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Conserved domains on  [gi|145335077|ref|NP_171926|]
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TRAF-like superfamily protein [Arabidopsis thaliana]

Protein Classification

MATH domain-containing protein( domain architecture ID 10062363)

MATH (meprin and TRAF-C homology) domain-containing protein similar to Arabidopsis thaliana MATH domain and coiled-coil domain-containing proteins

Gene Ontology:  GO:0005515
PubMed:  17633013|12387856

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
68-191 8.71e-36

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: 132.12  E-value: 8.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   68 GQYTWKIPKFSEITKREHRSNVFEAGGYKWYILIYPQGCDVC-NHLSLFLCVANYDKLLPGWSQFAQFTISVLSQDLKKS 146
Cdd:cd00121     1 GKHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGESgDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 145335077  147 -KFSDTLHRFWKKEHDWGWKKFMELPKLKDGFIDESGCLTIEAKVQ 191
Cdd:cd00121    81 lSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEVK 126
2A1904 super family cl36772
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
638-836 2.55e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


The actual alignment was detected with superfamily member TIGR00927:

Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.90  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   638 PSTLGTDPKGQNYSSEASnVGESDWVVVSHIQEPEGSRnRIPVGRERKTVQSIVNSVDMDRPKEKSTAVLSSPRNVAKNP 717
Cdd:TIGR00927  204 PSTFMTMPRSHGITPRTT-VKDSEITATYKMLETNPSK-RTAGKTTPTPLKGMTDNTPTFLTREVETDLLTSPRSVVEKN 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   718 SPLTQTKPEKKSISTADGI--------PNRKVLATGPPSSS-QVVL-------PSDIQSQTVG--LRADMQKLSAP--KQ 777
Cdd:TIGR00927  282 TLTTPRRVESNSSTNHWGLvgknnlttPQGTVLEHTPATSEgQVTIsimtgssPAETKASTAAwkIRNPLSRTSAPavRI 361
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   778 PPAT---TISRPSSAPIIPA-----------------MRPSPI--TVSSSVQTTTSLPRSVSSAGRLGPD--PSLHNQQT 833
Cdd:TIGR00927  362 ASATfrgLEKNPSTAPSTPAtprvravlttqvhhcvvVKPAPAvpTTPSPSLTTALFPEAPSPSPSALPPgqPDLHPKAE 441

                   ...
gi 145335077   834 YTP 836
Cdd:TIGR00927  442 YPP 444
 
Name Accession Description Interval E-value
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
68-191 8.71e-36

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: 132.12  E-value: 8.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   68 GQYTWKIPKFSEITKREHRSNVFEAGGYKWYILIYPQGCDVC-NHLSLFLCVANYDKLLPGWSQFAQFTISVLSQDLKKS 146
Cdd:cd00121     1 GKHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGESgDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 145335077  147 -KFSDTLHRFWKKEHDWGWKKFMELPKLKDGFIDESGCLTIEAKVQ 191
Cdd:cd00121    81 lSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEVK 126
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
74-192 4.06e-28

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: 109.65  E-value: 4.06e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077    74 IPKFSEITKREHR-SNVFEAGGYKWYILIYPQGCdvcnHLSLFLCVANYDKLLPGWSQFAQFTISVLSQDLKKSKFSDTl 152
Cdd:pfam00917    1 IKNFSKIKEGESYySPVEERFNIPWRLQIYRKGG----FLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDT- 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 145335077   153 HRFWkKEHDWGWKKFMELPKLKDGFIDEsGCLTIEAKVQV 192
Cdd:pfam00917   76 HVFE-KPKGWGWGKFISWDDLEKDYLVD-DSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
72-168 4.92e-19

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 83.12  E-value: 4.92e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077     72 WKIPKFSEITKREHR----SNVFEAGGYKWYILIYPQGcdvcNHLSLFLCVANYDKLLPGWSQFAQFTISVLSQDLKKSK 147
Cdd:smart00061    1 VLSHTFKNVSRLEEGesyfSPSEEHFNIPWRLKIYRKN----GFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLS 76
                            90       100
                    ....*....|....*....|.
gi 145335077    148 FSDTlHRFWKKEhDWGWKKFM 168
Cdd:smart00061   77 KKDK-HVFEKPS-GWGFSKFI 95
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
66-195 1.05e-09

