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Conserved domains on  [gi|1397668432|ref|XP_025086090|]
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LOW QUALITY PROTEIN: mothers against decapentaplegic homolog 1-like [Pomacea canaliculata]

Protein Classification

mothers against decapentaplegic homolog( domain architecture ID 10180328)

mothers against decapentaplegic homolog such as SMAD1, SMAD5 and SMAD9 (also known as SMAD8); all closely related receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in bone morphogenetic proteins (BMP) signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway

CATH:  2.60.200.10
Gene Ontology:  GO:0071141|GO:0000981|GO:0046872
PubMed:  8799132
SCOP:  4002600

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MH2_SMAD_1_5_9 cd10497
C-terminal Mad Homology 2 (MH2) domain in SMAD1, SMAD5 and SMAD9; The MH2 domain is located at ...
 258-458 2.16e-162

C-terminal Mad Homology 2 (MH2) domain in SMAD1, SMAD5 and SMAD9; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD1, SMAD5 and SMAD9 (also known as SMAD8), are receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in BMP signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway.


:

Pssm-ID: 199822  Cd Length: 201  Bit Score: 456.26  E-value: 2.16e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 258 YQEPQYWCSIVYYELNNRVGEAFHASHTSIVTDGFCDPSNNADRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVF 337
Cdd:cd10497     1 YQEPKYWCSIAYYELNNRVGEAFHASSTSIIVDGFTDPSNNSDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 338 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAALLSQSVNHGFEAVYDLTKMCTIRMSFVKGWGAEY 417
Cdd:cd10497    81 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1397668432 418 HRQDVTSTPCWIEIHLNGPLQWLDKVLTQMGSPHNPISSVS 458
Cdd:cd10497   161 HRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS 201
MH1_SMAD_1_5_9 cd10490
N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The ...
 11-134 9.22e-89

N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 domain is found in SMAD1, SMAD5 and SMAD9, all closely related receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in bone morphogenetic proteins (BMP) signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway.


:

Pssm-ID: 199814  Cd Length: 124  Bit Score: 265.91  E-value: 9.22e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  11 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEDLEKALSCPGRPSKCVTIPRSLDGRLQVSHRKGLPHVIY 90
Cdd:cd10490     1 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEELEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1397668432  91 CRVWRWPDLQSHHELKPLECCEYPFSAKQKEVCINPYHYKRVES 134
Cdd:cd10490    81 CRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVES 124
PABP-1234 super family cl31127
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 150-260 1.07e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


The actual alignment was detected with superfamily member TIGR01628:

Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 44.80  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 150 GTMPAFQSVPEPNMphnvtYPFQQqhsPNPPSSGPGSPFGLPADTPPPAYQAQDDSQQNSMGMSQGNGMPRPPPSQNGPQ 229
Cdd:TIGR01628 402 GQGPQQQFNGQPLG-----WPRMS---MMPTPMGPGGPLRPNGLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPL 473

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1397668432 230 PMDTSMPPTIPIPKQLSGRGIVDLQPVTYQE 260
Cdd:TIGR01628 474 SQDLPQPQSTASQGGQNKKLAQVLASATPQM 504
 
Name Accession Description Interval E-value
MH2_SMAD_1_5_9 cd10497
C-terminal Mad Homology 2 (MH2) domain in SMAD1, SMAD5 and SMAD9; The MH2 domain is located at ...
 258-458 2.16e-162

C-terminal Mad Homology 2 (MH2) domain in SMAD1, SMAD5 and SMAD9; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD1, SMAD5 and SMAD9 (also known as SMAD8), are receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in BMP signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway.


Pssm-ID: 199822  Cd Length: 201  Bit Score: 456.26  E-value: 2.16e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 258 YQEPQYWCSIVYYELNNRVGEAFHASHTSIVTDGFCDPSNNADRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVF 337
Cdd:cd10497     1 YQEPKYWCSIAYYELNNRVGEAFHASSTSIIVDGFTDPSNNSDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 338 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAALLSQSVNHGFEAVYDLTKMCTIRMSFVKGWGAEY 417
Cdd:cd10497    81 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1397668432 418 HRQDVTSTPCWIEIHLNGPLQWLDKVLTQMGSPHNPISSVS 458
Cdd:cd10497   161 HRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS 201
MH2 pfam03166
MH2 domain; This is the MH2 (MAD homology 2) domain found at the carboxy terminus of MAD ...
 262-434 6.32e-100

MH2 domain; This is the MH2 (MAD homology 2) domain found at the carboxy terminus of MAD related proteins such as Smads. This domain is separated from the MH1 domain by a non-conserved linker region. The MH2 domain mediates interaction with a wide variety of proteins and provides specificity and selectivity to Smad function and also is critical for mediating interactions in Smad oligomers. Unlike MH1, MH2 does not bind DNA. The well-studied MH2 domain of Smad4 is composed of five alpha helices and three loops enclosing a beta sandwich. Smads are involved in the propagation of TGF-beta signals by direct association with the TGF-beta receptor kinase which phosphorylates the last two Ser of a conserved 'SSXS' motif located at the C-terminus of MH2.


Pssm-ID: 460834  Cd Length: 172  Bit Score: 296.46  E-value: 6.32e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 262 QYWCSIVYYELNNRVGEAFHASHTSIVTDGFCDPSNNaDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVFAECL 341
Cdd:pfam03166   1 EIWCSVAYYELNTRVGEAFKVSSPNVTVDGFTDPSDG-NRFCLGLLSNVNRNEAVEKVRKHIGKGVRLSYDGGEVWIYNL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 342 SDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAALLSQSVNHGFEAVYDLTKMCTIRMSFVKGWGAEYHRQD 421
Cdd:pfam03166  80 SDHPVFVQSPYLNREAGRAPDTVHKVPPGESLKVFDMRKFQQLLSQELRRARLGPQDANKLCSVRISFVKGWGPDYSRQD 159

                         170
                  ....*....|...
gi 1397668432 422 VTSTPCWIEIHLN 434
Cdd:pfam03166 160 ITSTPCWIEIHLH 172
DWB smart00524
Domain B in dwarfin family proteins;
263-434 4.15e-98

