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Conserved domains on  [gi|1846360069|gb|KAF4794756|]
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hypothetical protein TURU_099041 [Turdus rufiventris]

Protein Classification

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 ...
 632-832 4.17e-153

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: 445.86  E-value: 4.17e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 632 YEEPQHWCSVAYYELNNRVGETFQASSRSILIDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 711
Cdd:cd10497     1 YQEPKYWCSIAYYELNNRVGEAFHASSTSIIVDGFTDPSNNSDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 712 AECVSDSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKIFNNQLFAQLLAQSVNHGFEVVYELTKMCTIRMSFVKGWGAEY 791
Cdd:cd10497    81 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1846360069 792 HRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS 832
Cdd:cd10497   161 HRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS 201
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 67-285 1.95e-117

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


:

Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 354.18  E-value: 1.95e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  67 VVVPSYNEENRLPLMMDEALDYLEKRqkqdPSFTYEVIVVNDGSKDQTAKVAKEYSKKYGSDkVRVISLEKNRGKGGAVR 146
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEER----PSFSYEIIVVDDGSKDGTAEVARKLARKNPAL-IRVLTLPKNRGKGGAVR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 147 TGVFSSRGQKILMADADGATKFADIEKVEEGLKNlrpwpKGMAISCGSRAHLEKDSIAKRSYFRTLLMYGFHFLVWFLCV 226
Cdd:cd04188    76 AGMLAARGDYILFADADLATPFEELEKLEEALKT-----SGYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1846360069 227 KEIRDTQCGFKLLTREAALQTFSNLHIERWAFDVELLYIAQCMKIPIAEVAVNWTEIED 285
Cdd:cd04188   151 LGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPG 209
MH1_SMAD_1_5_9 cd10490
N-terminal Mad Homology 1 (MH1) domain in SMAD1, SMAD5 and SMAD9 (also known as SMAD8); The ...
 378-501 1.24e-92

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: 1.24e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 378 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGAMEELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 457
Cdd:cd10490     1 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEELEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1846360069 458 CRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVET 501
Cdd:cd10490    81 CRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVES 124
 
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 ...
 632-832 4.17e-153

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: 445.86  E-value: 4.17e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 632 YEEPQHWCSVAYYELNNRVGETFQASSRSILIDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 711
Cdd:cd10497     1 YQEPKYWCSIAYYELNNRVGEAFHASSTSIIVDGFTDPSNNSDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 712 AECVSDSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKIFNNQLFAQLLAQSVNHGFEVVYELTKMCTIRMSFVKGWGAEY 791
Cdd:cd10497    81 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1846360069 792 HRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS 832
Cdd:cd10497   161 HRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS 201
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 67-285 1.95e-117

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 354.18  E-value: 1.95e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  67 VVVPSYNEENRLPLMMDEALDYLEKRqkqdPSFTYEVIVVNDGSKDQTAKVAKEYSKKYGSDkVRVISLEKNRGKGGAVR 146
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEER----PSFSYEIIVVDDGSKDGTAEVARKLARKNPAL-IRVLTLPKNRGKGGAVR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 147 TGVFSSRGQKILMADADGATKFADIEKVEEGLKNlrpwpKGMAISCGSRAHLEKDSIAKRSYFRTLLMYGFHFLVWFLCV 226
Cdd:cd04188    76 AGMLAARGDYILFADADLATPFEELEKLEEALKT-----SGYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1846360069 227 KEIRDTQCGFKLLTREAALQTFSNLHIERWAFDVELLYIAQCMKIPIAEVAVNWTEIED 285
Cdd:cd04188   151 LGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPG 209
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 65-284 4.72e-103

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 321.72  E-value: 4.72e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  65 LSVVVPSYNEENRLPLMMDEALDYLEKRQKQDPSFTYEVIVVNDGSKDQTAKVAKEYSKKYGSDKV--RVISLEKNRGKG 142
Cdd:PTZ00260   72 LSIVIPAYNEEDRLPKMLKETIKYLESRSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINPNIdiRLLSLLRNKGKG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 143 GAVRTGVFSSRGQKILMADADGATKFADIEKVEEglKNLRPWPKGMAISCGSRAHLEK-DSIAKRSYFRTLLMYGFHFLV 221
Cdd:PTZ00260  152 GAVRIGMLASRGKYILMVDADGATDIDDFDKLED--IMLKIEQNGLGIVFGSRNHLVDsDVVAKRKWYRNILMYGFHFIV 229

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1846360069 222 WFLCVKEIRDTQCGFKLLTREAALQTFSNLHIERWAFDVELLYIAQCMKIPIAEVAVNWTEIE 284
Cdd:PTZ00260  230 NTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTEVE 292
MH2 pfam03166
MH2 domain; This is the MH2 (MAD homology 2) domain found at the carboxy terminus of MAD ...
 636-808 6.00e-96

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: 296.84  E-value: 6.00e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 636 QHWCSVAYYELNNRVGETFQASSRSILIDGFTDPSNNkNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECV 715
Cdd:pfam03166   1 EIWCSVAYYELNTRVGEAFKVSSPNVTVDGFTDPSDG-NRFCLGLLSNVNRNEAVEKVRKHIGKGVRLSYDGGEVWIYNL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 716 SDSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKIFNNQLFAQLLAQSVNHGFEVVYELTKMCTIRMSFVKGWGAEYHRQD 795
Cdd:pfam03166  80 SDHPVFVQSPYLNREAGRAPDTVHKVPPGESLKVFDMRKFQQLLSQELRRARLGPQDANKLCSVRISFVKGWGPDYSRQD 159

                         170
                  ....*....|...
gi 1846360069 796 VTSTPCWIEIHLH 808
Cdd:pfam03166 160 ITSTPCWIEIHLH 172
DWB smart00524
Domain B in dwarfin family proteins;
637-808 2.50e-95

Domain B in dwarfin family proteins;


