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Conserved domains on  [gi|18411442|ref|NP_567187|]
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TRAF-like family 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 ...
 166-291 5.48e-22

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: 88.98  E-value: 5.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442 166 KVTWMMSKFSSFNpGKAHQSNEFVVGTRKWRLEVHPRGYmDEKDKSFSVYLSAEGFVNNAPMTKTYAKFKLRVLDQVSWN 245
Cdd:cd00121   2 KHTWKIVNFSELE-GESIYSPPFEVGGYKWRIRIYPNGD-GESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGK 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18411442 246 HVEESGLSWFDAEPSDQSGFADFMPLGKLNEPY-LVKDKLYVGVEFE 291
Cdd:cd00121  80 SLSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 21-142 9.79e-21

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: 85.51  E-value: 9.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442  21 SHLFKIDNFSLLKKhgiEKVESSVFDLAGHKWKLSVYPNGhKNAKGTHVSMFLVNQVPVNDMPT------YELLVVSQLE 94
Cdd:cd00121   2 KHTWKIVNFSELEG---ESIYSPPFEVGGYKWRIRIYPNG-DGESGDYLSLYLELDKGESDLEKwsvraeFTLKLVNQNG 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 18411442  95 RKWHTHGRDEFDINPEPASEGFLRFISLADLERKGFLIGDCCMFGVKF 142
Cdd:cd00121  78 GKSLSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEV 125
 
Name Accession Description Interval E-value
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 166-291 5.48e-22

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: 88.98  E-value: 5.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442 166 KVTWMMSKFSSFNpGKAHQSNEFVVGTRKWRLEVHPRGYmDEKDKSFSVYLSAEGFVNNAPMTKTYAKFKLRVLDQVSWN 245
Cdd:cd00121   2 KHTWKIVNFSELE-GESIYSPPFEVGGYKWRIRIYPNGD-GESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGK 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18411442 246 HVEESGLSWFDAEPSDQSGFADFMPLGKLNEPY-LVKDKLYVGVEFE 291
Cdd:cd00121  80 SLSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 21-142 9.79e-21

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: 85.51  E-value: 9.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442  21 SHLFKIDNFSLLKKhgiEKVESSVFDLAGHKWKLSVYPNGhKNAKGTHVSMFLVNQVPVNDMPT------YELLVVSQLE 94
Cdd:cd00121   2 KHTWKIVNFSELEG---ESIYSPPFEVGGYKWRIRIYPNG-DGESGDYLSLYLELDKGESDLEKwsvraeFTLKLVNQNG 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 18411442  95 RKWHTHGRDEFDINPEPASEGFLRFISLADLERKGFLIGDCCMFGVKF 142
Cdd:cd00121  78 GKSLSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEV 125
MATH smart00061
meprin and TRAF homology;
168-269 1.95e-12

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 62.32  E-value: 1.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442    168 TWMMSKFSSFNPGKAHQSNEFVVGTRKWRLEVHPrgymdeKDKSFSVYLSAEGFVNNAPMTKTYAKFKLRVLDQvSWNHV 247
Cdd:smart00061   3 SHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYR------KNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQ-NGKSL 75

                           90       100
                   ....*....|....*....|..
gi 18411442    248 EESGLSWFDAEPSdqSGFADFM 269
Cdd:smart00061  76 SKKDKHVFEKPSG--WGFSKFI 95
MATH smart00061
meprin and TRAF homology;
20-120 1.56e-06

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 45.75  E-value: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442     20 TSHLFKidNFSLLKKHgiEKVESSVFDLAGHKWKLSVYPNghknakGTHVSMFLVNQVPVND------MPTYELLVVSQL 93
Cdd:smart00061   2 LSHTFK--NVSRLEEG--ESYFSPSEEHFNIPWRLKIYRK------NGFLSLYLHCEKEECDsrkwsiEAEFTLKLVSQN 71

                           90       100
                   ....*....|....*....|....*..
gi 18411442     94 ERKWHTHGRDEFDinpEPASEGFLRFI 120
Cdd:smart00061  72 GKSLSKKDKHVFE---KPSGWGFSKFI 95
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 172-292 2.20e-03

