NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1932671850|ref|XP_037506886|]
View 

protein mothers against dpp isoform X3 [Rhipicephalus sanguineus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 284-484 1.64e-156

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: 442.40  E-value: 1.64e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 284 YQEPQYWCTIAYYELNSRVGEIFHAQSHSIVIDGFTDPSNNSNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 363
Cdd:cd10497     1 YQEPKYWCSIAYYELNNRVGEAFHASSTSIIVDGFTDPSNNSDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 364 AECLSDSAIFVQSRNCNHSHQFHPTTVCKIPSGCSLKIFNNREFAELLTMAVNNGFEAVYELTKMCIIRMSFVKGWGAEY 443
Cdd:cd10497    81 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1932671850 444 HRQDVTSTPCWIEVHLSGPLQWLDKVLTQMGSPHNPISSVS 484
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 ...
 33-156 2.63e-96

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: 286.32  E-value: 2.63e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  33 FTSPAVKKLLGWKQGDEEEKWAEKAVDSLVKKLKKRKGAIEDLEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 112
Cdd:cd10490     1 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEELEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1932671850 113 CRVWRWPDLQSHHELKPLECCEYPFSAKQKEVCINPYHYKRVES 156
Cdd:cd10490    81 CRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVES 124
KREPA super family cl49620
Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, ...
 133-315 1.33e-03

Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, respectively) proteins are components of the RNA editing complex of parasitic protozoans such as Trypanosoma and Leishmania species. These parasites have a uniquely organized mitochondrial genome, the kinetoplast. Most kinetoplast-transcribed mRNAs are cryptic and encode multiple subunits for the electron transport chain following maturation through a uridine insertion/deletion process called RNA editing. KREPAs participate in the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. The editosome, a high molecular mass enzyme complex, carries out the reaction with the help of critical enzymes and structural proteins. Five related editosome proteins KREPA1 (TbMP81), KREPA2 (TbMP63), KREPA3 (TbMP42), KREPA4 (TbMP24), KREPA5 (TbMP19), and KREPA6 (TbMP18) play critical roles in the structure and auxiliary functions of the editing process without any predicted catalytic function. The KREPA1, KREPA2, and KREPA3 proteins contain C2H2 zinc finger motifs and KREPA4 and KREPA6, contain RNA-binding domains but all have a conserved C-terminal sequences that resemble an oligonucleotide-binding (OB)-fold domain. Thus, this group of five proteins is likely to be involved in protein-protein and/or protein-RNA interactions. RNA editing is crucial for the parasite's survival in both its bloodstream and procyclic form life cycle stages which allows the parasite to adapt to its environment and maintain its viability.


The actual alignment was detected with superfamily member cd23959:

Pssm-ID: 483960 [Multi-domain]  Cd Length: 424  Bit Score: 41.01  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 133 CEYPFSAKQkevciNPYHYKRVESPVLPPVLVPRHSEYPPGGHTmipPVFQQVAESGMPhnvsfsaQGFSAATSGSSATT 212
Cdd:cd23959   115 VPNPFSASS-----STQRETHKTAQVAPPKAEPQTAPVTPFGQL---PMFGQHPPPAKP-------LPAAAAAQQSSASP 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 213 GVavavgtnaaagVPSPGPSLGSSApnSPFGLPADTPPPAYSAQDDSQSATDDQP---QSMDTSTVPPDVSPVTYQEPQY 289
Cdd:cd23959   180 GE-----------VASPFASGTVSA--SPFATATDTAPSSGAPDGFPAEASAPSPfaaPASAASFPAAPVANGEAATPTH 246

                         170       180
                  ....*....|....*....|....*..
gi 1932671850 290 WCTIAYYELNSRVGEIFHAQS-HSIVI 315
Cdd:cd23959   247 ACTICGKAFSTHEGLRMHSKAkHGVEL 273
 
