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Conserved domains on  [gi|291045198|ref|NP_001166953|]
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protein cereblon isoform 2 [Homo sapiens]

Protein Classification

LON peptidase substrate-binding domain-containing protein; LON peptidase N-terminal domain and RING finger protein( domain architecture ID 12032068)

LON peptidase substrate-binding domain-containing protein similar to the N-terminal polypeptide interaction domain of ATP-dependent protease La (LON) that degrades polypeptides processively to yield small peptide fragments; LON peptidase N-terminal domain and RING finger (LONRF) family protein contains a LON (ATP-dependent protease La) substrate-binding domain that is part of the PUA superfamily and RING finger domain(s)

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 ...
 320-421 5.51e-53

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: 172.43  E-value: 5.51e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198 320 LCCKQCQeTEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHIGW 399
Cdd:cd15777    1 LLCRSCG-APITRKSDIFSMSGEGHVHTFVNPHGYVFEIGTFSKAPGCALVGPPSTEFSWFPGYAWTIALCARCGSHLGW 79

                         90       100
                 ....*....|....*....|..
gi 291045198 400 KFTATKKDMSPQKFWGLTRSAL 421
Cdd:cd15777   80 KFTAVEKNLSPKSFYGLILDRL 101
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
 79-316 1.70e-34

ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be part of the PUA superfamily. This domain represents a general protein and polypeptide interaction domain for the ATP-dependent serine peptidase, LON, Peptidase_S16, pfam05362. ATP-dependent Lon proteases are conserved in all living organizms and catalyze rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins.


:

Pssm-ID: 426647 [Multi-domain]  Cd Length: 195  Bit Score: 127.07  E-value: 1.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198   79 VIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQERE--------AQFGTTAEIYAYREEQDfg 150
Cdd:pfam02190   1 ELPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLYGVLLVSQKDAEDeeptpddlYEVGTVAKIVQILKLPD-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198  151 iEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPEcvlpstMSAVQLESLNKcqifpskpvsredqcsykwwqkyqkrk 230
Cdd:pfam02190  79 -GTYKVLVEGLERVRIVELVKKEEPYLRAEVEDLPE------DSDELSEALKA--------------------------- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198  231 fhcanltswprwlySLYDAETLMDRIKKQLREWDENLKDDSLPsNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCE 310
Cdd:pfam02190 125 --------------LVKELIEKLRRLLKLLLPLELLLKIKDIE-NPGRLADLVAAILPLSPEEKQELLETLDVKERLEKV 189


                  ....*.
gi 291045198  311 LDIMNK 316
Cdd:pfam02190 190 LELLNR 195
 
Name Accession Description Interval E-value
CRBN_C_like cd15777
Thalidomide-binding C-terminal domain of cereblon (CRBN) and similar protein domains; Cereblon ...
 320-421 5.51e-53

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: 172.43  E-value: 5.51e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198 320 LCCKQCQeTEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHIGW 399
Cdd:cd15777    1 LLCRSCG-APITRKSDIFSMSGEGHVHTFVNPHGYVFEIGTFSKAPGCALVGPPSTEFSWFPGYAWTIALCARCGSHLGW 79

                         90       100
                 ....*....|....*....|..
gi 291045198 400 KFTATKKDMSPQKFWGLTRSAL 421
Cdd:cd15777   80 KFTAVEKNLSPKSFYGLILDRL 101
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
 79-316 1.70e-34

ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be part of the PUA superfamily. This domain represents a general protein and polypeptide interaction domain for the ATP-dependent serine peptidase, LON, Peptidase_S16, pfam05362. ATP-dependent Lon proteases are conserved in all living organizms and catalyze rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins.