Domain B in dwarfin family proteins;


Pssm-ID: 197770  Cd Length: 171  Bit Score: 291.52  E-value: 4.15e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  263 YWCSIVYYELNNRVGEAFHASHTSIVTDGFCDPSNNaDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVFAECLS 342
Cdd:smart00524   1 SWCKIAYYELNTRVGETFKVSSPSVTVDGFTDPSDG-NRFCLGQLSNVNRNEATELIRKHIGKGVQLSYENGDVWLYNRS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  343 DSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAALLSQSVNHGFEAVYDLTKMCTIRMSFVKGWGAEYHRQDV 422
Cdd:smart00524  80 DSPIFVQSPYLDEPGGRTLDTVHKLPPGYSIKVFDMEKFAQLLARELAKGFEGVYDLARMCTIRISFVKGWGPDYSRQTI 159

                          170
                   ....*....|..
gi 1397668432  423 TSTPCWIEIHLN 434
Cdd:smart00524 160 TSTPCWIEVHLN 171
MH1_SMAD_1_5_9 cd10490
N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The ...
 11-134 9.22e-89

N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 domain is found in SMAD1, SMAD5 and SMAD9, all closely related receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in bone morphogenetic proteins (BMP) signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway.


Pssm-ID: 199814  Cd Length: 124  Bit Score: 265.91  E-value: 9.22e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  11 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEDLEKALSCPGRPSKCVTIPRSLDGRLQVSHRKGLPHVIY 90
Cdd:cd10490     1 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEELEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1397668432  91 CRVWRWPDLQSHHELKPLECCEYPFSAKQKEVCINPYHYKRVES 134
Cdd:cd10490    81 CRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVES 124
DWA smart00523
Domain A in dwarfin family proteins;
27-136 1.50e-53

Domain A in dwarfin family proteins;


Pssm-ID: 214708  Cd Length: 109  Bit Score: 174.87  E-value: 1.50e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432   27 EEEKWAEKAVDSLVKKLKKkkGALEDLEKALSCPGR-PSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHEL 105
Cdd:smart00523   1 VEEKWAKKATESLLKKLKK--KQLEELLQAVESKGGpPTRCVLIPRSLDGRLQVAHRKGLPHVLYCRLFRWPDLQSPHEL 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1397668432  106 KPLECCEYPFSAKQKEVCINPYHYKRVESPV 136
Cdd:smart00523  79 KALPTCEHAFESKSDEVCCNPYHYSRVERPE 109
MH1 pfam03165
MH1 domain; The MH1 (MAD homology 1) domain is found at the amino terminus of MAD related ...
 32-133 1.78e-50

MH1 domain; The MH1 (MAD homology 1) domain is found at the amino terminus of MAD related proteins such as Smads. This domain is separated from the MH2 domain by a non-conserved linker region. The crystal structure of the MH1 domain shows that a highly conserved 11 residue beta hairpin is used to bind the DNA consensus sequence GNCN in the major groove, shown to be vital for the transcriptional activation of target genes. Not all examples of MH1 can bind to DNA however. Smad2 cannot bind DNA and has a large insertion within the hairpin that presumably abolishes DNA binding. A basic helix (H2) in MH1 with the nuclear localization signal KKLKK has been shown to be essential for Smad3 nuclear import. Smads also use the MH1 domain to interact with transcription factors such as Jun, TFE3, Sp1, and Runx.


Pssm-ID: 460833  Cd Length: 103  Bit Score: 166.78  E-value: 1.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  32 AEKAVDSLVKKLKKKKGALEDLEKALSCPG-RPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLEC 110
Cdd:pfam03165   1 LKKAVESLLKKLKKKIQQLEELELAVESRGdPPTGCVTIPRSLDGRLQVAGRKGLPHVIYCRLWRWPDLQSQHELKAIPT 80

                          90       100
                  ....*....|....*....|...
gi 1397668432 111 CEYPFSAKQKEVCINPYHYKRVE 133
Cdd:pfam03165  81 CETAFESKKDEVCINPYHYSRVE 103
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 150-260 1.07e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 44.80  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 150 GTMPAFQSVPEPNMphnvtYPFQQqhsPNPPSSGPGSPFGLPADTPPPAYQAQDDSQQNSMGMSQGNGMPRPPPSQNGPQ 229
Cdd:TIGR01628 402 GQGPQQQFNGQPLG-----WPRMS---MMPTPMGPGGPLRPNGLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPL 473

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1397668432 230 PMDTSMPPTIPIPKQLSGRGIVDLQPVTYQE 260
Cdd:TIGR01628 474 SQDLPQPQSTASQGGQNKKLAQVLASATPQM 504
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 149-242 2.97e-04

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 43.46  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 149 SGTMPAFQSVPEPNMPHNVTYPFQQQHSPNP--PSSGPGsPFGLPADTPPPAYQaqddsQQNSMGMSQGNGMPRPPPSQN 226
Cdd:pfam09606 374 SSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPqgPGSQPP-QSHPGGMIPSPALI-----PSPSPQMSQQPAQQRTIGQDS 447

                          90
                  ....*....|....*.
gi 1397668432 227 GPQPMDTSMPPTIPIP 242
Cdd:pfam09606 448 PGGSLNTPGQSAVNSP 463
KLF5_N cd21579
N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also ...
 141-237 8.79e-04

N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also known as Krueppel-like factor 5; intestinal enriched Kruppel-like factor/IKLF; basic transcription element binding protein 2/BTEB2) a protein that in humans is encoded by the KLF5 gene. KLF5 is involved in numerous functions in eukaryotic cells, such as proliferation, migration, and differentiation. The loss of KLF5 expression is associated with tumors of the breast, cervix, endometrium, ovary, and prostate. KLF5 mediates the expression of several genes essential for proper cardiac structure and function, and plays a role in familial dilated cardiomyopathy. It functions as a transcriptional activator. KLF5 exhibits both transcriptional activation activity as well as trans-activating function. It belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF5.