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 ...
 284-484 1.64e-156

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: 442.40  E-value: 1.64e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 284 YQEPQYWCTIAYYELNSRVGEIFHAQSHSIVIDGFTDPSNNSNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 363
Cdd:cd10497     1 YQEPKYWCSIAYYELNNRVGEAFHASSTSIIVDGFTDPSNNSDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 364 AECLSDSAIFVQSRNCNHSHQFHPTTVCKIPSGCSLKIFNNREFAELLTMAVNNGFEAVYELTKMCIIRMSFVKGWGAEY 443
Cdd:cd10497    81 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1932671850 444 HRQDVTSTPCWIEVHLSGPLQWLDKVLTQMGSPHNPISSVS 484
Cdd:cd10497   161 HRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS 201
MH2 pfam03166
MH2 domain; This is the MH2 (MAD homology 2) domain found at the carboxy terminus of MAD ...
 288-459 1.03e-97

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: 291.45  E-value: 1.03e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 288 QYWCTIAYYELNSRVGEIFHAQSHSIVIDGFTDPSNNsNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECL 367
Cdd:pfam03166   1 EIWCSVAYYELNTRVGEAFKVSSPNVTVDGFTDPSDG-NRFCLGLLSNVNRNEAVEKVRKHIGKGVRLSYDGGEVWIYNL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 368 SDSAIFVQSRNCNHSHQFHPTTVCKIPSGCSLKIFNNREFAELLTMAVNNGFEAVYELTKMCIIRMSFVKGWGAEYHRQD 447
Cdd:pfam03166  80 SDHPVFVQSPYLNREAGRAPDTVHKVPPGESLKVFDMRKFQQLLSQELRRARLGPQDANKLCSVRISFVKGWGPDYSRQD 159

                         170
                  ....*....|..
gi 1932671850 448 VTSTPCWIEVHL 459
Cdd:pfam03166 160 ITSTPCWIEIHL 171
MH1_SMAD_1_5_9 cd10490
N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The ...
 33-156 2.63e-96

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: 286.32  E-value: 2.63e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  33 FTSPAVKKLLGWKQGDEEEKWAEKAVDSLVKKLKKRKGAIEDLEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 112
Cdd:cd10490     1 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEELEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1932671850 113 CRVWRWPDLQSHHELKPLECCEYPFSAKQKEVCINPYHYKRVES 156
Cdd:cd10490    81 CRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVES 124
DWB smart00524
Domain B in dwarfin family proteins;
289-460 7.98e-96

Domain B in dwarfin family proteins;


Pssm-ID: 197770  Cd Length: 171  Bit Score: 286.51  E-value: 7.98e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  289 YWCTIAYYELNSRVGEIFHAQSHSIVIDGFTDPSNnSNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLS 368
Cdd:smart00524   1 SWCKIAYYELNTRVGETFKVSSPSVTVDGFTDPSD-GNRFCLGQLSNVNRNEATELIRKHIGKGVQLSYENGDVWLYNRS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  369 DSAIFVQSRNCNHSHQFHPTTVCKIPSGCSLKIFNNREFAELLTMAVNNGFEAVYELTKMCIIRMSFVKGWGAEYHRQDV 448
Cdd:smart00524  80 DSPIFVQSPYLDEPGGRTLDTVHKLPPGYSIKVFDMEKFAQLLARELAKGFEGVYDLARMCTIRISFVKGWGPDYSRQTI 159

                          170
                   ....*....|..
gi 1932671850  449 TSTPCWIEVHLS 460
Cdd:smart00524 160 TSTPCWIEVHLN 171
DWA smart00523
Domain A in dwarfin family proteins;
49-158 1.23e-60

Domain A in dwarfin family proteins;


Pssm-ID: 214708  Cd Length: 109  Bit Score: 193.75  E-value: 1.23e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850   49 EEEKWAEKAVDSLVKKLKKRKgaIEDLEKALSCPG-QPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHEL 127
Cdd:smart00523   1 VEEKWAKKATESLLKKLKKKQ--LEELLQAVESKGgPPTRCVLIPRSLDGRLQVAHRKGLPHVLYCRLFRWPDLQSPHEL 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1932671850  128 KPLECCEYPFSAKQKEVCINPYHYKRVESPV 158
Cdd:smart00523  79 KALPTCEHAFESKSDEVCCNPYHYSRVERPE 109
MH1 pfam03165
MH1 domain; The MH1 (MAD homology 1) domain is found at the amino terminus of MAD related ...
 54-155 1.25e-57

