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Conserved domains on  [gi|1370472012|ref|XP_024306667|]
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tubulin-specific chaperone D isoform X26 [Homo sapiens]

Protein Classification

TFCD_C domain-containing protein( domain architecture ID 10576471)

TFCD_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TFCD_C pfam12612
Tubulin folding cofactor D C terminal; This domain family is found in eukaryotes, and is ...
 339-525 5.71e-85

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.


:

Pssm-ID: 463643  Cd Length: 187  Bit Score: 263.71  E-value: 5.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472012 339 RIMCCVAQQASEKIDRFRAHAASVFLTLLHFDsPPIPHVPHRGELEKLFPRsDVASVNWSAPSQAFPRITQLLGLPTYRY 418
Cdd:pfam12612   2 RLIGGLLKQAVEKIDRVRALAGKVLLRLLHHD-PPPPHIPHREELEEIFPE-DEEDLNWNSPSDTFPRLVQLLDIPEYRY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472012 419 HVLLGLVVSLGGLTESTIRHSTQSLFEYMKGIQ--SDPQALGSFSGTLLQIFEDNLLNERVSVPLLKTLDHVLTHGCFDI 496
Cdd:pfam12612  80 PLLLGLVVSVGGLTESLVKASSAALLEYLRSLPdeKDPDLLEDLLSDLLDILESNLKDDRVVVPLLKTLDFLLESGVFED 159

                         170       180
                  ....*....|....*....|....*....
gi 1370472012 497 FTTEEDhPFAVKLLALCKKEIKNSKDIQK 525
Cdd:pfam12612 160 LLEDDS-SFLEKLLELVQKEIKKSKNVQK 187
TFCD_C super family cl19887
Tubulin folding cofactor D C terminal; This domain family is found in eukaryotes, and is ...
 290-352 1.99e-04

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: 44.55  E-value: 1.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370472012 290 LLGCMDDYTTDSRGDVGTWVRKAAMTSLMDLTLLLARSQPELIEAHTCERI--MCCVAQQASEKI 352
Cdd:COG5234   692 ILNVLSNYLTDTRGDVGSWIRKPAMKLMSSFLVKDSSGKKLYIIRQTFDKIdsLRGLAYQALEQI 756
 
Name Accession Description Interval E-value
TFCD_C pfam12612
Tubulin folding cofactor D C terminal; This domain family is found in eukaryotes, and is ...
 339-525 5.71e-85

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.


Pssm-ID: 463643  Cd Length: 187  Bit Score: 263.71  E-value: 5.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472012 339 RIMCCVAQQASEKIDRFRAHAASVFLTLLHFDsPPIPHVPHRGELEKLFPRsDVASVNWSAPSQAFPRITQLLGLPTYRY 418
Cdd:pfam12612   2 RLIGGLLKQAVEKIDRVRALAGKVLLRLLHHD-PPPPHIPHREELEEIFPE-DEEDLNWNSPSDTFPRLVQLLDIPEYRY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472012 419 HVLLGLVVSLGGLTESTIRHSTQSLFEYMKGIQ--SDPQALGSFSGTLLQIFEDNLLNERVSVPLLKTLDHVLTHGCFDI 496
Cdd:pfam12612  80 PLLLGLVVSVGGLTESLVKASSAALLEYLRSLPdeKDPDLLEDLLSDLLDILESNLKDDRVVVPLLKTLDFLLESGVFED 159

                         170       180
                  ....*....|....*....|....*....
gi 1370472012 497 FTTEEDhPFAVKLLALCKKEIKNSKDIQK 525
Cdd:pfam12612 160 LLEDDS-SFLEKLLELVQKEIKKSKNVQK 187
CIN1 COG5234
Beta-tubulin folding cofactor D [Posttranslational modification, protein turnover, chaperones ...
 290-352 1.99e-04

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


Pssm-ID: 227559  Cd Length: 993  Bit Score: 44.55  E-value: 1.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370472012 290 LLGCMDDYTTDSRGDVGTWVRKAAMTSLMDLTLLLARSQPELIEAHTCERI--MCCVAQQASEKI 352
Cdd:COG5234   692 ILNVLSNYLTDTRGDVGSWIRKPAMKLMSSFLVKDSSGKKLYIIRQTFDKIdsLRGLAYQALEQI 756
 
Name Accession Description Interval E-value
TFCD_C pfam12612
Tubulin folding cofactor D C terminal; This domain family is found in eukaryotes, and is ...
 339-525 5.71e-85

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.


Pssm-ID: 463643  Cd Length: 187  Bit Score: 263.71  E-value: 5.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472012 339 RIMCCVAQQASEKIDRFRAHAASVFLTLLHFDsPPIPHVPHRGELEKLFPRsDVASVNWSAPSQAFPRITQLLGLPTYRY 418
Cdd:pfam12612   2 RLIGGLLKQAVEKIDRVRALAGKVLLRLLHHD-PPPPHIPHREELEEIFPE-DEEDLNWNSPSDTFPRLVQLLDIPEYRY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472012 419 HVLLGLVVSLGGLTESTIRHSTQSLFEYMKGIQ--SDPQALGSFSGTLLQIFEDNLLNERVSVPLLKTLDHVLTHGCFDI 496
Cdd:pfam12612  80 PLLLGLVVSVGGLTESLVKASSAALLEYLRSLPdeKDPDLLEDLLSDLLDILESNLKDDRVVVPLLKTLDFLLESGVFED 159

                         170       180
                  ....*....|....*....|....*....
gi 1370472012 497 FTTEEDhPFAVKLLALCKKEIKNSKDIQK 525
Cdd:pfam12612 160 LLEDDS-SFLEKLLELVQKEIKKSKNVQK 187
CIN1 COG5234
Beta-tubulin folding cofactor D [Posttranslational modification, protein turnover, chaperones ...
 290-352 1.99e-04

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


Pssm-ID: 227559  Cd Length: 993  Bit Score: 44.55  E-value: 1.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370472012 290 LLGCMDDYTTDSRGDVGTWVRKAAMTSLMDLTLLLARSQPELIEAHTCERI--MCCVAQQASEKI 352
Cdd:COG5234   692 ILNVLSNYLTDTRGDVGSWIRKPAMKLMSSFLVKDSSGKKLYIIRQTFDKIdsLRGLAYQALEQI 756
 
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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