Pssm-ID: 410335  Cd Length: 273  Bit Score: 41.05  E-value: 8.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 141 SVYSefPSSGTMPAF---QSVPEPNMPHNVTYpFQ-------QQHS-----PNPPSSGPGSPFG----LPADTPPPAYQA 201
Cdd:cd21579   153 SVFS--APQSAVNNVfikQEMPSFDDQQQGPL-FQllnsdldQQQQptylpPSPPNSEPGSPDRqkelLHNLSPPPSYAA 229

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1397668432 202 QDDSQqnSMGMSQGNGMPRPPPSQNGPQPMdtsMPP 237
Cdd:cd21579   230 SIASK--LAGQTPGLPPPGVGPLSPGQAQS---APV 260
 
Name Accession Description Interval E-value
MH2_SMAD_1_5_9 cd10497
C-terminal Mad Homology 2 (MH2) domain in SMAD1, SMAD5 and SMAD9; The MH2 domain is located at ...
 258-458 2.16e-162

C-terminal Mad Homology 2 (MH2) domain in SMAD1, SMAD5 and SMAD9; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD1, SMAD5 and SMAD9 (also known as SMAD8), are receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in BMP signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway.


Pssm-ID: 199822  Cd Length: 201  Bit Score: 456.26  E-value: 2.16e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 258 YQEPQYWCSIVYYELNNRVGEAFHASHTSIVTDGFCDPSNNADRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVF 337
Cdd:cd10497     1 YQEPKYWCSIAYYELNNRVGEAFHASSTSIIVDGFTDPSNNSDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 338 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAALLSQSVNHGFEAVYDLTKMCTIRMSFVKGWGAEY 417
Cdd:cd10497    81 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1397668432 418 HRQDVTSTPCWIEIHLNGPLQWLDKVLTQMGSPHNPISSVS 458
Cdd:cd10497   161 HRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS 201
MH2_R-SMAD cd10495
C-terminal Mad Homology 2 (MH2) domain in receptor regulated SMADs; The MH2 domain is located ...
 264-445 1.50e-141

C-terminal Mad Homology 2 (MH2) domain in receptor regulated SMADs; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain. Receptor regulated SMADs (R-SMADs) include SMAD1, SMAD2, SMAD3, SMAD5 and SMAD9. SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD2 regulates multiple cellular processes, such as cell proliferation, apoptosis and differentiation, while SMAD3 modulates signals of activin and TGF-beta. SMAD5 is involved in BMP signal modulation, possibly playing a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 (also known as SMAD8) can mediate the differentiation of mesenchymal stem cells into tendon-like cells by inhibiting the osteogenic pathway.


Pssm-ID: 199820  Cd Length: 182  Bit Score: 402.53  E-value: 1.50e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 264 WCSIVYYELNNRVGEAFHASHTSIVTDGFCDPSNNADRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVFAECLSD 343
Cdd:cd10495     1 WCSISYYELNSRVGEQFKASNPSIIVDGFTDPSNNSDRFCLGLLSNVNRNATIENTRRHIGRGVHLFYVGGEVYAECLSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 344 SSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAALLSQSVNHGFEAVYDLTKMCTIRMSFVKGWGAEYHRQDVT 423
Cdd:cd10495    81 SAIFVQSRNCNLRHGFHPATVCKIPPGCSLKIFNNQSFAQLLEQSVNRGFEAVYELTKMCTIRISFVKGWGAEYHRQDVT 160

                         170       180
                  ....*....|....*....|..
gi 1397668432 424 STPCWIEIHLNGPLQWLDKVLT 445
Cdd:cd10495   161 STPCWIEIHLHGPLQWLDKVLT 182
MH2_SMAD_2_3 cd10985
C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3; The MH2 domain is located at the ...
 256-447 6.97e-133

C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain. SMAD2 and SMAD3 are receptor regulated SMADs (R-SMADs). SMAD2 regulates multiple cellular processes, such as cell proliferation, apoptosis and differentiation, while SMAD3 modulates signals of activin and TGF-beta.


Pssm-ID: 199826  Cd Length: 191  Bit Score: 380.81  E-value: 6.97e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 256 VTYQEPQYWCSIVYYELNNRVGEAFHASHTSIVTDGFCDPSNnADRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGE 335
Cdd:cd10985     1 VTYCEPAFWCSISYYEMNTRVGETFHASQPSLTVDGFTDPSN-SERFCLGLLSNVNRNPQVELTRRHIGKGVRLYYIGGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 336 VFAECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAALLSQSVNHGFEAVYDLTKMCTIRMSFVKGWGA 415
Cdd:cd10985    80 VFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLSQSVNQGFEAVYQLTRMCTIRMSFVKGWGA 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1397668432 416 EYHRQDVTSTPCWIEIHLNGPLQWLDKVLTQM 447
Cdd:cd10985   160 EYRRQTVTSTPCWIELHLNGPLQWLDRVLTQM 191
MH2 cd00050
C-terminal Mad Homology 2 (MH2) domain; The MH2 domain is found in the SMAD (small mothers ...
 264-434 6.01e-112

C-terminal Mad Homology 2 (MH2) domain; The MH2 domain is found in the SMAD (small mothers against decapentaplegic) family of proteins and is responsible for type I receptor interactions, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain which prevents it from forming a complex with SMAD4. The MH2 domain is multifunctional and provides SMADs with their specificity and selectivity, as well as transcriptional activity. Several transcriptional co-activators and repressors have also been reported to regulate SMAD signaling by interacting with the MH2 domain. Mutations in the MH2 domains of SMAD2 and especially SMAD4 have been detected in colorectal and other human cancers.


