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Conserved domains on  [gi|30694322|ref|NP_851125|]
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TRAF-like superfamily protein [Arabidopsis thaliana]

Protein Classification

MATH domain-containing protein( domain architecture ID 10062363)

MATH (meprin and TRAF-C homology) domain-containing protein similar to Arabidopsis thaliana MATH domain and coiled-coil domain-containing proteins

Gene Ontology:  GO:0005515
PubMed:  17633013|12387856

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 69-192 4.41e-33

MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane and are capable of cleaving growth factors, extracellular matrix proteins, and biologically active peptides. TRAF molecules serve as adapter proteins that link cell surface receptors of the Tumor Necrosis Factor and 1nterleukin-1/Toll-like families to downstream kinase cascades, which results in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses in the immune and inflammatory systems. Other members include the ubiquitin ligases, TRIM37 and SPOP, and the ubiquitin-specific proteases, HAUSP and Ubp21p. A large number of uncharacterized members mostly from lineage-specific expansions in C. elegans and rice contain MATH and BTB domains, similar to SPOP. The MATH domain has been shown to bind peptide/protein substrates in TRAFs and HAUSP. It is possible that the MATH domain in other members of this superfamily also interacts with various protein substrates. The TRAF domain may also be involved in the trimerization of TRAFs. Based on homology, it is postulated that the MATH domain in meprins may be involved in its tetramer assembly and that the MATH domain, in general, may take part in diverse modular arrangements defined by adjacent multimerization domains.


:

Pssm-ID: 238068  Cd Length: 126  Bit Score: 124.03  E-value: 4.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   69 GKNTWTIEKFSDINKRELRGDVFEVGGYKWYILIYPQGCDVC-NHLSLFLCVAHHEKLLPGWSHFAQFTIAVSNKDPKKS 147
Cdd:cd00121    1 GKHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGESgDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 30694322  148 -KHSDTLHRFWKKEHDWGWKKFIELPKLKEGFIDDSGCLTIKAQVQ 192
Cdd:cd00121   81 lSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEVK 126
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 518-846 5.98e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 53.62  E-value: 5.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    518 QLDSEDRESSPVHWEMDASEVHPPSAGDTSRGRGNSFSI-------------PNGVAER---KGLSTMDDSSSTCSNDSI 581
Cdd:pfam03154   24 QTASPDGRASPTNEDLRSSGRNSPSAASTSSNDSKAESMkksskkikeeapsPLKSAKRqreKGASDTEEPERATAKKSK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    582 QSGVAngsykgnVLNCQSQKwfsngkiqPGKVSDSNSLASEKEHQPSRLASDPKNQSHSsdirrvgeadivishIQKPES 661
Cdd:pfam03154  104 TQEIS-------RPNSPSEG--------EGESSDGRSVNDEGSSDPKDIDQDNRSTSPS---------------IPSPQD 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    662 PKERSPVSKDPNMIQMKEKSAAVLSPSRAAPWNPPSPVQAKPEKKGVSNVEAVPNRKVISVKSPSSHHASPSREAQLQTV 741
Cdd:pfam03154  154 NESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQ 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    742 GPRADIQKIASPKPVEQPAPPMSRPLSAPIIPPTQAA------PVISAVQTSTASLARSMSSTGRLGSPTHSQAYNPQSY 815
Cdd:pfam03154  234 TPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSlhgqmpPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGP 313

                          330       340       350
                   ....*....|....*....|....*....|...
gi 30694322    816 KHAIVG--SSGFTHPSSQSSGTSTLPPYSHPSP 846
Cdd:pfam03154  314 SPAAPGqsQQRIHTPPSQSQLQSQQPPREQPLP 346
 
Name Accession Description Interval E-value
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 69-192 4.41e-33

MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane and are capable of cleaving growth factors, extracellular matrix proteins, and biologically active peptides. TRAF molecules serve as adapter proteins that link cell surface receptors of the Tumor Necrosis Factor and 1nterleukin-1/Toll-like families to downstream kinase cascades, which results in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses in the immune and inflammatory systems. Other members include the ubiquitin ligases, TRIM37 and SPOP, and the ubiquitin-specific proteases, HAUSP and Ubp21p. A large number of uncharacterized members mostly from lineage-specific expansions in C. elegans and rice contain MATH and BTB domains, similar to SPOP. The MATH domain has been shown to bind peptide/protein substrates in TRAFs and HAUSP. It is possible that the MATH domain in other members of this superfamily also interacts with various protein substrates. The TRAF domain may also be involved in the trimerization of TRAFs. Based on homology, it is postulated that the MATH domain in meprins may be involved in its tetramer assembly and that the MATH domain, in general, may take part in diverse modular arrangements defined by adjacent multimerization domains.


Pssm-ID: 238068  Cd Length: 126  Bit Score: 124.03  E-value: 4.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   69 GKNTWTIEKFSDINKRELRGDVFEVGGYKWYILIYPQGCDVC-NHLSLFLCVAHHEKLLPGWSHFAQFTIAVSNKDPKKS 147
Cdd:cd00121    1 GKHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGESgDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 30694322  148 -KHSDTLHRFWKKEHDWGWKKFIELPKLKEGFIDDSGCLTIKAQVQ 192
Cdd:cd00121   81 lSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEVK 126
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 75-193 2.84e-21

MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This domain is hugely expanded in the nematode C. elegans.


Pssm-ID: 425944 [Multi-domain]  Cd Length: 113  Bit Score: 90.01  E-value: 2.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322     75 IEKFSDINKRELR-GDVFEVGGYKWYILIYPQGCdvcnHLSLFLCVAHHEKLLPGWSHFAQFTIAVSNKDPKKSKHSDTl 153
Cdd:pfam00917    1 IKNFSKIKEGESYySPVEERFNIPWRLQIYRKGG----FLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDT- 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 30694322    154 HRFWKkEHDWGWKKFIELPKLKEGFIDDsGCLTIKAQVQV 193
Cdd:pfam00917   76 HVFEK-PKGWGWGKFISWDDLEKDYLVD-DSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
72-169 5.25e-17

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 77.34  E-value: 5.25e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322      72 TWTIEKFSDINKRE-LRGDVFEVGGYKWYILIYPQGcdvcNHLSLFLCVAHHEKLLPGWSHFAQFTIAVSNKDPKKSKHS 150
Cdd:smart00061    3 SHTFKNVSRLEEGEsYFSPSEEHFNIPWRLKIYRKN----GFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKK 78

                            90
                    ....*....|....*....
gi 30694322     151 DTlHRFWKKEhDWGWKKFI 169
Cdd:smart00061   79 DK-HVFEKPS-GWGFSKFI 95
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 67-196 8.14e-11

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 66.43  E-value: 8.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   67 LFGKNTWTIEKFSDINKReLRGDVFEVGGYKWYILIYPQGCDVCNhLSLFLCVAHHEKLLPG---WSHFAQFTIAVSN-K 142
Cdd:COG5077   37 LEMSFTWKVKRWSELAKK-VESPPFSVGGHTWKIILFPQGNNQCN-VSVYLEYEPQELEETGgkyYDCCAQFAFDISNpK 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30694322  143 DPKKSKHSDTLHRFWKKEHDWGWKKFIELPKLKEGFID-----DSGCLTIKAQVQVIRE 196
Cdd:COG5077  115 YPTIEYINKSHHRFSMESTDWGFTNFIDLNKLIEPSPGrppflEEGTLVITVYVRVLKD 173
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 518-846 5.98e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 53.62  E-value: 5.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    518 QLDSEDRESSPVHWEMDASEVHPPSAGDTSRGRGNSFSI-------------PNGVAER---KGLSTMDDSSSTCSNDSI 581
Cdd:pfam03154   24 QTASPDGRASPTNEDLRSSGRNSPSAASTSSNDSKAESMkksskkikeeapsPLKSAKRqreKGASDTEEPERATAKKSK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    582 QSGVAngsykgnVLNCQSQKwfsngkiqPGKVSDSNSLASEKEHQPSRLASDPKNQSHSsdirrvgeadivishIQKPES 661
Cdd:pfam03154  104 TQEIS-------RPNSPSEG--------EGESSDGRSVNDEGSSDPKDIDQDNRSTSPS---------------IPSPQD 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    662 PKERSPVSKDPNMIQMKEKSAAVLSPSRAAPWNPPSPVQAKPEKKGVSNVEAVPNRKVISVKSPSSHHASPSREAQLQTV 741
Cdd:pfam03154  154 NESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQ 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    742 GPRADIQKIASPKPVEQPAPPMSRPLSAPIIPPTQAA------PVISAVQTSTASLARSMSSTGRLGSPTHSQAYNPQSY 815
Cdd:pfam03154  234 TPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSlhgqmpPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGP 313

