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Conserved domains on  [gi|87044901|ref|NP_848472|]
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tubulin-specific chaperone C [Mus musculus]

Protein Classification

TBCC_N and TBCC domain-containing protein( domain architecture ID 11245415)

TBCC_N and TBCC domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TBCC pfam07986
Tubulin binding cofactor C; Members of this family are involved in the folding pathway of ...
 199-316 1.04e-55

Tubulin binding cofactor C; Members of this family are involved in the folding pathway of tubulins and form a beta helix structure.


:

Pssm-ID: 462331  Cd Length: 119  Bit Score: 177.41  E-value: 1.04e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87044901   199 RDVLLSDLTNCTVKLCGNPNTLRLAKARGCKVLCGPVTTSVFLEDCRDCVLAVACQQLRVHTTKDTRVFLQVTSRAIVED 278
Cdd:pfam07986   2 VDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIED 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 87044901   279 CSGIQFAPYTWSYPGIDKDFQDSGLDRSKNNWDQVDDF 316
Cdd:pfam07986  82 STGIRFAPYNTSYPGLEEHLKSAGLDPENNNWSQVDDF 119
TBCC_N pfam16752
Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific ...
 26-134 1.24e-25

Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific chaperone C has a spectrin-like fold and binds to tubulin.


:

Pssm-ID: 465258 [Multi-domain]  Cd Length: 115  Bit Score: 99.27  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87044901    26 ERLQRREQERQIEVERRKQKRQDQEVEEEKSGFFAAAFARERAAVEELLRG------EASAERLEEAANRLQGLRKLLND 99
Cdd:pfam16752   1 ERLEKRHQERQEQLEKRKEERESEAVPEESVDYFLSAFNEEKASIEELLSQcrsadkSKLKSHLDEITEEIQDLQKFLAD 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 87044901   100 SVLFLAAYDLRQGQAALAQLQAVLTERRQELQPKK 134
Cdd:pfam16752  81 SSYFLPSYDIRSAQEALQKLQKSLEEARAELLPKK 115
 
Name Accession Description Interval E-value
TBCC pfam07986
Tubulin binding cofactor C; Members of this family are involved in the folding pathway of ...
 199-316 1.04e-55

Tubulin binding cofactor C; Members of this family are involved in the folding pathway of tubulins and form a beta helix structure.


Pssm-ID: 462331  Cd Length: 119  Bit Score: 177.41  E-value: 1.04e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87044901   199 RDVLLSDLTNCTVKLCGNPNTLRLAKARGCKVLCGPVTTSVFLEDCRDCVLAVACQQLRVHTTKDTRVFLQVTSRAIVED 278
Cdd:pfam07986   2 VDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIED 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 87044901   279 CSGIQFAPYTWSYPGIDKDFQDSGLDRSKNNWDQVDDF 316
Cdd:pfam07986  82 STGIRFAPYNTSYPGLEEHLKSAGLDPENNNWSQVDDF 119
TBCC_N pfam16752
Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific ...
 26-134 1.24e-25

Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific chaperone C has a spectrin-like fold and binds to tubulin.


Pssm-ID: 465258 [Multi-domain]  Cd Length: 115  Bit Score: 99.27  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87044901    26 ERLQRREQERQIEVERRKQKRQDQEVEEEKSGFFAAAFARERAAVEELLRG------EASAERLEEAANRLQGLRKLLND 99
Cdd:pfam16752   1 ERLEKRHQERQEQLEKRKEERESEAVPEESVDYFLSAFNEEKASIEELLSQcrsadkSKLKSHLDEITEEIQDLQKFLAD 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 87044901   100 SVLFLAAYDLRQGQAALAQLQAVLTERRQELQPKK 134
Cdd:pfam16752  81 SSYFLPSYDIRSAQEALQKLQKSLEEARAELLPKK 115
CARP smart00673
Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;
208-243 2.48e-06

Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;


Pssm-ID: 197827  Cd Length: 38  Bit Score: 43.66  E-value: 2.48e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 87044901    208 NCTVKLCGNPNTLRLAKARGCKVLCGPVTTSVFLED 243
Cdd:smart00673   3 SCTIQVSGKVNTISIDKCKKCSIYLGPVSGSPEIVN 38
 
Name Accession Description Interval E-value
TBCC pfam07986
Tubulin binding cofactor C; Members of this family are involved in the folding pathway of ...
 199-316 1.04e-55

Tubulin binding cofactor C; Members of this family are involved in the folding pathway of tubulins and form a beta helix structure.


Pssm-ID: 462331  Cd Length: 119  Bit Score: 177.41  E-value: 1.04e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87044901   199 RDVLLSDLTNCTVKLCGNPNTLRLAKARGCKVLCGPVTTSVFLEDCRDCVLAVACQQLRVHTTKDTRVFLQVTSRAIVED 278
Cdd:pfam07986   2 VDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIED 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 87044901   279 CSGIQFAPYTWSYPGIDKDFQDSGLDRSKNNWDQVDDF 316
Cdd:pfam07986  82 STGIRFAPYNTSYPGLEEHLKSAGLDPENNNWSQVDDF 119
TBCC_N pfam16752
Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific ...
 26-134 1.24e-25

Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific chaperone C has a spectrin-like fold and binds to tubulin.


Pssm-ID: 465258 [Multi-domain]  Cd Length: 115  Bit Score: 99.27  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87044901    26 ERLQRREQERQIEVERRKQKRQDQEVEEEKSGFFAAAFARERAAVEELLRG------EASAERLEEAANRLQGLRKLLND 99
Cdd:pfam16752   1 ERLEKRHQERQEQLEKRKEERESEAVPEESVDYFLSAFNEEKASIEELLSQcrsadkSKLKSHLDEITEEIQDLQKFLAD 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 87044901   100 SVLFLAAYDLRQGQAALAQLQAVLTERRQELQPKK 134
Cdd:pfam16752  81 SSYFLPSYDIRSAQEALQKLQKSLEEARAELLPKK 115
CARP smart00673
Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;
208-243 2.48e-06

Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;


Pssm-ID: 197827  Cd Length: 38  Bit Score: 43.66  E-value: 2.48e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 87044901    208 NCTVKLCGNPNTLRLAKARGCKVLCGPVTTSVFLED 243
Cdd:smart00673   3 SCTIQVSGKVNTISIDKCKKCSIYLGPVSGSPEIVN 38
CARP smart00673
Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;
244-278 2.41e-03

Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;


Pssm-ID: 197827  Cd Length: 38  Bit Score: 35.19  E-value: 2.41e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 87044901    244 CRDCVLAVA--CQQLRVHTTKDTRVFL-QVTSRAIVED 278
Cdd:smart00673   1 CESCTIQVSgkVNTISIDKCKKCSIYLgPVSGSPEIVN 38
 
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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