Pssm-ID: 199819  Cd Length: 170  Bit Score: 326.87  E-value: 6.01e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 264 WCSIVYYELNNRVGEAFHASHTSIVTDGFCDPSNnADRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVFAECLSD 343
Cdd:cd00050     1 WCSIAYYELNTRVGELFHVYSPSVAVDGFTDPSN-GDRFCLGQLSNVNRNETIERTRRHIGKGVHLYYVGGEVWAECLSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 344 SSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAALLSQSVNHGFEAVYDLTKMCTIRMSFVKGWGAEYHRQDVT 423
Cdd:cd00050    80 HAIFVQSRNLDYPHGRHPLTVCKIPPGCSIKVFDNQEFAQLLHQSVNTGFEGVYELTKMCTIRMSFVKGWGPEYHRQDIT 159

                         170
                  ....*....|.
gi 1397668432 424 STPCWIEIHLN 434
Cdd:cd00050   160 STPCWIEIHLH 170
MH2 pfam03166
MH2 domain; This is the MH2 (MAD homology 2) domain found at the carboxy terminus of MAD ...
 262-434 6.32e-100

MH2 domain; This is the MH2 (MAD homology 2) domain found at the carboxy terminus of MAD related proteins such as Smads. This domain is separated from the MH1 domain by a non-conserved linker region. The MH2 domain mediates interaction with a wide variety of proteins and provides specificity and selectivity to Smad function and also is critical for mediating interactions in Smad oligomers. Unlike MH1, MH2 does not bind DNA. The well-studied MH2 domain of Smad4 is composed of five alpha helices and three loops enclosing a beta sandwich. Smads are involved in the propagation of TGF-beta signals by direct association with the TGF-beta receptor kinase which phosphorylates the last two Ser of a conserved 'SSXS' motif located at the C-terminus of MH2.


Pssm-ID: 460834  Cd Length: 172  Bit Score: 296.46  E-value: 6.32e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 262 QYWCSIVYYELNNRVGEAFHASHTSIVTDGFCDPSNNaDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVFAECL 341
Cdd:pfam03166   1 EIWCSVAYYELNTRVGEAFKVSSPNVTVDGFTDPSDG-NRFCLGLLSNVNRNEAVEKVRKHIGKGVRLSYDGGEVWIYNL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 342 SDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAALLSQSVNHGFEAVYDLTKMCTIRMSFVKGWGAEYHRQD 421
Cdd:pfam03166  80 SDHPVFVQSPYLNREAGRAPDTVHKVPPGESLKVFDMRKFQQLLSQELRRARLGPQDANKLCSVRISFVKGWGPDYSRQD 159

                         170
                  ....*....|...
gi 1397668432 422 VTSTPCWIEIHLN 434
Cdd:pfam03166 160 ITSTPCWIEIHLH 172
DWB smart00524
Domain B in dwarfin family proteins;
263-434 4.15e-98

Domain B in dwarfin family proteins;


Pssm-ID: 197770  Cd Length: 171  Bit Score: 291.52  E-value: 4.15e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  263 YWCSIVYYELNNRVGEAFHASHTSIVTDGFCDPSNNaDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVFAECLS 342
Cdd:smart00524   1 SWCKIAYYELNTRVGETFKVSSPSVTVDGFTDPSDG-NRFCLGQLSNVNRNEATELIRKHIGKGVQLSYENGDVWLYNRS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  343 DSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAALLSQSVNHGFEAVYDLTKMCTIRMSFVKGWGAEYHRQDV 422
Cdd:smart00524  80 DSPIFVQSPYLDEPGGRTLDTVHKLPPGYSIKVFDMEKFAQLLARELAKGFEGVYDLARMCTIRISFVKGWGPDYSRQTI 159

                          170
                   ....*....|..
gi 1397668432  423 TSTPCWIEIHLN 434
Cdd:smart00524 160 TSTPCWIEVHLN 171
MH1_SMAD_1_5_9 cd10490
N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The ...
 11-134 9.22e-89

N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 domain is found in SMAD1, SMAD5 and SMAD9, all closely related receptor regulated SMADs (R-SMADs). SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD5 is involved in bone morphogenetic proteins (BMP) signal modulation and may also play a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 mediates the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway.


Pssm-ID: 199814  Cd Length: 124  Bit Score: 265.91  E-value: 9.22e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  11 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEDLEKALSCPGRPSKCVTIPRSLDGRLQVSHRKGLPHVIY 90
Cdd:cd10490     1 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEELEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1397668432  91 CRVWRWPDLQSHHELKPLECCEYPFSAKQKEVCINPYHYKRVES 134
Cdd:cd10490    81 CRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVES 124
MH1_R-SMAD cd10488
N-terminal Mad Homology 1 (MH1) domain of receptor regulated SMADs; The MH1 is a small ...
 14-134 1.03e-70

N-terminal Mad Homology 1 (MH1) domain of receptor regulated SMADs; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. It binds to the major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 domain is found in all receptor regulated SMADs (R-SMADs) including SMAD1, SMAD2, SMAD3, SMAD5 and SMAD9. SMAD1 plays an essential role in bone development and postnatal bone formation through activation by bone morphogenetic protein (BMP) type 1 receptor kinase. SMAD2 regulates multiple cellular processes, such as cell proliferation, apoptosis and differentiation, while SMAD3 modulates signals of activin and TGF-beta. SMAD4, a common mediator SMAD (co-SMAD) binds R-SMADs, forming an oligomeric complex that binds to DNA and serves as a transcription factor. SMAD5 is involved in bone morphogenetic proteins (BMP) signal modulation, possibly playing a role in the pathway involving inhibition of hematopoietic progenitor cells by TGF-beta. SMAD9 (also known as SMAD8) can mediate the differentiation of mesenchymal stem cells (MSCs) into tendon-like cells by inhibiting the osteogenic pathway


Pssm-ID: 199812  Cd Length: 123  Bit Score: 219.75  E-value: 1.03e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  14 PAVKRLLGWKQG---DEEEKWAEKAVDSLVKKLKKKkGALEDLEKALSCPGRPSKCVTIPRSLDGRLQVSHRKGLPHVIY 90
Cdd:cd10488     1 PIVKRLLGWKKGeqnGEEEKWAEKAVKSLVKKLKKK-GQLEELEKAISTQNVNTRCVTIPRSLDGRLQVSHRKGLPHVIY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1397668432  91 CRVWRWPDLQSHHELKPLECCEYPFSAKQKEVCINPYHYKRVES 134
Cdd:cd10488    80 CRLWRWPDLQSHHELKPLELCEFAFNMKKEEVCINPYHYKRVET 123
MH1_SMAD_2_3 cd10491
N-terminal Mad Homology 1 (MH1) domain in SMAD2 and SMAD3; The MH1 is a small DNA-binding ...
 12-134 2.37e-70

