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Conserved domains on  [gi|1063740855|ref|NP_001331622|]
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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 ...
 19-142 4.90e-29

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: 109.39  E-value: 4.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855  19 GKNTWKIKKFSQISKREFASSVFEIGGYSWHILMYPEGCDVS-NHLSLFLCVANHDELLPGWSQLAQFTISVMHKDPKKS 97
Cdd:cd00121     1 GKHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGESgDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063740855  98 -KFSDTLHRFWKKEHDWGWKKFMELPKLRDGFIDDSGCLTIETKVQ 142
Cdd:cd00121    81 lSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEVK 126
 
Name Accession Description Interval E-value
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 19-142 4.90e-29

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: 109.39  E-value: 4.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855  19 GKNTWKIKKFSQISKREFASSVFEIGGYSWHILMYPEGCDVS-NHLSLFLCVANHDELLPGWSQLAQFTISVMHKDPKKS 97
Cdd:cd00121     1 GKHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGESgDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063740855  98 -KFSDTLHRFWKKEHDWGWKKFMELPKLRDGFIDDSGCLTIETKVQ 142
Cdd:cd00121    81 lSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEVK 126
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 25-141 2.26e-19

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: 82.69  E-value: 2.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855  25 IKKFSQISKREFA-SSVFEIGGYSWHILMYPEGCdvsnHLSLFLCVANHDELLPGWSQLAQFTISVMHKDPKKSKFSDTl 103
Cdd:pfam00917   1 IKNFSKIKEGESYySPVEERFNIPWRLQIYRKGG----FLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDT- 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063740855 104 HRFWkKEHDWGWKKFMELPKLRDGF-IDDSGCLTIETKV 141
Cdd:pfam00917  76 HVFE-KPKGWGWGKFISWDDLEKDYlVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
22-119 3.89e-12

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 61.93  E-value: 3.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855   22 TWKIKKFSQISKREFASS-VFEIGGYSWHILMYPEGcdvsNHLSLFLCVANHDELLPGWSQLAQFTISVMHKDPKKSKFS 100
Cdd:smart00061   3 SHTFKNVSRLEEGESYFSpSEEHFNIPWRLKIYRKN----GFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKK 78

                           90
                   ....*....|....*....
gi 1063740855  101 DTlHRFWKKEhDWGWKKFM 119
Cdd:smart00061  79 DK-HVFEKPS-GWGFSKFI 95
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 22-169 2.16e-11

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 65.66  E-value: 2.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855   22 TWKIKKFSQISKReFASSVFEIGGYSWHILMYPEGCDVSNhLSLFLCVANHDELLPG---WSQLAQFTISVMH-KDPKKS 97
Cdd:COG5077     42 TWKVKRWSELAKK-VESPPFSVGGHTWKIILFPQGNNQCN-VSVYLEYEPQELEETGgkyYDCCAQFAFDISNpKYPTIE 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855   98 KFSDTLHRFWKKEHDWGWKKFMELPKL------RDGFIDDsGCLTIETKVQVIRDR--VDRPFFLDYGYKTEIVRVYFRN 169
Cdd:COG5077    120 YINKSHHRFSMESTDWGFTNFIDLNKLiepspgRPPFLEE-GTLVITVYVRVLKDPtgVLWHSFLNYNSKKETGYVGLRN 198
 
Name Accession Description Interval E-value
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 19-142 4.90e-29

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: 109.39  E-value: 4.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855  19 GKNTWKIKKFSQISKREFASSVFEIGGYSWHILMYPEGCDVS-NHLSLFLCVANHDELLPGWSQLAQFTISVMHKDPKKS 97
Cdd:cd00121     1 GKHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGESgDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063740855  98 -KFSDTLHRFWKKEHDWGWKKFMELPKLRDGFIDDSGCLTIETKVQ 142
Cdd:cd00121    81 lSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEVK 126
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 25-141 2.26e-19

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: 82.69  E-value: 2.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855  25 IKKFSQISKREFA-SSVFEIGGYSWHILMYPEGCdvsnHLSLFLCVANHDELLPGWSQLAQFTISVMHKDPKKSKFSDTl 103
Cdd:pfam00917   1 IKNFSKIKEGESYySPVEERFNIPWRLQIYRKGG----FLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDT- 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063740855 104 HRFWkKEHDWGWKKFMELPKLRDGF-IDDSGCLTIETKV 141
Cdd:pfam00917  76 HVFE-KPKGWGWGKFISWDDLEKDYlVDDSITVEAHVKI 113
MATH_Ubp21p cd03775
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ...
 22-125 1.84e-17