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 62.97  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   66 LYGQYTWKIPKFSEITKREHrSNVFEAGGYKWYILIYPQGCDVCNhLSLFLCVANYDKLLPG---WSQFAQFTISVLS-Q 141
Cdd:COG5077    37 LEMSFTWKVKRWSELAKKVE-SPPFSVGGHTWKIILFPQGNNQCN-VSVYLEYEPQELEETGgkyYDCCAQFAFDISNpK 114
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145335077  142 DLKKSKFSDTLHRFWKKEHDWGWKKFMELPKLKDGFID-----ESGCLTIEAKVQVIRE 195
Cdd:COG5077   115 YPTIEYINKSHHRFSMESTDWGFTNFIDLNKLIEPSPGrppflEEGTLVITVYVRVLKD 173
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
638-836 2.55e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.90  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   638 PSTLGTDPKGQNYSSEASnVGESDWVVVSHIQEPEGSRnRIPVGRERKTVQSIVNSVDMDRPKEKSTAVLSSPRNVAKNP 717
Cdd:TIGR00927  204 PSTFMTMPRSHGITPRTT-VKDSEITATYKMLETNPSK-RTAGKTTPTPLKGMTDNTPTFLTREVETDLLTSPRSVVEKN 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   718 SPLTQTKPEKKSISTADGI--------PNRKVLATGPPSSS-QVVL-------PSDIQSQTVG--LRADMQKLSAP--KQ 777
Cdd:TIGR00927  282 TLTTPRRVESNSSTNHWGLvgknnlttPQGTVLEHTPATSEgQVTIsimtgssPAETKASTAAwkIRNPLSRTSAPavRI 361
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   778 PPAT---TISRPSSAPIIPA-----------------MRPSPI--TVSSSVQTTTSLPRSVSSAGRLGPD--PSLHNQQT 833
Cdd:TIGR00927  362 ASATfrgLEKNPSTAPSTPAtprvravlttqvhhcvvVKPAPAvpTTPSPSLTTALFPEAPSPSPSALPPgqPDLHPKAE 441

                   ...
gi 145335077   834 YTP 836
Cdd:TIGR00927  442 YPP 444
 
Name Accession Description Interval E-value
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
68-191 8.71e-36

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: 132.12  E-value: 8.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   68 GQYTWKIPKFSEITKREHRSNVFEAGGYKWYILIYPQGCDVC-NHLSLFLCVANYDKLLPGWSQFAQFTISVLSQDLKKS 146
Cdd:cd00121     1 GKHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGESgDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 145335077  147 -KFSDTLHRFWKKEHDWGWKKFMELPKLKDGFIDESGCLTIEAKVQ 191
Cdd:cd00121    81 lSKSFTHVFFSEKGSGWGFPKFISWDDLEDSYYLVDDSLTIEVEVK 126
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
74-192 4.06e-28

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: 109.65  E-value: 4.06e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077    74 IPKFSEITKREHR-SNVFEAGGYKWYILIYPQGCdvcnHLSLFLCVANYDKLLPGWSQFAQFTISVLSQDLKKSKFSDTl 152
Cdd:pfam00917    1 IKNFSKIKEGESYySPVEERFNIPWRLQIYRKGG----FLGLYLHCDKEEELERGWSIETEFTLKLVSSNGKSVTKTDT- 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 145335077   153 HRFWkKEHDWGWKKFMELPKLKDGFIDEsGCLTIEAKVQV 192
Cdd:pfam00917   76 HVFE-KPKGWGWGKFISWDDLEKDYLVD-DSITVEAHVKI 113
MATH_Ubp21p cd03775
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ...
68-174 3.27e-19

Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with similarity to Ubp21p of fission yeast. Ubp21p is a deubiquitinating enzyme that may be involved in the regulation of the protein kinase Prp4p, which controls the formation of active spliceosomes. Members of this family are similar to human HAUSP (Herpesvirus-associated ubiquitin-specific protease) in that they contain an N-terminal MATH domain and a C-terminal catalytic protease (C19 family) domain. HAUSP is also an ubiquitin-specific protease that specifically catalyzes the deubiquitylation of p53 and MDM2. The MATH domain of HAUSP contains the binding site for p53 and MDM2. Similarly, the MATH domain of members in this family may be involved in substrate binding.