                          330       340       350
                   ....*....|....*....|....*....|...
gi 30694322    816 KHAIVG--SSGFTHPSSQSSGTSTLPPYSHPSP 846
Cdd:pfam03154  314 SPAAPGqsQQRIHTPPSQSQLQSQQPPREQPLP 346
PHA03247 PHA03247
large tegument protein UL36; Provisional
 620-923 2.32e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   620 ASEKEHQPSRLASDPKNQSHSSDIRRVGEADIVISHIQKPESPKERSPVSkdpnmiqmkeksaavlspSRAAPWNPPSPv 699
Cdd:PHA03247 2644 PTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVG------------------SLTSLADPPPP- 2704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   700 QAKPEKKGVSNVEAVPNRKVISVKSPSSHHASPSREAQLQTVGPRADIQKIASPKPVEQPAPPMSRPLSAPIIPPTQAAP 779
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLT 2784

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   780 VISAvqtstASLARSMSStgrLGSPthsqaYNPQSYKHAIVGSSGFTHPSSQSSGTstLPPYSHPSPISVSNQSGFPINv 859
Cdd:PHA03247 2785 RPAV-----ASLSESRES---LPSP-----WDPADPPAAVLAPAAALPPAASPAGP--LPPPTSAQPTAPPPPPGPPPP- 2848

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694322   860 gswDVSSGGLLWTGGSSSTRDTTTTIsgnhktntynAPVVTTSIRPTNVQIGRTAQSLMTDEFP 923
Cdd:PHA03247 2849 ---SLPLGGSVAPGGDVRRRPPSRSP----------AAKPAAPARPPVRRLARPAVSRSTESFA 2899
 
Name Accession Description Interval E-value
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 69-192 4.41e-33

MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane and are capable of cleaving growth factors, extracellular matrix proteins, and biologically active peptides. TRAF molecules serve as adapter proteins that link cell surface receptors of the Tumor Necrosis Factor and 1nterleukin-1/Toll-like families to downstream kinase cascades, which results in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses in the immune and inflammatory systems. Other members include the ubiquitin ligases, TRIM37 and SPOP, and the ubiquitin-specific proteases, HAUSP and Ubp21p. A large number of uncharacterized members mostly from lineage-specific expansions in C. elegans and rice contain MATH and BTB domains, similar to SPOP. The MATH domain has been shown to bind peptide/protein substrates in TRAFs and HAUSP. It is possible that the MATH domain in other members of this superfamily also interacts with various protein substrates. The TRAF domain may also be involved in the trimerization of TRAFs. Based on homology, it is postulated that the MATH domain in meprins may be involved in its tetramer assembly and that the MATH domain, in general, may take part in diverse modular arrangements defined by adjacent multimerization domains.


