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Conserved domains on  [gi|530389084|ref|XP_005251004|]
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regulator of microtubule dynamics protein 1 isoform X8 [Homo sapiens]

Protein Classification

tetratricopeptide repeat protein( domain architecture ID 1001445)

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
SCOP:  3001345

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LapB super family cl34526
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
87-256 2.14e-03

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


The actual alignment was detected with superfamily member COG2956:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 39.33  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389084  87 LEQADYLYESG---ETEKLYQLLTQyKESEDAELLWRLAR---ASRDVAQLSRTSEEEKKLLVYEA---LEYAKRALEKN 157
Cdd:COG2956   80 LELAQDYLKAGlldRAEELLEKLLE-LDPDDAEALRLLAEiyeQEGDWEKAIEVLERLLKLGPENAhayCELAELYLEQG 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389084 158 --ESSFASHKKAIELNPKDAtsihlmgiwcytfaempWYQRRIAKMLFATppsSTYEKALGYFHRAEQVDPNfYSKNLLL 235
Cdd:COG2956  159 dyDEAIEALEKALKLDPDCA-----------------RALLLLAELYLEQ---GDYEEAIAALERALEQDPD-YLPALPR 217
                        170       180
                 ....*....|....*....|.
gi 530389084 236 LGKTYLKLHNKKLAAFWLMKA 256
Cdd:COG2956  218 LAELYEKLGDPEEALELLRKA 238
 
Name Accession Description Interval E-value
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
87-256 2.14e-03

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: 39.33  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389084  87 LEQADYLYESG---ETEKLYQLLTQyKESEDAELLWRLAR---ASRDVAQLSRTSEEEKKLLVYEA---LEYAKRALEKN 157
Cdd:COG2956   80 LELAQDYLKAGlldRAEELLEKLLE-LDPDDAEALRLLAEiyeQEGDWEKAIEVLERLLKLGPENAhayCELAELYLEQG 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389084 158 --ESSFASHKKAIELNPKDAtsihlmgiwcytfaempWYQRRIAKMLFATppsSTYEKALGYFHRAEQVDPNfYSKNLLL 235
Cdd:COG2956  159 dyDEAIEALEKALKLDPDCA-----------------RALLLLAELYLEQ---GDYEEAIAALERALEQDPD-YLPALPR 217
                        170       180
                 ....*....|....*....|.
gi 530389084 236 LGKTYLKLHNKKLAAFWLMKA 256
Cdd:COG2956  218 LAELYEKLGDPEEALELLRKA 238
 
Name Accession Description Interval E-value
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
87-256 2.14e-03

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: 39.33  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389084  87 LEQADYLYESG---ETEKLYQLLTQyKESEDAELLWRLAR---ASRDVAQLSRTSEEEKKLLVYEA---LEYAKRALEKN 157
Cdd:COG2956   80 LELAQDYLKAGlldRAEELLEKLLE-LDPDDAEALRLLAEiyeQEGDWEKAIEVLERLLKLGPENAhayCELAELYLEQG 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389084 158 --ESSFASHKKAIELNPKDAtsihlmgiwcytfaempWYQRRIAKMLFATppsSTYEKALGYFHRAEQVDPNfYSKNLLL 235
Cdd:COG2956  159 dyDEAIEALEKALKLDPDCA-----------------RALLLLAELYLEQ---GDYEEAIAALERALEQDPD-YLPALPR 217
                        170       180
                 ....*....|....*....|.
gi 530389084 236 LGKTYLKLHNKKLAAFWLMKA 256
Cdd:COG2956  218 LAELYEKLGDPEEALELLRKA 238
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
88-256 2.91e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 38.02  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389084  88 EQADYLYESGETEKLYQLLTQYKESEDAELLWRLARASRDVAQLSRTSEEEKKLLVYEALEYAKRALEKNESSFASHKKA 167
Cdd:COG5010    1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389084 168 IELNPKDATSIHLMGiWCYTFAEMpwyqrriakmlfatppsstYEKALGYFHRAEQVDPNfYSKNLLLLGKTYLKLHNKK 247
Cdd:COG5010   81 LQLDPNNPELYYNLA-LLYSRSGD-------------------KDEAKEYYEKALALSPD-NPNAYSNLAALLLSLGQDD 139

                 ....*....
gi 530389084 248 LAAFWLMKA 256
Cdd:COG5010  140 EAKAALQRA 148
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
143-259 4.94e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 38.06  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389084 143 VYEALEYAKRALEKNESSFASHKKAIELNPKDATSIHLMGiWCYTFAEMpwyqrriakmlfatppsstYEKALGYFHRAE 222
Cdd:COG0457   78 ALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLG-LALLELGR-------------------YDEAIEAYERAL 137
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 530389084 223 QVDPNfYSKNLLLLGKTYLKLHNKKLAAFWLMKAKDY 259
Cdd:COG0457  138 ELDPD-DADALYNLGIALEKLGRYEEALELLEKLEAA 173
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
73-250 6.18e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 38.44  E-value: 6.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389084  73 QAAVVHATAKVEEILEQADYLYESGEteklyqLLTQYKESEDAELLWRLARASRDVAQLSRTSEEEKKLLVYEALEYakR 152
Cdd:COG3914   18 LAAAAAAELALAAELEAAALAAALGL------ALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLL--Q 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389084 153 ALEKNESSFASHKKAIELNPKDATSIHLMGIWCYtfaempwYQRRiakmlfatppsstYEKALGYFHRAEQVDPNFYSkN 232
Cdd:COG3914   90 ALGRYEEALALYRRALALNPDNAEALFNLGNLLL-------ALGR-------------LEEALAALRRALALNPDFAE-A 148
                        170
                 ....*....|....*...
gi 530389084 233 LLLLGKTYLKLHNKKLAA 250
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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