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: 78.17  E-value: 1.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855  22 TWKIKKFSQISKREFaSSVFEIGGYSWHILMYPEGCDVSNHLSLFL----CVANHDELLPGWSQLAQFTISVMHK-DPKK 96
Cdd:cd03775     4 TWRIKNWSELEKKVH-SPKFKCGGFEWRILLFPQGNSQTGGVSIYLephpEEEEKAPLDEDWSVCAQFALVISNPgDPSI 82

                          90       100
                  ....*....|....*....|....*....
gi 1063740855  97 SKFSDTLHRFWKKEHDWGWKKFMELPKLR 125
Cdd:cd03775    83 QLSNVAHHRFNAEDKDWGFTRFIELRKLA 111
MATH smart00061
meprin and TRAF homology;
22-119 3.89e-12

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 61.93  E-value: 3.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855   22 TWKIKKFSQISKREFASS-VFEIGGYSWHILMYPEGcdvsNHLSLFLCVANHDELLPGWSQLAQFTISVMHKDPKKSKFS 100
Cdd:smart00061   3 SHTFKNVSRLEEGESYFSpSEEHFNIPWRLKIYRKN----GFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKK 78

                           90
                   ....*....|....*....
gi 1063740855  101 DTlHRFWKKEhDWGWKKFM 119
Cdd:smart00061  79 DK-HVFEKPS-GWGFSKFI 95
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 22-169 2.16e-11

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 65.66  E-value: 2.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855   22 TWKIKKFSQISKReFASSVFEIGGYSWHILMYPEGCDVSNhLSLFLCVANHDELLPG---WSQLAQFTISVMH-KDPKKS 97
Cdd:COG5077     42 TWKVKRWSELAKK-VESPPFSVGGHTWKIILFPQGNNQCN-VSVYLEYEPQELEETGgkyYDCCAQFAFDISNpKYPTIE 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855   98 KFSDTLHRFWKKEHDWGWKKFMELPKL------RDGFIDDsGCLTIETKVQVIRDR--VDRPFFLDYGYKTEIVRVYFRN 169
Cdd:COG5077    120 YINKSHHRFSMESTDWGFTNFIDLNKLiepspgRPPFLEE-GTLVITVYVRVLKDPtgVLWHSFLNYNSKKETGYVGLRN 198
MATH_HAUSP cd03772
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ...
 25-142 1.30e-08

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: 53.23  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855  25 IKKFSQISKREFASSVFeIGGYSWHILMYPEGCDVSNH----LSLFL-CvaNHDELLPGWSQLAQFTISVMHKDPKKSKF 99
Cdd:cd03772     9 VERFSRLSESVLSPPCF-VRNLPWKIMVMPRNYPDRNPhqksVGFFLqC--NAESDSTSWSCHAQAVLRIINYKDDEPSF 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1063740855 100 S-DTLHRFWKKEHDWGWKKFMELPKLRD---GFIDDSGcLTIETKVQ 142
Cdd:cd03772    86 SrRISHLFFSKENDWGFSNFMTWSEVTDpekGFIEDDT-ITLEVYVQ 131
MATH_TRIM37 cd03773
Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal ...
 18-132 1.48e-05

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: 44.33  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855  18 YGKNTWKIKKFSQISKRE--FASSVFEIGGYSWHILMYPEGCDVS--NHLSLFLcvanhdELLPGWSQLAQF--TISVMH 91
Cdd:cd03773     4 YDSATFTLENFSTLRQSAdpVYSDPLNVDGLCWRLKVYPDGNGEVrgNFLSVFL------ELCSGLGEASKYeyRVEMVH 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1063740855  92 K-DPKKSKFSDTLHRFWKKEhDWGWKKFMELPKL-RDGFIDDS 132
Cdd:cd03773    78 QaNPTKNIKREFASDFEVGE-CWGYNRFFRLDLLiNEGYLLPE 119
MATH_SPOP cd03774
Speckle-type POZ protein (SPOP) family, MATH domain; composed of proteins with similarity to ...
 23-146 5.22e-04

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: 39.84  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855  23 WKIKKFS---QISKREFASSVFEIGG---YSWHILMYPEGCDVSN--HLSLFLCVANHDELlPGWsqlAQFTISVMHKDP 94
Cdd:cd03774     9 WTISNFSfcrEEMGEVIKSSTFSSGAndkLKWCLRVNPKGLDEESkdYLSLYLLLVSCPKS-EVR---AKFKFSILNAKG 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063740855  95 KKSKF--SDTLHRFWKKEhDWGWKKFMElpklRDGFIDDSGCL------TIETKVQVIRD 146
Cdd:cd03774    85 EETKAmeSQRAYRFVQGK-DWGFKKFIR----RDFLLDEANGLlpddklTLFCEVSVVQD 139
 
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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