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Conserved domains on  [gi|116875831|ref|NP_057117|]
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regulator of microtubule dynamics protein 1 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TPR super family cl33886
Tetratricopeptide (TPR) repeat [General function prediction only];
145-286 1.58e-05

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


The actual alignment was detected with superfamily member COG0457:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.38  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875831 145 EALEYAKRALEKNESSFASHKWYAICLSDVGDYEgiKAkianayiiKEHFEKAIELNPKDATSIHLMGIWCYTFAEmpwy 224
Cdd:COG0457   26 EAIEDYEKALELDPDDAEALYNLGLAYLRLGRYE--EA--------LADYEQALELDPDDAEALNNLGLALQALGR---- 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116875831 225 qrriakmlfatppsstYEKALGYFHRAEQVDPNfYSKNLLLLGKTYLKLHNKKLAAFWLMKA 286
Cdd:COG0457   92 ----------------YEEALEDYDKALELDPD-DAEALYNLGLALLELGRYDEAIEAYERA 136
 
Name Accession Description Interval E-value
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
145-286 1.58e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.38  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875831 145 EALEYAKRALEKNESSFASHKWYAICLSDVGDYEgiKAkianayiiKEHFEKAIELNPKDATSIHLMGIWCYTFAEmpwy 224
Cdd:COG0457   26 EAIEDYEKALELDPDDAEALYNLGLAYLRLGRYE--EA--------LADYEQALELDPDDAEALNNLGLALQALGR---- 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116875831 225 qrriakmlfatppsstYEKALGYFHRAEQVDPNfYSKNLLLLGKTYLKLHNKKLAAFWLMKA 286
Cdd:COG0457   92 ----------------YEEALEDYDKALELDPD-DAEALYNLGLALLELGRYDEAIEAYERA 136
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
145-207 1.87e-03

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: 39.53  E-value: 1.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116875831 145 EALEYAKRALEKNESSFASHKWYAICLSDVGDYEgikakiaNAYiikEHFEKAIELNPKDATS 207
Cdd:cd24142   18 LALKFLQRALELEPNNVEALELLGEILLELGDVE-------EAR---EVLLRAIELDPDGGYE 70
 