Pssm-ID: 197770  Cd Length: 171  Bit Score: 295.37  E-value: 2.50e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  637 HWCSVAYYELNNRVGETFQASSRSILIDGFTDPSNNkNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECVS 716
Cdd:smart00524   1 SWCKIAYYELNTRVGETFKVSSPSVTVDGFTDPSDG-NRFCLGQLSNVNRNEATELIRKHIGKGVQLSYENGDVWLYNRS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  717 DSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKIFNNQLFAQLLAQSVNHGFEVVYELTKMCTIRMSFVKGWGAEYHRQDV 796
Cdd:smart00524  80 DSPIFVQSPYLDEPGGRTLDTVHKLPPGYSIKVFDMEKFAQLLARELAKGFEGVYDLARMCTIRISFVKGWGPDYSRQTI 159

                          170
                   ....*....|..
gi 1846360069  797 TSTPCWIEIHLH 808
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 ...
 378-501 1.24e-92

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: 1.24e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 378 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGAMEELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 457
Cdd:cd10490     1 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEELEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1846360069 458 CRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVET 501
Cdd:cd10490    81 CRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVES 124
DWA smart00523
Domain A in dwarfin family proteins;
394-503 8.06e-51

Domain A in dwarfin family proteins;


Pssm-ID: 214708  Cd Length: 109  Bit Score: 173.33  E-value: 8.06e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  394 EEEKWAEKAVDSLVKKLKKkkGAMEELERALSCPG-QPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHEL 472
Cdd:smart00523   1 VEEKWAKKATESLLKKLKK--KQLEELLQAVESKGgPPTRCVLIPRSLDGRLQVAHRKGLPHVLYCRLFRWPDLQSPHEL 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1846360069  473 KPLECCEFPFGSKQKEVCINPYHYRRVETPV 503
Cdd:smart00523  79 KALPTCEHAFESKSDEVCCNPYHYSRVERPE 109
MH1 pfam03165
MH1 domain; The MH1 (MAD homology 1) domain is found at the amino terminus of MAD related ...
 399-500 1.60e-48

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: 1.60e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 399 AEKAVDSLVKKLKKKKGAMEELERALSCPG-QPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLEC 477
Cdd:pfam03165   1 LKKAVESLLKKLKKKIQQLEELELAVESRGdPPTGCVTIPRSLDGRLQVAGRKGLPHVIYCRLWRWPDLQSQHELKAIPT 80

                          90       100
                  ....*....|....*....|...
gi 1846360069 478 CEFPFGSKQKEVCINPYHYRRVE 500
Cdd:pfam03165  81 CETAFESKKDEVCINPYHYSRVE 103
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 65-282 5.91e-31

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 120.58  E-value: 5.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  65 LSVVVPSYNEENRLPlmmdEALDYLEKRQKQDpsftYEVIVVNDGSKDQTAKVAKEYSKKYgsDKVRVISLEKNRGKGGA 144
Cdd:COG0463     4 VSVVIPTYNEEEYLE----EALESLLAQTYPD----FEIIVVDDGSTDGTAEILRELAAKD--PRIRVIRLERNRGKGAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 145 VRTGVFSSRGQKILMADADGatkFADIEKVEEGLKNLRPWPKGMAIscGSRAHLEKDSIakrsyFRTLLMYGFHFLVWFL 224
Cdd:COG0463    74 RNAGLAAARGDYIAFLDADD---QLDPEKLEELVAALEEGPADLVY--GSRLIREGESD-----LRRLGSRLFNLVRLLT 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1846360069 225 CvkeIRDTQCGFKLLTREAALQTFSNlhiERWAFDVELLYIAQcMKIPIAEVAVNWTE 282
Cdd:COG0463   144 N---LPDSTSGFRLFRREVLEELGFD---EGFLEDTELLRALR-HGFRIAEVPVRYRA 194
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 66-243 4.70e-25

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 102.47  E-value: 4.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  66 SVVVPSYNEENRLPlmmdEALDYLeKRQKQDPsftYEVIVVNDGSKDQTAKVAKEYSKKYgsDKVRVISLEKNRGKGGAV 145
Cdd:pfam00535   1 SVIIPTYNEEKYLL----ETLESL-LNQTYPN---FEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGAR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 146 RTGVFSSRGQKILMADADGATKFADIEKVEEGLKNLRPwpkgmAISCGSRAHLEKDSIAKRSYFRTLLMYGFHFLVWFLC 225
Cdd:pfam00535  71 NAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGA-----DVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLL 145

                         170
                  ....*....|....*...
gi 1846360069 226 VKEIRDTQCGFKLLTREA 243
Cdd:pfam00535 146 GLNLPFLIGGFALYRREA 163
 
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 ...
 632-832 4.17e-153

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: 445.86  E-value: 4.17e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 632 YEEPQHWCSVAYYELNNRVGETFQASSRSILIDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 711
Cdd:cd10497     1 YQEPKYWCSIAYYELNNRVGEAFHASSTSIIVDGFTDPSNNSDRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 712 AECVSDSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKIFNNQLFAQLLAQSVNHGFEVVYELTKMCTIRMSFVKGWGAEY 791
Cdd:cd10497    81 AECLSDSSIFVQSRNCNYHHGFHPTTVCKIPPGCSLKIFNNQEFAQLLSQSVNHGFEAVYELTKMCTIRMSFVKGWGAEY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1846360069 792 HRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS 832
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 ...
 638-819 3.71e-136

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: 401.37  E-value: 3.71e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 638 WCSVAYYELNNRVGETFQASSRSILIDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECVSD 717
Cdd:cd10495     1 WCSISYYELNSRVGEQFKASNPSIIVDGFTDPSNNSDRFCLGLLSNVNRNATIENTRRHIGRGVHLFYVGGEVYAECLSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 718 SSIFVQSRNCNYQHGFHPATVCKIPSGCSLKIFNNQLFAQLLAQSVNHGFEVVYELTKMCTIRMSFVKGWGAEYHRQDVT 797
Cdd:cd10495    81 SAIFVQSRNCNLRHGFHPATVCKIPPGCSLKIFNNQSFAQLLEQSVNRGFEAVYELTKMCTIRISFVKGWGAEYHRQDVT 160