N-terminal Mad Homology 1 (MH1) domain in SMAD2 and SMAD3; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 is found in SMAD2 as well as SMAD3. SMAD2 mediates the signal of the transforming growth factor (TGF)-beta, and thereby regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. It plays a role in the transmission of extracellular signals from ligands of the TGF-beta superfamily growth factors into the cell nucleus. SMAD3 modulates signals of activin and TGF-beta. It binds SMAD4, enabling its transmigration into the nucleus where it forms complexes with other proteins and acts as a transcription factor. Increased SMAD3 activity has been implicated in the pathogenesis of scleroderma.


Pssm-ID: 199815  Cd Length: 124  Bit Score: 218.94  E-value: 2.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  12 TSPAVKRLLGWKQG--DEEEKWAEKAVDSLVKKLKKKkGALEDLEKALSCPGRPSKCVTIPRSLDGRLQVSHRKGLPHVI 89
Cdd:cd10491     1 TPPVVKRLLGWKKGenGQEEKWSEKAVKSLVKKLKKT-GGLDELEKAITTQNSNTKCITIPRSLDGRLQVSHRKGLPHVI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1397668432  90 YCRVWRWPDLQSHHELKPLECCEYPFSAKQKEVCINPYHYKRVES 134
Cdd:cd10491    80 YCRLWRWPDLQSHHELRAIETCEYAFNLKKDEVCVNPYHYQRVET 124
MH1 cd00049
N-terminal Mad Homology 1 (MH1) domain; The MH1 is a small DNA-binding domain present in SMAD ...
 14-134 7.42e-67

N-terminal Mad Homology 1 (MH1) domain; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. Receptor-regulated SMAD proteins (R-SMADs, including SMAD1, SMAD2, SMAD3, SMAD5, and SMAD9) are activated by phosphorylation by transforming growth factor (TGF)-beta type I receptors. The active R-SMAD associates with a common mediator SMAD (Co-SMAD or SMAD4) and other cofactors, which together translocate to the nucleus to regulate gene expression. The inhibitory or antagonistic SMADs (I-SMADs, including SMAD6 and SMAD7) negatively regulate TGF-beta signaling by competing with R-SMADs for type I receptor or Co-SMADs. MH1 domains of R-SMAD and SMAD4 contain a nuclear localization signal as well as DNA-binding activity. The activated R-SMAD/SMAD4 complex then binds with very low affinity to a DNA sequence CAGAC called SMAD-binding element (SBE) via the MH1 domain.


Pssm-ID: 199811  Cd Length: 121  Bit Score: 209.75  E-value: 7.42e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  14 PAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKkGALEDLEKALSCPG-RPSKCVTIPRSLDGRLQVSHRKGLPHVIYCR 92
Cdd:cd00049     1 PIVKRLLGWKQGGEEEKWAKKAVKSLVKKLKEK-KQLDSLEKAITTQGgVPSKCVTIPRSLDGRLQVAHRKGLPHVIYCR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1397668432  93 VWRWPDLQSHHELKPLECCEYPFSAKQKEVCINPYHYKRVES 134
Cdd:cd00049    80 LWRWPDLHSHHELKALELCQFAFNMKKDEVCVNPYHYQRVES 121
MH2_SMAD_4 cd10498
C-terminal Mad Homology 2 (MH2) domain in SMAD4; The MH2 domain is located at the C-terminus ...
 261-444 1.37e-55

C-terminal Mad Homology 2 (MH2) domain in SMAD4; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain. SMAD4, which belongs to the Dwarfin family of proteins, is involved in many cell functions such as differentiation, apoptosis, gastrulation, embryonic development and the cell cycle. SMAD4 binds receptor regulated SMADs (R-SMADs) such as SMAD1 or SMAD2, and forms an oligomeric complex that binds to DNA and serves as a transcription factor. SMAD4 is often mutated in several cancers, such as multiploid colorectal cancer, cervical cancer and pancreatic carcinoma, as well as in juvenile polyposis syndrome.


Pssm-ID: 199823  Cd Length: 222  Bit Score: 184.21  E-value: 1.37e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 261 PQYWCSIVYYELNNRVGEAFH--ASHTSIVTDGFCDPSNnADRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVG-GEVF 337
Cdd:cd10498     1 PEYWCSIAYFELDTQVGETFKvpSSCPTVTVDGYVDPSG-GNRFCLGQLSNVHRTEASERARLHIGKGVQLDCKGeGDVW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 338 AECLSDSSIFVQSRNCNYHHGFHP-TTVCKIPPGCSLKIFN-NQEFAALLSQSVNHGFEA-------------------- 395
Cdd:cd10498    80 LRCLSDHSVFVQSYYLDREAGRAPgDAVHKIYPSAYIKVFDlRQCHRQMQQQAATAQAAAaaqaaavagnipgpgsvggi 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397668432 396 -------------VYDLTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLNGPLQWLDKVL 444
Cdd:cd10498   160 apaislsaaagigVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVL 221
DWA smart00523
Domain A in dwarfin family proteins;
27-136 1.50e-53

Domain A in dwarfin family proteins;


Pssm-ID: 214708  Cd Length: 109  Bit Score: 174.87  E-value: 1.50e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432   27 EEEKWAEKAVDSLVKKLKKkkGALEDLEKALSCPGR-PSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHEL 105
Cdd:smart00523   1 VEEKWAKKATESLLKKLKK--KQLEELLQAVESKGGpPTRCVLIPRSLDGRLQVAHRKGLPHVLYCRLFRWPDLQSPHEL 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1397668432  106 KPLECCEYPFSAKQKEVCINPYHYKRVESPV 136
Cdd:smart00523  79 KALPTCEHAFESKSDEVCCNPYHYSRVERPE 109
MH1 pfam03165
MH1 domain; The MH1 (MAD homology 1) domain is found at the amino terminus of MAD related ...
 32-133 1.78e-50

MH1 domain; The MH1 (MAD homology 1) domain is found at the amino terminus of MAD related proteins such as Smads. This domain is separated from the MH2 domain by a non-conserved linker region. The crystal structure of the MH1 domain shows that a highly conserved 11 residue beta hairpin is used to bind the DNA consensus sequence GNCN in the major groove, shown to be vital for the transcriptional activation of target genes. Not all examples of MH1 can bind to DNA however. Smad2 cannot bind DNA and has a large insertion within the hairpin that presumably abolishes DNA binding. A basic helix (H2) in MH1 with the nuclear localization signal KKLKK has been shown to be essential for Smad3 nuclear import. Smads also use the MH1 domain to interact with transcription factors such as Jun, TFE3, Sp1, and Runx.