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: 37.24  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442   172 SKFSSFNPGKAHQSNEFVVGTRKWRLEVHPrgymdeKDKSFSVYLSAEGFVNNAPMTKTYAKFKLRVLDQvSWNHVEESG 251
Cdd:pfam00917   2 KNFSKIKEGESYYSPVEERFNIPWRLQIYR------KGGFLGLYLHCDKEEELERGWSIETEFTLKLVSS-NGKSVTKTD 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 18411442   252 LSWFDAEPSdqSGFADFMPLGKLNEPYLVKDKLYVGVEFEV 292
Cdd:pfam00917  75 THVFEKPKG--WGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 26-135 4.55e-03

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: 36.08  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442    26 IDNFSLLKKHGIEKveSSVFDLAGHKWKLSVYPnghknaKGTHVSMFL--VNQVPVNDMPT----YELLVVSQLERKWHT 99
Cdd:pfam00917   1 IKNFSKIKEGESYY--SPVEERFNIPWRLQIYR------KGGFLGLYLhcDKEEELERGWSieteFTLKLVSSNGKSVTK 72

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 18411442   100 HGRDEFDinpEPASEGFLRFISLADLERKgFLIGDC 135
Cdd:pfam00917  73 TDTHVFE---KPKGWGWGKFISWDDLEKD-YLVDDS 104
 
Name Accession Description Interval E-value
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 166-291 5.48e-22

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: 88.98  E-value: 5.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442 166 KVTWMMSKFSSFNpGKAHQSNEFVVGTRKWRLEVHPRGYmDEKDKSFSVYLSAEGFVNNAPMTKTYAKFKLRVLDQVSWN 245
Cdd:cd00121   2 KHTWKIVNFSELE-GESIYSPPFEVGGYKWRIRIYPNGD-GESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGK 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18411442 246 HVEESGLSWFDAEPSDQSGFADFMPLGKLNEPY-LVKDKLYVGVEFE 291
Cdd:cd00121  80 SLSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 21-142 9.79e-21

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: 85.51  E-value: 9.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442  21 SHLFKIDNFSLLKKhgiEKVESSVFDLAGHKWKLSVYPNGhKNAKGTHVSMFLVNQVPVNDMPT------YELLVVSQLE 94
Cdd:cd00121   2 KHTWKIVNFSELEG---ESIYSPPFEVGGYKWRIRIYPNG-DGESGDYLSLYLELDKGESDLEKwsvraeFTLKLVNQNG 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 18411442  95 RKWHTHGRDEFDINPEPASEGFLRFISLADLERKGFLIGDCCMFGVKF 142
Cdd:cd00121  78 GKSLSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEV 125
MATH smart00061
meprin and TRAF homology;
168-269 1.95e-12

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 62.32  E-value: 1.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442    168 TWMMSKFSSFNPGKAHQSNEFVVGTRKWRLEVHPrgymdeKDKSFSVYLSAEGFVNNAPMTKTYAKFKLRVLDQvSWNHV 247
Cdd:smart00061   3 SHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYR------KNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQ-NGKSL 75

                           90       100
                   ....*....|....*....|..
gi 18411442    248 EESGLSWFDAEPSdqSGFADFM 269
Cdd:smart00061  76 SKKDKHVFEKPSG--WGFSKFI 95
MATH smart00061
meprin and TRAF homology;
20-120 1.56e-06

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 45.75  E-value: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442     20 TSHLFKidNFSLLKKHgiEKVESSVFDLAGHKWKLSVYPNghknakGTHVSMFLVNQVPVND------MPTYELLVVSQL 93
Cdd:smart00061   2 LSHTFK--NVSRLEEG--ESYFSPSEEHFNIPWRLKIYRK------NGFLSLYLHCEKEECDsrkwsiEAEFTLKLVSQN 71

