1CA9,2CR2,2FOP,2FOJ,1YY6,1FLL,1LB6,2F1Z


Conserved Protein Domain Family
MATH
?
cd00121: MATH 
Click on image for an interactive view with Cn3D
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.
Links
?
Statistics
?
PSSM-Id: 238068
Aligned: 352 rows
Threshold Bit Score: 35.0475
Created: 1-Nov-2000
Updated: 2-Oct-2020
Structure
?
Program:
Drawing:
Aligned Rows:
Download Cn3D
 
putative
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1:putative substrate binding site [chemical binding site]
Evidence:
  • Comment:Based on the substrate binding site of TRAFs and HAUSP. The binding site residues involved in the binding of TRAFs to TNFRs and of HAUSP to p53/MDM2 partially overlap, but are not conserved. The substrate binding pocket located in the MATH domain for members of this superfamily may be in the same location, but the specific interactions are different.
  • Structure:1CA9_A; Human TRAF2 binds TNFR-2 peptide; contacts calculated at 3.5A
    - View structure with Cn3D
  • Structure:1FLL; Human TRAF3 binds CD40 peptide; contacts calculated at 3.5A
    - View structure with Cn3D
  • Structure:2FOP; Human HAUSP N-terminal MATH domain binds MDM2 peptide; contacts calculated at 3.5A
    - View structure with Cn3D
  • Structure:2FOJ; Human HAUSP N-terminal MATh domain binds p53 peptide; contacts calculated at 3.5A
    - View structure with Cn3D
Download Cn3D for Viewing 3D StructureScroll to Sequence Alignment Display
Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection: 

Feature 1                                                      #                              
1CA9_A     43 GVFIWKISD.[13].PAIFSPAFY.[5].YKMCLRIYLNG.[7].HLSLFFVVM.[11].FNQKVTLMLLD.[4].EHVI 135 human
NP_494635  10 STYTIKAIS.[ 5].TTYCSEVKE.[3].IPWKLHVNRRT.[1].QLEVYLSCD.[ 7].VQANVEVKLRS.[7].KTAT 85  nematode
CAB02991   51 VTLVFNIYN.[ 5].GSYTSDLKE.[3].IYWCVRIQSNK.[7].RVSIYLVCN.[ 9].VTTSFGFRIIN.[3].KSRN 130 nematode
CAA91323   82 LKLEIPNFS.[ 2].RSKVSTPFQ.[4].LPWRLAAKTEK.[8].FFSVYIDCN.[ 9].CDAVVEFRLVS.[3].TIPP 160 nematode
AAK31402   21 MGYVFKVSN.[21].GRILSAPVE.[4].ATWKIATFQWK.[1].FLAVELDCK.[10].LNTNLWFKLVS.[3].RSLT 112 nematode
AAL05589  312 FTFSYLVKN.[ 7].FTYNSPTIE.[3].IPWKIAVNEKD.[1].FLILALICE.[10].IETNFELSLKS.[3].KIFT 388 nematode
CAE63875    8 FAIIYEIKN.[ 5].KTNFSVGQN.[5].LKWRISLMRNE.[1].DVTINLLCD.[12].VDVCMEVVLAS     KYPC 83  Caenorhabditis briggsae
NP_494005  26 ITHRIKNIS.[ 5].NTYTSDVED.[3].FLWHLSYIYDG.[1].FLRTTLNID.[ 9].VGMKVRHMFVT.[4].DHFH 100 nematode
CAE64147   24 MQFMMVDLD.[ 3].DKIYICQSD.[1].FNWTVHLYRGT.[5].YLVMDAYCH.[ 7].CDANIQVYIWD.[3].QLIK 95  Caenorhabditis briggsae
NP_506750   8 GSIRFEIQN.[ 5].KATEHKPVQ.[3].VEWILGAFTST.[8].HLGIHLKCN.[ 9].CDASIRFSLLR.[7].DAFS 92  nematode


Feature 1                ###                             
1CA9_A    136 DAFR.[16].IASGC.[2].FCPVSKME.[8].DAIFIKAIVD 188 human
NP_494635  86 VNFN.[ 6].NSWGW.[2].FADWEKVA.[6].DALHFKVHVQ 126 nematode
CAB02991  131 KIST.[10].TSKGT.[2].YCTWDELT.[9].GRFQIEFDLN 178 nematode
CAA91323  161 FSRQ.[ 9].NNWGF.[2].FMAWEDVN.[7].EMVTVTARVV 205 nematode
AAK31402  113 KGIK.[ 7].TTRIF.[1].FIRWDDME.[6].GWVDVEVHVE 153 nematode
AAL05589  389 KYAE.[ 6].YVYRF.[2].FVDLKDVE.[3].GRFIIEAFIK 426 nematode
CAE63875   84 KTLR.[10].GDRIY.[4].IAKWSDLN.[9].DTLRIELNVQ 133 Caenorhabditis briggsae
NP_494005 101 NSTD.[ 6].HNYGL.[4].FFEDIKNK.[4].DMVYVDVEVT 141 nematode
CAE64147   96 HHFE.[ 3].NCMSC.[2].FMKWADFV.[9].GRVIVDIHIT 136 Caenorhabditis briggsae
NP_506750  93 MEFQ.[ 6].NKIVV.[3].FKNWEEAI.[9].KHAVLEVQIT 137 nematode

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap