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Conserved domains on  [gi|256017227|ref|NP_080733|]
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protein chibby homolog 2 isoform 2 [Mus musculus]

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; ...
 40-155 6.34e-29

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: 108.97  E-value: 6.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256017227  40 LPRMSRRVASQHSYPLNRFSSMPFDPMERPTSQADLELDYNPPRVQLSDEMFVFQDGRWVNESCRlqppyfSPPSSFHHK 119
Cdd:cd07429    1 MPLFGRKFSPKKTPPRKSASLSNLRLLDRSTRQAELGLDYGPIRLKLGGQELVFEDGRWISESGG------SSGVSGREV 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 256017227 120 LHHRRlaKEYQLQEENKSLRDENRALRDENKALRKE 155
Cdd:cd07429   75 LRLKK--KNQQLEEENNLLKLKIEVLLDMLAETTAE 108
MreC super family cl46468
rod shape-determining protein MreC; MreC (murein formation C) is involved in the rod shape ...
 325-384 1.90e-03

rod shape-determining protein MreC; MreC (murein formation C) is involved in the rod shape determination in E. coli, and more generally in cell shape determination of bacteria whether or not they are rod-shaped.


The actual alignment was detected with superfamily member COG1792:

Pssm-ID: 480808  Cd Length: 282  Bit Score: 39.86  E-value: 1.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256017227 325 QALQALQEENRLLQEENRALHILREEHRVFQEENKALweNNKLKLQQRLVIDTVT-EVTAR 384
Cdd:COG1792   68 RSLFNLREENERLKEENAELRAELQRLEELEAENARL--RELLDLKERLDYKFVAaEVIGR 126
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 118-392 9.53e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member pfam02463:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1161  Bit Score: 38.41  E-value: 9.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256017227   118 HKLHHRRLAKEYQLQEENKSLRDENRALRDENKALRKENKILQVFWEEHKVTLGHEESQTSSLLHKDTTSqevvkrdntt 197
Cdd:pfam02463  176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL---------- 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256017227   198 lpaQRSKESTLQLIREENRALQQLLEQRQAYWAQAEENAASTEEGKSTSSPKEESHNSGLLPDQSTNHSSPFEDPKVPPT 277
Cdd:pfam02463  246 ---LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256017227   278 TQEDSKTLRALREMVNNLSGASGEEDGKvgpnlpdsaqpLQLLREMNQALQALQEENRLLQEENRALHILREEHrvFQEE 357
Cdd:pfam02463  323 KKKAEKELKKEKEEIEELEKELKELEIK-----------REAEEEEEEELEKLQEKLEQLEEELLAKKKLESER--LSSA 389

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 256017227   358 NKALWENNKLKLQQRLVIDTVTEVTARMEMLIEEL 392
Cdd:pfam02463  390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEE 424
 
Name Accession Description Interval E-value
Cby_like cd07429
Chibby, a nuclear inhibitor of Wnt/beta-catenin mediated transcription, and similar proteins; ...
 40-155 6.34e-29

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: 108.97  E-value: 6.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256017227  40 LPRMSRRVASQHSYPLNRFSSMPFDPMERPTSQADLELDYNPPRVQLSDEMFVFQDGRWVNESCRlqppyfSPPSSFHHK 119
Cdd:cd07429    1 MPLFGRKFSPKKTPPRKSASLSNLRLLDRSTRQAELGLDYGPIRLKLGGQELVFEDGRWISESGG------SSGVSGREV 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 256017227 120 LHHRRlaKEYQLQEENKSLRDENRALRDENKALRKE 155
Cdd:cd07429   75 LRLKK--KNQQLEEENNLLKLKIEVLLDMLAETTAE 108
Chibby pfam14645
Chibby family; This family includes the eukaryotic chibby proteins. These proteins inhibit the ...
 54-161 1.15e-09

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: 55.39  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256017227   54 PLNRFSSMP-FDPMERPTSQADLELDYNPPRVQLSDEMFVFQDGRWVNEScrlqppyfsppssfhhklhhrrlakeyqlq 132
Cdd:pfam14645  13 PLRKSSSLSnLYLLDPSTREAELGLDYGPIKLRLGGQELVFEDGQWVSES------------------------------ 62

                          90       100
                  ....*....|....*....|....*....
gi 256017227  133 EENKSLRDENRALRDENKALRKENKILQV 161
Cdd:pfam14645  63 GGAGGTGKEMQRLKKRNQQLEEENNLLKL 91
MreC COG1792
Cell shape-determining protein MreC [Cell cycle control, cell division, chromosome ...
 325-384 1.90e-03

