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Conserved domains on  [gi|42568927|ref|NP_178503|]
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TRAF-like family 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 ...
 123-252 8.45e-18

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


:

Pssm-ID: 238068  Cd Length: 126  Bit Score: 78.96  E-value: 8.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568927 123 ILTITNFSEIIGreEPYESSVFEAyFEHKWRLILYVNGNQNDGgsNHISLYLRSEETDHLTYDGSINFVLKLFVYNGKQD 202
Cdd:cd00121   4 TWKIVNFSELEG--ESIYSPPFEV-GGYKWRIRIYPNGDGESG--DYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGG 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 42568927 203 KYLTVTDGiQKRYNYKNKEWGYGKLIPLSTFLDtsQGYLEQDTASFGAEI 252
Cdd:cd00121  79 KSLSKSFT-HVFFSEKGSGWGFPKFISWDDLED--SYYLVDDSLTIEVEV 125
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 275-400 2.37e-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: 2.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568927 275 FTWKILHFSTLEDIVYYSDDFLVEDRYWRLGVNPKGTGDGRSQaIKIFLYAQGHKPNAVVSSTWGAVNLRVKNQRSSNHS 354
Cdd:cd00121   3 HTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGESGDY-LSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKSL 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 42568927 355 QIYSAALYPIRNDYGVGVNTVLSLAELNDavKEYLVNDSIIFEAEM 400
Cdd:cd00121  82 SKSFTHVFFSEKGSGWGFPKFISWDDLED--SYYLVDDSLTIEVEV 125
 
Name Accession Description Interval E-value
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 123-252 8.45e-18

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


Pssm-ID: 238068  Cd Length: 126  Bit Score: 78.96  E-value: 8.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568927 123 ILTITNFSEIIGreEPYESSVFEAyFEHKWRLILYVNGNQNDGgsNHISLYLRSEETDHLTYDGSINFVLKLFVYNGKQD 202
Cdd:cd00121   4 TWKIVNFSELEG--ESIYSPPFEV-GGYKWRIRIYPNGDGESG--DYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGG 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 42568927 203 KYLTVTDGiQKRYNYKNKEWGYGKLIPLSTFLDtsQGYLEQDTASFGAEI 252
Cdd:cd00121  79 KSLSKSFT-HVFFSEKGSGWGFPKFISWDDLED--SYYLVDDSLTIEVEV 125
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 275-400 2.37e-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: 2.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568927 275 FTWKILHFSTLEDIVYYSDDFLVEDRYWRLGVNPKGTGDGRSQaIKIFLYAQGHKPNAVVSSTWGAVNLRVKNQRSSNHS 354
Cdd:cd00121   3 HTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGESGDY-LSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKSL 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 42568927 355 QIYSAALYPIRNDYGVGVNTVLSLAELNDavKEYLVNDSIIFEAEM 400
Cdd:cd00121  82 SKSFTHVFFSEKGSGWGFPKFISWDDLED--SYYLVDDSLTIEVEV 125
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 126-254 1.20e-11

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: 61.12  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568927   126 ITNFSEIIGREEPYESsvFEAYFEHKWRLILYVNGNqndggsnHISLYLRSEETDHLTYDGSIN--FVLKLFVYNGKqdk 203
Cdd:pfam00917   1 IKNFSKIKEGESYYSP--VEERFNIPWRLQIYRKGG-------FLGLYLHCDKEEELERGWSIEteFTLKLVSSNGK--- 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 42568927   204 ylTVTDGIQKRYNyKNKEWGYGKLIPLSTFLDtsqGYLEQDTASFGAEIFL 254
Cdd:pfam00917  69 --SVTKTDTHVFE-KPKGWGWGKFISWDDLEK---DYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
274-359 5.57e-08

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 50.38  E-value: 5.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568927    274 VFTWKILHFSTLED-IVYYSDDFLVEDRYWRLGVNPKGTGDGrsqaikIFLYAQGHKPNAVVSSTWGAVNLRVKNQRSSN 352
Cdd:smart00061   1 VLSHTFKNVSRLEEgESYFSPSEEHFNIPWRLKIYRKNGFLS------LYLHCEKEECDSRKWSIEAEFTLKLVSQNGKS 74


                   ....*..
gi 42568927    353 HSQIYSA 359
Cdd:smart00061  75 LSKKDKH 81
MATH smart00061
meprin and TRAF homology;
125-228 5.96e-06

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 44.60  E-value: 5.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568927    125 TITNFSEIiGREEPYESSVFEaYFEHKWRLILYVNGNqndggsnHISLYLRSEETDHLTYDGSIN--FVLKLFVYNGkqd 202
Cdd:smart00061   5 TFKNVSRL-EEGESYFSPSEE-HFNIPWRLKIYRKNG-------FLSLYLHCEKEECDSRKWSIEaeFTLKLVSQNG--- 72

                           90       100
                   ....*....|....*....|....*.
gi 42568927    203 KYLTVTDgiqKRYNYKNKEWGYGKLI 228
Cdd:smart00061  73 KSLSKKD---KHVFEKPSGWGFSKFI 95
 
Name Accession Description Interval E-value
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 123-252 8.45e-18

