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Conserved domains on  [gi|17532359|ref|NP_494146|]
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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 ...
 284-397 4.16e-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: 149.71  E-value: 4.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359   284 VKNMSSIEEGRIIFSDTQTRFNILWKLKIRKQDGFFELFLLCDKQLCKSRKWSIETVFQLKIVSSNGRSlVLLKTTRVFN 363
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKS-VTKTDTHVFE 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17532359   364 KATGYGWLKLIRWDSLEEKYIVDDTLTIEAHVKI 397
Cdd:pfam00917  80 KPKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 12-125 9.94e-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: 135.46  E-value: 9.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359    12 FKDISKLGEGQSYYNDNDVRYNIPWRLQIFRKAGFLGLNLRCEKEECFgERKWSFQTKFTMKLVAVSGKFFRRTVQYEFQ 91
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEEL-ERGWSIETEFTLKLVSSNGKSVTKTDTHVFE 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17532359    92 KPEGHGMNEFISWENMLRDYVDNESIIIEIHADI 125
Cdd:pfam00917  80 KPKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 154-265 3.04e-35

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: 126.22  E-value: 3.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359   154 FKNISRLVERRSDYSDLEEHFNIPWRMQIEKYNEFLATYLCCDKEMYEGRKLSIECEYEFKLISASGKLHSKQNKAIFGA 233
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 17532359   234 S-NRGIPNFISWNDMEKDYVTNGSIDVEVHVKI 265
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 ...
 284-397 4.16e-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: 149.71  E-value: 4.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359   284 VKNMSSIEEGRIIFSDTQTRFNILWKLKIRKQDGFFELFLLCDKQLCKSRKWSIETVFQLKIVSSNGRSlVLLKTTRVFN 363
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKS-VTKTDTHVFE 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17532359   364 KATGYGWLKLIRWDSLEEKYIVDDTLTIEAHVKI 397
Cdd:pfam00917  80 KPKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 12-125 9.94e-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: 135.46  E-value: 9.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359    12 FKDISKLGEGQSYYNDNDVRYNIPWRLQIFRKAGFLGLNLRCEKEECFgERKWSFQTKFTMKLVAVSGKFFRRTVQYEFQ 91
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEEL-ERGWSIETEFTLKLVSSNGKSVTKTDTHVFE 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17532359    92 KPEGHGMNEFISWENMLRDYVDNESIIIEIHADI 125
Cdd:pfam00917  80 KPKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 154-265 3.04e-35

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: 126.22  E-value: 3.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359   154 FKNISRLVERRSDYSDLEEHFNIPWRMQIEKYNEFLATYLCCDKEMYEGRKLSIECEYEFKLISASGKLHSKQNKAIFGA 233
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 17532359   234 S-NRGIPNFISWNDMEKDYVTNGSIDVEVHVKI 265
Cdd:pfam00917  81 PkGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
279-374 2.37e-30

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 112.78  E-value: 2.37e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359    279 VLSHTVKNMSSIEEGRIIFSDTQTRFNILWKLKIRKQDGFFELFLLCDKQLCKSRKWSIETVFQLKIVSSNGRSLvLLKT 358
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSL-SKKD 79

                           90
                   ....*....|....*.
gi 17532359    359 TRVFNKATGYGWLKLI 374
Cdd:smart00061  80 KHVFEKPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
7-102 4.35e-30

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 112.01  E-value: 4.35e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359      7 LLIHTFKDISKLGEGQSYYNDNDVRYNIPWRLQIFRKAGFLGLNLRCEKEECFgERKWSFQTKFTMKLVAVSGKFFRRTV 86
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECD-SRKWSIEAEFTLKLVSQNGKSLSKKD 79

                           90
                   ....*....|....*.
gi 17532359     87 QYEFQKPEGHGMNEFI 102
Cdd:smart00061  80 KHVFEKPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
149-242 9.65e-29

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 108.16  E-value: 9.65e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359    149 VLKHTFKNISRLVERRSDYSDLEEHFNIPWRMQIEKYNEFLATYLCCDKEMYEGRKLSIECEYEFKLISASGKLHSKQNK 228
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|....*
gi 17532359    229 AIFGASN-RGIPNFI 242
Cdd:smart00061  81 HVFEKPSgWGFSKFI 95
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 280-396 7.62e-24

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: 95.91  E-value: 7.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359 280 LSHTVKNMS-SIEEGRIIFSDTQTRFNILWKLKI-----RKQDGFFELFLLCDKQLCKSRKWSIETVFQLKIVSSNGRSL 353
Cdd:cd00121   1 GKHTWKIVNfSELEGESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17532359 354 VLLKTTRVFN--KATGYGWLKLIRWDSLEEKY-IVDDTLTIEAHVK 396
Cdd:cd00121  81 LSKSFTHVFFseKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 150-264 7.39e-21

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: 87.82  E-value: 7.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359 150 LKHTFKNISRLVER-RSDYSDLEEHFNIPWRMQI-----EKYNEFLATYLCCDKEMYEGRKLSIECEYEFKLISAS-GKL 222
Cdd:cd00121   1 GKHTWKIVNFSELEgESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNgGKS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17532359 223 HSKQNKAIF---GASNRGIPNFISWNDMEKDY-VTNGSIDVEVHVK 264
Cdd:cd00121  81 LSKSFTHVFfseKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 10-122 2.23e-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: 75.11  E-value: 2.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359  10 HTFKDISKL-GEGQSYYNDNDVRYNIPWRLQIFRK-----AGFLGLNLRCEKEECFGErKWSFQTKFTMKLV-AVSGKFF 82
Cdd:cd00121   3 HTWKIVNFSeLEGESIYSPPFEVGGYKWRIRIYPNgdgesGDYLSLYLELDKGESDLE-KWSVRAEFTLKLVnQNGGKSL 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 17532359  83 RRTVQYEF--QKPEGHGMNEFISWENMLRDY-VDNESIIIEIH 122
Cdd:cd00121  82 SKSFTHVFfsEKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVE 124
 
