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Conserved domains on  [gi|17537847|ref|NP_494138|]
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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 ...
 12-125 1.67e-44

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: 150.48  E-value: 1.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847    12 FKDVSKLDEGGSYYSDIEIRHNIPWRLSISKKDGFLGVNLHCENKECSETKkWSFQTKFTMKLVAVSGKFFQRTVQHEFQ 91
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERG-WSIETEFTLKLVSSNGKSVTKTDTHVFE 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17537847    92 KPEGHGMDKLISWENMLRDYVDEDSIIIEIHADI 125
Cdd:pfam00917  80 KPKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 281-387 4.80e-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: 120.44  E-value: 4.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847   281 IKNMSNIKEGGSIFTDIQTWFNIPWRMKIEKQNGFLGLYLLHGKSQPESKKSSIEHDFQLKIVSPNGKILS------IER 354
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTktdthvFEK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 17537847   355 GGGVGWDMFLRWDVLEEDYLVNDTIIVEARVWI 387
Cdd:pfam00917  81 PKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
149-241 1.35e-20

meprin and TRAF homology;


:

Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 85.81  E-value: 1.35e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847    149 VLKHTFKNLSRILEGEYQYSDVEVHYNIPWKIELQEENGSFGFHLH---HVSEDRTKTVVVEREIKLIAANGKFHSVpKR 225
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHcekEECDSRKWSIEAEFTLKLVSQNGKSLSK-KD 79

                           90
                   ....*....|....*.
gi 17537847    226 TCTFGAKSGSVFLIYC 241
Cdd:smart00061  80 KHVFEKPSGWGFSKFI 95
 
Name Accession Description Interval E-value
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 12-125 1.67e-44

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: 150.48  E-value: 1.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847    12 FKDVSKLDEGGSYYSDIEIRHNIPWRLSISKKDGFLGVNLHCENKECSETKkWSFQTKFTMKLVAVSGKFFQRTVQHEFQ 91
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERG-WSIETEFTLKLVSSNGKSVTKTDTHVFE 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17537847    92 KPEGHGMDKLISWENMLRDYVDEDSIIIEIHADI 125
Cdd:pfam00917  80 KPKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 281-387 4.80e-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: 120.44  E-value: 4.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847   281 IKNMSNIKEGGSIFTDIQTWFNIPWRMKIEKQNGFLGLYLLHGKSQPESKKSSIEHDFQLKIVSPNGKILS------IER 354
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTktdthvFEK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 17537847   355 GGGVGWDMFLRWDVLEEDYLVNDTIIVEARVWI 387
Cdd:pfam00917  81 PKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
7-102 4.32e-31

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 114.32  E-value: 4.32e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847      7 LLTHTFKDVSKLDEGGSYYSDIEIRHNIPWRLSISKKDGFLGVNLHCENKECsETKKWSFQTKFTMKLVAVSGKFFQRTV 86
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEEC-DSRKWSIEAEFTLKLVSQNGKSLSKKD 79

                           90
                   ....*....|....*.
gi 17537847     87 QHEFQKPEGHGMDKLI 102
Cdd:smart00061  80 KHVFEKPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
276-364 4.89e-27

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 103.53  E-value: 4.89e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847    276 VLSHTIKNMSNIKEGGSIFTDIQTWFNIPWRMKIEKQNGFLGLYLLHGKSQPESKKSSIEHDFQLKIVSPNGKILS---- 351
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSkkdk 80

                           90
                   ....*....|....*
gi 17537847    352 --IERGGGVGWDMFL 364
Cdd:smart00061  81 hvFEKPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
149-241 1.35e-20

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 85.81  E-value: 1.35e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847    149 VLKHTFKNLSRILEGEYQYSDVEVHYNIPWKIELQEENGSFGFHLH---HVSEDRTKTVVVEREIKLIAANGKFHSVpKR 225
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHcekEECDSRKWSIEAEFTLKLVSQNGKSLSK-KD 79

                           90
                   ....*....|....*.
gi 17537847    226 TCTFGAKSGSVFLIYC 241
Cdd:smart00061  80 KHVFEKPSGWGFSKFI 95
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 8-122 6.69e-20

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: 85.12  E-value: 6.69e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847   8 LTHTFKDVSKL-DEGGSYYSDIEIRHNIPWRLSI-----SKKDGFLGVNLHCENKECsETKKWSFQTKFTMKLV-AVSGK 80
Cdd:cd00121   1 GKHTWKIVNFSeLEGESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGES-DLEKWSVRAEFTLKLVnQNGGK 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 17537847  81 FFQRTVQHEF--QKPEGHGMDKLISWENMLRDY-VDEDSIIIEIH 122
Cdd:cd00121  80 SLSKSFTHVFfsEKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVE 124
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 277-385 8.11e-18