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: 186.04  E-value: 1.25e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  54 AEKAVDSLVKKLKKRKGAIEDLEKALSCPG-QPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLEC 132
Cdd:pfam03165   1 LKKAVESLLKKLKKKIQQLEELELAVESRGdPPTGCVTIPRSLDGRLQVAGRKGLPHVIYCRLWRWPDLQSQHELKAIPT 80

                          90       100
                  ....*....|....*....|...
gi 1932671850 133 CEYPFSAKQKEVCINPYHYKRVE 155
Cdd:pfam03165  81 CETAFESKKDEVCINPYHYSRVE 103
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 133-315 1.33e-03

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 41.01  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 133 CEYPFSAKQkevciNPYHYKRVESPVLPPVLVPRHSEYPPGGHTmipPVFQQVAESGMPhnvsfsaQGFSAATSGSSATT 212
Cdd:cd23959   115 VPNPFSASS-----STQRETHKTAQVAPPKAEPQTAPVTPFGQL---PMFGQHPPPAKP-------LPAAAAAQQSSASP 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 213 GVavavgtnaaagVPSPGPSLGSSApnSPFGLPADTPPPAYSAQDDSQSATDDQP---QSMDTSTVPPDVSPVTYQEPQY 289
Cdd:cd23959   180 GE-----------VASPFASGTVSA--SPFATATDTAPSSGAPDGFPAEASAPSPfaaPASAASFPAAPVANGEAATPTH 246

                         170       180
                  ....*....|....*....|....*..
gi 1932671850 290 WCTIAYYELNSRVGEIFHAQS-HSIVI 315
Cdd:cd23959   247 ACTICGKAFSTHEGLRMHSKAkHGVEL 273
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 157-281 7.53e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.00  E-value: 7.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  157 PVLPPVLVPRHSEYPPGGHTMIPPvfqqvaesgmphNVSFSAQGFSAATSGSSAttgVAVAVGTNAAAGVPSPGPSLGss 236
Cdd:PHA03307   132 PDLSEMLRPVGSPGPPPAASPPAA------------GASPAAVASDAASSRQAA---LPLSSPEETARAPSSPPAEPP-- 194

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1932671850  237 aPNSPFGLPADTPPPAYSaqDDSQSATDDQPQSMDTSTVPPDVSP 281
Cdd:PHA03307   195 -PSTPPAAASPRPPRRSS--PISASASSPAPAPGRSAADDAGASS 236
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
164-277 8.47e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 38.58  E-value: 8.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 164 VPRHSEYPPGGHTMIPPVFQQVAESGMPHNVSFSAQGFSAATSGSSATTGVAVAVGTNAAAGVPSPGPSLGSSAPNSPfG 243
Cdd:COG3469   100 STASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSAST-T 178

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1932671850 244 LPADTPPPAYSAQDDSQSATDDQPQSMDTSTVPP 277
Cdd:COG3469   179 PSATTTATATTASGATTPSATTTATTTGPPTPGL 212
 
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 ...
 284-484 1.64e-156

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: 442.40  E-value: 1.64e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 284 YQEPQYWCTIAYYELNSRVGEIFHAQSHSIVIDGFTDPSNNSNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 363
Cdd:cd10497     1 YQEPKYWCSIAYYELNNRVGEAFHASSTSIIVDGFTDPSNNSDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 364 AECLSDSAIFVQSRNCNHSHQFHPTTVCKIPSGCSLKIFNNREFAELLTMAVNNGFEAVYELTKMCIIRMSFVKGWGAEY 443
Cdd:cd10497    81 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1932671850 444 HRQDVTSTPCWIEVHLSGPLQWLDKVLTQMGSPHNPISSVS 484
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 ...
 290-471 3.12e-133