                         170       180
                  ....*....|....*....|..
gi 1846360069 798 STPCWIEIHLHGPLQWLDKVLT 819
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 ...
 630-821 1.01e-123

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: 370.03  E-value: 1.01e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 630 VCYEEPQHWCSVAYYELNNRVGETFQASSRSILIDGFTDPSNNkNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGE 709
Cdd:cd10985     1 VTYCEPAFWCSISYYEMNTRVGETFHASQPSLTVDGFTDPSNS-ERFCLGLLSNVNRNPQVELTRRHIGKGVRLYYIGGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 710 VYAECVSDSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKIFNNQLFAQLLAQSVNHGFEVVYELTKMCTIRMSFVKGWGA 789
Cdd:cd10985    80 VFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLSQSVNQGFEAVYQLTRMCTIRMSFVKGWGA 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1846360069 790 EYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQM 821
Cdd:cd10985   160 EYRRQTVTSTPCWIELHLNGPLQWLDRVLTQM 191
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 67-285 1.95e-117

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 354.18  E-value: 1.95e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  67 VVVPSYNEENRLPLMMDEALDYLEKRqkqdPSFTYEVIVVNDGSKDQTAKVAKEYSKKYGSDkVRVISLEKNRGKGGAVR 146
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEER----PSFSYEIIVVDDGSKDGTAEVARKLARKNPAL-IRVLTLPKNRGKGGAVR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 147 TGVFSSRGQKILMADADGATKFADIEKVEEGLKNlrpwpKGMAISCGSRAHLEKDSIAKRSYFRTLLMYGFHFLVWFLCV 226
Cdd:cd04188    76 AGMLAARGDYILFADADLATPFEELEKLEEALKT-----SGYDIAIGSRAHLASAAVVKRSWLRNLLGRGFNFLVRLLLG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1846360069 227 KEIRDTQCGFKLLTREAALQTFSNLHIERWAFDVELLYIAQCMKIPIAEVAVNWTEIED 285
Cdd:cd04188   151 LGIKDTQCGFKLFTRDAARRLFPRLHLERWAFDVELLVLARRLGYPIEEVPVRWVEIPG 209
MH2 cd00050
C-terminal Mad Homology 2 (MH2) domain; The MH2 domain is found in the SMAD (small mothers ...
 638-808 3.38e-108

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: 328.80  E-value: 3.38e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 638 WCSVAYYELNNRVGETFQASSRSILIDGFTDPSNnKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECVSD 717
Cdd:cd00050     1 WCSIAYYELNTRVGELFHVYSPSVAVDGFTDPSN-GDRFCLGQLSNVNRNETIERTRRHIGKGVHLYYVGGEVWAECLSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 718 SSIFVQSRNCNYQHGFHPATVCKIPSGCSLKIFNNQLFAQLLAQSVNHGFEVVYELTKMCTIRMSFVKGWGAEYHRQDVT 797
Cdd:cd00050    80 HAIFVQSRNLDYPHGRHPLTVCKIPPGCSIKVFDNQEFAQLLHQSVNTGFEGVYELTKMCTIRMSFVKGWGPEYHRQDIT 159

                         170
                  ....*....|.
gi 1846360069 798 STPCWIEIHLH 808
Cdd:cd00050   160 STPCWIEIHLH 170
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 65-284 4.72e-103

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 321.72  E-value: 4.72e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  65 LSVVVPSYNEENRLPLMMDEALDYLEKRQKQDPSFTYEVIVVNDGSKDQTAKVAKEYSKKYGSDKV--RVISLEKNRGKG 142
Cdd:PTZ00260   72 LSIVIPAYNEEDRLPKMLKETIKYLESRSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINPNIdiRLLSLLRNKGKG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 143 GAVRTGVFSSRGQKILMADADGATKFADIEKVEEglKNLRPWPKGMAISCGSRAHLEK-DSIAKRSYFRTLLMYGFHFLV 221
Cdd:PTZ00260  152 GAVRIGMLASRGKYILMVDADGATDIDDFDKLED--IMLKIEQNGLGIVFGSRNHLVDsDVVAKRKWYRNILMYGFHFIV 229

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1846360069 222 WFLCVKEIRDTQCGFKLLTREAALQTFSNLHIERWAFDVELLYIAQCMKIPIAEVAVNWTEIE 284
Cdd:PTZ00260  230 NTICGTNLKDTQCGFKLFTRETARIIFPSLHLERWAFDIEIVMIAQKLNLPIAEVPVNWTEVE 292
MH2 pfam03166
MH2 domain; This is the MH2 (MAD homology 2) domain found at the carboxy terminus of MAD ...
 636-808 6.00e-96

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: 296.84  E-value: 6.00e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 636 QHWCSVAYYELNNRVGETFQASSRSILIDGFTDPSNNkNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECV 715
Cdd:pfam03166   1 EIWCSVAYYELNTRVGEAFKVSSPNVTVDGFTDPSDG-NRFCLGLLSNVNRNEAVEKVRKHIGKGVRLSYDGGEVWIYNL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 716 SDSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKIFNNQLFAQLLAQSVNHGFEVVYELTKMCTIRMSFVKGWGAEYHRQD 795
Cdd:pfam03166  80 SDHPVFVQSPYLNREAGRAPDTVHKVPPGESLKVFDMRKFQQLLSQELRRARLGPQDANKLCSVRISFVKGWGPDYSRQD 159

                         170
                  ....*....|...
gi 1846360069 796 VTSTPCWIEIHLH 808
Cdd:pfam03166 160 ITSTPCWIEIHLH 172
DWB smart00524
Domain B in dwarfin family proteins;
637-808 2.50e-95

Domain B in dwarfin family proteins;