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: 78.96  E-value: 8.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847 277 LSHTIKNMSNIK-EGGSIFTDIQTWFNIPWRMKI-----EKQNGFLGLYLLHGKSQPESKKSSIEHDFQLKIVSPN-GKI 349
Cdd:cd00121   1 GKHTWKIVNFSElEGESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNgGKS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 17537847 350 LSI--------ERGGGVGWDMFLRWDVLEEDY-LVNDTIIVEARV 385
Cdd:cd00121  81 LSKsfthvffsEKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVEV 125
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 154-262 1.33e-16

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: 75.37  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847   154 FKNLSRILEGEYQYSDVEVHYNIPWKIELQEENGSFGFHLH---HVSEDRTKTVVVEREIKLIAANGKFHSVpKRTCTFG 230
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHcdkEEELERGWSIETEFTLKLVSSNGKSVTK-TDTHVFE 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17537847   231 AKS--GSVFLIYCNGIEKDYVSNDSIDVEVRVKI 262
Cdd:pfam00917  80 KPKgwGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 150-261 2.53e-09

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: 55.08  E-value: 2.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847 150 LKHTFKNLSRI-LEGEYQYSDVEVHYNIPWKIELQ-----EENGSFGFHLH---HVSEDRTKTVVVEREIKLIAAN-GKF 219
Cdd:cd00121   1 GKHTWKIVNFSeLEGESIYSPPFEVGGYKWRIRIYpngdgESGDYLSLYLEldkGESDLEKWSVRAEFTLKLVNQNgGKS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17537847 220 HSVPKRTCTFGAKS---GSVFLIYCNGIEKDY-VSNDSIDVEVRVK 261
Cdd:cd00121  81 LSKSFTHVFFSEKGsgwGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126
 
Name Accession Description Interval E-value
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 12-125 1.67e-44

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: 150.48  E-value: 1.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847    12 FKDVSKLDEGGSYYSDIEIRHNIPWRLSISKKDGFLGVNLHCENKECSETKkWSFQTKFTMKLVAVSGKFFQRTVQHEFQ 91
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERG-WSIETEFTLKLVSSNGKSVTKTDTHVFE 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17537847    92 KPEGHGMDKLISWENMLRDYVDEDSIIIEIHADI 125
Cdd:pfam00917  80 KPKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 281-387 4.80e-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: 120.44  E-value: 4.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847   281 IKNMSNIKEGGSIFTDIQTWFNIPWRMKIEKQNGFLGLYLLHGKSQPESKKSSIEHDFQLKIVSPNGKILS------IER 354
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTktdthvFEK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 17537847   355 GGGVGWDMFLRWDVLEEDYLVNDTIIVEARVWI 387
Cdd:pfam00917  81 PKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
7-102 4.32e-31

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 114.32  E-value: 4.32e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847      7 LLTHTFKDVSKLDEGGSYYSDIEIRHNIPWRLSISKKDGFLGVNLHCENKECsETKKWSFQTKFTMKLVAVSGKFFQRTV 86
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEEC-DSRKWSIEAEFTLKLVSQNGKSLSKKD 79

                           90
                   ....*....|....*.
gi 17537847     87 QHEFQKPEGHGMDKLI 102
Cdd:smart00061  80 KHVFEKPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
276-364 4.89e-27

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 103.53  E-value: 4.89e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847    276 VLSHTIKNMSNIKEGGSIFTDIQTWFNIPWRMKIEKQNGFLGLYLLHGKSQPESKKSSIEHDFQLKIVSPNGKILS---- 351
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSkkdk 80

                           90
                   ....*....|....*
gi 17537847    352 --IERGGGVGWDMFL 364
Cdd:smart00061  81 hvFEKPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
149-241 1.35e-20

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 85.81  E-value: 1.35e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847    149 VLKHTFKNLSRILEGEYQYSDVEVHYNIPWKIELQEENGSFGFHLH---HVSEDRTKTVVVEREIKLIAANGKFHSVpKR 225
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHcekEECDSRKWSIEAEFTLKLVSQNGKSLSK-KD 79

                           90
                   ....*....|....*.
gi 17537847    226 TCTFGAKSGSVFLIYC 241
Cdd:smart00061  80 KHVFEKPSGWGFSKFI 95
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 8-122 6.69e-20