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: 382.50  E-value: 3.12e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 290 WCTIAYYELNSRVGEIFHAQSHSIVIDGFTDPSNNSNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSD 369
Cdd:cd10495     1 WCSISYYELNSRVGEQFKASNPSIIVDGFTDPSNNSDRFCLGLLSNVNRNATIENTRRHIGRGVHLFYVGGEVYAECLSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 370 SAIFVQSRNCNHSHQFHPTTVCKIPSGCSLKIFNNREFAELLTMAVNNGFEAVYELTKMCIIRMSFVKGWGAEYHRQDVT 449
Cdd:cd10495    81 SAIFVQSRNCNLRHGFHPATVCKIPPGCSLKIFNNQSFAQLLEQSVNRGFEAVYELTKMCTIRISFVKGWGAEYHRQDVT 160

                         170       180
                  ....*....|....*....|..
gi 1932671850 450 STPCWIEVHLSGPLQWLDKVLT 471
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 ...
 282-473 1.88e-126

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: 365.79  E-value: 1.88e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 282 VTYQEPQYWCTIAYYELNSRVGEIFHAQSHSIVIDGFTDPSNnSNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGE 361
Cdd:cd10985     1 VTYCEPAFWCSISYYEMNTRVGETFHASQPSLTVDGFTDPSN-SERFCLGLLSNVNRNPQVELTRRHIGKGVRLYYIGGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 362 VYAECLSDSAIFVQSRNCNHSHQFHPTTVCKIPSGCSLKIFNNREFAELLTMAVNNGFEAVYELTKMCIIRMSFVKGWGA 441
Cdd:cd10985    80 VFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLSQSVNQGFEAVYQLTRMCTIRMSFVKGWGA 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1932671850 442 EYHRQDVTSTPCWIEVHLSGPLQWLDKVLTQM 473
Cdd:cd10985   160 EYRRQTVTSTPCWIELHLNGPLQWLDRVLTQM 191
MH2 cd00050
C-terminal Mad Homology 2 (MH2) domain; The MH2 domain is found in the SMAD (small mothers ...
 290-459 1.85e-106

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: 313.77  E-value: 1.85e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 290 WCTIAYYELNSRVGEIFHAQSHSIVIDGFTDPSNnSNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSD 369
Cdd:cd00050     1 WCSIAYYELNTRVGELFHVYSPSVAVDGFTDPSN-GDRFCLGQLSNVNRNETIERTRRHIGKGVHLYYVGGEVWAECLSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 370 SAIFVQSRNCNHSHQFHPTTVCKIPSGCSLKIFNNREFAELLTMAVNNGFEAVYELTKMCIIRMSFVKGWGAEYHRQDVT 449
Cdd:cd00050    80 HAIFVQSRNLDYPHGRHPLTVCKIPPGCSIKVFDNQEFAQLLHQSVNTGFEGVYELTKMCTIRMSFVKGWGPEYHRQDIT 159

                         170
                  ....*....|
gi 1932671850 450 STPCWIEVHL 459
Cdd:cd00050   160 STPCWIEIHL 169
MH2 pfam03166
MH2 domain; This is the MH2 (MAD homology 2) domain found at the carboxy terminus of MAD ...
 288-459 1.03e-97

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: 291.45  E-value: 1.03e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 288 QYWCTIAYYELNSRVGEIFHAQSHSIVIDGFTDPSNNsNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECL 367
Cdd:pfam03166   1 EIWCSVAYYELNTRVGEAFKVSSPNVTVDGFTDPSDG-NRFCLGLLSNVNRNEAVEKVRKHIGKGVRLSYDGGEVWIYNL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 368 SDSAIFVQSRNCNHSHQFHPTTVCKIPSGCSLKIFNNREFAELLTMAVNNGFEAVYELTKMCIIRMSFVKGWGAEYHRQD 447
Cdd:pfam03166  80 SDHPVFVQSPYLNREAGRAPDTVHKVPPGESLKVFDMRKFQQLLSQELRRARLGPQDANKLCSVRISFVKGWGPDYSRQD 159

