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Conserved domains on  [gi|24645583|ref|NP_649973|]
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ohgata [Drosophila melanogaster]

Protein Classification

cereblon family protein( domain architecture ID 10204949)

cereblon family protein such as protein cereblon, a substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CRBN_C_like cd15777
Thalidomide-binding C-terminal domain of cereblon (CRBN) and similar protein domains; Cereblon ...
 453-555 4.56e-40

Thalidomide-binding C-terminal domain of cereblon (CRBN) and similar protein domains; Cereblon is part of an E3 ubiquitin ligase complex, together with damaged DNA-binding protein 1 (DDB1), CUL4A and ROC1. Cereblon interacts directly with DDB1, although the C-terminal domain characterized here does not contribute to that interaction. Ubiquination of cellular targets by this complex increases levels of FGF8 and FGF10, which was shown to affect the development of limbs and auditory vesicles in embryogenesis. The C-terminal domain of Cereblon was shown to contain the binding site for thalidomide and its analogs, a class of teratogenic drugs that exhibit an antiproliferative effect on myelomas. Mutations in CRBN, some of which map onto the C-terminal domain, were associated with autosomal recessive mental retardation, which may have to do with interactions between CRBN and ion channels in the brain.


:

Pssm-ID: 276940  Cd Length: 101  Bit Score: 141.23  E-value: 4.56e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645583 453 FFCRYCNSSLALCSDLFAMSKHGVQTQYCNPEGYIHETNTVYRVISHAigYSGEPSTKFSWFPGYQWHIILCKFCAQHVG 532
Cdd:cd15777   1 LLCRSCGAPITRKSDIFSMSGEGHVHTFVNPHGYVFEIGTFSKAPGCA--LVGPPSTEFSWFPGYAWTIALCARCGSHLG 78

                        90       100
                ....*....|....*....|...
gi 24645583 533 WEFKAVHPNLTPKVFFGLAGSSV 555
Cdd:cd15777  79 WKFTAVEKNLSPKSFYGLILDRL 101
PHA02664 super family cl22678
hypothetical protein; Provisional
 35-109 2.57e-03

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PHA02664:

Pssm-ID: 177447  Cd Length: 534  Bit Score: 40.75  E-value: 2.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24645583   35 DVIEQAWNNAMPDEPSPPAEDAFQDPLATDGEGGDALEAMVENVLQDDTASEGSHPSSDMSLESPGSEDDSDLES 109
Cdd:PHA02664 380 EVIAAGAAAAMIAAAERAANGARGSPMAAPEEGRAAAAAAAANAPADQDVEAEAHDEFDQDPGAPAHADRADSDE 454
 
Name Accession Description Interval E-value
CRBN_C_like cd15777
Thalidomide-binding C-terminal domain of cereblon (CRBN) and similar protein domains; Cereblon ...
 453-555 4.56e-40

Thalidomide-binding C-terminal domain of cereblon (CRBN) and similar protein domains; Cereblon is part of an E3 ubiquitin ligase complex, together with damaged DNA-binding protein 1 (DDB1), CUL4A and ROC1. Cereblon interacts directly with DDB1, although the C-terminal domain characterized here does not contribute to that interaction. Ubiquination of cellular targets by this complex increases levels of FGF8 and FGF10, which was shown to affect the development of limbs and auditory vesicles in embryogenesis. The C-terminal domain of Cereblon was shown to contain the binding site for thalidomide and its analogs, a class of teratogenic drugs that exhibit an antiproliferative effect on myelomas. Mutations in CRBN, some of which map onto the C-terminal domain, were associated with autosomal recessive mental retardation, which may have to do with interactions between CRBN and ion channels in the brain.