Pssm-ID: 197770  Cd Length: 171  Bit Score: 295.37  E-value: 2.50e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  637 HWCSVAYYELNNRVGETFQASSRSILIDGFTDPSNNkNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECVS 716
Cdd:smart00524   1 SWCKIAYYELNTRVGETFKVSSPSVTVDGFTDPSDG-NRFCLGQLSNVNRNEATELIRKHIGKGVQLSYENGDVWLYNRS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  717 DSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKIFNNQLFAQLLAQSVNHGFEVVYELTKMCTIRMSFVKGWGAEYHRQDV 796
Cdd:smart00524  80 DSPIFVQSPYLDEPGGRTLDTVHKLPPGYSIKVFDMEKFAQLLARELAKGFEGVYDLARMCTIRISFVKGWGPDYSRQTI 159

                          170
                   ....*....|..
gi 1846360069  797 TSTPCWIEIHLH 808
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 ...
 378-501 1.24e-92

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: 1.24e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 378 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGAMEELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 457
Cdd:cd10490     1 FTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGALEELEKALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1846360069 458 CRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVET 501
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 ...
 381-501 9.73e-69

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: 222.84  E-value: 9.73e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 381 PAVKRLLGWKQG---DEEEKWAEKAVDSLVKKLKKKkGAMEELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIY 457
Cdd:cd10488     1 PIVKRLLGWKKGeqnGEEEKWAEKAVKSLVKKLKKK-GQLEELEKAISTQNVNTRCVTIPRSLDGRLQVSHRKGLPHVIY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1846360069 458 CRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVET 501
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 ...
 379-501 3.32e-65

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: 213.55  E-value: 3.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 379 TSPAVKRLLGWKQG--DEEEKWAEKAVDSLVKKLKKKkGAMEELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVI 456
Cdd:cd10491     1 TPPVVKRLLGWKKGenGQEEKWSEKAVKSLVKKLKKT-GGLDELEKAITTQNSNTKCITIPRSLDGRLQVSHRKGLPHVI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1846360069 457 YCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVET 501
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 ...
 381-501 1.04e-63

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: 209.37  E-value: 1.04e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 381 PAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKkGAMEELERALSCPG-QPSKCVTIPRSLDGRLQVSHRKGLPHVIYCR 459
Cdd:cd00049     1 PIVKRLLGWKQGGEEEKWAKKAVKSLVKKLKEK-KQLDSLEKAITTQGgVPSKCVTIPRSLDGRLQVAHRKGLPHVIYCR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1846360069 460 VWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVET 501
Cdd:cd00049    80 LWRWPDLHSHHELKALELCQFAFNMKKDEVCVNPYHYQRVES 121
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 67-266 2.88e-57

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 193.94  E-value: 2.88e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  67 VVVPSYNEENRLPLMMDEALDYLEKrqkqdpSFTYEVIVVNDGSKDQTAKVAKEYSKKYGsdKVRVISLEKNRGKGGAVR 146
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEE------GYDYEIIVVDDGSTDGTAEIARELAARVP--RVRVIRLSRNFGKGAAVR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 147 TGVFSSRGQKILMADADGATKFADIEKVEEglknlRPWPKGMAISCGSRAHleKDSIAKRSYFRTLLMYGFHFLVWFLCV 226
Cdd:cd04179    73 AGFKAARGDIVVTMDADLQHPPEDIPKLLE-----KLLEGGADVVIGSRFV--RGGGAGMPLLRRLGSRLFNFLIRLLLG 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1846360069 227 KEIRDTQCGFKLLTREAALQTFSNLHIERWAFDVELLYIA 266
Cdd:cd04179   146 VRISDTQSGFRLFRREVLEALLSLLESNGFEFGLELLVGA 185
MH2_SMAD_4 cd10498
C-terminal Mad Homology 2 (MH2) domain in SMAD4; The MH2 domain is located at the C-terminus ...
 635-818 1.73e-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: 193.46  E-value: 1.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 635 PQHWCSVAYYELNNRVGETFQASSR--SILIDGFTDPSNNkNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVG-GEVY 711
Cdd:cd10498     1 PEYWCSIAYFELDTQVGETFKVPSScpTVTVDGYVDPSGG-NRFCLGQLSNVHRTEASERARLHIGKGVQLDCKGeGDVW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 712 AECVSDSSIFVQSRNCNYQHGFHPA-TVCKIPSGCSLKIFN-NQLFAQLLAQSVNHGFEV-------------------- 769
Cdd:cd10498    80 LRCLSDHSVFVQSYYLDREAGRAPGdAVHKIYPSAYIKVFDlRQCHRQMQQQAATAQAAAaaqaaavagnipgpgsvggi 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1846360069 770 -------------VYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVL 818
Cdd:cd10498   160 apaislsaaagigVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVL 221
DWA smart00523
Domain A in dwarfin family proteins;
394-503 8.06e-51

Domain A in dwarfin family proteins;


Pssm-ID: 214708  Cd Length: 109  Bit Score: 173.33  E-value: 8.06e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  394 EEEKWAEKAVDSLVKKLKKkkGAMEELERALSCPG-QPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHEL 472
Cdd:smart00523   1 VEEKWAKKATESLLKKLKK--KQLEELLQAVESKGgPPTRCVLIPRSLDGRLQVAHRKGLPHVLYCRLFRWPDLQSPHEL 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1846360069  473 KPLECCEFPFGSKQKEVCINPYHYRRVETPV 503
Cdd:smart00523  79 KALPTCEHAFESKSDEVCCNPYHYSRVERPE 109
MH1 pfam03165
MH1 domain; The MH1 (MAD homology 1) domain is found at the amino terminus of MAD related ...
 399-500 1.60e-48

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: 1.60e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 399 AEKAVDSLVKKLKKKKGAMEELERALSCPG-QPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLEC 477
Cdd:pfam03165   1 LKKAVESLLKKLKKKIQQLEELELAVESRGdPPTGCVTIPRSLDGRLQVAGRKGLPHVIYCRLWRWPDLQSQHELKAIPT 80

                          90       100
                  ....*....|....*....|...
gi 1846360069 478 CEFPFGSKQKEVCINPYHYRRVE 500
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 ...
 383-499 3.54e-37

