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Conserved domains on  [gi|767977391|ref|XP_011533273|]
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protein chibby homolog 2 isoform X1 [Homo sapiens]

Protein Classification

Cby_like and SMC_prok_B domain-containing protein( domain architecture ID 10164867)

Cby_like and SMC_prok_B domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cby_like cd07429
Chibby, a nuclear inhibitor of Wnt/beta-catenin mediated transcription, and similar proteins; ...
 104-219 1.98e-33

Chibby, a nuclear inhibitor of Wnt/beta-catenin mediated transcription, and similar proteins; Chibby(Cby) is a well-conserved nuclear protein that functions as part of the Wnt/beta-catenin signaling pathway. Specifically, Cby binds directly to beta-catenin by interacting with its central region, which harbors armadillo repeats. Cby-beta-catenin interactions may also involve 14-3-3 proteins. By competing with other binding partners of beta-catenin, the Tcf/Lef transcription factors, Cby inhibits transcriptional activation. Cby has been shown to play a role in adipocyte differentiation. The C-terminal region of Cby appears to contain an alpha-helical coiled-coil motif.


:

Pssm-ID: 143631  Cd Length: 108  Bit Score: 122.06  E-value: 1.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977391 104 LPRLSRRMASQHSYPLNRFSSVPLDPMERPMSQADLELDYNPPRVQLSDEMFVFQDGRWVNENCRlqspyfSPSASFHHK 183
Cdd:cd07429    1 MPLFGRKFSPKKTPPRKSASLSNLRLLDRSTRQAELGLDYGPIRLKLGGQELVFEDGRWISESGG------SSGVSGREV 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767977391 184 LHHKRlaKECMLQEENKSLREENKALREENRMLSKE 219
Cdd:cd07429   75 LRLKK--KNQQLEEENNLLKLKIEVLLDMLAETTAE 108
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 195-432 8.43e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 8.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977391   195 LQEENKSLREENKALREENRMLSKENKILQVFWEEHKASLGREESRAP--SPLLHKDSASLEVVKKDHVALQVPRGKEDS 272
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDelAEELAELEEKLEELKEELESLEAELEELEA 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977391   273 TLQLLREENRALQQLLEQKQAYWAQAEDTAAPAEESKpapspheepcspGLLQDQGSGLSSRFEEPKgPPARQEDSKELR 352
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI------------ERLEARLERLEDRRERLQ-QEIEELLKKLEE 432

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977391   353 ALRKMVSNMSGPSGEEEAKVGPGLPDGCQPL----QLLREMRQALQALLKENRLLQEENRTLQVLRAEHRGFQEENKALW 428
Cdd:TIGR02168  433 AELKELQAELEELEEELEELQEELERLEEALeelrEELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512


                   ....
gi 767977391   429 ENNK 432
Cdd:TIGR02168  513 KNQS 516
 
Name Accession Description Interval E-value
Cby_like cd07429
Chibby, a nuclear inhibitor of Wnt/beta-catenin mediated transcription, and similar proteins; ...
 104-219 1.98e-33

Chibby, a nuclear inhibitor of Wnt/beta-catenin mediated transcription, and similar proteins; Chibby(Cby) is a well-conserved nuclear protein that functions as part of the Wnt/beta-catenin signaling pathway. Specifically, Cby binds directly to beta-catenin by interacting with its central region, which harbors armadillo repeats. Cby-beta-catenin interactions may also involve 14-3-3 proteins. By competing with other binding partners of beta-catenin, the Tcf/Lef transcription factors, Cby inhibits transcriptional activation. Cby has been shown to play a role in adipocyte differentiation. The C-terminal region of Cby appears to contain an alpha-helical coiled-coil motif.


Pssm-ID: 143631  Cd Length: 108  Bit Score: 122.06  E-value: 1.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977391 104 LPRLSRRMASQHSYPLNRFSSVPLDPMERPMSQADLELDYNPPRVQLSDEMFVFQDGRWVNENCRlqspyfSPSASFHHK 183
Cdd:cd07429    1 MPLFGRKFSPKKTPPRKSASLSNLRLLDRSTRQAELGLDYGPIRLKLGGQELVFEDGRWISESGG------SSGVSGREV 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767977391 184 LHHKRlaKECMLQEENKSLREENKALREENRMLSKE 219
Cdd:cd07429   75 LRLKK--KNQQLEEENNLLKLKIEVLLDMLAETTAE 108
Chibby pfam14645
Chibby family; This family includes the eukaryotic chibby proteins. These proteins inhibit the ...
 105-216 1.46e-10

Chibby family; This family includes the eukaryotic chibby proteins. These proteins inhibit the wingless/Wnt pathway by binding to beta-catenin and inhibiting beta-catenin-mediated transcriptional activation. Chibby is Japanese for small, and is named after the RNAi phenotype seen in Drosophila.