Pssm-ID: 276940  Cd Length: 101  Bit Score: 141.23  E-value: 4.56e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645583 453 FFCRYCNSSLALCSDLFAMSKHGVQTQYCNPEGYIHETNTVYRVISHAigYSGEPSTKFSWFPGYQWHIILCKFCAQHVG 532
Cdd:cd15777   1 LLCRSCGAPITRKSDIFSMSGEGHVHTFVNPHGYVFEIGTFSKAPGCA--LVGPPSTEFSWFPGYAWTIALCARCGSHLG 78

                        90       100
                ....*....|....*....|...
gi 24645583 533 WEFKAVHPNLTPKVFFGLAGSSV 555
Cdd:cd15777  79 WKFTAVEKNLSPKSFYGLILDRL 101
Yippee-Mis18 pfam03226
Yippee zinc-binding/DNA-binding /Mis18, centromere assembly; This family includes both ...
 451-557 8.73e-19

Yippee zinc-binding/DNA-binding /Mis18, centromere assembly; This family includes both Yippee-type proteins and Mis18 kinetochore proteins. Yippee are putative zinc-binding/DNA-binding proteins. Mis18 are proteins involved in the priming of centromeres for recruiting CENP-A. Mis18-alpha and beta form part of a small complex with Mis18-binding protein. Mis18-alpha is found to interact with DNA de-methylases through a Leu-rich region located at its carboxyl terminus. This entry also includes the CULT domain proteins such as Cereblon.


Pssm-ID: 427204  Cd Length: 99  Bit Score: 81.59  E-value: 8.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645583   451 TLFFCRYCNSSLALCSDLFAMSKhgvqtqycnpegyihETNTV-YRVISHAIGYSGEPSTKFSWFPGYQWHIILCKFCAQ 529
Cdd:pfam03226   1 LVFQCKRCNTILGDSLALVSSGR---------------ELNTIvLKKVTRNVVVGKELVTSESGFDDCTYSPLFCAGCGA 65

                          90       100
                  ....*....|....*....|....*....
gi 24645583   530 HVGWEFKAVHPNLTPKV-FFGLAGSSVRI 557
Cdd:pfam03226  66 VLGRKYRSTPEELDYKRgLFCLETDAISS 94
PHA02664 PHA02664
hypothetical protein; Provisional
 35-109 2.57e-03

hypothetical protein; Provisional


Pssm-ID: 177447  Cd Length: 534  Bit Score: 40.75  E-value: 2.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24645583   35 DVIEQAWNNAMPDEPSPPAEDAFQDPLATDGEGGDALEAMVENVLQDDTASEGSHPSSDMSLESPGSEDDSDLES 109
Cdd:PHA02664 380 EVIAAGAAAAMIAAAERAANGARGSPMAAPEEGRAAAAAAAANAPADQDVEAEAHDEFDQDPGAPAHADRADSDE 454
 
Name Accession Description Interval E-value
CRBN_C_like cd15777
Thalidomide-binding C-terminal domain of cereblon (CRBN) and similar protein domains; Cereblon ...
 453-555 4.56e-40

Thalidomide-binding C-terminal domain of cereblon (CRBN) and similar protein domains; Cereblon is part of an E3 ubiquitin ligase complex, together with damaged DNA-binding protein 1 (DDB1), CUL4A and ROC1. Cereblon interacts directly with DDB1, although the C-terminal domain characterized here does not contribute to that interaction. Ubiquination of cellular targets by this complex increases levels of FGF8 and FGF10, which was shown to affect the development of limbs and auditory vesicles in embryogenesis. The C-terminal domain of Cereblon was shown to contain the binding site for thalidomide and its analogs, a class of teratogenic drugs that exhibit an antiproliferative effect on myelomas. Mutations in CRBN, some of which map onto the C-terminal domain, were associated with autosomal recessive mental retardation, which may have to do with interactions between CRBN and ion channels in the brain.


Pssm-ID: 276940  Cd Length: 101  Bit Score: 141.23  E-value: 4.56e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645583 453 FFCRYCNSSLALCSDLFAMSKHGVQTQYCNPEGYIHETNTVYRVISHAigYSGEPSTKFSWFPGYQWHIILCKFCAQHVG 532
Cdd:cd15777   1 LLCRSCGAPITRKSDIFSMSGEGHVHTFVNPHGYVFEIGTFSKAPGCA--LVGPPSTEFSWFPGYAWTIALCARCGSHLG 78

                        90       100
                ....*....|....*....|...
gi 24645583 533 WEFKAVHPNLTPKVFFGLAGSSV 555
Cdd:cd15777  79 WKFTAVEKNLSPKSFYGLILDRL 101
Yippee-Mis18 pfam03226
Yippee zinc-binding/DNA-binding /Mis18, centromere assembly; This family includes both ...
 451-557 8.73e-19