                         170
                  ....*....|..
gi 1932671850 448 VTSTPCWIEVHL 459
Cdd:pfam03166 160 ITSTPCWIEIHL 171
MH1_SMAD_1_5_9 cd10490
N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The ...
 33-156 2.63e-96

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: 286.32  E-value: 2.63e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  33 FTSPAVKKLLGWKQGDEEEKWAEKAVDSLVKKLKKRKGAIEDLEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 112
Cdd:cd10490     1 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEELEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1932671850 113 CRVWRWPDLQSHHELKPLECCEYPFSAKQKEVCINPYHYKRVES 156
Cdd:cd10490    81 CRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVES 124
DWB smart00524
Domain B in dwarfin family proteins;
289-460 7.98e-96

Domain B in dwarfin family proteins;


Pssm-ID: 197770  Cd Length: 171  Bit Score: 286.51  E-value: 7.98e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  289 YWCTIAYYELNSRVGEIFHAQSHSIVIDGFTDPSNnSNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLS 368
Cdd:smart00524   1 SWCKIAYYELNTRVGETFKVSSPSVTVDGFTDPSD-GNRFCLGQLSNVNRNEATELIRKHIGKGVQLSYENGDVWLYNRS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  369 DSAIFVQSRNCNHSHQFHPTTVCKIPSGCSLKIFNNREFAELLTMAVNNGFEAVYELTKMCIIRMSFVKGWGAEYHRQDV 448
Cdd:smart00524  80 DSPIFVQSPYLDEPGGRTLDTVHKLPPGYSIKVFDMEKFAQLLARELAKGFEGVYDLARMCTIRISFVKGWGPDYSRQTI 159

                          170
                   ....*....|..
gi 1932671850  449 TSTPCWIEVHLS 460
Cdd:smart00524 160 TSTPCWIEVHLN 171
MH1_R-SMAD cd10488
N-terminal Mad Homology 1 (MH1) domain of receptor regulated SMADs; The MH1 is a small ...
 36-156 1.98e-76

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: 235.16  E-value: 1.98e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  36 PAVKKLLGWKQG---DEEEKWAEKAVDSLVKKLKKrKGAIEDLEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 112
Cdd:cd10488     1 PIVKRLLGWKKGeqnGEEEKWAEKAVKSLVKKLKK-KGQLEELEKAISTQNVNTRCVTIPRSLDGRLQVSHRKGLPHVIY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1932671850 113 CRVWRWPDLQSHHELKPLECCEYPFSAKQKEVCINPYHYKRVES 156
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 ...
 34-156 2.41e-74

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: 229.72  E-value: 2.41e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  34 TSPAVKKLLGWKQG--DEEEKWAEKAVDSLVKKLKKrKGAIEDLEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVI 111
Cdd:cd10491     1 TPPVVKRLLGWKKGenGQEEKWSEKAVKSLVKKLKK-TGGLDELEKAITTQNSNTKCITIPRSLDGRLQVSHRKGLPHVI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1932671850 112 YCRVWRWPDLQSHHELKPLECCEYPFSAKQKEVCINPYHYKRVES 156
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 ...
 36-156 2.05e-72

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: 224.77  E-value: 2.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  36 PAVKKLLGWKQGDEEEKWAEKAVDSLVKKLKKRKgAIEDLEKALSCPG-QPSKCVTIPRSLDGRLQVSHRKGLPHVIYCR 114
Cdd:cd00049     1 PIVKRLLGWKQGGEEEKWAKKAVKSLVKKLKEKK-QLDSLEKAITTQGgVPSKCVTIPRSLDGRLQVAHRKGLPHVIYCR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1932671850 115 VWRWPDLQSHHELKPLECCEYPFSAKQKEVCINPYHYKRVES 156
Cdd:cd00049    80 LWRWPDLHSHHELKALELCQFAFNMKKDEVCVNPYHYQRVES 121
DWA smart00523
Domain A in dwarfin family proteins;
49-158 1.23e-60

Domain A in dwarfin family proteins;