                           90       100
                   ....*....|....*....|....*..
gi 18411442     94 ERKWHTHGRDEFDinpEPASEGFLRFI 120
Cdd:smart00061  72 GKSLSKKDKHVFE---KPSGWGFSKFI 95
MATH_TRIM37 cd03773
Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal ...
 21-131 1.33e-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: 43.94  E-value: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442  21 SHLFKIDNFSLLKKHGiEKVESSVFDLAGHKWKLSVYPNGHKNAKGTHVSMF--LVNQVPVNDMPTYELLVVSQLERKWH 98
Cdd:cd03773   6 SATFTLENFSTLRQSA-DPVYSDPLNVDGLCWRLKVYPDGNGEVRGNFLSVFleLCSGLGEASKYEYRVEMVHQANPTKN 84

                        90       100       110
                ....*....|....*....|....*....|....*
gi 18411442  99 ThgRDEFDiNPEPASE--GFLRFISLADLERKGFL 131
Cdd:cd03773  85 I--KREFA-SDFEVGEcwGYNRFFRLDLLINEGYL 116
MATH_TRAF_C cd00270
Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF domain, C-terminal ...
 22-135 1.67e-04

Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF domain, C-terminal MATH subdomain; TRAF molecules serve as adapter proteins that link cell surface TNFRs and receptors of the interleukin-1/Toll-like family to downstream kinase signaling 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. There are at least six mammalian and three Drosophila proteins containing TRAF domains. The mammalian TRAFs display varying expression profiles, indicating independent and cell type-specific regulation. They display distinct, as well as overlapping functions and interactions with receptors. Most TRAFs, except TRAF1, share N-terminal homology and contain a RING domain, multiple zinc finger domains, and a TRAF domain. TRAFs form homo- and heterotrimers through its TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 238168  Cd Length: 149  Bit Score: 41.05  E-value: 1.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442  22 HLFKIDNFSLLKKHGIEKVESSVFDLA------GHKWKLSVYPNGHKNAKGTHVSMFLVNqvpvndMP------------ 83
Cdd:cd00270   3 LIWKIKDYSRKLQEAVAGSNTVLYSPPfytsryGYKLCLRLYLNGDGTGKGTHLSLFVHV------MKgeydallewpfr 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18411442  84 -TYELLVVSQLERKWHTHGRDEFDINPEPASE------------GFLRFISLADLERKGFLIGDC 135
Cdd:cd00270  77 gKITLTLLDQSDDSKRKHITETFMPDPNSSAFqrpptgennigfGYPEFVPLEKLESRGYVKDDT 141
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 172-292 2.20e-03

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: 37.24  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442   172 SKFSSFNPGKAHQSNEFVVGTRKWRLEVHPrgymdeKDKSFSVYLSAEGFVNNAPMTKTYAKFKLRVLDQvSWNHVEESG 251
Cdd:pfam00917   2 KNFSKIKEGESYYSPVEERFNIPWRLQIYR------KGGFLGLYLHCDKEEELERGWSIETEFTLKLVSS-NGKSVTKTD 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 18411442   252 LSWFDAEPSdqSGFADFMPLGKLNEPYLVKDKLYVGVEFEV 292
Cdd:pfam00917  75 THVFEKPKG--WGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 26-135 4.55e-03

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: 36.08  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411442    26 IDNFSLLKKHGIEKveSSVFDLAGHKWKLSVYPnghknaKGTHVSMFL--VNQVPVNDMPT----YELLVVSQLERKWHT 99
Cdd:pfam00917   1 IKNFSKIKEGESYY--SPVEERFNIPWRLQIYR------KGGFLGLYLhcDKEEELERGWSieteFTLKLVSSNGKSVTK 72

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 18411442   100 HGRDEFDinpEPASEGFLRFISLADLERKgFLIGDC 135
Cdd:pfam00917  73 TDTHVFE---KPKGWGWGKFISWDDLEKD-YLVDDS 104
MATH_Ubp21p cd03775
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ...
 20-98 8.49e-03

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: 35.79  E-value: 8.49e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18411442  20 TSHLFKIDNFSLLKKhgieKVESSVFDLAGHKWKLSVYPNGHKNAKGthVSMFLvnqvpvndMPTYELLVVSQLERKWH 98
Cdd:cd03775   1 QSFTWRIKNWSELEK----KVHSPKFKCGGFEWRILLFPQGNSQTGG--VSIYL--------EPHPEEEEKAPLDEDWS 65
 
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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