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Conserved domains on  [gi|115532514|ref|NP_001040772|]
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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 ...
 440-552 8.47e-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: 105.42  E-value: 8.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514  440 ISNISRFEDDEKQWGNTEKRYNIPWRLRAKKSFDFLEINLFCDEENIMTTNKLVEAECTFCLVSSNGNSLKQKLKLYFGR 519
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 115532514  520 PGGQGVCRLVEWSELEEDYAVNDRVVIEAHVKI 552
Cdd:pfam00917  81 PKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 296-405 8.64e-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: 105.03  E-value: 8.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514  296 ISSVLEGETLIGSEEKRFNIPWTIKMQRRSGFVVIFLYCRRKSYPHQIWTVYAKCWFKLVSANGKSLMRLQNAVFQCEDT 375
Cdd:pfam00917   4 FSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEKPKG 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 115532514  376 CELDKFTRWEDMMTDYAIDDYVTIEAHVEI 405
Cdd:pfam00917  84 WGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
570-664 6.83e-25

meprin and TRAF homology;


:

Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 99.30  E-value: 6.83e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514   570 VLSHTVRNIANMEESNFIFNITEEWYYVLWGISLKCNSGFVELQLNWENELFENESWTIQTRFQLSLIGANEKRITQYFE 649
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|....*
gi 115532514   650 HTFDKPGSSGDSKFL 664
Cdd:smart00061  81 HVFEKPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
153-247 6.92e-19

meprin and TRAF homology;


:

Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 81.96  E-value: 6.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514   153 ELTYPIQNLARFENRESQSSDVRECFKVPWSIFVEKNHDFLSCHLMYEKELCTPNDWHIQGVCTFYLKSDEGKSFCNFYE 232
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|....*
gi 115532514   233 IDLKGPGTSGDDHFI 247
Cdd:smart00061  81 HVFEKPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
23-99 8.34e-14

meprin and TRAF homology;


:

Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 67.71  E-value: 8.34e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115532514    23 LTYAAKNLSQFVAGEKQFSNEKVLFGIPWRLVVFENHDEiVGLSLSCGQCVQDSRKWSLSIEVELKLMSSSEKGFSK 99
Cdd:smart00061   2 LSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGF-LSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSK 77
 
Name Accession Description Interval E-value
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 440-552 8.47e-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: 105.42  E-value: 8.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514  440 ISNISRFEDDEKQWGNTEKRYNIPWRLRAKKSFDFLEINLFCDEENIMTTNKLVEAECTFCLVSSNGNSLKQKLKLYFGR 519
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 115532514  520 PGGQGVCRLVEWSELEEDYAVNDRVVIEAHVKI 552
Cdd:pfam00917  81 PKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 296-405 8.64e-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: 105.03  E-value: 8.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514  296 ISSVLEGETLIGSEEKRFNIPWTIKMQRRSGFVVIFLYCRRKSYPHQIWTVYAKCWFKLVSANGKSLMRLQNAVFQCEDT 375
Cdd:pfam00917   4 FSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEKPKG 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 115532514  376 CELDKFTRWEDMMTDYAIDDYVTIEAHVEI 405
Cdd:pfam00917  84 WGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
570-664 6.83e-25

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 99.30  E-value: 6.83e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514   570 VLSHTVRNIANMEESNFIFNITEEWYYVLWGISLKCNSGFVELQLNWENELFENESWTIQTRFQLSLIGANEKRITQYFE 649
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|....*
gi 115532514   650 HTFDKPGSSGDSKFL 664
Cdd:smart00061  81 HVFEKPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
439-529 1.31e-23

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 95.44  E-value: 1.31e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514   439 TISNISRFEDDEKQWGNTEKRYNIPWRLRAKKSFDFLEINLFCDEENIMTTNKLVEAECTFCLVSSNGNSLKQKLKLYFG 518
Cdd:smart00061   5 TFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDKHVFE 84

                           90
                   ....*....|.
gi 115532514   519 RPGGQGVCRLV 529
Cdd:smart00061  85 KPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
288-381 8.50e-22

