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Conserved domains on  [gi|193204239|ref|NP_494201|]
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MATH domain-containing protein [Caenorhabditis elegans]

Protein Classification

MATH domain-containing protein( domain architecture ID 11110250)

MATH (meprin and TRAF-C homology) domain-containing protein similar to Caenorhabditis elegans MATH domain-containing protein

Gene Ontology:  GO:0005515
PubMed:  12387856|17633013

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 14-128 4.70e-39

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: 132.38  E-value: 4.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204239   14 FKNISSLKENENRYSNVERRYNTPWKLGISRKNGMLAVYLYCNKEFYMHRKWSIQTKYTMKLVAVSGKYVQRTMntNYEF 93
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTD--THVF 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 193204239   94 QNPTGNGFPELISWENMQRDYVNDDSILIEAHANI 128
Cdd:pfam00917  79 EKPKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 151-262 2.09e-27

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: 102.33  E-value: 2.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204239  151 FGNISRFVRGEQVYSDIEEHYNIPWRITISKCHERLGIYLYCKKAVCEGKKYEVKCEFEVQLISSSGKCDAGRRSVVFDQ 230
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 193204239  231 PYGRGM-TLISWEKMKKYYVDNDSINVEVIVNI 262
Cdd:pfam00917  81 PKGWGWgKFISWDDLEKDYLVDDSITVEAHVKI 113
 
Name Accession Description Interval E-value
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 14-128 4.70e-39

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: 132.38  E-value: 4.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204239   14 FKNISSLKENENRYSNVERRYNTPWKLGISRKNGMLAVYLYCNKEFYMHRKWSIQTKYTMKLVAVSGKYVQRTMntNYEF 93
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTD--THVF 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 193204239   94 QNPTGNGFPELISWENMQRDYVNDDSILIEAHANI 128
Cdd:pfam00917  79 EKPKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
9-105 2.38e-30

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 109.31  E-value: 2.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204239     9 VLLHTFKNISSLKENENRYSNVERRYNTPWKLGISRKNGMLAVYLYCNKEFYMHRKWSIQTKYTMKLVAVSGKYVQRTmn 88
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKK-- 78

                           90
                   ....*....|....*..
gi 193204239    89 TNYEFQNPTGNGFPELI 105
Cdd:smart00061  79 DKHVFEKPSGWGFSKFI 95
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 151-262 2.09e-27

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: 102.33  E-value: 2.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204239  151 FGNISRFVRGEQVYSDIEEHYNIPWRITISKCHERLGIYLYCKKAVCEGKKYEVKCEFEVQLISSSGKCDAGRRSVVFDQ 230
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 193204239  231 PYGRGM-TLISWEKMKKYYVDNDSINVEVIVNI 262
Cdd:pfam00917  81 PKGWGWgKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
146-237 6.27e-26

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 97.75  E-value: 6.27e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204239   146 VLKHTFGNISRFVRGEQVYSDIEEHYNIPWRITISKCHERLGIYLYCKKAVCEGKKYEVKCEFEVQLISSSGKCDAGRRS 225
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|..
gi 193204239   226 VVFDQPYGRGMT 237
Cdd:smart00061  81 HVFEKPSGWGFS 92
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 12-125 7.23e-23

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: 90.90  E-value: 7.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204239  12 HTFKNIS-SLKENENRYSNVERRYNTPWKLGISRKNGM-----LAVYLYCNKEFYMHRKWSIQTKYTMKLV-AVSGKYVQ 84
Cdd:cd00121    3 HTWKIVNfSELEGESIYSPPFEVGGYKWRIRIYPNGDGesgdyLSLYLELDKGESDLEKWSVRAEFTLKLVnQNGGKSLS 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 193204239  85 RTMNTNYEFQNPTGNGFPELISWENMQRDY-VNDDSILIEAH 125
Cdd:cd00121   83 KSFTHVFFSEKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVE 124
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 147-260 4.10e-16

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: 72.80  E-value: 4.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204239 147 LKHTFGNISRFV-RGEQVYSDIEEHYNIPWRITI-----SKCHERLGIYLYCKKAVCEGKKYEVKCEFEVQLIS-SSGKC 219
Cdd:cd00121    1 GKHTWKIVNFSElEGESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNqNGGKS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 193204239 220 DAGRRSVVF--DQPYGRGMT-LISWEKMKK-YYVDNDSINVEVIV 260
Cdd:cd00121   81 LSKSFTHVFfsEKGSGWGFPkFISWDDLEDsYYLVDDSLTIEVEV 125
 
Name Accession Description Interval E-value
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 14-128 4.70e-39

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: 132.38  E-value: 4.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204239   14 FKNISSLKENENRYSNVERRYNTPWKLGISRKNGMLAVYLYCNKEFYMHRKWSIQTKYTMKLVAVSGKYVQRTMntNYEF 93
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTD--THVF 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 193204239   94 QNPTGNGFPELISWENMQRDYVNDDSILIEAHANI 128
Cdd:pfam00917  79 EKPKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
9-105 2.38e-30

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 109.31  E-value: 2.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204239     9 VLLHTFKNISSLKENENRYSNVERRYNTPWKLGISRKNGMLAVYLYCNKEFYMHRKWSIQTKYTMKLVAVSGKYVQRTmn 88
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKK-- 78

                           90
                   ....*....|....*..
gi 193204239    89 TNYEFQNPTGNGFPELI 105
Cdd:smart00061  79 DKHVFEKPSGWGFSKFI 95
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 151-262 2.09e-27

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: 102.33  E-value: 2.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204239  151 FGNISRFVRGEQVYSDIEEHYNIPWRITISKCHERLGIYLYCKKAVCEGKKYEVKCEFEVQLISSSGKCDAGRRSVVFDQ 230
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 193204239  231 PYGRGM-TLISWEKMKKYYVDNDSINVEVIVNI 262
Cdd:pfam00917  81 PKGWGWgKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
146-237 6.27e-26

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 97.75  E-value: 6.27e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204239   146 VLKHTFGNISRFVRGEQVYSDIEEHYNIPWRITISKCHERLGIYLYCKKAVCEGKKYEVKCEFEVQLISSSGKCDAGRRS 225
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|..
gi 193204239   226 VVFDQPYGRGMT 237
Cdd:smart00061  81 HVFEKPSGWGFS 92
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 12-125 7.23e-23

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: 90.90  E-value: 7.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204239  12 HTFKNIS-SLKENENRYSNVERRYNTPWKLGISRKNGM-----LAVYLYCNKEFYMHRKWSIQTKYTMKLV-AVSGKYVQ 84
Cdd:cd00121    3 HTWKIVNfSELEGESIYSPPFEVGGYKWRIRIYPNGDGesgdyLSLYLELDKGESDLEKWSVRAEFTLKLVnQNGGKSLS 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 193204239  85 RTMNTNYEFQNPTGNGFPELISWENMQRDY-VNDDSILIEAH 125
Cdd:cd00121   83 KSFTHVFFSEKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVE 124
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 147-260 4.10e-16

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: 72.80  E-value: 4.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204239 147 LKHTFGNISRFV-RGEQVYSDIEEHYNIPWRITI-----SKCHERLGIYLYCKKAVCEGKKYEVKCEFEVQLIS-SSGKC 219
Cdd:cd00121    1 GKHTWKIVNFSElEGESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNqNGGKS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 193204239 220 DAGRRSVVF--DQPYGRGMT-LISWEKMKK-YYVDNDSINVEVIV 260
Cdd:cd00121   81 LSKSFTHVFfsEKGSGWGFPkFISWDDLEDsYYLVDDSLTIEVEV 125
 
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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