Pssm-ID: 239744  Cd Length: 134  Bit Score: 84.72  E-value: 3.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   68 GQYTWKIPKFSEITKREHrSNVFEAGGYKWYILIYPQGCDVCNHLSLFL----CVANYDKLLPGWSQFAQFTIsVLSQDL 143
Cdd:cd03775     1 QSFTWRIKNWSELEKKVH-SPKFKCGGFEWRILLFPQGNSQTGGVSIYLephpEEEEKAPLDEDWSVCAQFAL-VISNPG 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 145335077  144 KKSKF--SDTLHRFWKKEHDWGWKKFMELPKLK 174
Cdd:cd03775    79 DPSIQlsNVAHHRFNAEDKDWGFTRFIELRKLA 111
MATH smart00061
meprin and TRAF homology;
72-168 4.92e-19

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 83.12  E-value: 4.92e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077     72 WKIPKFSEITKREHR----SNVFEAGGYKWYILIYPQGcdvcNHLSLFLCVANYDKLLPGWSQFAQFTISVLSQDLKKSK 147
Cdd:smart00061    1 VLSHTFKNVSRLEEGesyfSPSEEHFNIPWRLKIYRKN----GFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLS 76
                            90       100
                    ....*....|....*....|.
gi 145335077    148 FSDTlHRFWKKEhDWGWKKFM 168
Cdd:smart00061   77 KKDK-HVFEKPS-GWGFSKFI 95
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
66-195 1.05e-09

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 62.97  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   66 LYGQYTWKIPKFSEITKREHrSNVFEAGGYKWYILIYPQGCDVCNhLSLFLCVANYDKLLPG---WSQFAQFTISVLS-Q 141
Cdd:COG5077    37 LEMSFTWKVKRWSELAKKVE-SPPFSVGGHTWKIILFPQGNNQCN-VSVYLEYEPQELEETGgkyYDCCAQFAFDISNpK 114
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145335077  142 DLKKSKFSDTLHRFWKKEHDWGWKKFMELPKLKDGFID-----ESGCLTIEAKVQVIRE 195
Cdd:COG5077   115 YPTIEYINKSHHRFSMESTDWGFTNFIDLNKLIEPSPGrppflEEGTLVITVYVRVLKD 173
MATH_TRAF_C cd00270
Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF domain, C-terminal ...
68-191 1.20e-05

Tumor Necrosis Factor Receptor (TNFR)-Associated Factor (TRAF) family, TRAF domain, C-terminal MATH subdomain; TRAF molecules serve as adapter proteins that link cell surface TNFRs and receptors of the interleukin-1/Toll-like family to downstream kinase signaling 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. There are at least six mammalian and three Drosophila proteins containing TRAF domains. The mammalian TRAFs display varying expression profiles, indicating independent and cell type-specific regulation. They display distinct, as well as overlapping functions and interactions with receptors. Most TRAFs, except TRAF1, share N-terminal homology and contain a RING domain, multiple zinc finger domains, and a TRAF domain. TRAFs form homo- and heterotrimers through its TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded beta-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors.


Pssm-ID: 238168  Cd Length: 149  Bit Score: 46.45  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   68 GQYTWKIPKFSEitKREHRSN-----VFEAG------GYKWYILIYPQG----CDvcNHLSLFLCVAN--YDKLLPgWSQ 130
Cdd:cd00270     1 GVLIWKIKDYSR--KLQEAVAgsntvLYSPPfytsryGYKLCLRLYLNGdgtgKG--THLSLFVHVMKgeYDALLE-WPF 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145335077  131 FAQFTISVLSQ--DLKKSKFSDTLH------RFWKKEHD-----WGWKKFMELPKLKD-GFIDEsGCLTIEAKVQ 191
Cdd:cd00270    76 RGKITLTLLDQsdDSKRKHITETFMpdpnssAFQRPPTGennigFGYPEFVPLEKLESrGYVKD-DTLFIKVEVD 149
MATH_HAUSP cd03772
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ...
94-191 1.42e-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: 42.83  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   94 GYKWYILIYPQGCDVCNH----LSLFL-CvaNYDKLLPGWSQFAQFTISVLSQDLKKSKFS-DTLHRFWKKEHDWGWKKF 167
Cdd:cd03772    28 NLPWKIMVMPRNYPDRNPhqksVGFFLqC--NAESDSTSWSCHAQAVLRIINYKDDEPSFSrRISHLFFSKENDWGFSNF 105
                          90       100
                  ....*....|....*....|....*..
gi 145335077  168 MELPKLKD---GFIDESGcLTIEAKVQ 191
Cdd:cd03772   106 MTWSEVTDpekGFIEDDT-ITLEVYVQ 131
MATH_TRIM37 cd03773
Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal ...
71-181 6.39e-04

Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal protein and is a member of the tripartite motif (TRIM) protein subfamily, also known as the RING-B-box-coiled-coil (RBCC) subfamily of zinc-finger proteins. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction and hepatomegaly. TRIM37, similar to other TRIMs, contains a cysteine-rich, zinc-binding RING-finger domain followed by another cysteine-rich zinc-binding domain, the B-box, and a coiled-coil domain. TRIM37 is autoubiquitinated in a RING domain-dependent manner, indicating that it functions as an ubiquitin E3 ligase. In addition to the tripartite motif, TRIM37 also contains a MATH domain C-terminal to the coiled-coil domain. The MATH domain of TRIM37 has been shown to interact with the TRAF domain of six known TRAFs in vitro, however, it is unclear whether this is physiologically relevant. Eleven TRIM37 mutations have been associated with Mulibrey nanism so far. One mutation, Gly322Val, is located in the MATH domain and is the only mutation that does not affect the length of the protein. It results in the incorrect subcellular localization of TRIM37.


Pssm-ID: 239742  Cd Length: 132  Bit Score: 40.86  E-value: 6.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   71 TWKIPKFSEITKREH--RSNVFEAGGYKWYILIYPQGCDVC--NHLSLFLCVANYdklLPGWSQFaQFTISVLSQ-DLKK 145
Cdd:cd03773     8 TFTLENFSTLRQSADpvYSDPLNVDGLCWRLKVYPDGNGEVrgNFLSVFLELCSG---LGEASKY-EYRVEMVHQaNPTK 83
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 145335077  146 SKFSDTLHRFWKKEhDWGWKKFMELPKLKD-GFIDES 181
Cdd:cd03773    84 NIKREFASDFEVGE-CWGYNRFFRLDLLINeGYLLPE 119
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
638-836 2.55e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.90  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   638 PSTLGTDPKGQNYSSEASnVGESDWVVVSHIQEPEGSRnRIPVGRERKTVQSIVNSVDMDRPKEKSTAVLSSPRNVAKNP 717
Cdd:TIGR00927  204 PSTFMTMPRSHGITPRTT-VKDSEITATYKMLETNPSK-RTAGKTTPTPLKGMTDNTPTFLTREVETDLLTSPRSVVEKN 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   718 SPLTQTKPEKKSISTADGI--------PNRKVLATGPPSSS-QVVL-------PSDIQSQTVG--LRADMQKLSAP--KQ 777
Cdd:TIGR00927  282 TLTTPRRVESNSSTNHWGLvgknnlttPQGTVLEHTPATSEgQVTIsimtgssPAETKASTAAwkIRNPLSRTSAPavRI 361
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145335077   778 PPAT---TISRPSSAPIIPA-----------------MRPSPI--TVSSSVQTTTSLPRSVSSAGRLGPD--PSLHNQQT 833
Cdd:TIGR00927  362 ASATfrgLEKNPSTAPSTPAtprvravlttqvhhcvvVKPAPAvpTTPSPSLTTALFPEAPSPSPSALPPgqPDLHPKAE 441

                   ...
gi 145335077   834 YTP 836
Cdd:TIGR00927  442 YPP 444
 
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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