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 90.44  E-value: 8.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514   288 VISQQFGGISSVLEGETLIGSEEKRFNIPWTIKMQRRSGFVVIFLYCRRKSYPHQIWTVYAKCWFKLVSANGKSLMRLQN 367
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|....
gi 115532514   368 AVFQCEDTCELDKF 381
Cdd:smart00061  81 HVFEKPSGWGFSKF 94
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 575-685 2.30e-21

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: 89.62  E-value: 2.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514  575 VRNIANMEESNFIFNITEEWYYVLWGISLKCNSGFVELQLNWENELFENESWTIQTRFQLSLIGANEKRITQYFEHTFDK 654
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 115532514  655 PGSSGDSKFLRWEDMVNNYAIEDSVRVEACV 685
Cdd:pfam00917  81 PKGWGWGKFISWDDLEKDYLVDDSITVEAHV 111
MATH smart00061
meprin and TRAF homology;
153-247 6.92e-19

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 81.96  E-value: 6.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514   153 ELTYPIQNLARFENRESQSSDVRECFKVPWSIFVEKNHDFLSCHLMYEKELCTPNDWHIQGVCTFYLKSDEGKSFCNFYE 232
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|....*
gi 115532514   233 IDLKGPGTSGDDHFI 247
Cdd:smart00061  81 HVFEKPSGWGFSKFI 95
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 158-270 6.35e-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: 74.21  E-value: 6.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514  158 IQNLARFENRESQSSDVRECFKVPWSIFVEKNHDFLSCHLMYEKELCTPNDWHIQGVCTFYLKSDEGKS--FCNFYEIDl 235
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSvtKTDTHVFE- 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 115532514  236 kGPGTSGDDHFIKWEDLIRNYSIDDSVTVIARVQI 270
Cdd:pfam00917  80 -KPKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 438-551 4.97e-15

MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane and are capable of cleaving growth factors, extracellular matrix proteins, and biologically active peptides. TRAF molecules serve as adapter proteins that link cell surface receptors of the Tumor Necrosis Factor and 1nterleukin-1/Toll-like families to downstream kinase cascades, which results in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses in the immune and inflammatory systems. Other members include the ubiquitin ligases, TRIM37 and SPOP, and the ubiquitin-specific proteases, HAUSP and Ubp21p. A large number of uncharacterized members mostly from lineage-specific expansions in C. elegans and rice contain MATH and BTB domains, similar to SPOP. The MATH domain has been shown to bind peptide/protein substrates in TRAFs and HAUSP. It is possible that the MATH domain in other members of this superfamily also interacts with various protein substrates. The TRAF domain may also be involved in the trimerization of TRAFs. Based on homology, it is postulated that the MATH domain in meprins may be involved in its tetramer assembly and that the MATH domain, in general, may take part in diverse modular arrangements defined by adjacent multimerization domains.


Pssm-ID: 238068  Cd Length: 126  Bit Score: 72.03  E-value: 4.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514 438 FTISNISRFEDdEKQWGNTEKRYNIPWRLRA-----KKSFDFLEINLFCDEENIMTTNKLVEAECTFCLVSSN-GNSLKQ 511
Cdd:cd00121    5 WKIVNFSELEG-ESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNgGKSLSK 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 115532514 512 KLKLYF--GRPGGQGVCRLVEWSELEEDYA-VNDRVVIEAHVK 551
Cdd:cd00121   84 SFTHVFfsEKGSGWGFPKFISWDDLEDSYYlVDDSLTIEVEVK 126
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 298-404 8.90e-15

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: 71.26  E-value: 8.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514 298 SVLEGETLIGSEEKRFNIPWTIKMQRR-----SGFVVIFLYCRRKSYPHQIWTVYAKCWFKLVSAN-GKSLMRLQNAVFQ 371
Cdd:cd00121   11 SELEGESIYSPPFEVGGYKWRIRIYPNgdgesGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNgGKSLSKSFTHVFF 90

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 115532514 372 CEDTCE--LDKFTRWEDMMTDYA-IDDYVTIEAHVE 404
Cdd:cd00121   91 SEKGSGwgFPKFISWDDLEDSYYlVDDSLTIEVEVK 126
MATH smart00061
meprin and TRAF homology;
23-99 8.34e-14