Name Accession Description Interval E-value
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
145-286 1.58e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.38  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875831 145 EALEYAKRALEKNESSFASHKWYAICLSDVGDYEgiKAkianayiiKEHFEKAIELNPKDATSIHLMGIWCYTFAEmpwy 224
Cdd:COG0457   26 EAIEDYEKALELDPDDAEALYNLGLAYLRLGRYE--EA--------LADYEQALELDPDDAEALNNLGLALQALGR---- 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116875831 225 qrriakmlfatppsstYEKALGYFHRAEQVDPNfYSKNLLLLGKTYLKLHNKKLAAFWLMKA 286
Cdd:COG0457   92 ----------------YEEALEDYDKALELDPD-DAEALYNLGLALLELGRYDEAIEAYERA 136
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
55-275 1.03e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 43.83  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875831  55 LLLSALSYLGFETYQVISQAAVVHATAKVEEILEQADYLYESGETEKLYQLLTQYKESEDAELLWRLARASRDVAQLSRT 134
Cdd:COG3914    6 LLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875831 135 SEEEKKLLVYEALEYAKRALEKNESSFASHKWYAICLSDVGDYEgiKAkianayiiKEHFEKAIELNPKDATSIHLMGiw 214
Cdd:COG3914   86 LLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLE--EA--------LAALRRALALNPDFAEAYLNLG-- 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116875831 215 cytfaempwyqrriaKMLFATppsSTYEKALGYFHRAEQVDPNfYSKNLLLLGKTYLKLHN 275
Cdd:COG3914  154 ---------------EALRRL---GRLEEAIAALRRALELDPD-NAEALNNLGNALQDLGR 195
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
97-292 3.22e-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: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875831  97 GETEKLYQLLTQYKeSEDAELLWRLARASRDVAQLSrtseeekkllvyEALEYAKRALEKNESSFASHKWYAICLSDVGD 176
Cdd:COG3914  129 EEALAALRRALALN-PDFAEAYLNLGEALRRLGRLE------------EAIAALRRALELDPDNAEALNNLGNALQDLGR 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875831 177 Y-EGIkakianayiikEHFEKAIELNPKDATSIHLMGIWCYTFAEMPWYQRRIAKMlfATPPSSTYEKALGYFHRAEQVD 255
Cdd:COG3914  196 LeEAI-----------AAYRRALELDPDNADAHSNLLFALRQACDWEVYDRFEELL--AALARGPSELSPFALLYLPDDD 262
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 116875831 256 PnfysKNLLLLGKTYLKLHNKKLAAFWLMKAKDYPAH 292
Cdd:COG3914  263 P----AELLALARAWAQLVAAAAAPELPPPPNPRDPD 295
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
101-286 7.68e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 40.48  E-value: 7.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875831 101 KLYQLLTQYKESEDAELLWRLARASRD-----VAQLSRTSEEEKKLLvyEALEYAKRALEKNESSFASHKWYAICLSDVG 175
Cdd:COG2956   81 ELAQDYLKAGLLDRAEELLEKLLELDPddaeaLRLLAEIYEQEGDWE--KAIEVLERLLKLGPENAHAYCELAELYLEQG 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875831 176 DYEgiKAKianayiikEHFEKAIELNPKDAtsihlmgiwcytfaempWYQRRIAKMLFATppsSTYEKALGYFHRAEQVD 255
Cdd:COG2956  159 DYD--EAI--------EALEKALKLDPDCA-----------------RALLLLAELYLEQ---GDYEEAIAALERALEQD 208
                        170       180       190
                 ....*....|....*....|....*....|.
gi 116875831 256 PNfYSKNLLLLGKTYLKLHNKKLAAFWLMKA 286
Cdd:COG2956  209 PD-YLPALPRLAELYEKLGDPEEALELLRKA 238
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
80-258 1.39e-03

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: 38.25  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875831  80 TAKVEEILEQADYLYESGETEKLYQLLTQY--KESEDAELLWRLARASRDVAQLSrtseeekkllvyEALEYAKRALEKN 157
Cdd:COG4783    1 AACAEALYALAQALLLAGDYDEAEALLEKAleLDPDNPEAFALLGEILLQLGDLD------------EAIVLLHEALELD 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875831 158 ESSFASHKWYAICLSDVGDYEgiKAkianayiiKEHFEKAIELNPKDatsihlmgiwcytfaemPWYQRRIAKMLFATPp 237
Cdd:COG4783   69 PDEPEARLNLGLALLKAGDYD--EA--------LALLEKALKLDPEH-----------------PEAYLRLARAYRALG- 120
                        170       180
                 ....*....|....*....|.
gi 116875831 238 ssTYEKALGYFHRAEQVDPNF 258
Cdd:COG4783  121 --RPDEAIAALEKALELDPDD 139
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
145-207 1.87e-03

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: 39.53  E-value: 1.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116875831 145 EALEYAKRALEKNESSFASHKWYAICLSDVGDYEgikakiaNAYiikEHFEKAIELNPKDATS 207
Cdd:cd24142   18 LALKFLQRALELEPNNVEALELLGEILLELGDVE-------EAR---EVLLRAIELDPDGGYE 70
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
145-259 8.63e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 35.15  E-value: 8.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875831 145 EALEYAKRALEKNESSFASHKWYAICLSDVGDYEgiKAkianayiikEHFEKAIELNPKDATSIHLMgiwcytfAEMPWY 224
Cdd:COG3063   10 EAEEYYEKALELDPDNADALNNLGLLLLEQGRYD--EA---------IALEKALKLDPNNAEALLNL-------AELLLE 71
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 116875831 225 QRRiakmlfatppsstYEKALGYFHRAEQVDPNFY 259
Cdd:COG3063   72 LGD-------------YDEALAYLERALELDPSAL 93
 
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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