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Conserved domains on  [gi|2217313474|ref|XP_047292582|]
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tubulin-specific chaperone D isoform X23 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TFCD_C super family cl19887
Tubulin folding cofactor D C terminal; This domain family is found in eukaryotes, and is ...
342-582 1.46e-22

Tubulin folding cofactor D C terminal; This domain family is found in eukaryotes, and is typically between 182 and 199 amino acids in length. The family is found in association with pfam02985. There is a single completely conserved residue R that may be functionally important. Tubulin folding cofactor D does not co-polymerize with microtubules either in vivo or in vitro, but instead modulates microtubule dynamics by sequestering beta-tubulin from GTP-bound alphabeta-heterodimers in microtubules.


The actual alignment was detected with superfamily member COG5234:

Pssm-ID: 473247  Cd Length: 993  Bit Score: 103.11  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217313474 342 ERVIEQLLVGLKDKDTVVRWSAAKGIGRMAGRLPRALADDVVG-----------SVLD--CFSFQETDKAWHGgclALAE 408
Cdd:COG5234   245 EVIVDFLLSSVSSIDSFVRFSAAKGLAKIISRLPWNLAESFIDiielmtenmflSPLEntCDIIITNELVWHG---AILF 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217313474 409 LGRRGLLlPSRLVD--VVAVILKALTYDEKRGACSVGTNVRDAACYVCWAFARAYEPQELKPFVTAISSALVIAAVFDRD 486
Cdd:COG5234   322 FALAGAG-LIDYSDclILPIIEKGLSYEVRYGTRVTGQSIRDSSCFFVWSFYRCYSKSAIEGLQTNLIHLLLQTALFDPE 400
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217313474 487 INCRRAASAAFQENVGRQGTFPHGIDILTTADYFAVGNRSNCFLVISVFIAGFPEYT--QPMIDHLVTMKISHWDGVIRE 564
Cdd:COG5234   401 LNVRRAATAALFEVIGRHASIADGLSLISLINYVSVTRISNCSGDLCRKVAHFPKFRscEDVFQDILLTNLQHWDVKVKQ 480
                         250
                  ....*....|....*...
gi 2217313474 565 LAARALHNLAQQAPEFSA 582
Cdd:COG5234   481 LSAYSLRQLIKYPKELPI 498
 
Name Accession Description Interval E-value
CIN1 COG5234
Beta-tubulin folding cofactor D [Posttranslational modification, protein turnover, chaperones ...
342-582 1.46e-22

Beta-tubulin folding cofactor D [Posttranslational modification, protein turnover, chaperones / Cytoskeleton];


Pssm-ID: 227559  Cd Length: 993  Bit Score: 103.11  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217313474 342 ERVIEQLLVGLKDKDTVVRWSAAKGIGRMAGRLPRALADDVVG-----------SVLD--CFSFQETDKAWHGgclALAE 408
Cdd:COG5234   245 EVIVDFLLSSVSSIDSFVRFSAAKGLAKIISRLPWNLAESFIDiielmtenmflSPLEntCDIIITNELVWHG---AILF 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217313474 409 LGRRGLLlPSRLVD--VVAVILKALTYDEKRGACSVGTNVRDAACYVCWAFARAYEPQELKPFVTAISSALVIAAVFDRD 486
Cdd:COG5234   322 FALAGAG-LIDYSDclILPIIEKGLSYEVRYGTRVTGQSIRDSSCFFVWSFYRCYSKSAIEGLQTNLIHLLLQTALFDPE 400
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217313474 487 INCRRAASAAFQENVGRQGTFPHGIDILTTADYFAVGNRSNCFLVISVFIAGFPEYT--QPMIDHLVTMKISHWDGVIRE 564
Cdd:COG5234   401 LNVRRAATAALFEVIGRHASIADGLSLISLINYVSVTRISNCSGDLCRKVAHFPKFRscEDVFQDILLTNLQHWDVKVKQ 480
                         250
                  ....*....|....*...
gi 2217313474 565 LAARALHNLAQQAPEFSA 582
Cdd:COG5234   481 LSAYSLRQLIKYPKELPI 498
 
Name Accession Description Interval E-value
CIN1 COG5234
Beta-tubulin folding cofactor D [Posttranslational modification, protein turnover, chaperones ...
342-582 1.46e-22

Beta-tubulin folding cofactor D [Posttranslational modification, protein turnover, chaperones / Cytoskeleton];


Pssm-ID: 227559  Cd Length: 993  Bit Score: 103.11  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217313474 342 ERVIEQLLVGLKDKDTVVRWSAAKGIGRMAGRLPRALADDVVG-----------SVLD--CFSFQETDKAWHGgclALAE 408
Cdd:COG5234   245 EVIVDFLLSSVSSIDSFVRFSAAKGLAKIISRLPWNLAESFIDiielmtenmflSPLEntCDIIITNELVWHG---AILF 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217313474 409 LGRRGLLlPSRLVD--VVAVILKALTYDEKRGACSVGTNVRDAACYVCWAFARAYEPQELKPFVTAISSALVIAAVFDRD 486
Cdd:COG5234   322 FALAGAG-LIDYSDclILPIIEKGLSYEVRYGTRVTGQSIRDSSCFFVWSFYRCYSKSAIEGLQTNLIHLLLQTALFDPE 400
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217313474 487 INCRRAASAAFQENVGRQGTFPHGIDILTTADYFAVGNRSNCFLVISVFIAGFPEYT--QPMIDHLVTMKISHWDGVIRE 564
Cdd:COG5234   401 LNVRRAATAALFEVIGRHASIADGLSLISLINYVSVTRISNCSGDLCRKVAHFPKFRscEDVFQDILLTNLQHWDVKVKQ 480
                         250
                  ....*....|....*...
gi 2217313474 565 LAARALHNLAQQAPEFSA 582
Cdd:COG5234   481 LSAYSLRQLIKYPKELPI 498
 
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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