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Conserved domains on  [gi|1972239294|ref|NP_001379639|]
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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 7.73e-32

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: 118.51  E-value: 7.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294  54 FSDVSRIEEGESRFSRFEKRFNIPWRIELQRVSGFLEIHLHrgIEIEKPDDVFTIIKADCWFNLVSTNGKNLMRQMSAVF 133
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLH--CDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVF 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1972239294 134 CRDVDMEsLKKVIRWDDMMTDYVINDSFIIEAHIEI 169
Cdd:pfam00917  79 EKPKGWG-WGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
332-426 1.74e-27

meprin and TRAF homology;


:

Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 105.84  E-value: 1.74e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294  332 LMSHVVRNVSNMVEGGVIFSASQEWYDIPWSISMKYINGFVELLLSCDKELNAHEAWSIETNFQLILVGANGKRLTDYFE 411
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|....*
gi 1972239294  412 HTFEKPDSIGDSKLI 426
Cdd:smart00061  81 HVFEKPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
197-289 8.99e-23

meprin and TRAF homology;


:

Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 92.36  E-value: 8.99e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294  197 ITCKVNNVSRFQDGEKQWGNTELRYDIPWRIQTKRSLDFLELYLFCD-EDDNVSKKLIQTKCTFNLVSTNGNNYRRTSKL 275
Cdd:smart00061   2 LSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEkEECDSRKWSIEAEFTLKLVSQNGKSLSKKDKH 81

                           90
                   ....*....|....
gi 1972239294  276 CFEKPGGQGISGFF 289
Cdd:smart00061  82 VFEKPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
463-520 1.37e-13

meprin and TRAF homology;


:

Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 66.55  E-value: 1.37e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1972239294  463 MSHTVKNLSNVHEGEFHFSKTEKHCDAPWRISLKKEEMCLLIYLHCDKLLSNDEHWSV 520
Cdd:smart00061   2 LSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSI 59
 
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 7.73e-32

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: 118.51  E-value: 7.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294  54 FSDVSRIEEGESRFSRFEKRFNIPWRIELQRVSGFLEIHLHrgIEIEKPDDVFTIIKADCWFNLVSTNGKNLMRQMSAVF 133
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLH--CDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVF 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1972239294 134 CRDVDMEsLKKVIRWDDMMTDYVINDSFIIEAHIEI 169
Cdd:pfam00917  79 EKPKGWG-WGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
332-426 1.74e-27

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 105.84  E-value: 1.74e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294  332 LMSHVVRNVSNMVEGGVIFSASQEWYDIPWSISMKYINGFVELLLSCDKELNAHEAWSIETNFQLILVGANGKRLTDYFE 411
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|....*
gi 1972239294  412 HTFEKPDSIGDSKLI 426
Cdd:smart00061  81 HVFEKPSGWGFSKFI 95
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 337-448 3.03e-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: 105.80  E-value: 3.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294 337 VRNVSNMVEGGVIFSASQEWYDIPWSISMKYINGFVELLLSCDKELNAHEAWSIETNFQLILVGANGKRLTDYFEHTFEK 416
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1972239294 417 PDSIGDSKLIRWEDMLDQYAVEDSLTVEARVN 448
Cdd:pfam00917  81 PKGWGWGKFISWDDLEKDYLVDDSITVEAHVK 112
MATH smart00061
meprin and TRAF homology;
197-289 8.99e-23

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 92.36  E-value: 8.99e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294  197 ITCKVNNVSRFQDGEKQWGNTELRYDIPWRIQTKRSLDFLELYLFCD-EDDNVSKKLIQTKCTFNLVSTNGNNYRRTSKL 275
Cdd:smart00061   2 LSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEkEECDSRKWSIEAEFTLKLVSQNGKSLSKKDKH 81

                           90
                   ....*....|....
gi 1972239294  276 CFEKPGGQGISGFF 289
Cdd:smart00061  82 VFEKPSGWGFSKFI 95
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 201-314 1.40e-22

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: 92.70  E-value: 1.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294 201 VNNVSRFQDGEKQWGNTELRYDIPWRIQTKRSLDFLELYLFCDEDDNVSKKL-IQTKCTFNLVSTNGNNYRRTSKLCFEK 279
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWsIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1972239294 280 PGGQGISGFFKWNDMIESFLNplEDSLIVEAHVKI 314
Cdd:pfam00917  81 PKGWGWGKFISWDDLEKDYLV--DDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
49-138 1.95e-20