Pssm-ID: 238068  Cd Length: 126  Bit Score: 124.03  E-value: 4.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   69 GKNTWTIEKFSDINKRELRGDVFEVGGYKWYILIYPQGCDVC-NHLSLFLCVAHHEKLLPGWSHFAQFTIAVSNKDPKKS 147
Cdd:cd00121    1 GKHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGESgDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 30694322  148 -KHSDTLHRFWKKEHDWGWKKFIELPKLKEGFIDDSGCLTIKAQVQ 192
Cdd:cd00121   81 lSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEVK 126
MATH_Ubp21p cd03775
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ...
 72-175 1.66e-22

Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with similarity to Ubp21p of fission yeast. Ubp21p is a deubiquitinating enzyme that may be involved in the regulation of the protein kinase Prp4p, which controls the formation of active spliceosomes. Members of this family are similar to human HAUSP (Herpesvirus-associated ubiquitin-specific protease) in that they contain an N-terminal MATH domain and a C-terminal catalytic protease (C19 family) domain. HAUSP is also an ubiquitin-specific protease that specifically catalyzes the deubiquitylation of p53 and MDM2. The MATH domain of HAUSP contains the binding site for p53 and MDM2. Similarly, the MATH domain of members in this family may be involved in substrate binding.


Pssm-ID: 239744  Cd Length: 134  Bit Score: 94.35  E-value: 1.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   72 TWTIEKFSDINKRElRGDVFEVGGYKWYILIYPQGCDVCNHLSLFLcvAHH------EKLLPGWSHFAQFTIAVSNK-DP 144
Cdd:cd03775    4 TWRIKNWSELEKKV-HSPKFKCGGFEWRILLFPQGNSQTGGVSIYL--EPHpeeeekAPLDEDWSVCAQFALVISNPgDP 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 30694322  145 KKSKHSDTLHRFWKKEHDWGWKKFIELPKLK 175
Cdd:cd03775   81 SIQLSNVAHHRFNAEDKDWGFTRFIELRKLA 111
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 75-193 2.84e-21

MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This domain is hugely expanded in the nematode C. elegans.


Pssm-ID: 425944 [Multi-domain]  Cd Length: 113  Bit Score: 90.01  E-value: 2.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322     75 IEKFSDINKRELR-GDVFEVGGYKWYILIYPQGCdvcnHLSLFLCVAHHEKLLPGWSHFAQFTIAVSNKDPKKSKHSDTl 153
Cdd:pfam00917    1 IKNFSKIKEGESYySPVEERFNIPWRLQIYRKGG----FLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDT- 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 30694322    154 HRFWKkEHDWGWKKFIELPKLKEGFIDDsGCLTIKAQVQV 193
Cdd:pfam00917   76 HVFEK-PKGWGWGKFISWDDLEKDYLVD-DSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
72-169 5.25e-17

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 77.34  E-value: 5.25e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322      72 TWTIEKFSDINKRE-LRGDVFEVGGYKWYILIYPQGcdvcNHLSLFLCVAHHEKLLPGWSHFAQFTIAVSNKDPKKSKHS 150
Cdd:smart00061    3 SHTFKNVSRLEEGEsYFSPSEEHFNIPWRLKIYRKN----GFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKK 78

                            90
                    ....*....|....*....
gi 30694322     151 DTlHRFWKKEhDWGWKKFI 169
Cdd:smart00061   79 DK-HVFEKPS-GWGFSKFI 95
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 67-196 8.14e-11