Pssm-ID: 460833  Cd Length: 103  Bit Score: 166.78  E-value: 1.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  32 AEKAVDSLVKKLKKKKGALEDLEKALSCPG-RPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLEC 110
Cdd:pfam03165   1 LKKAVESLLKKLKKKIQQLEELELAVESRGdPPTGCVTIPRSLDGRLQVAGRKGLPHVIYCRLWRWPDLQSQHELKAIPT 80

                          90       100
                  ....*....|....*....|...
gi 1397668432 111 CEYPFSAKQKEVCINPYHYKRVE 133
Cdd:pfam03165  81 CETAFESKKDEVCINPYHYSRVE 103
MH1_SMAD_4 cd10492
N-terminal Mad Homology 1 (MH1) domain in SMAD4; The MH1 is a small DNA-binding domain present ...
 16-134 3.08e-40

N-terminal Mad Homology 1 (MH1) domain in SMAD4; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 belongs to SMAD4, a common mediator SMAD (co-SMAD), which belongs to the Dwarfin family of proteins and is involved in many cell functions such as differentiation, apoptosis, gastrulation, embryonic development and cell cycle. SMAD4 binds receptor regulated SMADs (R-SMADs) such as SMAD1 or SMAD2, and forms an oligomeric complex that binds to DNA and serves as a transcription factor. SMAD4 is often mutated in several cancers, such as multiploid colorectal cancer and pancreatic carcinoma, as well as in juvenile polyposis syndrome (JPS).


Pssm-ID: 199816  Cd Length: 125  Bit Score: 140.67  E-value: 3.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  16 VKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEDLEKALSCPGR-PSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVW 94
Cdd:cd10492     7 VHSLMCHRQGGESESFAKRAIESLVKKLKDKRDELDSLITAITSNGAhPSKCVTIQRTLDGRLQVAGRKGFPHVIYARIW 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1397668432  95 RWPDLQShHELKPLECCEYPFSAKQKEVCINPYHYKRVES 134
Cdd:cd10492    87 RWPDLHK-NELKHVKFCQYAFDLKCDSVCVNPYHYERVVS 125
MH2_I-SMAD cd10496
C-terminal Mad Homology 2 (MH2) domain in Inhibitory SMADs; The MH2 domain is located at the ...
 264-434 5.25e-35

C-terminal Mad Homology 2 (MH2) domain in Inhibitory SMADs; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD6 and SMAD7 are inhibitory SMADs (I-SMADs) that function as negative regulators of signaling mediated by the TGF-beta superfamily. SMAD6 specifically inhibits bone morphogenetic protein (BMP) type I receptor mediated signaling, while SMAD7 enhances muscle differentiation and is often associated with cancer, tissue fibrosis and inflammatory diseases.


Pssm-ID: 199821  Cd Length: 165  Bit Score: 127.86  E-value: 5.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 264 WCSIVYYELNNRVGEAFHASHTSI-VTDGFCDPsnnaDRFCLG-LLSNVNRNSTIENTRRHIGKGVHLYYVGGEVFAECL 341
Cdd:cd10496     1 WCTIAYWELRERVGRLYPVKQPAVnIFDDLPKG----DGFCLGaLNRQGNASEAVARVRSKIGLGVTLSREPDGVWIYNR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 342 SDSSIFVQSRNCNYHHGfHPTTVCKIPPGCSLKIFNNQEFAALLSQSVNHGFEAVYDLTkmcTIRMSFVKGWGAEYHRQD 421
Cdd:cd10496    77 SEYPIFVNSPTLDSPPS-RNLLVTKVPPGYSLKVFDYERAALLQRRDDHFSPQGPVDPN---SVRISFVKGWGPNYSRQF 152

                         170
                  ....*....|...
gi 1397668432 422 VTSTPCWIEIHLN 434
Cdd:cd10496   153 ITSCPCWLEILLN 165
MH2_SMAD_6 cd10499
C-terminal Mad Homology 2 (MH2) domain in SMAD6; The MH2 domain is located at the C-terminus ...
 260-434 5.61e-28

C-terminal Mad Homology 2 (MH2) domain in SMAD6; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD6, an inhibitory or antagonistic SMAD (I-SMAD), acts as a negative regulator of signaling mediated by the TGF-beta superfamily of ligands, by competing with SMAD4 and preventing the transcription of SMAD4's gene products. SMAD6 specifically inhibits bone morphogenetic protein (BMP) type I receptor mediated signaling. SMAD6 and SMAD7 act as critical mediators for effective TGF-beta I-mediated suppression of Interleukin-1/Toll-like receptor (IL-1R/TLR) signaling through simultaneous binding to Pellino-1, an adaptor protein of interleukin-1 receptor associated kinase 1 (IRAK1), via their MH2 domains.