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 67.71  E-value: 8.34e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115532514    23 LTYAAKNLSQFVAGEKQFSNEKVLFGIPWRLVVFENHDEiVGLSLSCGQCVQDSRKWSLSIEVELKLMSSSEKGFSK 99
Cdd:smart00061   2 LSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGF-LSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSK 77
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 571-686 9.76e-14

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: 68.56  E-value: 9.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514 571 LSHTVRNIANME-ESNFIFNITEEWYYVLWGISLKCN-----SGFVELQLNWENELFENESWTIQTRFQLSLIGAN-EKR 643
Cdd:cd00121    1 GKHTWKIVNFSElEGESIYSPPFEVGGYKWRIRIYPNgdgesGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNgGKS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 115532514 644 ITQYFEHTF--DKPGSSGDSKFLRWEDMVNNYAIE-DSVRVEACVR 686
Cdd:cd00121   81 LSKSFTHVFfsEKGSGWGFPKFISWDDLEDSYYLVdDSLTIEVEVK 126
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 155-269 2.08e-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: 61.63  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514 155 TYPIQNLARFENrESQSSDVRECFKVPWSIFV-----EKNHDFLSCHLMYEKELCTPNDWHIQGVCTFYLKS-DEGKSFC 228
Cdd:cd00121    4 TWKIVNFSELEG-ESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNqNGGKSLS 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 115532514 229 NFYEIDL--KGPGTSGDDHFIKWEDLIRNYS-IDDSVTVIARVQ 269
Cdd:cd00121   83 KSFTHVFfsEKGSGWGFPKFISWDDLEDSYYlVDDSLTIEVEVK 126
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 28-139 2.86e-09

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: 55.34  E-value: 2.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514   28 KNLSQFVAGEKQFSNEKVLFGIPWRLVVFENHDEIvGLSLSCGQCVQDSRKWSLSIEVELKLMSSSEKgfsKVRRLLVKT 107
Cdd:pfam00917   2 KNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFL-GLYLHCDKEEELERGWSIETEFTLKLVSSNGK---SVTKTDTHV 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 115532514  108 LTKIE----LQLLDTEDLIENFVSAESVRIQVDVKI 139
Cdd:pfam00917  78 FEKPKgwgwGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 36-138 7.59e-06

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: 45.83  E-value: 7.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514  36 GEKQFSNEKVLFGIPWRLVVFENHDEI----VGLSLSCGQCVQDSRKWSLSIEVELKLMSSSEKGFSKVRRLLVKTLTKI 111
Cdd:cd00121   15 GESIYSPPFEVGGYKWRIRIYPNGDGEsgdyLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKSLSKSFTHVFFSEKG 94

                         90       100       110
                 ....*....|....*....|....*....|..
gi 115532514 112 E----LQLLDTEDLI-ENFVSAESVRIQVDVK 138
Cdd:cd00121   95 SgwgfPKFISWDDLEdSYYLVDDSLTIEVEVK 126
 
Name Accession Description Interval E-value
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 440-552 8.47e-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: 105.42  E-value: 8.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514  440 ISNISRFEDDEKQWGNTEKRYNIPWRLRAKKSFDFLEINLFCDEENIMTTNKLVEAECTFCLVSSNGNSLKQKLKLYFGR 519
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 115532514  520 PGGQGVCRLVEWSELEEDYAVNDRVVIEAHVKI 552
Cdd:pfam00917  81 PKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 296-405 8.64e-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: 105.03  E-value: 8.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514  296 ISSVLEGETLIGSEEKRFNIPWTIKMQRRSGFVVIFLYCRRKSYPHQIWTVYAKCWFKLVSANGKSLMRLQNAVFQCEDT 375
Cdd:pfam00917   4 FSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEKPKG 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 115532514  376 CELDKFTRWEDMMTDYAIDDYVTIEAHVEI 405
Cdd:pfam00917  84 WGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
570-664 6.83e-25

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 99.30  E-value: 6.83e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514   570 VLSHTVRNIANMEESNFIFNITEEWYYVLWGISLKCNSGFVELQLNWENELFENESWTIQTRFQLSLIGANEKRITQYFE 649
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|....*
gi 115532514   650 HTFDKPGSSGDSKFL 664
Cdd:smart00061  81 HVFEKPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
439-529 1.31e-23

