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Conserved domains on  [gi|76156823|gb|AAX27945|]
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SJCHGC05924 protein, partial [Schistosoma japonicum]

Protein Classification

MATH domain-containing protein( domain architecture ID 10133188)

MATH (meprin and TRAF-C homology) domain-containing protein similar to Homo sapiens speckle-type POZ protein (SPOP), a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation

Gene Ontology:  GO:0005515
PubMed:  12387856

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MATH_SPOP cd03774
Speckle-type POZ protein (SPOP) family, MATH domain; composed of proteins with similarity to ...
 67-206 7.40e-90

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: 261.33  E-value: 7.40e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823  67 RVTKMKYVWTISNFSFCREEMGEVVKSSFFSCGPNDKLKWCLRINPKGLDEESREYLSLYLLLVNCGtKSEARAKFKFSI 146
Cdd:cd03774   1 KVVKFCYMWTISNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCP-KSEVRAKFKFSI 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823 147 LNAKREETKAMESQRAYRFVQGKDWGFKKFIRRDVLMDEANGLLPNDRLTILCEVSVVGE 206
Cdd:cd03774  80 LNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQD 139
 
Name Accession Description Interval E-value
MATH_SPOP cd03774
Speckle-type POZ protein (SPOP) family, MATH domain; composed of proteins with similarity to ...
 67-206 7.40e-90

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: 261.33  E-value: 7.40e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823  67 RVTKMKYVWTISNFSFCREEMGEVVKSSFFSCGPNDKLKWCLRINPKGLDEESREYLSLYLLLVNCGtKSEARAKFKFSI 146
Cdd:cd03774   1 KVVKFCYMWTISNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCP-KSEVRAKFKFSI 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823 147 LNAKREETKAMESQRAYRFVQGKDWGFKKFIRRDVLMDEANGLLPNDRLTILCEVSVVGE 206
Cdd:cd03774  80 LNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQD 139
MATH smart00061
meprin and TRAF homology;
74-177 9.30e-11

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 56.92  E-value: 9.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823     74 VWTISNFSfcREEMGEVVKSSFFSCGpndKLKWCLRINPKGldeesrEYLSLYLLLVNCGTKSEA---RAKFKFSILNAk 150
Cdd:smart00061   3 SHTFKNVS--RLEEGESYFSPSEEHF---NIPWRLKIYRKN------GFLSLYLHCEKEECDSRKwsiEAEFTLKLVSQ- 70

                           90       100
                   ....*....|....*....|....*..
gi 76156823    151 reETKAMESQRAYRFVQGKDWGFKKFI 177
Cdd:smart00061  71 --NGKSLSKKDKHVFEKPSGWGFSKFI 95
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 104-197 3.37e-04

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: 39.16  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823   104 LKWCLRINPKGldeesrEYLSLYLllvNCGTKSEA------RAKFKFSILNAKReetKAMESQRAYRFVQGKDWGFKKFI 177
Cdd:pfam00917  23 IPWRLQIYRKG------GFLGLYL---HCDKEEELergwsiETEFTLKLVSSNG---KSVTKTDTHVFEKPKGWGWGKFI 90

                          90       100
                  ....*....|....*....|
gi 76156823   178 RRDVLMDEangLLPNDRLTI 197
Cdd:pfam00917  91 SWDDLEKD---YLVDDSITV 107
 
Name Accession Description Interval E-value
MATH_SPOP cd03774
Speckle-type POZ protein (SPOP) family, MATH domain; composed of proteins with similarity to ...
 67-206 7.40e-90

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: 261.33  E-value: 7.40e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823  67 RVTKMKYVWTISNFSFCREEMGEVVKSSFFSCGPNDKLKWCLRINPKGLDEESREYLSLYLLLVNCGtKSEARAKFKFSI 146
Cdd:cd03774   1 KVVKFCYMWTISNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCP-KSEVRAKFKFSI 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823 147 LNAKREETKAMESQRAYRFVQGKDWGFKKFIRRDVLMDEANGLLPNDRLTILCEVSVVGE 206
Cdd:cd03774  80 LNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQD 139
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 71-201 1.94e-27

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: 101.69  E-value: 1.94e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823  71 MKYVWTISNFSfcrEEMGEVVKSSFFSCGpndKLKWCLRINPKGlDEESREYLSLYLLLVNCGTKSEA---RAKFKFSIL 147
Cdd:cd00121   1 GKHTWKIVNFS---ELEGESIYSPPFEVG---GYKWRIRIYPNG-DGESGDYLSLYLELDKGESDLEKwsvRAEFTLKLV 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 76156823 148 NAKREETKAMESQRAYRFVQGKDWGFKKFIRRDVLMDEANglLPNDRLTILCEV 201
Cdd:cd00121  74 NQNGGKSLSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYY--LVDDSLTIEVEV 125
MATH smart00061
meprin and TRAF homology;
74-177 9.30e-11

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 56.92  E-value: 9.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823     74 VWTISNFSfcREEMGEVVKSSFFSCGpndKLKWCLRINPKGldeesrEYLSLYLLLVNCGTKSEA---RAKFKFSILNAk 150
Cdd:smart00061   3 SHTFKNVS--RLEEGESYFSPSEEHF---NIPWRLKIYRKN------GFLSLYLHCEKEECDSRKwsiEAEFTLKLVSQ- 70

