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Conserved domains on  [gi|1831507667|ref|NP_001367464|]
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MATH domain-containing protein [Caenorhabditis elegans]

Protein Classification

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 ...
54-169 1.83e-33

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: 116.59  E-value: 1.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831507667  54 FSDVSRIEEGESRFSRFEKRFNIPWRIELQRVSGFLEIHLHrgIEIEKPDDVFTIIKADCWFNLVSTNGKNLMRQMSAVF 133
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLH--CDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVF 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1831507667 134 CRDVDMEsLKKVIRWDDMMTDYVINDSFIIEAHIEI 169
Cdd:pfam00917  79 EKPKGWG-WGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
197-225 1.11e-03

meprin and TRAF homology;


:

Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 37.28  E-value: 1.11e-03
                           10        20
                   ....*....|....*....|....*....
gi 1831507667  197 ITCKVNNVSRFQDGEKQWGNTELRYDIPW 225
Cdd:smart00061   2 LSHTFKNVSRLEEGESYFSPSEEHFNIPW 30
 
Name Accession Description Interval E-value
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
54-169 1.83e-33

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: 116.59  E-value: 1.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831507667  54 FSDVSRIEEGESRFSRFEKRFNIPWRIELQRVSGFLEIHLHrgIEIEKPDDVFTIIKADCWFNLVSTNGKNLMRQMSAVF 133
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLH--CDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVF 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1831507667 134 CRDVDMEsLKKVIRWDDMMTDYVINDSFIIEAHIEI 169
Cdd:pfam00917  79 EKPKGWG-WGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
49-138 1.54e-21

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 85.04  E-value: 1.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831507667   49 VLSQQFSDVSRIEEGESRFSRFEKRFNIPWRIELQRVSGFLEIHLHrgIEIEKPDDVFTIIKADCWFNLVSTNGKNLMRQ 128
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLH--CEKEECDSRKWSIEAEFTLKLVSQNGKSLSKK 78
                           90
                   ....*....|
gi 1831507667  129 MSAVFCRDVD 138
Cdd:smart00061  79 DKHVFEKPSG 88
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
62-168 4.61e-12

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: 60.86  E-value: 4.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831507667  62 EGESRFSRFEKRFNIPWRIELQR-----VSGFLEIHLHrgIEIEKPDDVFTIIKADCWFNLVSTN-GKNLMRQMSAVFCR 135
Cdd:cd00121    14 EGESIYSPPFEVGGYKWRIRIYPngdgeSGDYLSLYLE--LDKGESDLEKWSVRAEFTLKLVNQNgGKSLSKSFTHVFFS 91
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1831507667 136 DV-DMESLKKVIRWDDMMTDY-VINDSFIIEAHIE 168
Cdd:cd00121    92 EKgSGWGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126
MATH smart00061
meprin and TRAF homology;
197-225 1.11e-03

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 37.28  E-value: 1.11e-03
                           10        20
                   ....*....|....*....|....*....
gi 1831507667  197 ITCKVNNVSRFQDGEKQWGNTELRYDIPW 225
Cdd:smart00061   2 LSHTFKNVSRLEEGESYFSPSEEHFNIPW 30
 
Name Accession Description Interval E-value
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
54-169 1.83e-33

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: 116.59  E-value: 1.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831507667  54 FSDVSRIEEGESRFSRFEKRFNIPWRIELQRVSGFLEIHLHrgIEIEKPDDVFTIIKADCWFNLVSTNGKNLMRQMSAVF 133
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLH--CDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVF 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1831507667 134 CRDVDMEsLKKVIRWDDMMTDYVINDSFIIEAHIEI 169
Cdd:pfam00917  79 EKPKGWG-WGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
49-138 1.54e-21

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 85.04  E-value: 1.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831507667   49 VLSQQFSDVSRIEEGESRFSRFEKRFNIPWRIELQRVSGFLEIHLHrgIEIEKPDDVFTIIKADCWFNLVSTNGKNLMRQ 128
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLH--CEKEECDSRKWSIEAEFTLKLVSQNGKSLSKK 78
                           90
                   ....*....|
gi 1831507667  129 MSAVFCRDVD 138
Cdd:smart00061  79 DKHVFEKPSG 88
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
62-168 4.61e-12

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: 60.86  E-value: 4.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831507667  62 EGESRFSRFEKRFNIPWRIELQR-----VSGFLEIHLHrgIEIEKPDDVFTIIKADCWFNLVSTN-GKNLMRQMSAVFCR 135
Cdd:cd00121    14 EGESIYSPPFEVGGYKWRIRIYPngdgeSGDYLSLYLE--LDKGESDLEKWSVRAEFTLKLVNQNgGKSLSKSFTHVFFS 91
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1831507667 136 DV-DMESLKKVIRWDDMMTDY-VINDSFIIEAHIE 168
Cdd:cd00121    92 EKgSGWGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126
MATH smart00061
meprin and TRAF homology;
197-225 1.11e-03

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 37.28  E-value: 1.11e-03
                           10        20
                   ....*....|....*....|....*....
gi 1831507667  197 ITCKVNNVSRFQDGEKQWGNTELRYDIPW 225
Cdd:smart00061   2 LSHTFKNVSRLEEGESYFSPSEEHFNIPW 30
 
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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