Pssm-ID: 199824  Cd Length: 174  Bit Score: 109.14  E-value: 5.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 260 EPQYWCSIVYYELNNRVGEAFhashtsivtdGFCDPSNN-------ADRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYV 332
Cdd:cd10499     6 KRSHWCSVAYWEHRTRVGRLY----------AVYDQSVSifydlpqGSGFCLGQLNLEQRSESVRRTRSKIGYGILLSKE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 333 GGEVFAECLSDSSIFVQSRNCNYHHGfHPTTVCKIPPGCSLKIFNNQEFAALLSQSVNHGFEAVYDLTkmcTIRMSFVKG 412
Cdd:cd10499    76 PDGVWAYNRSEHPIFVNSPTLDIPGS-RTLVVRKVPPGYSIKVFDYERSCLLQHTAEPELADGPYDPN---SVRISFAKG 151

                         170       180
                  ....*....|....*....|..
gi 1397668432 413 WGAEYHRQDVTSTPCWIEIHLN 434
Cdd:cd10499   152 WGPCYSRQFITSCPCWLEILLN 173
MH2_SMAD_7 cd10500
C-terminal Mad Homology 2 (MH2) domain in SMAD7; The MH2 domain is located at the C-terminus ...
 260-434 1.54e-17

C-terminal Mad Homology 2 (MH2) domain in SMAD7; The MH2 domain is located at the C-terminus of the SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The MH2 domain is responsible for type I receptor interaction, phosphorylation-triggered homo- and hetero-oligomerization, and transactivation. It is negatively regulated by the N-terminal MH1 domain, which prevents it from forming a complex with SMAD4. SMAD7, an inhibitory or antagonistic SMAD (I-SMAD), acts as a negative regulator of signaling mediated by the TGF-beta superfamily of ligands, by blocking TGF-beta type 1 and activin association with the receptor as well as access to SMAD2. SMAD7 enhances muscle differentiation, playing pivotal roles in embryonic development and adult homoeostasis. SMAD7 and SMAD6 act as critical mediators for effective TGF-beta I-mediated suppression of Interleukin-1/Toll-like receptor (IL-1R/TLR) signaling through simultaneous binding to Pellino-1, an adaptor protein of interleukin-1 receptor associated kinase 1(IRAK1), via their MH2 domains. Altered expression of SMAD7 is often associated with cancer, tissue fibrosis and inflammatory diseases.


Pssm-ID: 199825  Cd Length: 171  Bit Score: 80.08  E-value: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 260 EPQYWCSIVYYELNNRVGEAFHASHTSIvtDGFCD-PSNNAdrFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVFA 338
Cdd:cd10500     4 DQSHWCVVAYWEEKTRVGRLYSVQEPSL--DIFYDlPQGNG--FCLGQLNSDNKSQLVQKVRSKIGYGIQLTREVDGVWV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 339 ECLSDSSIFVQSRNCNyHHGFHPTTVCKIPPGCSLKIFNNQEFAAL-------LSQSVNHGFeavydltkmcTIRMSFVK 411
Cdd:cd10500    80 YNRSSYPIFIKSATLD-NPDSRTLLVHKVFPGFSIKAFDYEKAYSLqrpndheFMQQPWTGF----------TVQISFVK 148

                         170       180
                  ....*....|....*....|...
gi 1397668432 412 GWGAEYHRQDVTSTPCWIEIHLN 434
Cdd:cd10500   149 GWGQCYTRQFISSCPCWLEVIFN 171
MH1_SMAD_6_7 cd10489
N-terminal Mad Homology 1 (MH1) domain in SMAD6 and SMAD7; The MH1 is a small DNA-binding ...
 50-135 1.71e-16

N-terminal Mad Homology 1 (MH1) domain in SMAD6 and SMAD7; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 domain is found in SMAD6 and SMAD7, both inhibitory SMADs (I-SMADs) and negative regulators of signaling mediated by TGF-beta superfamily. SMAD6 specifically inhibits bone morphogenetic protein (BMP) type I receptor mediated signaling while SMAD7 enhances muscle differentiation and is often associated with cancer, tissue fibrosis and inflammatory diseases.


Pssm-ID: 199813  Cd Length: 119  Bit Score: 75.50  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  50 LEDLEKAL-SCPGRPSKCVTIPRSLdgrlqVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEypfSAKQKE-VCINPY 127
Cdd:cd10489    39 LELLLQAVeSRGGDYLACVLLPRRD-----PRSMPQDPHVLCCQLFRWPDLRHSSELKRLPTCE---SAKDPVyVCCNPY 110


                  ....*...
gi 1397668432 128 HYKRVESP 135
Cdd:cd10489   111 HWSRLCRP 118
MH1_SMAD_6 cd10493
N-terminal Mad Homology 1 (MH1) domain in SMAD6; The MH1 is a small DNA-binding domain present ...
 53-136 1.87e-16

N-terminal Mad Homology 1 (MH1) domain in SMAD6; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins, which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. MH1 binds to the DNA major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 belongs to SMAD6, an inhibitory SMAD (I-SMAD) or antagonistic SMAD, which acts as a negative regulator of signaling mediated by TGF-beta superfamily ligands, by competing with SMAD4 and preventing the transcription of SMAD4's gene products. SMAD6 specifically inhibits bone morphogenetic protein (BMP) type I receptor mediated signaling.


Pssm-ID: 199817  Cd Length: 113  Bit Score: 75.19  E-value: 1.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  53 LEKALSCPGRPSKCVTIPRSldgRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEYPFSAKQKEVCINPYHYKRV 132
Cdd:cd10493    33 LEAVESRGGLPSGCVMVPRT---ELRLGGRRVPPQLLLCRLFRWPDLQHPAQLKALCHCQSFGAQDGPTVCCNPYHYSRL 109


                  ....
gi 1397668432 133 ESPV 136
Cdd:cd10493   110 CGPE 113
MH1_SMAD_7 cd10494
N-terminal Mad Homology 1 (MH1) domain in SMAD7; The MH1 is a small DNA-binding domain present ...
 50-135 1.27e-11

N-terminal Mad Homology 1 (MH1) domain in SMAD7; The MH1 is a small DNA-binding domain present in SMAD (small mothers against decapentaplegic) family of proteins. It binds to the major groove in an unusual manner via a beta hairpin structure. It negatively regulates the functions of the MH2 domain, the C-terminal domain of SMAD. This MH1 belongs to SMAD7, an inhibitory SMAD (I-SMAD) or antagonistic SMAD, which acts as a negative regulator of signaling mediated by TGF-beta superfamily ligands, by blocking TGF-beta type 1 and activin association with the receptor as well as access to SMAD2. SMAD7 enhances muscle differentiation, playing pivotal roles in embryonic development and adult homoeostasis. Altered expression of SMAD7 is often associated with cancer, tissue fibrosis and inflammatory diseases.


