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Conserved domains on  [gi|544186107|ref|NP_001269612|]
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F-box only protein 31 isoform 2 [Homo sapiens]

Protein Classification

DUF3506 domain-containing protein( domain architecture ID 10572237)

DUF3506 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cyclin_D1_bind pfam12014
Cyclin D1 binding domain; Ubiquitin-dependent proteolysis of cyclin D1 is associated with ...
 114-340 1.08e-62

Cyclin D1 binding domain; Ubiquitin-dependent proteolysis of cyclin D1 is associated with normal and tumour cell proliferation and survival. The best characterized member of this family is the SCF FBXO31 (Skp1-Cul1-Rbx1-FBXO31) ubiquitin ligase complex mediates genotoxic stress-induced cyclin D1 degradation. FBXO31 possesses a unique substrate-binding beta barrel domain, whereas cyclin D1 binds to FBXO31 by tucking its free C-terminal carboxylate tail into an open cavity of the C-terminal FBXO31 beta-barrel. Biophysical and functional studies demonstrated that SCFFBXO31 is capable of recruiting and ubiquitinating cyclin D1 in a phosphorylation-independent manner.


:

Pssm-ID: 463431  Cd Length: 147  Bit Score: 197.06  E-value: 1.08e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186107  114 YRRIYLPPSrpddLIKP--GLFKGTYGSHGLEIVMLSF------HGRRARGTKITGDPNIPAGQQTVEIDlrhriqlpDL 185
Cdd:pfam12014   1 YRRLYLPPT----LIRPfrGLFVGDYGGHGLEILLLSFpdgareHGKYAEATKLTGDPNVPAGEVTFEAH--------DG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186107  186 ENQRNFNELSRIVLevrervrqeqqeggheagegrgrqgpresqpspaqpraeapskgpdgtpgedggepgdavaaaeqp 265
Cdd:pfam12014  69 EIFREFNEGSRVVQ------------------------------------------------------------------ 82

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544186107  266 aqcgqgqpfvlpVGVSSRNEDYPRTCRmcFYGTGLIAGHGFTSPERTPGVFILFDEDRFGFVWLELKSFSLYSRV 340
Cdd:pfam12014  83 ------------VGVRSRDQNYPRTCR--FYGVGHIAGHGFRNPRRIPGVLILFDEDHLGFIWLELKHFSLFSRV 143
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 203-273 4.31e-03

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 4.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544186107 203 ERVRQEQQEGGHEAGEGRGRQGPRESQPSPAQPRAEAPSKGPDGTPGEDGGEPGDAVAAAEQPAQCGQGQP 273
Cdd:PRK07764 379 ERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAP 449
 
Name Accession Description Interval E-value
Cyclin_D1_bind pfam12014
Cyclin D1 binding domain; Ubiquitin-dependent proteolysis of cyclin D1 is associated with ...
 114-340 1.08e-62

Cyclin D1 binding domain; Ubiquitin-dependent proteolysis of cyclin D1 is associated with normal and tumour cell proliferation and survival. The best characterized member of this family is the SCF FBXO31 (Skp1-Cul1-Rbx1-FBXO31) ubiquitin ligase complex mediates genotoxic stress-induced cyclin D1 degradation. FBXO31 possesses a unique substrate-binding beta barrel domain, whereas cyclin D1 binds to FBXO31 by tucking its free C-terminal carboxylate tail into an open cavity of the C-terminal FBXO31 beta-barrel. Biophysical and functional studies demonstrated that SCFFBXO31 is capable of recruiting and ubiquitinating cyclin D1 in a phosphorylation-independent manner.


Pssm-ID: 463431  Cd Length: 147  Bit Score: 197.06  E-value: 1.08e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186107  114 YRRIYLPPSrpddLIKP--GLFKGTYGSHGLEIVMLSF------HGRRARGTKITGDPNIPAGQQTVEIDlrhriqlpDL 185
Cdd:pfam12014   1 YRRLYLPPT----LIRPfrGLFVGDYGGHGLEILLLSFpdgareHGKYAEATKLTGDPNVPAGEVTFEAH--------DG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186107  186 ENQRNFNELSRIVLevrervrqeqqeggheagegrgrqgpresqpspaqpraeapskgpdgtpgedggepgdavaaaeqp 265
Cdd:pfam12014  69 EIFREFNEGSRVVQ------------------------------------------------------------------ 82

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544186107  266 aqcgqgqpfvlpVGVSSRNEDYPRTCRmcFYGTGLIAGHGFTSPERTPGVFILFDEDRFGFVWLELKSFSLYSRV 340
Cdd:pfam12014  83 ------------VGVRSRDQNYPRTCR--FYGVGHIAGHGFRNPRRIPGVLILFDEDHLGFIWLELKHFSLFSRV 143
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 203-273 4.31e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 4.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544186107 203 ERVRQEQQEGGHEAGEGRGRQGPRESQPSPAQPRAEAPSKGPDGTPGEDGGEPGDAVAAAEQPAQCGQGQP 273
Cdd:PRK07764 379 ERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAP 449
 
Name Accession Description Interval E-value
Cyclin_D1_bind pfam12014
Cyclin D1 binding domain; Ubiquitin-dependent proteolysis of cyclin D1 is associated with ...
 114-340 1.08e-62

Cyclin D1 binding domain; Ubiquitin-dependent proteolysis of cyclin D1 is associated with normal and tumour cell proliferation and survival. The best characterized member of this family is the SCF FBXO31 (Skp1-Cul1-Rbx1-FBXO31) ubiquitin ligase complex mediates genotoxic stress-induced cyclin D1 degradation. FBXO31 possesses a unique substrate-binding beta barrel domain, whereas cyclin D1 binds to FBXO31 by tucking its free C-terminal carboxylate tail into an open cavity of the C-terminal FBXO31 beta-barrel. Biophysical and functional studies demonstrated that SCFFBXO31 is capable of recruiting and ubiquitinating cyclin D1 in a phosphorylation-independent manner.


Pssm-ID: 463431  Cd Length: 147  Bit Score: 197.06  E-value: 1.08e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186107  114 YRRIYLPPSrpddLIKP--GLFKGTYGSHGLEIVMLSF------HGRRARGTKITGDPNIPAGQQTVEIDlrhriqlpDL 185
Cdd:pfam12014   1 YRRLYLPPT----LIRPfrGLFVGDYGGHGLEILLLSFpdgareHGKYAEATKLTGDPNVPAGEVTFEAH--------DG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186107  186 ENQRNFNELSRIVLevrervrqeqqeggheagegrgrqgpresqpspaqpraeapskgpdgtpgedggepgdavaaaeqp 265
Cdd:pfam12014  69 EIFREFNEGSRVVQ------------------------------------------------------------------ 82

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544186107  266 aqcgqgqpfvlpVGVSSRNEDYPRTCRmcFYGTGLIAGHGFTSPERTPGVFILFDEDRFGFVWLELKSFSLYSRV 340
Cdd:pfam12014  83 ------------VGVRSRDQNYPRTCR--FYGVGHIAGHGFRNPRRIPGVLILFDEDHLGFIWLELKHFSLFSRV 143
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 203-273 4.31e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 4.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544186107 203 ERVRQEQQEGGHEAGEGRGRQGPRESQPSPAQPRAEAPSKGPDGTPGEDGGEPGDAVAAAEQPAQCGQGQP 273
Cdd:PRK07764 379 ERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAP 449
 
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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