Pssm-ID: 426647 [Multi-domain]  Cd Length: 195  Bit Score: 127.07  E-value: 1.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198   79 VIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQERE--------AQFGTTAEIYAYREEQDfg 150
Cdd:pfam02190   1 ELPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLYGVLLVSQKDAEDeeptpddlYEVGTVAKIVQILKLPD-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198  151 iEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPEcvlpstMSAVQLESLNKcqifpskpvsredqcsykwwqkyqkrk 230
Cdd:pfam02190  79 -GTYKVLVEGLERVRIVELVKKEEPYLRAEVEDLPE------DSDELSEALKA--------------------------- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198  231 fhcanltswprwlySLYDAETLMDRIKKQLREWDENLKDDSLPsNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCE 310
Cdd:pfam02190 125 --------------LVKELIEKLRRLLKLLLPLELLLKIKDIE-NPGRLADLVAAILPLSPEEKQELLETLDVKERLEKV 189


                  ....*.
gi 291045198  311 LDIMNK 316
Cdd:pfam02190 190 LELLNR 195
LON/PUA COG2802
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function ...
 74-315 1.41e-13

Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown];


Pssm-ID: 442054 [Multi-domain]  Cd Length: 194  Bit Score: 69.13  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198  74 DDSCQVIPVLP-QVmmILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQERE-----AQFGTTAEIYAYREEQ 147
Cdd:COG2802    1 ADLPMELPLFPlGA--VLFPGGRLPLHIFEPRYLDMVRDCLAGDRPFGVVLIREGREVGgppplYDVGTLARITDFEELE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198 148 D--FGIEIVkvkaiGRQRFKVLELRTQSDGIQQAKVQILPEcvlpstmsavqleslnkcqiFPSKPVSRedqcsykwwqk 225
Cdd:COG2802   79 DgrLDITLR-----GVQRFRILEELQEDDPYRVAEVEWLPD--------------------EPDLPVPE----------- 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198 226 yqkrkfhcanltswprwlyslyDAETLMDRIKKQLREWDE--NLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSA 303
Cdd:COG2802  123 ----------------------ELEALRERLLRLLRRYPElaGLEADPDLDDPEWLSNRLAELLPLDPEEKQALLEAPDL 180

                        250
                 ....*....|..
gi 291045198 304 IQRLRCELDIMN 315
Cdd:COG2802  181 LERLELLLALLE 192
Yippee-Mis18 pfam03226
Yippee zinc-binding/DNA-binding /Mis18, centromere assembly; This family includes both ...
 320-428 6.97e-13

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: 64.26  E-value: 6.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198  320 LCCKQCQeTEITTKNEIFSlslcgpMAAYVNphgyvhetLTVYKACNLNLI--GRPSTEHSWFPGYAWTVAQCKICASHI 397
Cdd:pfam03226   3 FQCKRCN-TILGDSLALVS------SGRELN--------TIVLKKVTRNVVvgKELVTSESGFDDCTYSPLFCAGCGAVL 67

                          90       100       110
                  ....*....|....*....|....*....|..
gi 291045198  398 GWKFTATKKDMSPQK-FWGLTRSALLPTIPDT 428
Cdd:pfam03226  68 GRKYRSTPEELDYKRgLFCLETDAISSYQLGS 99
 
Name Accession Description Interval E-value
CRBN_C_like cd15777
Thalidomide-binding C-terminal domain of cereblon (CRBN) and similar protein domains; Cereblon ...
 320-421 5.51e-53

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: 172.43  E-value: 5.51e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198 320 LCCKQCQeTEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHIGW 399
Cdd:cd15777    1 LLCRSCG-APITRKSDIFSMSGEGHVHTFVNPHGYVFEIGTFSKAPGCALVGPPSTEFSWFPGYAWTIALCARCGSHLGW 79

                         90       100
                 ....*....|....*....|..
gi 291045198 400 KFTATKKDMSPQKFWGLTRSAL 421
Cdd:cd15777   80 KFTAVEKNLSPKSFYGLILDRL 101
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
 79-316 1.70e-34

ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be part of the PUA superfamily. This domain represents a general protein and polypeptide interaction domain for the ATP-dependent serine peptidase, LON, Peptidase_S16, pfam05362. ATP-dependent Lon proteases are conserved in all living organizms and catalyze rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins.


