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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705576 277 RFTWKITQFSSFDGEEHSSYEFTVGPRRWKLVMYPKGNGDgKGNSLSLYLFASDYVTNGPKGGTLAIYKLRVLDQLNRNH 356
Cdd:cd00121     2 KHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGE-SGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80

                  ..
gi 1063705576 357 CE 358
Cdd:cd00121    81 LS 82

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705576 277 RFTWKITQFSSFDGEEHSSYEFTVGPRRWKLVMYPKGNGDgKGNSLSLYLFASDYVTNGPKGGTLAIYKLRVLDQLNRNH 356
Cdd:cd00121     2 KHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGE-SGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80

                  ..
gi 1063705576 357 CE 358
Cdd:cd00121    81 LS 82

meprin and TRAF homology;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705576  137 EKVKNCQSLDFQVSGVKWRLVIRLsrgRKDHLSFVLEITDEKCTGSTWDVKFNFKIGIVPQTGPDYcFVLVGHQNEKKRS 216
Cdd:smart00061  13 EEGESYFSPSEEHFNIPWRLKIYR---KNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSL-SKKDKHVFEKPSG 88

                   ....*..
gi 1063705576  217 QGLANFI 223
Cdd:smart00061  89 WGFSKFI 95

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705576 128 VDGMSKLltEKVKNCQSLDFQVSGVKWRLVIRlsrgRK-DHLSFVLEITDEKCTGSTWDVKFNFKIGIVPQTGPDYCFVL 206
Cdd:pfam00917   1 IKNFSKI--KEGESYYSPVEERFNIPWRLQIY----RKgGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTD 74

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1063705576 207 VgHQNEKKRSQGLANFISHTDLKERFLVNDKAGFYAEI 244
Cdd:pfam00917  75 T-HVFEKPKGWGWGKFISWDDLEKDYLVDDSITVEAHV 111

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705576 277 RFTWKITQFSSFDGEEHSSYEFTVGPRRWKLVMYPKGNGDgKGNSLSLYLFASDYVTNGPKGGTLAIYKLRVLDQLNRNH 356
Cdd:cd00121     2 KHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGE-SGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80

                  ..
gi 1063705576 357 CE 358
Cdd:cd00121    81 LS 82

meprin and TRAF homology;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705576  137 EKVKNCQSLDFQVSGVKWRLVIRLsrgRKDHLSFVLEITDEKCTGSTWDVKFNFKIGIVPQTGPDYcFVLVGHQNEKKRS 216
Cdd:smart00061  13 EEGESYFSPSEEHFNIPWRLKIYR---KNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSL-SKKDKHVFEKPSG 88

                   ....*..
gi 1063705576  217 QGLANFI 223
Cdd:smart00061  89 WGFSKFI 95

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063705576 277 RFTWKITQFSSFDGEEHSSyEFTVGPRRWKLVMYPKGNGDGKGnsLSLYL 326
Cdd:cd03775     2 SFTWRIKNWSELEKKVHSP-KFKCGGFEWRILLFPQGNSQTGG--VSIYL 48