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 85.81  E-value: 1.95e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294   49 VLSQQFSDVSRIEEGESRFSRFEKRFNIPWRIELQRVSGFLEIHLHrgIEIEKPDDVFTIIKADCWFNLVSTNGKNLMRQ 128
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLH--CEKEECDSRKWSIEAEFTLKLVSQNGKSLSKK 78

                           90
                   ....*....|
gi 1972239294  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 ...
 333-447 2.05e-17

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: 78.58  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294 333 MSHVVRNVSNMV-EGGVIFSASQEWYDIPWSISM-----KYINGFVELLLSCDKELNAHEAWSIETNFQLILVGAN-GKR 405
Cdd:cd00121     1 GKHTWKIVNFSElEGESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNgGKS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1972239294 406 LTDYFEHTF--EKPDSIGDSKLIRWEDMLDQYA-VEDSLTVEARV 447
Cdd:cd00121    81 LSKSFTHVFfsEKGSGWGFPKFISWDDLEDSYYlVDDSLTIEVEV 125
MATH smart00061
meprin and TRAF homology;
463-520 1.37e-13

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 66.55  E-value: 1.37e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1972239294  463 MSHTVKNLSNVHEGEFHFSKTEKHCDAPWRISLKKEEMCLLIYLHCDKLLSNDEHWSV 520
Cdd:smart00061   2 LSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSI 59
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 200-313 2.89e-13

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: 66.63  E-value: 2.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294 200 KVNNVSRfQDGEKQWGNTELRYDIPWRIQ-----TKRSLDFLELYLFC-DEDDNVSKKLIQTKCTFNLVSTNGNNY---R 270
Cdd:cd00121     6 KIVNFSE-LEGESIYSPPFEVGGYKWRIRiypngDGESGDYLSLYLELdKGESDLEKWSVRAEFTLKLVNQNGGKSlskS 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1972239294 271 RTSKLCFEKPGGQGISGFFKWNDMIESFlNPLEDSLIVEAHVK 313
Cdd:cd00121    85 FTHVFFSEKGSGWGFPKFISWDDLEDSY-YLVDDSLTIEVEVK 126
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 62-168 1.03e-11

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: 62.01  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294  62 EGESRFSRFEKRFNIPWRIELQR-----VSGFLEIHLHrgIEIEKPDDVFTIIKADCWFNLVSTN-GKNLMRQMSAVFCR 135
Cdd:cd00121    14 EGESIYSPPFEVGGYKWRIRIYPngdgeSGDYLSLYLE--LDKGESDLEKWSVRAEFTLKLVNQNgGKSLSKSFTHVFFS 91

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1972239294 136 DV-DMESLKKVIRWDDMMTDY-VINDSFIIEAHIE 168
Cdd:cd00121    92 EKgSGWGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 467-520 4.57e-06

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: 45.71  E-value: 4.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972239294 467 VKNLSNVHEGEFHFSKTEKHCDAPWRISLKKEEMCLLIYLHCDKLLSNDEHWSV 520
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSI 54
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 463-520 1.97e-05

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: 44.29  E-value: 1.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972239294 463 MSHTVKNLSN-VHEGEFHFSKTEKHCDAPWRISL-----KKEEMCLLIYLHCDKLLSNDEHWSV 520
Cdd:cd00121     1 GKHTWKIVNFsELEGESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSV 64
 
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 7.73e-32

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: 118.51  E-value: 7.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294  54 FSDVSRIEEGESRFSRFEKRFNIPWRIELQRVSGFLEIHLHrgIEIEKPDDVFTIIKADCWFNLVSTNGKNLMRQMSAVF 133
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLH--CDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVF 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1972239294 134 CRDVDMEsLKKVIRWDDMMTDYVINDSFIIEAHIEI 169
Cdd:pfam00917  79 EKPKGWG-WGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
332-426 1.74e-27

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 105.84  E-value: 1.74e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294  332 LMSHVVRNVSNMVEGGVIFSASQEWYDIPWSISMKYINGFVELLLSCDKELNAHEAWSIETNFQLILVGANGKRLTDYFE 411
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|....*
gi 1972239294  412 HTFEKPDSIGDSKLI 426
Cdd:smart00061  81 HVFEKPSGWGFSKFI 95
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 337-448 3.03e-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: 105.80  E-value: 3.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294 337 VRNVSNMVEGGVIFSASQEWYDIPWSISMKYINGFVELLLSCDKELNAHEAWSIETNFQLILVGANGKRLTDYFEHTFEK 416
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1972239294 417 PDSIGDSKLIRWEDMLDQYAVEDSLTVEARVN 448
Cdd:pfam00917  81 PKGWGWGKFISWDDLEKDYLVDDSITVEAHVK 112
MATH smart00061
meprin and TRAF homology;
197-289 8.99e-23