Pssm-ID: 214708  Cd Length: 109  Bit Score: 193.75  E-value: 1.23e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850   49 EEEKWAEKAVDSLVKKLKKRKgaIEDLEKALSCPG-QPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHEL 127
Cdd:smart00523   1 VEEKWAKKATESLLKKLKKKQ--LEELLQAVESKGgPPTRCVLIPRSLDGRLQVAHRKGLPHVLYCRLFRWPDLQSPHEL 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1932671850  128 KPLECCEYPFSAKQKEVCINPYHYKRVESPV 158
Cdd:smart00523  79 KALPTCEHAFESKSDEVCCNPYHYSRVERPE 109
MH1 pfam03165
MH1 domain; The MH1 (MAD homology 1) domain is found at the amino terminus of MAD related ...
 54-155 1.25e-57

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: 186.04  E-value: 1.25e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  54 AEKAVDSLVKKLKKRKGAIEDLEKALSCPG-QPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLEC 132
Cdd:pfam03165   1 LKKAVESLLKKLKKKIQQLEELELAVESRGdPPTGCVTIPRSLDGRLQVAGRKGLPHVIYCRLWRWPDLQSQHELKAIPT 80

                          90       100
                  ....*....|....*....|...
gi 1932671850 133 CEYPFSAKQKEVCINPYHYKRVE 155
Cdd:pfam03165  81 CETAFESKKDEVCINPYHYSRVE 103
MH2_SMAD_4 cd10498
C-terminal Mad Homology 2 (MH2) domain in SMAD4; The MH2 domain is located at the C-terminus ...
 287-470 3.64e-56

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: 186.52  E-value: 3.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 287 PQYWCTIAYYELNSRVGEIFHAQS--HSIVIDGFTDPSNnSNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVG-GEVY 363
Cdd:cd10498     1 PEYWCSIAYFELDTQVGETFKVPSscPTVTVDGYVDPSG-GNRFCLGQLSNVHRTEASERARLHIGKGVQLDCKGeGDVW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 364 AECLSDSAIFVQSRNCNHSHQFHP-TTVCKIPSGCSLKIFNNRE-FAELLTMAVNNGFEA-------------------- 421
Cdd:cd10498    80 LRCLSDHSVFVQSYYLDREAGRAPgDAVHKIYPSAYIKVFDLRQcHRQMQQQAATAQAAAaaqaaavagnipgpgsvggi 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1932671850 422 -------------VYELTKMCIIRMSFVKGWGAEYHRQDVTSTPCWIEVHLSGPLQWLDKVL 470
Cdd:cd10498   160 apaislsaaagigVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVL 221
MH1_SMAD_4 cd10492
N-terminal Mad Homology 1 (MH1) domain in SMAD4; The MH1 is a small DNA-binding domain present ...
 38-156 5.11e-46

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: 156.46  E-value: 5.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  38 VKKLLGWKQGDEEEKWAEKAVDSLVKKLKKRKGAIEDLEKALSCPG-QPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVW 116
Cdd:cd10492     7 VHSLMCHRQGGESESFAKRAIESLVKKLKDKRDELDSLITAITSNGaHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARIW 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1932671850 117 RWPDLQShHELKPLECCEYPFSAKQKEVCINPYHYKRVES 156
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 ...
 290-460 1.47e-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: 129.78  E-value: 1.47e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 290 WCTIAYYELNSRVGEIFHAQSHSIVIdgFTD-PSNNSnrFCLG-LLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECL 367
Cdd:cd10496     1 WCTIAYWELRERVGRLYPVKQPAVNI--FDDlPKGDG--FCLGaLNRQGNASEAVARVRSKIGLGVTLSREPDGVWIYNR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 368 SDSAIFVQSRNCNHSHQfHPTTVCKIPSGCSLKIFNnREFAELLTMAvNNGFEAVYELTKMCIiRMSFVKGWGAEYHRQD 447
Cdd:cd10496    77 SEYPIFVNSPTLDSPPS-RNLLVTKVPPGYSLKVFD-YERAALLQRR-DDHFSPQGPVDPNSV-RISFVKGWGPNYSRQF 152

