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hypothetical protein TURU_099041 [Turdus rufiventris]
List of domain hits
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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Blast search parameters | ||||
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