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: 135.66  E-value: 3.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 383 VKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGAMEELERALSCPG-QPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVW 461
Cdd:cd10492     7 VHSLMCHRQGGESESFAKRAIESLVKKLKDKRDELDSLITAITSNGaHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARIW 86

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1846360069 462 RWPDLQShHELKPLECCEFPFGSKQKEVCINPYHYRRV 499
Cdd:cd10492    87 RWPDLHK-NELKHVKFCQYAFDLKCDSVCVNPYHYERV 123
MH2_I-SMAD cd10496
C-terminal Mad Homology 2 (MH2) domain in Inhibitory SMADs; The MH2 domain is located at the ...
 638-807 1.24e-32

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: 124.00  E-value: 1.24e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 638 WCSVAYYELNNRVGETFQASSRSILIdgFTDPSNNKNrFCLG-LLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECVS 716
Cdd:cd10496     1 WCTIAYWELRERVGRLYPVKQPAVNI--FDDLPKGDG-FCLGaLNRQGNASEAVARVRSKIGLGVTLSREPDGVWIYNRS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 717 DSSIFVQSRNCNYQHGFHPaTVCKIPSGCSLKIFNNQLFAQLlaQSVNHGFE----VVYEltkmcTIRMSFVKGWGAEYH 792
Cdd:cd10496    78 EYPIFVNSPTLDSPPSRNL-LVTKVPPGYSLKVFDYERAALL--QRRDDHFSpqgpVDPN-----SVRISFVKGWGPNYS 149

                         170
                  ....*....|....*
gi 1846360069 793 RQDVTSTPCWIEIHL 807
Cdd:cd10496   150 RQFITSCPCWLEILL 164
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 65-282 5.91e-31

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 120.58  E-value: 5.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  65 LSVVVPSYNEENRLPlmmdEALDYLEKRQKQDpsftYEVIVVNDGSKDQTAKVAKEYSKKYgsDKVRVISLEKNRGKGGA 144
Cdd:COG0463     4 VSVVIPTYNEEEYLE----EALESLLAQTYPD----FEIIVVDDGSTDGTAEILRELAAKD--PRIRVIRLERNRGKGAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 145 VRTGVFSSRGQKILMADADGatkFADIEKVEEGLKNLRPWPKGMAIscGSRAHLEKDSIakrsyFRTLLMYGFHFLVWFL 224
Cdd:COG0463    74 RNAGLAAARGDYIAFLDADD---QLDPEKLEELVAALEEGPADLVY--GSRLIREGESD-----LRRLGSRLFNLVRLLT 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1846360069 225 CvkeIRDTQCGFKLLTREAALQTFSNlhiERWAFDVELLYIAQcMKIPIAEVAVNWTE 282
Cdd:COG0463   144 N---LPDSTSGFRLFRREVLEELGFD---EGFLEDTELLRALR-HGFRIAEVPVRYRA 194
MH2_SMAD_6 cd10499
C-terminal Mad Homology 2 (MH2) domain in SMAD6; The MH2 domain is located at the C-terminus ...
 634-807 1.14e-27

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: 110.30  E-value: 1.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 634 EPQHWCSVAYYELNNRVGETFQASSRSILIdgFTD-PSNNKnrFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYA 712
Cdd:cd10499     6 KRSHWCSVAYWEHRTRVGRLYAVYDQSVSI--FYDlPQGSG--FCLGQLNLEQRSESVRRTRSKIGYGILLSKEPDGVWA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 713 ECVSDSSIFVQSRNCNYQHGfHPATVCKIPSGCSLKIFNNQLfAQLLAQSvnHGFEVVYELTKMCTIRMSFVKGWGAEYH 792
Cdd:cd10499    82 YNRSEHPIFVNSPTLDIPGS-RTLVVRKVPPGYSIKVFDYER-SCLLQHT--AEPELADGPYDPNSVRISFAKGWGPCYS 157

                         170
                  ....*....|....*
gi 1846360069 793 RQDVTSTPCWIEIHL 807
Cdd:cd10499   158 RQFITSCPCWLEILL 172
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 66-243 4.70e-25

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 102.47  E-value: 4.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  66 SVVVPSYNEENRLPlmmdEALDYLeKRQKQDPsftYEVIVVNDGSKDQTAKVAKEYSKKYgsDKVRVISLEKNRGKGGAV 145
Cdd:pfam00535   1 SVIIPTYNEEKYLL----ETLESL-LNQTYPN---FEIIVVDDGSTDGTVEIAEEYAKKD--PRVRVIRLPENRGKAGAR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 146 RTGVFSSRGQKILMADADGATKFADIEKVEEGLKNLRPwpkgmAISCGSRAHLEKDSIAKRSYFRTLLMYGFHFLVWFLC 225
Cdd:pfam00535  71 NAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGA-----DVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLL 145

                         170
                  ....*....|....*...
gi 1846360069 226 VKEIRDTQCGFKLLTREA 243
Cdd:pfam00535 146 GLNLPFLIGGFALYRREA 163
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 67-276 8.07e-21

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 91.83  E-value: 8.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  67 VVVPSYNEENRLPLMMDEALDYLEKrqkqdpsFTYEVIVVNDGSKDQTAKVAKEYSKKYGsdKVRVISLEKNRGKGGAVR 146
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKG-------IDYEIIVVDDNSPDGTAEIVRELAKEYP--RVRLIVRPGKRGLGSAYI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 147 TGVFSSRGQKILMADADGATKFADIEKVEEGLKNlrpwpKGMAISCGSRaHLEKDSIAKRSYFRTLLMYGFHFLVWFLCV 226
Cdd:cd06442    72 EGFKAARGDVIVVMDADLSHPPEYIPELLEAQLE-----GGADLVIGSR-YVEGGGVEGWGLKRKLISRGANLLARLLLG 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1846360069 227 KEIRDTQCGFKLLTREAALQTFSNLHIERWAFDVELLYIAQCMKIPIAEV 276
Cdd:cd06442   146 RKVSDPTSGFRAYRREVLEKLIDSLVSKGYKFQLELLVRARRLGYRIVEV 195
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 67-244 4.22e-20

