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Conserved domains on  [gi|81879251|sp|Q8VCN9|]
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RecName: Full=Tubulin-specific chaperone C; AltName: Full=Tubulin-folding cofactor C; Short=CFC

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 81879251   199 RDVLLSDLTNCTVKLCGNPNTLRLAKARGCKVLCGPVTTSVFLEDCRDCVLAVACQQLRVHTTKDTRVFLQVTSRAIVED 278
Cdd:pfam07986   2 VDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIED 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 81879251   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 4.65e-26

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: 100.04  E-value: 4.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81879251    26 ERLQRREQERQIEVERRKQKRQDQEVEEEKSGFFAAAFARERAAVEELLRG------EASAERLEEAANRLQGLRKLLND 99
Cdd:pfam16752   1 ERLEKRHQERQEQLEKRKEERESEAVPEESVDYFLSAFNEEKASIEELLSQcrsadkSKLKSHLDEITEEIQDLQKFLAD 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 81879251   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 81879251   199 RDVLLSDLTNCTVKLCGNPNTLRLAKARGCKVLCGPVTTSVFLEDCRDCVLAVACQQLRVHTTKDTRVFLQVTSRAIVED 278
Cdd:pfam07986   2 VDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIED 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 81879251   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 4.65e-26

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: 100.04  E-value: 4.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81879251    26 ERLQRREQERQIEVERRKQKRQDQEVEEEKSGFFAAAFARERAAVEELLRG------EASAERLEEAANRLQGLRKLLND 99
Cdd:pfam16752   1 ERLEKRHQERQEQLEKRKEERESEAVPEESVDYFLSAFNEEKASIEELLSQcrsadkSKLKSHLDEITEEIQDLQKFLAD 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 81879251   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 81879251    208 NCTVKLCGNPNTLRLAKARGCKVLCGPVTTSVFLED 243
Cdd:smart00673   3 SCTIQVSGKVNTISIDKCKKCSIYLGPVSGSPEIVN 38
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
26-208 3.29e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.02  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81879251   26 ERLQRREQERQIEVERRKQKRQDQEVEEEKSGFFAAAFARERAAVEelLRGEASAERLEEAANRLQGLRKLlndsvlfLA 105
Cdd:PRK09510 101 ERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK--AKAEAEAKRAAAAAKKAAAEAKK-------KA 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81879251  106 AYDLRQGQAALAQLQAVLTERRQELQPKKRFAFKARKKDAAGTAQVDAAPVTSAAPSPPVTKEEEGAPGASWAcgfsnlE 185
Cdd:PRK09510 172 EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAA------K 245
                        170       180
                 ....*....|....*....|...
gi 81879251  186 SQDLEKRAEELHQRDVLLSDLTN 208
Cdd:PRK09510 246 AAEKAAAAKAAAEVDDLFGGLDS 268
 
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 81879251   199 RDVLLSDLTNCTVKLCGNPNTLRLAKARGCKVLCGPVTTSVFLEDCRDCVLAVACQQLRVHTTKDTRVFLQVTSRAIVED 278
Cdd:pfam07986   2 VDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIED 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 81879251   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 4.65e-26

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: 100.04  E-value: 4.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81879251    26 ERLQRREQERQIEVERRKQKRQDQEVEEEKSGFFAAAFARERAAVEELLRG------EASAERLEEAANRLQGLRKLLND 99
Cdd:pfam16752   1 ERLEKRHQERQEQLEKRKEERESEAVPEESVDYFLSAFNEEKASIEELLSQcrsadkSKLKSHLDEITEEIQDLQKFLAD 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 81879251   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 81879251    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 81879251    244 CRDCVLAVA--CQQLRVHTTKDTRVFL-QVTSRAIVED 278
Cdd:smart00673   1 CESCTIQVSgkVNTISIDKCKKCSIYLgPVSGSPEIVN 38
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
26-208 3.29e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.02  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81879251   26 ERLQRREQERQIEVERRKQKRQDQEVEEEKSGFFAAAFARERAAVEelLRGEASAERLEEAANRLQGLRKLlndsvlfLA 105
Cdd:PRK09510 101 ERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK--AKAEAEAKRAAAAAKKAAAEAKK-------KA 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81879251  106 AYDLRQGQAALAQLQAVLTERRQELQPKKRFAFKARKKDAAGTAQVDAAPVTSAAPSPPVTKEEEGAPGASWAcgfsnlE 185
Cdd:PRK09510 172 EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAA------K 245
                        170       180
                 ....*....|....*....|...
gi 81879251  186 SQDLEKRAEELHQRDVLLSDLTN 208
Cdd:PRK09510 246 AAEKAAAAKAAAEVDDLFGGLDS 268
 
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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