Name Accession Description Interval E-value
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 284-397 4.16e-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: 149.71  E-value: 4.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359   284 VKNMSSIEEGRIIFSDTQTRFNILWKLKIRKQDGFFELFLLCDKQLCKSRKWSIETVFQLKIVSSNGRSlVLLKTTRVFN 363
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKS-VTKTDTHVFE 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17532359   364 KATGYGWLKLIRWDSLEEKYIVDDTLTIEAHVKI 397
Cdd:pfam00917  80 KPKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 12-125 9.94e-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: 135.46  E-value: 9.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359    12 FKDISKLGEGQSYYNDNDVRYNIPWRLQIFRKAGFLGLNLRCEKEECFgERKWSFQTKFTMKLVAVSGKFFRRTVQYEFQ 91
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEEL-ERGWSIETEFTLKLVSSNGKSVTKTDTHVFE 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 17532359    92 KPEGHGMNEFISWENMLRDYVDNESIIIEIHADI 125
Cdd:pfam00917  80 KPKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 154-265 3.04e-35

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: 126.22  E-value: 3.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359   154 FKNISRLVERRSDYSDLEEHFNIPWRMQIEKYNEFLATYLCCDKEMYEGRKLSIECEYEFKLISASGKLHSKQNKAIFGA 233
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 17532359   234 S-NRGIPNFISWNDMEKDYVTNGSIDVEVHVKI 265
Cdd:pfam00917  81 PkGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
279-374 2.37e-30

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 112.78  E-value: 2.37e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359    279 VLSHTVKNMSSIEEGRIIFSDTQTRFNILWKLKIRKQDGFFELFLLCDKQLCKSRKWSIETVFQLKIVSSNGRSLvLLKT 358
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSL-SKKD 79

                           90
                   ....*....|....*.
gi 17532359    359 TRVFNKATGYGWLKLI 374
Cdd:smart00061  80 KHVFEKPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
7-102 4.35e-30

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 112.01  E-value: 4.35e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359      7 LLIHTFKDISKLGEGQSYYNDNDVRYNIPWRLQIFRKAGFLGLNLRCEKEECFgERKWSFQTKFTMKLVAVSGKFFRRTV 86
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECD-SRKWSIEAEFTLKLVSQNGKSLSKKD 79

                           90
                   ....*....|....*.
gi 17532359     87 QYEFQKPEGHGMNEFI 102
Cdd:smart00061  80 KHVFEKPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
149-242 9.65e-29

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 108.16  E-value: 9.65e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359    149 VLKHTFKNISRLVERRSDYSDLEEHFNIPWRMQIEKYNEFLATYLCCDKEMYEGRKLSIECEYEFKLISASGKLHSKQNK 228
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|....*
gi 17532359    229 AIFGASN-RGIPNFI 242
Cdd:smart00061  81 HVFEKPSgWGFSKFI 95
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 280-396 7.62e-24

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: 95.91  E-value: 7.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359 280 LSHTVKNMS-SIEEGRIIFSDTQTRFNILWKLKI-----RKQDGFFELFLLCDKQLCKSRKWSIETVFQLKIVSSNGRSL 353
Cdd:cd00121   1 GKHTWKIVNfSELEGESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17532359 354 VLLKTTRVFN--KATGYGWLKLIRWDSLEEKY-IVDDTLTIEAHVK 396
Cdd:cd00121  81 LSKSFTHVFFseKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 150-264 7.39e-21

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: 87.82  E-value: 7.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359 150 LKHTFKNISRLVER-RSDYSDLEEHFNIPWRMQI-----EKYNEFLATYLCCDKEMYEGRKLSIECEYEFKLISAS-GKL 222
Cdd:cd00121   1 GKHTWKIVNFSELEgESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNgGKS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17532359 223 HSKQNKAIF---GASNRGIPNFISWNDMEKDY-VTNGSIDVEVHVK 264
Cdd:cd00121  81 LSKSFTHVFfseKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVEVK 126
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 10-122 2.23e-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: 75.11  E-value: 2.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359  10 HTFKDISKL-GEGQSYYNDNDVRYNIPWRLQIFRK-----AGFLGLNLRCEKEECFGErKWSFQTKFTMKLV-AVSGKFF 82
Cdd:cd00121   3 HTWKIVNFSeLEGESIYSPPFEVGGYKWRIRIYPNgdgesGDYLSLYLELDKGESDLE-KWSVRAEFTLKLVnQNGGKSL 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 17532359  83 RRTVQYEF--QKPEGHGMNEFISWENMLRDY-VDNESIIIEIH 122
Cdd:cd00121  82 SKSFTHVFfsEKGSGWGFPKFISWDDLEDSYyLVDDSLTIEVE 124
MATH_HAUSP cd03772
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ...
 33-122 8.11e-03

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: 36.66  E-value: 8.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532359  33 NIPWRLQIF--------RKAGFLGLNLRCEKEECFgeRKWSFQTKFTMKLVAV--SGKFFRRTVQYEFQKPEGH-GMNEF 101
Cdd:cd03772  28 NLPWKIMVMprnypdrnPHQKSVGFFLQCNAESDS--TSWSCHAQAVLRIINYkdDEPSFSRRISHLFFSKENDwGFSNF 105

                        90       100
                ....*....|....*....|....
gi 17532359 102 ISWENML---RDYVDNESIIIEIH 122
Cdd:cd03772 106 MTWSEVTdpeKGFIEDDTITLEVY 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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