                           90       100
                   ....*....|....*....|....*..
gi 76156823    151 reETKAMESQRAYRFVQGKDWGFKKFI 177
Cdd:smart00061  71 --NGKSLSKKDKHVFEKPSGWGFSKFI 95
MATH_TRIM37 cd03773
Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal ...
 74-197 2.23e-08

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: 51.26  E-value: 2.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823  74 VWTISNFSFCREEmGEVVKSSFFScgpNDKLKWCLRINPKGLDEESREYLSLYLLLVNcGTKSEARAKFKFSILNaKREE 153
Cdd:cd03773   8 TFTLENFSTLRQS-ADPVYSDPLN---VDGLCWRLKVYPDGNGEVRGNFLSVFLELCS-GLGEASKYEYRVEMVH-QANP 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 76156823 154 TKAMESQRAYRFVQGKDWGFKKFIRRDVLMDEANGLLPNDRLTI 197
Cdd:cd03773  82 TKNIKREFASDFEVGECWGYNRFFRLDLLINEGYLLPENDTLIL 125
MATH_TRAF6 cd03776
Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF6 subfamily, TRAF ...
 73-202 2.64e-06

Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF6 subfamily, TRAF domain, C-terminal MATH subdomain; composed of proteins with similarity to human TRAF6, including the Drosophila protein DTRAF2. TRAF molecules serve as adapter proteins that link TNFRs and downstream kinase cascades resulting in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses. TRAF6 is the most divergent in its TRAF domain among the mammalian TRAFs. In addition to mediating TNFR family signaling, it is also an essential signaling molecule of the interleukin-1/Toll-like receptor superfamily. Whereas other TRAF molecules display similar and overlapping TNFR-binding specificities, TRAF6 binds completely different sites on receptors such as CD40 and RANK. TRAF6 serves as a molecular bridge between innate and adaptive immunity and plays a central role in osteoimmunology. DTRAF2, as an activator of nuclear factor-kappaB, plays a pivotal role in Drosophila development and innate immunity. TRAF6 contains a RING finger domain, five zinc finger domains, and a 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: 239745  Cd Length: 147  Bit Score: 45.78  E-value: 2.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823  73 YVWTISNFSFCREEMGE----VVKSSFFSCGPNDkLKWCLRINPKGLDEESREYLSLYLLLVncgtKSEA--------RA 140
Cdd:cd03776   3 YVWKIKNFSNLRRSMEAgspvVIHSPGFYTSPPG-YKLCARLNLSLPEARCPNYISLFVHLM----QGENdshldwpfQG 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 76156823 141 KFKFSILNAKREE---TKAMES-------QRAYRFVQGKDWGFKKFIRRDVLMDEanGLLPNDRLTILCEVS 202
Cdd:cd03776  78 TITLTLLDQSEPRqniHETMMSkpellafQRPTTDRNPKGFGYVEFAHIEDLLQR--GFVKNDTLLIKIEVN 147
MATH_Ubp21p cd03775
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ...
 73-197 2.08e-05

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: 43.11  E-value: 2.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823  73 YVWTISNFSfcreEMGEVVKSSFFSCGpndKLKWCLRINPKGldEESREYLSLYL-------LLVNCGTKSEARAKFKFS 145
Cdd:cd03775   3 FTWRIKNWS----ELEKKVHSPKFKCG---GFEWRILLFPQG--NSQTGGVSIYLephpeeeEKAPLDEDWSVCAQFALV 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 76156823 146 ILNaKREETKAMESQRAYRFV-QGKDWGFKKFIRRDVLM----DEANGLLPNDRLTI 197
Cdd:cd03775  74 ISN-PGDPSIQLSNVAHHRFNaEDKDWGFTRFIELRKLAhrtpDKPSPFLENGELNI 129
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 104-197 3.37e-04

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: 39.16  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823   104 LKWCLRINPKGldeesrEYLSLYLllvNCGTKSEA------RAKFKFSILNAKReetKAMESQRAYRFVQGKDWGFKKFI 177
Cdd:pfam00917  23 IPWRLQIYRKG------GFLGLYL---HCDKEEELergwsiETEFTLKLVSSNG---KSVTKTDTHVFEKPKGWGWGKFI 90

                          90       100
                  ....*....|....*....|
gi 76156823   178 RRDVLMDEangLLPNDRLTI 197
Cdd:pfam00917  91 SWDDLEKD---YLVDDSITV 107
MATH_TRAF_C cd00270
Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF domain, C-terminal ...
 72-201 2.56e-03

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: 37.20  E-value: 2.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76156823  72 KYVWTISNFSFCREEMGE----VVKSSFFSCGPND-KLkwCLRINPKGLDEESREYLSLYLLLvncgTKSE--------A 138
Cdd:cd00270   2 VLIWKIKDYSRKLQEAVAgsntVLYSPPFYTSRYGyKL--CLRLYLNGDGTGKGTHLSLFVHV----MKGEydallewpF 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76156823 139 RAKFKFSIL----NAKREE-TKAMES-------QRAYRFVQGKDWGFKKFIRRDVLmdEANGLLPNDRLTILCEV 201
Cdd:cd00270  76 RGKITLTLLdqsdDSKRKHiTETFMPdpnssafQRPPTGENNIGFGYPEFVPLEKL--ESRGYVKDDTLFIKVEV 148
 
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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