Pssm-ID: 199818  Cd Length: 123  Bit Score: 61.82  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432  50 LEDLEKALSCPGRP-SKCVTIPRSLDGRLQvSHRKGLPhVIYCRVWRWPDLQSHHELKPLECCEYPFSAKQKEVCINPYH 128
Cdd:cd10494    36 LEGLLQAVESRGGArTPCLLLPARLDARLG-QQSYSLP-LLLCKVFRWPDLRHSSEVKRLSCCESYGKINPELVCCNPHH 113

                          90
                  ....*....|
gi 1397668432 129 YKR---VESP 135
Cdd:cd10494   114 LSRlceLESP 123
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 150-260 1.07e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 44.80  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 150 GTMPAFQSVPEPNMphnvtYPFQQqhsPNPPSSGPGSPFGLPADTPPPAYQAQDDSQQNSMGMSQGNGMPRPPPSQNGPQ 229
Cdd:TIGR01628 402 GQGPQQQFNGQPLG-----WPRMS---MMPTPMGPGGPLRPNGLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPL 473

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1397668432 230 PMDTSMPPTIPIPKQLSGRGIVDLQPVTYQE 260
Cdd:TIGR01628 474 SQDLPQPQSTASQGGQNKKLAQVLASATPQM 504
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 149-242 2.97e-04

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 43.46  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 149 SGTMPAFQSVPEPNMPHNVTYPFQQQHSPNP--PSSGPGsPFGLPADTPPPAYQaqddsQQNSMGMSQGNGMPRPPPSQN 226
Cdd:pfam09606 374 SSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPqgPGSQPP-QSHPGGMIPSPALI-----PSPSPQMSQQPAQQRTIGQDS 447

                          90
                  ....*....|....*.
gi 1397668432 227 GPQPMDTSMPPTIPIP 242
Cdd:pfam09606 448 PGGSLNTPGQSAVNSP 463
KLF5_N cd21579
N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also ...
 141-237 8.79e-04

N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also known as Krueppel-like factor 5; intestinal enriched Kruppel-like factor/IKLF; basic transcription element binding protein 2/BTEB2) a protein that in humans is encoded by the KLF5 gene. KLF5 is involved in numerous functions in eukaryotic cells, such as proliferation, migration, and differentiation. The loss of KLF5 expression is associated with tumors of the breast, cervix, endometrium, ovary, and prostate. KLF5 mediates the expression of several genes essential for proper cardiac structure and function, and plays a role in familial dilated cardiomyopathy. It functions as a transcriptional activator. KLF5 exhibits both transcriptional activation activity as well as trans-activating function. It belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF5.


Pssm-ID: 410335  Cd Length: 273  Bit Score: 41.05  E-value: 8.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 141 SVYSefPSSGTMPAF---QSVPEPNMPHNVTYpFQ-------QQHS-----PNPPSSGPGSPFG----LPADTPPPAYQA 201
Cdd:cd21579   153 SVFS--APQSAVNNVfikQEMPSFDDQQQGPL-FQllnsdldQQQQptylpPSPPNSEPGSPDRqkelLHNLSPPPSYAA 229

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1397668432 202 QDDSQqnSMGMSQGNGMPRPPPSQNGPQPMdtsMPP 237
Cdd:cd21579   230 SIASK--LAGQTPGLPPPGVGPLSPGQAQS---APV 260
Jun pfam03957
Jun-like transcription factor;
170-262 1.08e-03

Jun-like transcription factor;


Pssm-ID: 461108 [Multi-domain]  Cd Length: 231  Bit Score: 40.67  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 170 PFQQQHSPNPPSSGPGSPFGLPADTPPPAYqaqddsqQNSMGMSQGNGMPRPPPSQNGPQPMD-TSMPPTIPIPKQLSGR 248
Cdd:pfam03957 133 PAPQALAAGGGGSGPGALAAGGIATEPPVY-------ANLSSFNPAAAPASGAAPAQPPQPVSyAAEPPPFAVPVQHPPP 205

                          90
                  ....*....|....
gi 1397668432 249 GIVDLQPVTYQEPQ 262
Cdd:pfam03957 206 GRPPRLQALKEEPQ 219
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 144-257 4.43e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 39.75  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 144 SEFPSSGTMPAFQSVPEPNMPhNVTYPFQQQHSPNPP----SSGPG-SPFGLPADTPP------PAYQAQDDSQQNSMGM 212
Cdd:pfam03154 192 TQAATAGPTPSAPSVPPQGSP-ATSQPPNQTQSTAAPhtliQQTPTlHPQRLPSPHPPlqpmtqPPPPSQVSPQPLPQPS 270

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1397668432 213 SQGNGMPRPPPSQNGPQPMDTSMPPT-IPIPKQlSGRGIVDLQPVT 257
Cdd:pfam03154 271 LHGQMPPMPHSLQTGPSHMQHPVPPQpFPLTPQ-SSQSQVPPGPSP 315
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 127-246 4.59e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 39.75  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397668432 127 YHYKRVESPVLLLFSVYSEFPSSGTMPAF----QSVPEPNMPHNVTYPFQQ--QHSPNPPSS--GPGSPFGLPADTPPPA 198
Cdd:pfam03154 405 HHPPSAHPPPLQLMPQSQQLPPPPAQPPVltqsQSLPPPAASHPPTSGLHQvpSQSPFPQHPfvPGGPPPITPPSGPPTS 484

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1397668432 199 YQAQDDSQQNSMGMSQGNGMPRP-------PPSQNGPQPMDTSMPPTIPIPKQLS 246
Cdd:pfam03154 485 TSSAMPGIQPPSSASVSSSGPVPaavscplPPVQIKEEALDEAEEPESPPPPPRS 539
 
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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