   196 LeEAI-----------AAYRRALELDPDNADAHSNL 220
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 69-226 3.62e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 38.82  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619694  69 LLLSALSYLGFETYQVISQAAVVHATAKVEEILEQADYLYESGETEKLYQLLTQYKESEDAELLWRLARASRDVAQLSRT 148
Cdd:COG3914     6 LLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAA 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619694 149 SEEEKKLLVYEALEYAKRALEKNESSFASHKWYAICLSDVGDYEgiKAkianayiiKEHFEKAIELNPKDATSIHLMG 226
Cdd:COG3914    86 LLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLE--EA--------LAALRRALALNPDFAEAYLNLG 153
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
159-226 3.85e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 35.92  E-value: 3.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619694 159 EALEYAKRALEKNESSFASHKWYAICLSDVGDYEgiKAkianayiikEHFEKAIELNPKDATSIHLMG 226
Cdd:COG3063    10 EAEEYYEKALELDPDNADALNNLGLLLLEQGRYD--EA---------IALEKALKLDPNNAEALLNLA 66
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
159-227 5.53e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 37.68  E-value: 5.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619694 159 EALEYAKRALEKNESSFASHKWYAICLSDVGDYEgiKAkianayiiKEHFEKAIELNPKDATSIHLMGI 227
Cdd:COG0457    94 EALEDYDKALELDPDDAEALYNLGLALLELGRYD--EA--------IEAYERALELDPDDADALYNLGI 152
 
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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