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 66.43  E-value: 8.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   67 LFGKNTWTIEKFSDINKReLRGDVFEVGGYKWYILIYPQGCDVCNhLSLFLCVAHHEKLLPG---WSHFAQFTIAVSN-K 142
Cdd:COG5077   37 LEMSFTWKVKRWSELAKK-VESPPFSVGGHTWKIILFPQGNNQCN-VSVYLEYEPQELEETGgkyYDCCAQFAFDISNpK 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30694322  143 DPKKSKHSDTLHRFWKKEHDWGWKKFIELPKLKEGFID-----DSGCLTIKAQVQVIRE 196
Cdd:COG5077  115 YPTIEYINKSHHRFSMESTDWGFTNFIDLNKLIEPSPGrppflEEGTLVITVYVRVLKD 173
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 518-846 5.98e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 53.62  E-value: 5.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    518 QLDSEDRESSPVHWEMDASEVHPPSAGDTSRGRGNSFSI-------------PNGVAER---KGLSTMDDSSSTCSNDSI 581
Cdd:pfam03154   24 QTASPDGRASPTNEDLRSSGRNSPSAASTSSNDSKAESMkksskkikeeapsPLKSAKRqreKGASDTEEPERATAKKSK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    582 QSGVAngsykgnVLNCQSQKwfsngkiqPGKVSDSNSLASEKEHQPSRLASDPKNQSHSsdirrvgeadivishIQKPES 661
Cdd:pfam03154  104 TQEIS-------RPNSPSEG--------EGESSDGRSVNDEGSSDPKDIDQDNRSTSPS---------------IPSPQD 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    662 PKERSPVSKDPNMIQMKEKSAAVLSPSRAAPWNPPSPVQAKPEKKGVSNVEAVPNRKVISVKSPSSHHASPSREAQLQTV 741
Cdd:pfam03154  154 NESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQ 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    742 GPRADIQKIASPKPVEQPAPPMSRPLSAPIIPPTQAA------PVISAVQTSTASLARSMSSTGRLGSPTHSQAYNPQSY 815
Cdd:pfam03154  234 TPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSlhgqmpPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGP 313

                          330       340       350
                   ....*....|....*....|....*....|...
gi 30694322    816 KHAIVG--SSGFTHPSSQSSGTSTLPPYSHPSP 846
Cdd:pfam03154  314 SPAAPGqsQQRIHTPPSQSQLQSQQPPREQPLP 346
MATH_SPOP cd03774
Speckle-type POZ protein (SPOP) family, MATH domain; composed of proteins with similarity to ...
 73-196 1.08e-06

Speckle-type POZ protein (SPOP) family, MATH domain; composed of proteins with similarity to human SPOP. SPOP was isolated as a novel antigen recognized by serum from a scleroderma patient, whose overexpression in COS cells results in a discrete speckled pattern in the nuclei. It contains an N-terminal MATH domain and a C-terminal BTB (also called POZ) domain. Together with Cul3, SPOP constitutes an ubiquitin E3 ligase which is able to ubiquitinate the PcG protein BMI1, the variant histone macroH2A1 and the death domain-associated protein Daxx. Therefore, SPOP may be involved in the regulation of these proteins and may play a role in transcriptional regulation, apoptosis and X-chromosome inactivation. Cul3 binds to the BTB domain of SPOP whereas Daxx and the macroH2A1 nonhistone region have been shown to bind to the MATH domain. Both MATH and BTB domains are necessary for the nuclear speckled accumulation of SPOP. There are many proteins, mostly uncharacterized, containing both MATH and BTB domains from C. elegans and plants which are excluded from this family.


Pssm-ID: 239743  Cd Length: 139  Bit Score: 49.08  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   73 WTIEKFS---DINKRELRGDVFEVGG---YKWYILIYPQGCDVCN--HLSLFLCVAHHEKLlPGWSHFaQFTIAVSNKDP 144
Cdd:cd03774    9 WTISNFSfcrEEMGEVIKSSTFSSGAndkLKWCLRVNPKGLDEESkdYLSLYLLLVSCPKS-EVRAKF-KFSILNAKGEE 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30694322  145 KKSKHSDTLHRFWKKEhDWGWKKFIElpklKEGFIDDSGCL------TIKAQVQVIRE 196
Cdd:cd03774   87 TKAMESQRAYRFVQGK-DWGFKKFIR----RDFLLDEANGLlpddklTLFCEVSVVQD 139
MATH_HAUSP cd03772
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ...
 74-196 4.47e-06

Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, N-terminal MATH (TRAF-like) domain; composed of proteins similar to human HAUSP, an enzyme that specifically catalyzes the deubiquitylation of p53 and MDM2, hence playing an important role in the p53-MDM2 pathway. It contains an N-terminal TRAF-like domain and a C-terminal catalytic protease (C19 family) domain. The tumor suppressor p53 protein is a transcription factor that responds to many cellular stress signals and is regulated primarily through ubiquitylation and subsequent degradation. MDM2 is a RING-finger E3 ubiquitin ligase that promotes p53 ubiquitinylation. p53 and MDM2 bind to the same site in the N-terminal TRAF-like domain of HAUSP in a mutually exclusive manner. HAUSP also interacts with the Epstein-Barr nuclear antigen 1 (EBNA1) protein of the Epstein-Barr virus (EBV), which efficiently immortalizes infected cells predisposing the host to a variety of cancers. EBNA1 plays several important roles in EBV latent infection and cellular transformation. It binds the same pocket as p53 in the HAUSP TRAF-like domain. Through interactions with p53, MDM2 and EBNA1, HAUSP plays a role in cell proliferation, apoptosis and EBV-mediated immortalization.


Pssm-ID: 239741  Cd Length: 137  Bit Score: 47.45  E-value: 4.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   74 TIEKFSDINKRELRGDVFeVGGYKWYILIYPQGCDVCNH----LSLFL-CVAhhEKLLPGWSHFAQFTIAVSNKDP-KKS 147
Cdd:cd03772    8 TVERFSRLSESVLSPPCF-VRNLPWKIMVMPRNYPDRNPhqksVGFFLqCNA--ESDSTSWSCHAQAVLRIINYKDdEPS 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30694322  148 KHSDTLHRFWKKEHDWGWKKFI---ELPKLKEGFIDDSgclTIKAQVQVIRE 196
Cdd:cd03772   85 FSRRISHLFFSKENDWGFSNFMtwsEVTDPEKGFIEDD---TITLEVYVQAD 133
MATH_TRIM37 cd03773
Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal ...
 72-182 5.64e-06

Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal protein and is a member of the tripartite motif (TRIM) protein subfamily, also known as the RING-B-box-coiled-coil (RBCC) subfamily of zinc-finger proteins. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction and hepatomegaly. TRIM37, similar to other TRIMs, contains a cysteine-rich, zinc-binding RING-finger domain followed by another cysteine-rich zinc-binding domain, the B-box, and a coiled-coil domain. TRIM37 is autoubiquitinated in a RING domain-dependent manner, indicating that it functions as an ubiquitin E3 ligase. In addition to the tripartite motif, TRIM37 also contains a MATH domain C-terminal to the coiled-coil domain. The MATH domain of TRIM37 has been shown to interact with the TRAF domain of six known TRAFs in vitro, however, it is unclear whether this is physiologically relevant. Eleven TRIM37 mutations have been associated with Mulibrey nanism so far. One mutation, Gly322Val, is located in the MATH domain and is the only mutation that does not affect the length of the protein. It results in the incorrect subcellular localization of TRIM37.


Pssm-ID: 239742  Cd Length: 132  Bit Score: 47.02  E-value: 5.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   72 TWTIEKFSDINKRE--LRGDVFEVGGYKWYILIYPQGCDVC--NHLSLFLCVAhheKLLPGWSHFaQFTIAVSNK-DPKK 146
Cdd:cd03773    8 TFTLENFSTLRQSAdpVYSDPLNVDGLCWRLKVYPDGNGEVrgNFLSVFLELC---SGLGEASKY-EYRVEMVHQaNPTK 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 30694322  147 SKHSDTLHRFWKKEhDWGWKKFIELPKL-KEGFIDDS 182
Cdd:cd03773   84 NIKREFASDFEVGE-CWGYNRFFRLDLLiNEGYLLPE 119
PHA03247 PHA03247
large tegument protein UL36; Provisional
 620-923 2.32e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   620 ASEKEHQPSRLASDPKNQSHSSDIRRVGEADIVISHIQKPESPKERSPVSkdpnmiqmkeksaavlspSRAAPWNPPSPv 699
Cdd:PHA03247 2644 PTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVG------------------SLTSLADPPPP- 2704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   700 QAKPEKKGVSNVEAVPNRKVISVKSPSSHHASPSREAQLQTVGPRADIQKIASPKPVEQPAPPMSRPLSAPIIPPTQAAP 779
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLT 2784