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 88.69  E-value: 4.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  67 VVVPSYNEENRLPLMMDEALDYLEkrqkqDPSFTYEVIVVNDGSKDQTAKVAKEYSKKYgsDKVRVISLEKNRGKGGAVR 146
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLE-----SLGYDYEIIFVDDGSTDRTLEILRELAARD--PRVKVIRLSRNFGQQAALL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 147 TGVFSSRGQKILMADADGATKFADI----EKVEEGLKnlrpwpkgmaISCGSRAHlEKDSIAKRSYFRtllmyGFHFLVW 222
Cdd:cd04187    74 AGLDHARGDAVITMDADLQDPPELIpemlAKWEEGYD----------VVYGVRKN-RKESWLKRLTSK-----LFYRLIN 137

                         170       180
                  ....*....|....*....|..
gi 1846360069 223 FLCVKEIRDTQCGFKLLTREAA 244
Cdd:cd04187   138 KLSGVDIPDNGGDFRLMDRKVV 159
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 67-163 1.39e-19

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 86.41  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  67 VVVPSYNEENRLPlmmdEALDYLekrQKQDPSFtYEVIVVNDGSKDQTAKVAKEYSKKYgsDKVRVISLEKNRGKGGAVR 146
Cdd:cd00761     1 VIIPAYNEEPYLE----RCLESL---LAQTYPN-FEVIVVDDGSTDGTLEILEEYAKKD--PRVIRVINEENQGLAAARN 70

                          90
                  ....*....|....*..
gi 1846360069 147 TGVFSSRGQKILMADAD 163
Cdd:cd00761    71 AGLKAARGEYILFLDAD 87
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 65-163 1.67e-19

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 90.19  E-value: 1.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  65 LSVVVPSYNEENRLPlmmdEALDYLekrQKQD-PSFTYEVIVVNDGSKDQTAKVAKEYSKKYgsDKVRVISLEKNRGKGG 143
Cdd:COG1215    31 VSVIIPAYNEEAVIE----ETLRSL---LAQDyPKEKLEVIVVDDGSTDETAEIARELAAEY--PRVRVIERPENGGKAA 101

                          90       100
                  ....*....|....*....|
gi 1846360069 144 AVRTGVFSSRGQKILMADAD 163
Cdd:COG1215   102 ALNAGLKAARGDIVVFLDAD 121
MH2_SMAD_7 cd10500
C-terminal Mad Homology 2 (MH2) domain in SMAD7; The MH2 domain is located at the C-terminus ...
 634-805 1.24e-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: 81.24  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 634 EPQHWCSVAYYELNNRVGETFQASSRSIliDGFTDPSNNkNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAE 713
Cdd:cd10500     4 DQSHWCVVAYWEEKTRVGRLYSVQEPSL--DIFYDLPQG-NGFCLGQLNSDNKSQLVQKVRSKIGYGIQLTREVDGVWVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 714 CVSDSSIFVQSRNCNYQHGfHPATVCKIPSGCSLKIFNNQLfAQLLAQSVNHgfEVVYELTKMCTIRMSFVKGWGAEYHR 793
Cdd:cd10500    81 NRSSYPIFIKSATLDNPDS-RTLLVHKVFPGFSIKAFDYEK-AYSLQRPNDH--EFMQQPWTGFTVQISFVKGWGQCYTR 156

                         170
                  ....*....|..
gi 1846360069 794 QDVTSTPCWIEI 805
Cdd:cd10500   157 QFISSCPCWLEV 168
MH1_SMAD_6 cd10493
N-terminal Mad Homology 1 (MH1) domain in SMAD6; The MH1 is a small DNA-binding domain present ...
 420-503 5.82e-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: 74.42  E-value: 5.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 420 LERALSCPGQPSKCVTIPRSldgRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRV 499
Cdd:cd10493    33 LEAVESRGGLPSGCVMVPRT---ELRLGGRRVPPQLLLCRLFRWPDLQHPAQLKALCHCQSFGAQDGPTVCCNPYHYSRL 109


                  ....
gi 1846360069 500 ETPV 503
Cdd:cd10493   110 CGPE 113
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 63-276 2.33e-15

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 76.66  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  63 RELSVVVPSYNEENRLPLMMdealdYLEKRQKQDPSfTYEVIVVNDGSKDQTAKVAKEYSKKYGSDKVRVISLEKNRGKG 142
Cdd:PLN02726    9 MKYSIIVPTYNERLNIALIV-----YLIFKALQDVK-DFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 143 GAVRTGVFSSRGQKILMADADGA--TKF--ADIEKVEEglknlrpwpKGMAISCGSRaHLEKDSIAKRSYFRTLLMYGFH 218
Cdd:PLN02726   83 TAYIHGLKHASGDFVVIMDADLShhPKYlpSFIKKQRE---------TGADIVTGTR-YVKGGGVHGWDLRRKLTSRGAN 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1846360069 219 FLVWFLCVKEIRDTQCGFKLLTREAALQTFSNLHIERWAFDVELLYIAQCMKIPIAEV 276
Cdd:PLN02726  153 VLAQTLLWPGVSDLTGSFRLYKRSALEDLVSSVVSKGYVFQMEIIVRASRKGYRIEEV 210
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 67-163 4.18e-15

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 74.19  E-value: 4.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  67 VVVPSYNEENRLPlmmdEALDYLeKRQKQDPsftYEVIVVNDGSKDQTAKVAKEYSKKYGSDKVRVIsLEKNRGKGGAVR 146
Cdd:cd06423     1 IIVPAYNEEAVIE----RTIESL-LALDYPK---LEVIVVDDGSTDDTLEILEELAALYIRRVLVVR-DKENGGKAGALN 71