                         170
                  ....*....|...
gi 1932671850 448 VTSTPCWIEVHLS 460
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 ...
 286-460 3.76e-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: 109.91  E-value: 3.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 286 EPQYWCTIAYYELNSRVGEIFHAQSHSIVIdgFTDPSNNSNrFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAE 365
Cdd:cd10499     6 KRSHWCSVAYWEHRTRVGRLYAVYDQSVSI--FYDLPQGSG-FCLGQLNLEQRSESVRRTRSKIGYGILLSKEPDGVWAY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 366 CLSDSAIFVQSRNCNHSHQfHPTTVCKIPSGCSLKIFNNREFAELLTMAVNNGFEAVYELTKmciIRMSFVKGWGAEYHR 445
Cdd:cd10499    83 NRSEHPIFVNSPTLDIPGS-RTLVVRKVPPGYSIKVFDYERSCLLQHTAEPELADGPYDPNS---VRISFAKGWGPCYSR 158

                         170
                  ....*....|....*
gi 1932671850 446 QDVTSTPCWIEVHLS 460
Cdd:cd10499   159 QFITSCPCWLEILLN 173
MH1_SMAD_6_7 cd10489
N-terminal Mad Homology 1 (MH1) domain in SMAD6 and SMAD7; The MH1 is a small DNA-binding ...
 56-157 5.31e-20

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: 85.51  E-value: 5.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  56 KAVDSLVKKLKKRKgaIEDLEKAL-SCPGQPSKCVTIPRSLdgrlqVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCE 134
Cdd:cd10489    25 AAFHALLKRLKEKQ--LELLLQAVeSRGGDYLACVLLPRRD-----PRSMPQDPHVLCCQLFRWPDLRHSSELKRLPTCE 97

                          90       100
                  ....*....|....*....|....
gi 1932671850 135 ypfSAKQKE-VCINPYHYKRVESP 157
Cdd:cd10489    98 ---SAKDPVyVCCNPYHWSRLCRP 118
MH2_SMAD_7 cd10500
C-terminal Mad Homology 2 (MH2) domain in SMAD7; The MH2 domain is located at the C-terminus ...
 286-457 3.74e-19

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: 84.71  E-value: 3.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 286 EPQYWCTIAYYELNSRVGEIFHAQSHSIviDGFTD-PSNNSnrFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYA 364
Cdd:cd10500     4 DQSHWCVVAYWEEKTRVGRLYSVQEPSL--DIFYDlPQGNG--FCLGQLNSDNKSQLVQKVRSKIGYGIQLTREVDGVWV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 365 ECLSDSAIFVQSRNCNHSHQfHPTTVCKIPSGCSLKIFnnrEFAELLTMAVNNGFEAVYELTKMCIIRMSFVKGWGAEYH 444
Cdd:cd10500    80 YNRSSYPIFIKSATLDNPDS-RTLLVHKVFPGFSIKAF---DYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYT 155

                         170
                  ....*....|...
gi 1932671850 445 RQDVTSTPCWIEV 457
Cdd:cd10500   156 RQFISSCPCWLEV 168
MH1_SMAD_6 cd10493
N-terminal Mad Homology 1 (MH1) domain in SMAD6; The MH1 is a small DNA-binding domain present ...
 47-158 1.51e-18

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: 80.97  E-value: 1.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  47 GDEEEKwaeKAVDSLVKKLKKRkgAIEDLEKAL-SCPGQPSKCVTIPRSldgRLQVSHRKGLPHVIYCRVWRWPDLQSHH 125
Cdd:cd10493     9 LEQELK---SVTYALLKRLKER--SLDVLLEAVeSRGGLPSGCVMVPRT---ELRLGGRRVPPQLLLCRLFRWPDLQHPA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1932671850 126 ELKPLECCEYPFSAKQKEVCINPYHYKRVESPV 158
Cdd:cd10493    81 QLKALCHCQSFGAQDGPTVCCNPYHYSRLCGPE 113
MH1_SMAD_7 cd10494
N-terminal Mad Homology 1 (MH1) domain in SMAD7; The MH1 is a small DNA-binding domain present ...
 60-157 7.78e-14