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


Pssm-ID: 238068  Cd Length: 126  Bit Score: 78.96  E-value: 8.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568927 123 ILTITNFSEIIGreEPYESSVFEAyFEHKWRLILYVNGNQNDGgsNHISLYLRSEETDHLTYDGSINFVLKLFVYNGKQD 202
Cdd:cd00121   4 TWKIVNFSELEG--ESIYSPPFEV-GGYKWRIRIYPNGDGESG--DYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGG 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 42568927 203 KYLTVTDGiQKRYNYKNKEWGYGKLIPLSTFLDtsQGYLEQDTASFGAEI 252
Cdd:cd00121  79 KSLSKSFT-HVFFSEKGSGWGFPKFISWDDLED--SYYLVDDSLTIEVEV 125
MATH cd00121
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ...
 275-400 2.37e-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: 2.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568927 275 FTWKILHFSTLEDIVYYSDDFLVEDRYWRLGVNPKGTGDGRSQaIKIFLYAQGHKPNAVVSSTWGAVNLRVKNQRSSNHS 354
Cdd:cd00121   3 HTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGESGDY-LSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKSL 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 42568927 355 QIYSAALYPIRNDYGVGVNTVLSLAELNDavKEYLVNDSIIFEAEM 400
Cdd:cd00121  82 SKSFTHVFFSEKGSGWGFPKFISWDDLED--SYYLVDDSLTIEVEV 125
MATH pfam00917
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ...
 126-254 1.20e-11

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: 61.12  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568927   126 ITNFSEIIGREEPYESsvFEAYFEHKWRLILYVNGNqndggsnHISLYLRSEETDHLTYDGSIN--FVLKLFVYNGKqdk 203
Cdd:pfam00917   1 IKNFSKIKEGESYYSP--VEERFNIPWRLQIYRKGG-------FLGLYLHCDKEEELERGWSIEteFTLKLVSSNGK--- 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 42568927   204 ylTVTDGIQKRYNyKNKEWGYGKLIPLSTFLDtsqGYLEQDTASFGAEIFL 254
Cdd:pfam00917  69 --SVTKTDTHVFE-KPKGWGWGKFISWDDLEK---DYLVDDSITVEAHVKI 113
MATH smart00061
meprin and TRAF homology;
274-359 5.57e-08

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 50.38  E-value: 5.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568927    274 VFTWKILHFSTLED-IVYYSDDFLVEDRYWRLGVNPKGTGDGrsqaikIFLYAQGHKPNAVVSSTWGAVNLRVKNQRSSN 352
Cdd:smart00061   1 VLSHTFKNVSRLEEgESYFSPSEEHFNIPWRLKIYRKNGFLS------LYLHCEKEECDSRKWSIEAEFTLKLVSQNGKS 74


                   ....*..
gi 42568927    353 HSQIYSA 359
Cdd:smart00061  75 LSKKDKH 81
MATH smart00061
meprin and TRAF homology;
125-228 5.96e-06

meprin and TRAF homology;


Pssm-ID: 214496 [Multi-domain]  Cd Length: 95  Bit Score: 44.60  E-value: 5.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568927    125 TITNFSEIiGREEPYESSVFEaYFEHKWRLILYVNGNqndggsnHISLYLRSEETDHLTYDGSIN--FVLKLFVYNGkqd 202
Cdd:smart00061   5 TFKNVSRL-EEGESYFSPSEE-HFNIPWRLKIYRKNG-------FLSLYLHCEKEECDSRKWSIEaeFTLKLVSQNG--- 72

                           90       100
                   ....*....|....*....|....*.
gi 42568927    203 KYLTVTDgiqKRYNYKNKEWGYGKLI 228
Cdd:smart00061  73 KSLSKKD---KHVFEKPSGWGFSKFI 95
MATH_Ubp21p cd03775
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ...
 275-340 2.39e-04

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: 40.80  E-value: 2.39e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42568927 275 FTWKILHFSTLEDiVYYSDDFLVEDRYWRLGVNPKGTGDGRSqaIKIFL-YAQGHKPNAVVSSTWGA 340
Cdd:cd03775   3 FTWRIKNWSELEK-KVHSPKFKCGGFEWRILLFPQGNSQTGG--VSIYLePHPEEEEKAPLDEDWSV 66
MATH_SPOP cd03774
Speckle-type POZ protein (SPOP) family, MATH domain; composed of proteins with similarity to ...
 125-244 6.71e-04

Speckle-type POZ protein (SPOP) family, MATH domain; composed of proteins with similarity to human SPOP. SPOP was isolated as a novel antigen recognized by serum from a scleroderma patient, whose overexpression in COS cells results in a discrete speckled pattern in the nuclei. It contains an N-terminal MATH domain and a C-terminal BTB (also called POZ) domain. Together with Cul3, SPOP constitutes an ubiquitin E3 ligase which is able to ubiquitinate the PcG protein BMI1, the variant histone macroH2A1 and the death domain-associated protein Daxx. Therefore, SPOP may be involved in the regulation of these proteins and may play a role in transcriptional regulation, apoptosis and X-chromosome inactivation. Cul3 binds to the BTB domain of SPOP whereas Daxx and the macroH2A1 nonhistone region have been shown to bind to the MATH domain. Both MATH and BTB domains are necessary for the nuclear speckled accumulation of SPOP. There are many proteins, mostly uncharacterized, containing both MATH and BTB domains from C. elegans and plants which are excluded from this family.


Pssm-ID: 239743  Cd Length: 139  Bit Score: 39.84  E-value: 6.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568927 125 TITNFSEIIGR-EEPYESSVF--EAYFEHKWRLILYVNGnQNDGGSNHISLYLRSEETDHltydGSINFVLKLFVYNGKQ 201
Cdd:cd03774  10 TISNFSFCREEmGEVIKSSTFssGANDKLKWCLRVNPKG-LDEESKDYLSLYLLLVSCPK----SEVRAKFKFSILNAKG 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 42568927 202 DKYLTVTDGIQKRYnYKNKEWGYGKLIPLSTFLDTSQGYLEQD 244
Cdd:cd03774  85 EETKAMESQRAYRF-VQGKDWGFKKFIRRDFLLDEANGLLPDD 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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