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 92.36  E-value: 8.99e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294  197 ITCKVNNVSRFQDGEKQWGNTELRYDIPWRIQTKRSLDFLELYLFCD-EDDNVSKKLIQTKCTFNLVSTNGNNYRRTSKL 275
Cdd:smart00061   2 LSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEkEECDSRKWSIEAEFTLKLVSQNGKSLSKKDKH 81

                           90
                   ....*....|....
gi 1972239294  276 CFEKPGGQGISGFF 289
Cdd:smart00061  82 VFEKPSGWGFSKFI 95
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 201-314 1.40e-22

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: 92.70  E-value: 1.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294 201 VNNVSRFQDGEKQWGNTELRYDIPWRIQTKRSLDFLELYLFCDEDDNVSKKL-IQTKCTFNLVSTNGNNYRRTSKLCFEK 279
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWsIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1972239294 280 PGGQGISGFFKWNDMIESFLNplEDSLIVEAHVKI 314
Cdd:pfam00917  81 PKGWGWGKFISWDDLEKDYLV--DDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
49-138 1.95e-20

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 85.81  E-value: 1.95e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294   49 VLSQQFSDVSRIEEGESRFSRFEKRFNIPWRIELQRVSGFLEIHLHrgIEIEKPDDVFTIIKADCWFNLVSTNGKNLMRQ 128
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLH--CEKEECDSRKWSIEAEFTLKLVSQNGKSLSKK 78

                           90
                   ....*....|
gi 1972239294  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 ...
 333-447 2.05e-17

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: 78.58  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294 333 MSHVVRNVSNMV-EGGVIFSASQEWYDIPWSISM-----KYINGFVELLLSCDKELNAHEAWSIETNFQLILVGAN-GKR 405
Cdd:cd00121     1 GKHTWKIVNFSElEGESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNgGKS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1972239294 406 LTDYFEHTF--EKPDSIGDSKLIRWEDMLDQYA-VEDSLTVEARV 447
Cdd:cd00121    81 LSKSFTHVFfsEKGSGWGFPKFISWDDLEDSYYlVDDSLTIEVEV 125
MATH smart00061
meprin and TRAF homology;
463-520 1.37e-13

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 66.55  E-value: 1.37e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1972239294  463 MSHTVKNLSNVHEGEFHFSKTEKHCDAPWRISLKKEEMCLLIYLHCDKLLSNDEHWSV 520
Cdd:smart00061   2 LSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSI 59
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 200-313 2.89e-13

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: 66.63  E-value: 2.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294 200 KVNNVSRfQDGEKQWGNTELRYDIPWRIQ-----TKRSLDFLELYLFC-DEDDNVSKKLIQTKCTFNLVSTNGNNY---R 270
Cdd:cd00121     6 KIVNFSE-LEGESIYSPPFEVGGYKWRIRiypngDGESGDYLSLYLELdKGESDLEKWSVRAEFTLKLVNQNGGKSlskS 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1972239294 271 RTSKLCFEKPGGQGISGFFKWNDMIESFlNPLEDSLIVEAHVK 313
Cdd:cd00121    85 FTHVFFSEKGSGWGFPKFISWDDLEDSY-YLVDDSLTIEVEVK 126
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 62-168 1.03e-11

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: 62.01  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972239294  62 EGESRFSRFEKRFNIPWRIELQR-----VSGFLEIHLHrgIEIEKPDDVFTIIKADCWFNLVSTN-GKNLMRQMSAVFCR 135
Cdd:cd00121    14 EGESIYSPPFEVGGYKWRIRIYPngdgeSGDYLSLYLE--LDKGESDLEKWSVRAEFTLKLVNQNgGKSLSKSFTHVFFS 91

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1972239294 136 DV-DMESLKKVIRWDDMMTDY-VINDSFIIEAHIE 168
Cdd:cd00121    92 EKgSGWGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 467-520 4.57e-06

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: 45.71  E-value: 4.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972239294 467 VKNLSNVHEGEFHFSKTEKHCDAPWRISLKKEEMCLLIYLHCDKLLSNDEHWSV 520
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSI 54
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 463-520 1.97e-05

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: 44.29  E-value: 1.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972239294 463 MSHTVKNLSN-VHEGEFHFSKTEKHCDAPWRISL-----KKEEMCLLIYLHCDKLLSNDEHWSV 520
Cdd:cd00121     1 GKHTWKIVNFsELEGESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSV 64
 
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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