                          90
                  ....*....|....*..
gi 1846360069 147 TGVFSSRGQKILMADAD 163
Cdd:cd06423    72 AGLRHAKGDIVVVLDAD 88
MH1_SMAD_6_7 cd10489
N-terminal Mad Homology 1 (MH1) domain in SMAD6 and SMAD7; The MH1 is a small DNA-binding ...
 418-499 7.23e-15

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: 71.65  E-value: 7.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 418 EELERAL-SCPGQPSKCVTIPRSLdgrlqVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCefPFGSKQKEVCINPYHY 496
Cdd:cd10489    40 ELLLQAVeSRGGDYLACVLLPRRD-----PRSMPQDPHVLCCQLFRWPDLRHSSELKRLPTC--ESAKDPVYVCCNPYHW 112


                  ...
gi 1846360069 497 RRV 499
Cdd:cd10489   113 SRL 115
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 50-163 1.44e-13

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 71.46  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  50 RKGPASNIHDPATRELSVVVPSYNEENRLPLMMDE--ALDYlekrqkqdPSFTYEVIVVNDGSKDQTAKVAKEYSKKygs 127
Cdd:cd06439    16 RPKPPSLPDPAYLPTVTIIIPAYNEEAVIEAKLENllALDY--------PRDRLEIIVVSDGSTDGTAEIAREYADK--- 84

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1846360069 128 dKVRVISLEKNRGKGGAVRTGVFSSRGQKILMADAD 163
Cdd:cd06439    85 -GVKLLRFPERRGKAAALNRALALATGEIVVFTDAN 119
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
61-163 8.59e-12

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 65.01  E-value: 8.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  61 ATRELSVVVPSYNEENRLplmmDEALDYLeKRQKQDPsftYEVIVVNDGSKDQTAKVAKEYSkkygSDKVRVISLEKNRG 140
Cdd:COG1216     1 MRPKVSVVIPTYNRPELL----RRCLESL-LAQTYPP---FEVIVVDNGSTDGTAELLAALA----FPRVRVIRNPENLG 68

                          90       100
                  ....*....|....*....|...
gi 1846360069 141 KGGAVRTGVFSSRGQKILMADAD 163
Cdd:COG1216    69 FAAARNLGLRAAGGDYLLFLDDD 91
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 59-163 1.94e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 66.22  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  59 DPATRELSVVVPSYNEENRLPLMMDEALdylekRQKQDpsfTYEVIVVNDGSKDQTAKVAKEYSKKYGsdKVRVISlEKN 138
Cdd:PRK10073    2 MNSTPKLSIIIPLYNAGKDFRAFMESLI-----AQTWT---ALEIIIVNDGSTDNSVEIAKHYAENYP--HVRLLH-QAN 70

                          90       100
                  ....*....|....*....|....*
gi 1846360069 139 RGKGGAVRTGVFSSRGQKILMADAD 163
Cdd:PRK10073   71 AGVSVARNTGLAVATGKYVAFPDAD 95
MH1_SMAD_7 cd10494
N-terminal Mad Homology 1 (MH1) domain in SMAD7; The MH1 is a small DNA-binding domain present ...
 417-502 3.65e-10

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: 58.35  E-value: 3.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069 417 MEELERALSCPGQP-SKCVTIPRSLDGRLQvSHRKGLPhVIYCRVWRWPDLQSHHELKPLECCEfPFGSKQKE-VCINPY 494
Cdd:cd10494    36 LEGLLQAVESRGGArTPCLLLPARLDARLG-QQSYSLP-LLLCKVFRWPDLRHSSEVKRLSCCE-SYGKINPElVCCNPH 112

                          90
                  ....*....|.
gi 1846360069 495 HYRR---VETP 502
Cdd:cd10494   113 HLSRlceLESP 123
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 60-163 3.32e-09

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 59.36  E-value: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  60 PATRELSVVVPSYNEENRLPLMMDEALDYLEKRQKQdpsftYEVIVVNDGSKDQTAKVAKEYSKKYGSDKVRVIsLEKNR 139
Cdd:PRK10714    3 HPIKKVSVVIPVYNEQESLPELIRRTTAACESLGKE-----YEILLIDDGSSDNSAEMLVEAAQAPDSHIVAIL-LNRNY 76

                          90       100
                  ....*....|....*....|....
gi 1846360069 140 GKGGAVRTGVFSSRGQKILMADAD 163
Cdd:PRK10714   77 GQHSAIMAGFSHVTGDLIITLDAD 100
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 67-163 1.26e-08

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 56.14  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  67 VVVPSYNEENRLPLMMD--EALDYlekrqkqdPSFTYEVIVVNDGSKDQTAK-VAKEYSKKYGSDKVRVISLEKNRGKGG 143
Cdd:cd04192     1 VVIAARNEAENLPRLLQslSALDY--------PKEKFEVILVDDHSTDGTVQiLEFAAAKPNFQLKILNNSRVSISGKKN 72

                          90       100
                  ....*....|....*....|
gi 1846360069 144 AVRTGVFSSRGQKILMADAD 163
Cdd:cd04192    73 ALTTAIKAAKGDWIVTTDAD 92
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 66-164 2.32e-08

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 55.70  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  66 SVVVPSYNEENRLplmmdEALdyLEKRQKQD-PSFTYEVIVVNDGSKDQTAKVAKEYSKKYgsDKVRVISLEKnRGKGGA 144
Cdd:cd02525     3 SIIIPVRNEEKYI-----EEL--LESLLNQSyPKDLIEIIVVDGGSTDGTREIVQEYAAKD--PRIRLIDNPK-RIQSAG 72

                          90       100
                  ....*....|....*....|
gi 1846360069 145 VRTGVFSSRGQKILMADADG 164
Cdd:cd02525    73 LNIGIRNSRGDIIIRVDAHA 92
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 65-141 7.40e-08