Yippee zinc-binding/DNA-binding /Mis18, centromere assembly; This family includes both Yippee-type proteins and Mis18 kinetochore proteins. Yippee are putative zinc-binding/DNA-binding proteins. Mis18 are proteins involved in the priming of centromeres for recruiting CENP-A. Mis18-alpha and beta form part of a small complex with Mis18-binding protein. Mis18-alpha is found to interact with DNA de-methylases through a Leu-rich region located at its carboxyl terminus. This entry also includes the CULT domain proteins such as Cereblon.


Pssm-ID: 427204  Cd Length: 99  Bit Score: 81.59  E-value: 8.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645583   451 TLFFCRYCNSSLALCSDLFAMSKhgvqtqycnpegyihETNTV-YRVISHAIGYSGEPSTKFSWFPGYQWHIILCKFCAQ 529
Cdd:pfam03226   1 LVFQCKRCNTILGDSLALVSSGR---------------ELNTIvLKKVTRNVVVGKELVTSESGFDDCTYSPLFCAGCGA 65

                          90       100
                  ....*....|....*....|....*....
gi 24645583   530 HVGWEFKAVHPNLTPKV-FFGLAGSSVRI 557
Cdd:pfam03226  66 VLGRKYRSTPEELDYKRgLFCLETDAISS 94
RLR_C_like cd15803
C-terminal domain of Retinoic acid-inducible gene (RIG)-I-like Receptors, Cereblon (CRBN), and ...
 453-537 8.67e-09

C-terminal domain of Retinoic acid-inducible gene (RIG)-I-like Receptors, Cereblon (CRBN), and similar protein domains; Retinoic acid-inducible gene (RIG)-I-like Receptors (RLRs) are cytoplasmic RNA receptors that recognize non-self RNA and act as molecular sensors to detect viral pathogens. They play crucial roles in innate antiviral responses, including the production of proinflammatory cytokines and type I interferon. There are three RLRs in vertebrates, RIG-I, LGP2, and MDA5. They are characterized by a central DExD/H-box helicase domain and a C-terminal domain, both of which are responsible for binding viral RNA. Cereblon is part of an E3 ubiquitin ligase complex, together with damaged DNA binding protein 1 (DDB1), CUL4A and ROC1. Cereblon interacts directly with DDB1, although the C-terminal domain characterized here does not contribute to that interaction. The C-terminal domain of Cereblon was shown to contain the binding site for thalidomide and its analogs, a class of teratogenic drugs that exhibit an antiproliferative effect on myelomas. Mutations in CRBN, some of which map onto the C-terminal domain, were associated with autosomal recessive mental retardation, which may have to do with interactions between CRBN and ion channels in the brain. RLRs and Cereblon contain a common conserved zinc binding site in their C-terminal domains.


Pssm-ID: 276941  Cd Length: 84  Bit Score: 52.52  E-value: 8.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645583 453 FFCRYCNSSLALCSDLFAMSKhgvqTQYCNpegYIHETNTVYRVISHaigysgePSTKFSWFPGYQWHIILCKFCAQHVG 532
Cdd:cd15803   1 LLCKNCSALACTGEDIRVIEL----CHHVV---YKPAFKNNYNVIGR-------PSTVHKWFDGYAWGIISCKICSSHWG 66


                ....*
gi 24645583 533 WEFKA 537
Cdd:cd15803  67 WHFTY 71
PHA02664 PHA02664
hypothetical protein; Provisional
 35-109 2.57e-03

hypothetical protein; Provisional


Pssm-ID: 177447  Cd Length: 534  Bit Score: 40.75  E-value: 2.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24645583   35 DVIEQAWNNAMPDEPSPPAEDAFQDPLATDGEGGDALEAMVENVLQDDTASEGSHPSSDMSLESPGSEDDSDLES 109
Cdd:PHA02664 380 EVIAAGAAAAMIAAAERAANGARGSPMAAPEEGRAAAAAAAANAPADQDVEAEAHDEFDQDPGAPAHADRADSDE 454
 
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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