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 95.44  E-value: 1.31e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514   439 TISNISRFEDDEKQWGNTEKRYNIPWRLRAKKSFDFLEINLFCDEENIMTTNKLVEAECTFCLVSSNGNSLKQKLKLYFG 518
Cdd:smart00061   5 TFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDKHVFE 84

                           90
                   ....*....|.
gi 115532514   519 RPGGQGVCRLV 529
Cdd:smart00061  85 KPSGWGFSKFI 95
MATH smart00061
meprin and TRAF homology;
288-381 8.50e-22

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 90.44  E-value: 8.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514   288 VISQQFGGISSVLEGETLIGSEEKRFNIPWTIKMQRRSGFVVIFLYCRRKSYPHQIWTVYAKCWFKLVSANGKSLMRLQN 367
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|....
gi 115532514   368 AVFQCEDTCELDKF 381
Cdd:smart00061  81 HVFEKPSGWGFSKF 94
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 575-685 2.30e-21

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: 89.62  E-value: 2.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514  575 VRNIANMEESNFIFNITEEWYYVLWGISLKCNSGFVELQLNWENELFENESWTIQTRFQLSLIGANEKRITQYFEHTFDK 654
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDTHVFEK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 115532514  655 PGSSGDSKFLRWEDMVNNYAIEDSVRVEACV 685
Cdd:pfam00917  81 PKGWGWGKFISWDDLEKDYLVDDSITVEAHV 111
MATH smart00061
meprin and TRAF homology;
153-247 6.92e-19

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 81.96  E-value: 6.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514   153 ELTYPIQNLARFENRESQSSDVRECFKVPWSIFVEKNHDFLSCHLMYEKELCTPNDWHIQGVCTFYLKSDEGKSFCNFYE 232
Cdd:smart00061   1 VLSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKKDK 80

                           90
                   ....*....|....*
gi 115532514   233 IDLKGPGTSGDDHFI 247
Cdd:smart00061  81 HVFEKPSGWGFSKFI 95
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 158-270 6.35e-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: 74.21  E-value: 6.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514  158 IQNLARFENRESQSSDVRECFKVPWSIFVEKNHDFLSCHLMYEKELCTPNDWHIQGVCTFYLKSDEGKS--FCNFYEIDl 235
Cdd:pfam00917   1 IKNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSvtKTDTHVFE- 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 115532514  236 kGPGTSGDDHFIKWEDLIRNYSIDDSVTVIARVQI 270
Cdd:pfam00917  80 -KPKGWGWGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 438-551 4.97e-15

MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane and are capable of cleaving growth factors, extracellular matrix proteins, and biologically active peptides. TRAF molecules serve as adapter proteins that link cell surface receptors of the Tumor Necrosis Factor and 1nterleukin-1/Toll-like families to downstream kinase cascades, which results in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses in the immune and inflammatory systems. Other members include the ubiquitin ligases, TRIM37 and SPOP, and the ubiquitin-specific proteases, HAUSP and Ubp21p. A large number of uncharacterized members mostly from lineage-specific expansions in C. elegans and rice contain MATH and BTB domains, similar to SPOP. The MATH domain has been shown to bind peptide/protein substrates in TRAFs and HAUSP. It is possible that the MATH domain in other members of this superfamily also interacts with various protein substrates. The TRAF domain may also be involved in the trimerization of TRAFs. Based on homology, it is postulated that the MATH domain in meprins may be involved in its tetramer assembly and that the MATH domain, in general, may take part in diverse modular arrangements defined by adjacent multimerization domains.