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: 85.12  E-value: 6.69e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847   8 LTHTFKDVSKL-DEGGSYYSDIEIRHNIPWRLSI-----SKKDGFLGVNLHCENKECsETKKWSFQTKFTMKLV-AVSGK 80
Cdd:cd00121   1 GKHTWKIVNFSeLEGESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGES-DLEKWSVRAEFTLKLVnQNGGK 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 17537847  81 FFQRTVQHEF--QKPEGHGMDKLISWENMLRDY-VDEDSIIIEIH 122
Cdd:cd00121  80 SLSKSFTHVFfsEKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVE 124
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 277-385 8.11e-18

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: 78.96  E-value: 8.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847 277 LSHTIKNMSNIK-EGGSIFTDIQTWFNIPWRMKI-----EKQNGFLGLYLLHGKSQPESKKSSIEHDFQLKIVSPN-GKI 349
Cdd:cd00121   1 GKHTWKIVNFSElEGESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNgGKS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 17537847 350 LSI--------ERGGGVGWDMFLRWDVLEEDY-LVNDTIIVEARV 385
Cdd:cd00121  81 LSKsfthvffsEKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVEV 125
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 154-262 1.33e-16

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: 75.37  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847   154 FKNLSRILEGEYQYSDVEVHYNIPWKIELQEENGSFGFHLH---HVSEDRTKTVVVEREIKLIAANGKFHSVpKRTCTFG 230
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHcdkEEELERGWSIETEFTLKLVSSNGKSVTK-TDTHVFE 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17537847   231 AKS--GSVFLIYCNGIEKDYVSNDSIDVEVRVKI 262
Cdd:pfam00917  80 KPKgwGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 150-261 2.53e-09

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: 55.08  E-value: 2.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847 150 LKHTFKNLSRI-LEGEYQYSDVEVHYNIPWKIELQ-----EENGSFGFHLH---HVSEDRTKTVVVEREIKLIAAN-GKF 219
Cdd:cd00121   1 GKHTWKIVNFSeLEGESIYSPPFEVGGYKWRIRIYpngdgESGDYLSLYLEldkGESDLEKWSVRAEFTLKLVNQNgGKS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17537847 220 HSVPKRTCTFGAKS---GSVFLIYCNGIEKDY-VSNDSIDVEVRVK 261
Cdd:cd00121  81 LSKSFTHVFFSEKGsgwGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126
MATH_HAUSP cd03772
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ...
 8-122 1.83e-04

Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, N-terminal MATH (TRAF-like) domain; composed of proteins similar to human HAUSP, an enzyme that specifically catalyzes the deubiquitylation of p53 and MDM2, hence playing an important role in the p53-MDM2 pathway. It contains an N-terminal TRAF-like domain and a C-terminal catalytic protease (C19 family) domain. The tumor suppressor p53 protein is a transcription factor that responds to many cellular stress signals and is regulated primarily through ubiquitylation and subsequent degradation. MDM2 is a RING-finger E3 ubiquitin ligase that promotes p53 ubiquitinylation. p53 and MDM2 bind to the same site in the N-terminal TRAF-like domain of HAUSP in a mutually exclusive manner. HAUSP also interacts with the Epstein-Barr nuclear antigen 1 (EBNA1) protein of the Epstein-Barr virus (EBV), which efficiently immortalizes infected cells predisposing the host to a variety of cancers. EBNA1 plays several important roles in EBV latent infection and cellular transformation. It binds the same pocket as p53 in the HAUSP TRAF-like domain. Through interactions with p53, MDM2 and EBNA1, HAUSP plays a role in cell proliferation, apoptosis and EBV-mediated immortalization.


Pssm-ID: 239741  Cd Length: 137  Bit Score: 41.28  E-value: 1.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537847   8 LTHTFKDVSKLDEggSYYSDIEIRHNIPWRLSI-------SKKDGF-LGVNLHCENKECSETkkWSFQTKFTMKLVAV-- 77
Cdd:cd03772   5 FSFTVERFSRLSE--SVLSPPCFVRNLPWKIMVmprnypdRNPHQKsVGFFLQCNAESDSTS--WSCHAQAVLRIINYkd 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 17537847  78 SGKFFQRTVQHEFQKPEGH-GMDKLISWENML---RDYVDEDSIIIEIH 122
Cdd:cd03772  81 DEPSFSRRISHLFFSKENDwGFSNFMTWSEVTdpeKGFIEDDTITLEVY 129
 
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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