Cell shape-determining protein MreC [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 441397  Cd Length: 282  Bit Score: 39.86  E-value: 1.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256017227 325 QALQALQEENRLLQEENRALHILREEHRVFQEENKALweNNKLKLQQRLVIDTVT-EVTAR 384
Cdd:COG1792   68 RSLFNLREENERLKEENAELRAELQRLEELEAENARL--RELLDLKERLDYKFVAaEVIGR 126
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 118-392 9.53e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 38.41  E-value: 9.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256017227   118 HKLHHRRLAKEYQLQEENKSLRDENRALRDENKALRKENKILQVFWEEHKVTLGHEESQTSSLLHKDTTSqevvkrdntt 197
Cdd:pfam02463  176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL---------- 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256017227   198 lpaQRSKESTLQLIREENRALQQLLEQRQAYWAQAEENAASTEEGKSTSSPKEESHNSGLLPDQSTNHSSPFEDPKVPPT 277
Cdd:pfam02463  246 ---LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256017227   278 TQEDSKTLRALREMVNNLSGASGEEDGKvgpnlpdsaqpLQLLREMNQALQALQEENRLLQEENRALHILREEHrvFQEE 357
Cdd:pfam02463  323 KKKAEKELKKEKEEIEELEKELKELEIK-----------REAEEEEEEELEKLQEKLEQLEEELLAKKKLESER--LSSA 389

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 256017227   358 NKALWENNKLKLQQRLVIDTVTEVTARMEMLIEEL 392
Cdd:pfam02463  390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEE 424
 
Name Accession Description Interval E-value
Cby_like cd07429
Chibby, a nuclear inhibitor of Wnt/beta-catenin mediated transcription, and similar proteins; ...
 40-155 6.34e-29

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: 108.97  E-value: 6.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256017227  40 LPRMSRRVASQHSYPLNRFSSMPFDPMERPTSQADLELDYNPPRVQLSDEMFVFQDGRWVNESCRlqppyfSPPSSFHHK 119
Cdd:cd07429    1 MPLFGRKFSPKKTPPRKSASLSNLRLLDRSTRQAELGLDYGPIRLKLGGQELVFEDGRWISESGG------SSGVSGREV 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 256017227 120 LHHRRlaKEYQLQEENKSLRDENRALRDENKALRKE 155
Cdd:cd07429   75 LRLKK--KNQQLEEENNLLKLKIEVLLDMLAETTAE 108
Chibby pfam14645
Chibby family; This family includes the eukaryotic chibby proteins. These proteins inhibit the ...
 54-161 1.15e-09

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: 55.39  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256017227   54 PLNRFSSMP-FDPMERPTSQADLELDYNPPRVQLSDEMFVFQDGRWVNEScrlqppyfsppssfhhklhhrrlakeyqlq 132
Cdd:pfam14645  13 PLRKSSSLSnLYLLDPSTREAELGLDYGPIKLRLGGQELVFEDGQWVSES------------------------------ 62

                          90       100
                  ....*....|....*....|....*....
gi 256017227  133 EENKSLRDENRALRDENKALRKENKILQV 161
Cdd:pfam14645  63 GGAGGTGKEMQRLKKRNQQLEEENNLLKL 91
MreC COG1792
Cell shape-determining protein MreC [Cell cycle control, cell division, chromosome ...
 325-384 1.90e-03

Cell shape-determining protein MreC [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 441397  Cd Length: 282  Bit Score: 39.86  E-value: 1.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256017227 325 QALQALQEENRLLQEENRALHILREEHRVFQEENKALweNNKLKLQQRLVIDTVT-EVTAR 384
Cdd:COG1792   68 RSLFNLREENERLKEENAELRAELQRLEELEAENARL--RELLDLKERLDYKFVAaEVIGR 126
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 118-392 9.53e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 38.41  E-value: 9.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256017227   118 HKLHHRRLAKEYQLQEENKSLRDENRALRDENKALRKENKILQVFWEEHKVTLGHEESQTSSLLHKDTTSqevvkrdntt 197
Cdd:pfam02463  176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL---------- 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256017227   198 lpaQRSKESTLQLIREENRALQQLLEQRQAYWAQAEENAASTEEGKSTSSPKEESHNSGLLPDQSTNHSSPFEDPKVPPT 277
Cdd:pfam02463  246 ---LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256017227   278 TQEDSKTLRALREMVNNLSGASGEEDGKvgpnlpdsaqpLQLLREMNQALQALQEENRLLQEENRALHILREEHrvFQEE 357
Cdd:pfam02463  323 KKKAEKELKKEKEEIEELEKELKELEIK-----------REAEEEEEEELEKLQEKLEQLEEELLAKKKLESER--LSSA 389

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 256017227   358 NKALWENNKLKLQQRLVIDTVTEVTARMEMLIEEL 392
Cdd:pfam02463  390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEE 424
 
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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