Pssm-ID: 238068  Cd Length: 126  Bit Score: 72.03  E-value: 4.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514 438 FTISNISRFEDdEKQWGNTEKRYNIPWRLRA-----KKSFDFLEINLFCDEENIMTTNKLVEAECTFCLVSSN-GNSLKQ 511
Cdd:cd00121    5 WKIVNFSELEG-ESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNgGKSLSK 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 115532514 512 KLKLYF--GRPGGQGVCRLVEWSELEEDYA-VNDRVVIEAHVK 551
Cdd:cd00121   84 SFTHVFfsEKGSGWGFPKFISWDDLEDSYYlVDDSLTIEVEVK 126
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 298-404 8.90e-15

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: 71.26  E-value: 8.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514 298 SVLEGETLIGSEEKRFNIPWTIKMQRR-----SGFVVIFLYCRRKSYPHQIWTVYAKCWFKLVSAN-GKSLMRLQNAVFQ 371
Cdd:cd00121   11 SELEGESIYSPPFEVGGYKWRIRIYPNgdgesGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNgGKSLSKSFTHVFF 90

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 115532514 372 CEDTCE--LDKFTRWEDMMTDYA-IDDYVTIEAHVE 404
Cdd:cd00121   91 SEKGSGwgFPKFISWDDLEDSYYlVDDSLTIEVEVK 126
MATH smart00061
meprin and TRAF homology;
23-99 8.34e-14

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 67.71  E-value: 8.34e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115532514    23 LTYAAKNLSQFVAGEKQFSNEKVLFGIPWRLVVFENHDEiVGLSLSCGQCVQDSRKWSLSIEVELKLMSSSEKGFSK 99
Cdd:smart00061   2 LSHTFKNVSRLEEGESYFSPSEEHFNIPWRLKIYRKNGF-LSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSK 77
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 571-686 9.76e-14

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: 68.56  E-value: 9.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514 571 LSHTVRNIANME-ESNFIFNITEEWYYVLWGISLKCN-----SGFVELQLNWENELFENESWTIQTRFQLSLIGAN-EKR 643
Cdd:cd00121    1 GKHTWKIVNFSElEGESIYSPPFEVGGYKWRIRIYPNgdgesGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNgGKS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 115532514 644 ITQYFEHTF--DKPGSSGDSKFLRWEDMVNNYAIE-DSVRVEACVR 686
Cdd:cd00121   81 LSKSFTHVFfsEKGSGWGFPKFISWDDLEDSYYLVdDSLTIEVEVK 126
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 155-269 2.08e-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: 61.63  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514 155 TYPIQNLARFENrESQSSDVRECFKVPWSIFV-----EKNHDFLSCHLMYEKELCTPNDWHIQGVCTFYLKS-DEGKSFC 228
Cdd:cd00121    4 TWKIVNFSELEG-ESIYSPPFEVGGYKWRIRIypngdGESGDYLSLYLELDKGESDLEKWSVRAEFTLKLVNqNGGKSLS 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 115532514 229 NFYEIDL--KGPGTSGDDHFIKWEDLIRNYS-IDDSVTVIARVQ 269
Cdd:cd00121   83 KSFTHVFfsEKGSGWGFPKFISWDDLEDSYYlVDDSLTIEVEVK 126
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 28-139 2.86e-09

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: 55.34  E-value: 2.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514   28 KNLSQFVAGEKQFSNEKVLFGIPWRLVVFENHDEIvGLSLSCGQCVQDSRKWSLSIEVELKLMSSSEKgfsKVRRLLVKT 107
Cdd:pfam00917   2 KNFSKIKEGESYYSPVEERFNIPWRLQIYRKGGFL-GLYLHCDKEEELERGWSIETEFTLKLVSSNGK---SVTKTDTHV 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 115532514  108 LTKIE----LQLLDTEDLIENFVSAESVRIQVDVKI 139
Cdd:pfam00917  78 FEKPKgwgwGKFISWDDLEKDYLVDDSITVEAHVKI 113
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 36-138 7.59e-06

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: 45.83  E-value: 7.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532514  36 GEKQFSNEKVLFGIPWRLVVFENHDEI----VGLSLSCGQCVQDSRKWSLSIEVELKLMSSSEKGFSKVRRLLVKTLTKI 111
Cdd:cd00121   15 GESIYSPPFEVGGYKWRIRIYPNGDGEsgdyLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKSLSKSFTHVFFSEKG 94

                         90       100       110
                 ....*....|....*....|....*....|..
gi 115532514 112 E----LQLLDTEDLI-ENFVSAESVRIQVDVK 138
Cdd:cd00121   95 SgwgfPKFISWDDLEdSYYLVDDSLTIEVEVK 126
 
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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