Pssm-ID: 464233  Cd Length: 113  Bit Score: 58.47  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977391  105 PRLSRRMASQhSYPLNRFSSVP-LDPMERPMSQADLELDYNPPRVQLSDEMFVFQDGRWVNEncrlqspyfSPSASFHHK 183
Cdd:pfam14645   1 PLFSNKFSPK-KIPLRKSSSLSnLYLLDPSTREAELGLDYGPIKLRLGGQELVFEDGQWVSE---------SGGAGGTGK 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767977391  184 lhhkrlakecmlqeENKSLREENKALREENRML 216
Cdd:pfam14645  71 --------------EMQRLKKRNQQLEEENNLL 89
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 195-432 8.43e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 8.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977391   195 LQEENKSLREENKALREENRMLSKENKILQVFWEEHKASLGREESRAP--SPLLHKDSASLEVVKKDHVALQVPRGKEDS 272
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDelAEELAELEEKLEELKEELESLEAELEELEA 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977391   273 TLQLLREENRALQQLLEQKQAYWAQAEDTAAPAEESKpapspheepcspGLLQDQGSGLSSRFEEPKgPPARQEDSKELR 352
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI------------ERLEARLERLEDRRERLQ-QEIEELLKKLEE 432

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977391   353 ALRKMVSNMSGPSGEEEAKVGPGLPDGCQPL----QLLREMRQALQALLKENRLLQEENRTLQVLRAEHRGFQEENKALW 428
Cdd:TIGR02168  433 AELKELQAELEELEEELEELQEELERLEEALeelrEELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512


                   ....
gi 767977391   429 ENNK 432
Cdd:TIGR02168  513 KNQS 516
 
Name Accession Description Interval E-value
Cby_like cd07429
Chibby, a nuclear inhibitor of Wnt/beta-catenin mediated transcription, and similar proteins; ...
 104-219 1.98e-33

Chibby, a nuclear inhibitor of Wnt/beta-catenin mediated transcription, and similar proteins; Chibby(Cby) is a well-conserved nuclear protein that functions as part of the Wnt/beta-catenin signaling pathway. Specifically, Cby binds directly to beta-catenin by interacting with its central region, which harbors armadillo repeats. Cby-beta-catenin interactions may also involve 14-3-3 proteins. By competing with other binding partners of beta-catenin, the Tcf/Lef transcription factors, Cby inhibits transcriptional activation. Cby has been shown to play a role in adipocyte differentiation. The C-terminal region of Cby appears to contain an alpha-helical coiled-coil motif.


Pssm-ID: 143631  Cd Length: 108  Bit Score: 122.06  E-value: 1.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977391 104 LPRLSRRMASQHSYPLNRFSSVPLDPMERPMSQADLELDYNPPRVQLSDEMFVFQDGRWVNENCRlqspyfSPSASFHHK 183
Cdd:cd07429    1 MPLFGRKFSPKKTPPRKSASLSNLRLLDRSTRQAELGLDYGPIRLKLGGQELVFEDGRWISESGG------SSGVSGREV 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767977391 184 LHHKRlaKECMLQEENKSLREENKALREENRMLSKE 219
Cdd:cd07429   75 LRLKK--KNQQLEEENNLLKLKIEVLLDMLAETTAE 108
Chibby pfam14645
Chibby family; This family includes the eukaryotic chibby proteins. These proteins inhibit the ...
 105-216 1.46e-10

Chibby family; This family includes the eukaryotic chibby proteins. These proteins inhibit the wingless/Wnt pathway by binding to beta-catenin and inhibiting beta-catenin-mediated transcriptional activation. Chibby is Japanese for small, and is named after the RNAi phenotype seen in Drosophila.


Pssm-ID: 464233  Cd Length: 113  Bit Score: 58.47  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977391  105 PRLSRRMASQhSYPLNRFSSVP-LDPMERPMSQADLELDYNPPRVQLSDEMFVFQDGRWVNEncrlqspyfSPSASFHHK 183
Cdd:pfam14645   1 PLFSNKFSPK-KIPLRKSSSLSnLYLLDPSTREAELGLDYGPIKLRLGGQELVFEDGQWVSE---------SGGAGGTGK 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767977391  184 lhhkrlakecmlqeENKSLREENKALREENRML 216
Cdd:pfam14645  71 --------------EMQRLKKRNQQLEEENNLL 89
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 195-432 8.43e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 8.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977391   195 LQEENKSLREENKALREENRMLSKENKILQVFWEEHKASLGREESRAP--SPLLHKDSASLEVVKKDHVALQVPRGKEDS 272
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDelAEELAELEEKLEELKEELESLEAELEELEA 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977391   273 TLQLLREENRALQQLLEQKQAYWAQAEDTAAPAEESKpapspheepcspGLLQDQGSGLSSRFEEPKgPPARQEDSKELR 352
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI------------ERLEARLERLEDRRERLQ-QEIEELLKKLEE 432

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977391   353 ALRKMVSNMSGPSGEEEAKVGPGLPDGCQPL----QLLREMRQALQALLKENRLLQEENRTLQVLRAEHRGFQEENKALW 428
Cdd:TIGR02168  433 AELKELQAELEELEEELEELQEELERLEEALeelrEELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512


                   ....
gi 767977391   429 ENNK 432
Cdd:TIGR02168  513 KNQS 516
 
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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