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322   780 VISAvqtstASLARSMSStgrLGSPthsqaYNPQSYKHAIVGSSGFTHPSSQSSGTstLPPYSHPSPISVSNQSGFPINv 859
Cdd:PHA03247 2785 RPAV-----ASLSESRES---LPSP-----WDPADPPAAVLAPAAALPPAASPAGP--LPPPTSAQPTAPPPPPGPPPP- 2848

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694322   860 gswDVSSGGLLWTGGSSSTRDTTTTIsgnhktntynAPVVTTSIRPTNVQIGRTAQSLMTDEFP 923
Cdd:PHA03247 2849 ---SLPLGGSVAPGGDVRRRPPSRSP----------AAKPAAPARPPVRRLARPAVSRSTESFA 2899
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 626-853 1.22e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    626 QPSRLASDPKNQSHSSDIRRVGEADIVISHIQK---PESPKERSPVSKDPNMIQMKEKSAAVLS--------PSRAAPWN 694
Cdd:pfam03154  209 QGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRlpsPHPPLQPMTQPPPPSQVSPQPLPQPSLHgqmppmphSLQTGPSH 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    695 PPSPVQAKP----EKKGVSNVEAVPNRKVisvkspsshhasPSREAQLQTVGPRADIQKIASPkPVEQPAPPMsrPLSAP 770
Cdd:pfam03154  289 MQHPVPPQPfpltPQSSQSQVPPGPSPAA------------PGQSQQRIHTPPSQSQLQSQQP-PREQPLPPA--PLSMP 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    771 IIPPTQAAPVisavqtstaslarsmsstgrlgspthSQAYNPQSYKHA--IVGSSGFTHPSS---------QSSGTSTLP 839
Cdd:pfam03154  354 HIKPPPTTPI--------------------------PQLPNPQSHKHPphLSGPSPFQMNSNlppppalkpLSSLSTHHP 407

                          250
                   ....*....|....
gi 30694322    840 PYSHPSPISVSNQS 853
Cdd:pfam03154  408 PSAHPPPLQLMPQS 421
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 609-846 2.94e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 41.56  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    609 QPGKVSDsnslASEKEH------QPSRLASDPKNQSHSSDIRRVGEADIVISHIQKP-----ESPKERSPVskdPNMiqm 677
Cdd:pfam09770   87 QTAKVSD----AIEEEQvrfnrqQPAARAAQSSAQPPASSLPQYQYASQQSQQPSKPvrtgyEKYKEPEPI---PDL--- 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    678 kEKSAAV--LSPSRAAPWNPPSPVQAKPEKKGVsnveavPNRKVISVKSPsshhaspsrEAQLqtvgpRADiqkiaSPKP 755
Cdd:pfam09770  157 -QVDASLwgVAPKKAAAPAPAPQPAAQPASLPA------PSRKMMSLEEV---------EAAM-----RAQ-----AKKP 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694322    756 VEQPAPPMSRPlsaPIIPPTQAAPVISAVQTSTASLARSMSSTGRlGSPTHSQAYNPQSYKH--AIVGSSGFTHPSSQSS 833
Cdd:pfam09770  211 AQQPAPAPAQP---PAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQ-PQQHPGQGHPVTILQRpqSPQPDPAQPSIQPQAQ 286

                          250
                   ....*....|...
gi 30694322    834 GTSTLPPYSHPSP 846
Cdd:pfam09770  287 QFHQQPPPVPVQP 299
 
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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