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 53.73  E-value: 7.40e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1846360069  65 LSVVVPSYNEENRLPLmmdeALDYLekRQKQDPSFtyEVIVVNDGSKDQTAKVAKEYSkkygsdkVRVISLEKNRGK 141
Cdd:cd02522     1 LSIIIPTLNEAENLPR----LLASL--RRLNPLPL--EIIVVDGGSTDGTVAIARSAG-------VVVISSPKGRAR 62
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 67-158 4.31e-06

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 47.55  E-value: 4.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  67 VVVPSYNEENRLPlmmdEALDYLEKRQKQDpsftYEVIVVNDGSKDQTAKVAKEYSKkygsdKVRVISLEKNRGKGGAVR 146
Cdd:cd04186     1 IIIVNYNSLEYLK----ACLDSLLAQTYPD----FEVIVVDNASTDGSVELLRELFP-----EVRLIRNGENLGFGAGNN 67

                          90
                  ....*....|..
gi 1846360069 147 TGVFSSRGQKIL 158
Cdd:cd04186    68 QGIREAKGDYVL 79
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 63-163 6.23e-06

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 48.14  E-value: 6.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  63 RELSVVVPSYNEENRLPLMMDEALDYLEKRqkqdpsftYEVIVVNDGSKDQTAKVAKEYSKKYGSDKVRVISLEKNRGKG 142
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPP--------VEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPT 73

                          90       100
                  ....*....|....*....|....
gi 1846360069 143 GAVRT--GVFSS-RGQKILMADAD 163
Cdd:pfam13641  74 GKSRGlnHGFRAvKSDLVVLHDDD 97
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 66-148 1.06e-05

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 47.31  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  66 SVVVPSYNEENrlPLMMDEALDYLEKRQKQdPSftyEVIVVNDGSKDQTAK-VAKEYSKKYGsdkVRVISLEKNRGKGGA 144
Cdd:cd04195     1 SVLMSVYIKEK--PEFLREALESILKQTLP-PD---EVVLVKDGPVTQSLNeVLEEFKRKLP---LKVVPLEKNRGLGKA 71


                  ....
gi 1846360069 145 VRTG 148
Cdd:cd04195    72 LNEG 75
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 63-163 3.42e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 46.83  E-value: 3.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  63 RELSVVVPSYNEENR--------LPLMMDEALDylekrqkqdpsftyEVIVVNDGSKDQTAKVAKEyskkYGSdkvRVIS 134
Cdd:PRK13915   31 RTVSVVLPALNEEETvgkvvdsiRPLLMEPLVD--------------ELIVIDSGSTDATAERAAA----AGA---RVVS 89

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1846360069 135 -------LEKNRGKGGAVRTGVFSSRGQKILMADAD 163
Cdd:PRK13915   90 reeilpeLPPRPGKGEALWRSLAATTGDIVVFVDAD 125
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 65-163 3.90e-04

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 42.66  E-value: 3.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  65 LSVVVPSYNEENRLPlmmdEALDYLEKrqkqdpsFTYEVIVVNDGSKDQTAKVAKEYskkygsdKVRVISlEKNRGKGGA 144
Cdd:cd02511     2 LSVVIITKNEERNIE----RCLESVKW-------AVDEIIVVDSGSTDRTVEIAKEY-------GAKVYQ-RWWDGFGAQ 62

                          90
                  ....*....|....*....
gi 1846360069 145 VRTGVFSSRGQKILMADAD 163
Cdd:cd02511    63 RNFALELATNDWVLSLDAD 81
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 67-161 4.32e-04

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 42.24  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  67 VVVPSYNeenRLPLMMdEALDYLeKRQKQDPSftyEVIVVNDGSKDQTAkvakEY-SKKYGSDKVRVISLEKNrgKGGAv 145
Cdd:cd04185     1 AVVVTYN---RLDLLK-ECLDAL-LAQTRPPD---HIIVIDNASTDGTA----EWlTSLGDLDNIVYLRLPEN--LGGA- 65

                          90
                  ....*....|....*.
gi 1846360069 146 rtGVFsSRGQKILMAD 161
Cdd:cd04185    66 --GGF-YEGVRRAYEL 78
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 102-140 2.12e-03

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 40.31  E-value: 2.12e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1846360069 102 EVIVVNDGSKDQTAKVAKEYSKKYgSDKVRVISLEKNRG 140
Cdd:cd04196    29 ELIISDDGSTDGTVEIIKEYIDKD-PFIIILIRNGKNLG 66
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 64-163 3.47e-03

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 39.93  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  64 ELSVVVPSYneenrlplmmDEALDYLEKR----QKQDPSftyEVIVVNDGSKDqtaKVAKEYSKKYGSDKVRVIsLEKNR 139
Cdd:cd06434     1 DVTVIIPVY----------DEDPDVFREClrsiLRQKPL---EIIVVTDGDDE---PYLSILSQTVKYGGIFVI-TVPHP 63

                          90       100
                  ....*....|....*....|....
gi 1846360069 140 GKGGAVRTGVFSSRGQKILMADAD 163
Cdd:cd06434    64 GKRRALAEGIRHVTTDIVVLLDSD 87
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 67-163 3.54e-03

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 39.75  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  67 VVVPSYNEENRLplmmDEALdylEKRQKQDPSFTYEVIVVNDGSKDQTAKVAKEYSKKYGSDKVRVISLEKN----RGKG 142
Cdd:cd06913     1 IILPVHNGEQWL----DECL---ESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNspspKGVG 73

                          90       100
                  ....*....|....*....|.
gi 1846360069 143 GAVRTGVFSSRGQKILMADAD 163
Cdd:cd06913    74 YAKNQAIAQSSGRYLCFLDSD 94
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 66-140 4.94e-03

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 39.88  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846360069  66 SVVVPSYNEE------------NRLPlmmdealdylekrqkqdPSFTYEVIVVNDGSKDQTAKVAKEYSKKYGSDKVRVI 133
Cdd:cd02510     1 SVIIIFHNEAlstllrtvhsviNRTP-----------------PELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVL 63


                  ....*..
gi 1846360069 134 SLEKNRG 140
Cdd:cd02510    64 RLKKREG 70
 
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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