Pssm-ID: 426647 [Multi-domain]  Cd Length: 195  Bit Score: 127.07  E-value: 1.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198   79 VIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQERE--------AQFGTTAEIYAYREEQDfg 150
Cdd:pfam02190   1 ELPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLYGVLLVSQKDAEDeeptpddlYEVGTVAKIVQILKLPD-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198  151 iEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPEcvlpstMSAVQLESLNKcqifpskpvsredqcsykwwqkyqkrk 230
Cdd:pfam02190  79 -GTYKVLVEGLERVRIVELVKKEEPYLRAEVEDLPE------DSDELSEALKA--------------------------- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198  231 fhcanltswprwlySLYDAETLMDRIKKQLREWDENLKDDSLPsNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCE 310
Cdd:pfam02190 125 --------------LVKELIEKLRRLLKLLLPLELLLKIKDIE-NPGRLADLVAAILPLSPEEKQELLETLDVKERLEKV 189


                  ....*.
gi 291045198  311 LDIMNK 316
Cdd:pfam02190 190 LELLNR 195
RLR_C_like cd15803
C-terminal domain of Retinoic acid-inducible gene (RIG)-I-like Receptors, Cereblon (CRBN), and ...
 320-421 7.95e-25

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: 97.20  E-value: 7.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198 320 LCCKQCQETeITTKNEIFSLSLCgpmaayvnphgyvheTLTVYKAC---NLNLIGRPSTEHSWFPGYAWTVAQCKICASH 396
Cdd:cd15803    1 LLCKNCSAL-ACTGEDIRVIELC---------------HHVVYKPAfknNYNVIGRPSTVHKWFDGYAWGIISCKICSSH 64

                         90       100
                 ....*....|....*....|....*
gi 291045198 397 IGWKFTATkkdmsPQKFWGLTRSAL 421
Cdd:cd15803   65 WGWHFTYK-----PQKLPVLKRESF 84
LON/PUA COG2802
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function ...
 74-315 1.41e-13

Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown];


Pssm-ID: 442054 [Multi-domain]  Cd Length: 194  Bit Score: 69.13  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198  74 DDSCQVIPVLP-QVmmILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQERE-----AQFGTTAEIYAYREEQ 147
Cdd:COG2802    1 ADLPMELPLFPlGA--VLFPGGRLPLHIFEPRYLDMVRDCLAGDRPFGVVLIREGREVGgppplYDVGTLARITDFEELE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198 148 D--FGIEIVkvkaiGRQRFKVLELRTQSDGIQQAKVQILPEcvlpstmsavqleslnkcqiFPSKPVSRedqcsykwwqk 225
Cdd:COG2802   79 DgrLDITLR-----GVQRFRILEELQEDDPYRVAEVEWLPD--------------------EPDLPVPE----------- 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198 226 yqkrkfhcanltswprwlyslyDAETLMDRIKKQLREWDE--NLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSA 303
Cdd:COG2802  123 ----------------------ELEALRERLLRLLRRYPElaGLEADPDLDDPEWLSNRLAELLPLDPEEKQALLEAPDL 180

                        250
                 ....*....|..
gi 291045198 304 IQRLRCELDIMN 315
Cdd:COG2802  181 LERLELLLALLE 192
Yippee-Mis18 pfam03226
Yippee zinc-binding/DNA-binding /Mis18, centromere assembly; This family includes both ...
 320-428 6.97e-13

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: 64.26  E-value: 6.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198  320 LCCKQCQeTEITTKNEIFSlslcgpMAAYVNphgyvhetLTVYKACNLNLI--GRPSTEHSWFPGYAWTVAQCKICASHI 397
Cdd:pfam03226   3 FQCKRCN-TILGDSLALVS------SGRELN--------TIVLKKVTRNVVvgKELVTSESGFDDCTYSPLFCAGCGAVL 67

                          90       100       110
                  ....*....|....*....|....*....|..
gi 291045198  398 GWKFTATKKDMSPQK-FWGLTRSALLPTIPDT 428
Cdd:pfam03226  68 GRKYRSTPEELDYKRgLFCLETDAISSYQLGS 99
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 78-186 4.76e-03

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 39.23  E-value: 4.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045198  78 QVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQF------GTTAEIYAYREEQDfgi 151
Cdd:COG0466   12 ETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPddlyevGTVAKILQLLKLPD--- 88

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 291045198 152 EIVKVKAIGRQRFKVLELrTQSDGIQQAKVQILPE 186
Cdd:COG0466   89 GTVKVLVEGLQRARIKEF-VQEEPYLEAEVEPLEE 122
 
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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