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: 67.98  E-value: 7.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  60 SLVKKLKKRKgaIEDLEKALSCPGQP-SKCVTIPRSLDGRLQvSHRKGLPhVIYCRVWRWPDLQSHHELKPLECCEYPFS 138
Cdd:cd10494    26 SVLKKLKERQ--LEGLLQAVESRGGArTPCLLLPARLDARLG-QQSYSLP-LLLCKVFRWPDLRHSSEVKRLSCCESYGK 101

                          90       100
                  ....*....|....*....|..
gi 1932671850 139 AKQKEVCINPYHYKR---VESP 157
Cdd:cd10494   102 INPELVCCNPHHLSRlceLESP 123
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 133-315 1.33e-03

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 41.01  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 133 CEYPFSAKQkevciNPYHYKRVESPVLPPVLVPRHSEYPPGGHTmipPVFQQVAESGMPhnvsfsaQGFSAATSGSSATT 212
Cdd:cd23959   115 VPNPFSASS-----STQRETHKTAQVAPPKAEPQTAPVTPFGQL---PMFGQHPPPAKP-------LPAAAAAQQSSASP 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 213 GVavavgtnaaagVPSPGPSLGSSApnSPFGLPADTPPPAYSAQDDSQSATDDQP---QSMDTSTVPPDVSPVTYQEPQY 289
Cdd:cd23959   180 GE-----------VASPFASGTVSA--SPFATATDTAPSSGAPDGFPAEASAPSPfaaPASAASFPAAPVANGEAATPTH 246

                         170       180
                  ....*....|....*....|....*..
gi 1932671850 290 WCTIAYYELNSRVGEIFHAQS-HSIVI 315
Cdd:cd23959   247 ACTICGKAFSTHEGLRMHSKAkHGVEL 273
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 157-281 7.53e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.00  E-value: 7.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850  157 PVLPPVLVPRHSEYPPGGHTMIPPvfqqvaesgmphNVSFSAQGFSAATSGSSAttgVAVAVGTNAAAGVPSPGPSLGss 236
Cdd:PHA03307   132 PDLSEMLRPVGSPGPPPAASPPAA------------GASPAAVASDAASSRQAA---LPLSSPEETARAPSSPPAEPP-- 194

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1932671850  237 aPNSPFGLPADTPPPAYSaqDDSQSATDDQPQSMDTSTVPPDVSP 281
Cdd:PHA03307   195 -PSTPPAAASPRPPRRSS--PISASASSPAPAPGRSAADDAGASS 236
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
164-277 8.47e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 38.58  E-value: 8.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 164 VPRHSEYPPGGHTMIPPVFQQVAESGMPHNVSFSAQGFSAATSGSSATTGVAVAVGTNAAAGVPSPGPSLGSSAPNSPfG 243
Cdd:COG3469   100 STASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSAST-T 178

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1932671850 244 LPADTPPPAYSAQDDSQSATDDQPQSMDTSTVPP 277
Cdd:COG3469   179 PSATTTATATTASGATTPSATTTATTTGPPTPGL 212
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 162-281 9.26e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 38.81  E-value: 9.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1932671850 162 VLVPRHSEYPPGGHTMIPPVfqqvaESGMPhnvsFSAQGFSAATSGSSATTGVAVAV-GTNAAAGVPSPGPSLGSSAPNS 240
Cdd:PRK07764  362 MLLPSASDDERGLLARLERL-----ERRLG----VAGGAGAPAAAAPSAAAAAPAAApAPAAAAPAAAAAPAPAAAPQPA 432

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1932671850 241 PFGLPADTPPPAYSAQDDSQSATDD-------QPQSMDTSTVPPDVSP 281
Cdd:PRK07764  433 PAPAPAPAPPSPAGNAPAGGAPSPPpaaapsaQPAPAPAAAPEPTAAP 480
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH