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Conserved domains on  [gi|1737379504|emb|VAK76662|]
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glycosyl transferase family protein [Enterobacter cloacae]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10118426)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  9445404|12691742|10508766|12200473|10521532
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 3-226 4.87e-56

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: 179.41  E-value: 4.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   3 KITVCLLTFNSERLLRDVIPPLLKIADEIIIVDSGSTDNTLHICQSYGLSPVYKKYGWHGEQMNHAVSLASHDWVLCIDS 82
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRWWDGFGAQRNFALELATNDWVLSLDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  83 DEILDSDTVDAILKLKRSDEPDpvmAWRICRHWYVLGEKVRtlYPVSSPDFPVRLFNRKQARFNNRPVDDKVEGFRHSER 162
Cdd:cd02511    81 DERLTPELADEILALLATDDYD---GYYVPRRNFFLGRWIR--HGGWYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGI 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504 163 -IPGYVRHDTFHTLHELFSKLNGYTTRLV-----QYQTIRPSIGRGVISAIGAFFKWYLFSGAWRQGRVG 226
Cdd:cd02511   156 vLKGDILHYGYKSLEEFLEKHNRYSSLEAkdlaaKGKKRSLLKGLLLGRPLLAFLKMYILKRGFLDGRAG 225
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 3-226 4.87e-56

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: 179.41  E-value: 4.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   3 KITVCLLTFNSERLLRDVIPPLLKIADEIIIVDSGSTDNTLHICQSYGLSPVYKKYGWHGEQMNHAVSLASHDWVLCIDS 82
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRWWDGFGAQRNFALELATNDWVLSLDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  83 DEILDSDTVDAILKLKRSDEPDpvmAWRICRHWYVLGEKVRtlYPVSSPDFPVRLFNRKQARFNNRPVDDKVEGFRHSER 162
Cdd:cd02511    81 DERLTPELADEILALLATDDYD---GYYVPRRNFFLGRWIR--HGGWYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGI 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504 163 -IPGYVRHDTFHTLHELFSKLNGYTTRLV-----QYQTIRPSIGRGVISAIGAFFKWYLFSGAWRQGRVG 226
Cdd:cd02511   156 vLKGDILHYGYKSLEEFLEKHNRYSSLEAkdlaaKGKKRSLLKGLLLGRPLLAFLKMYILKRGFLDGRAG 225
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-163 1.63e-21

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 89.38  E-value: 1.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   1 MFKITVCLLTFNSERLLRDVIPPLLKIAD---EIIIVDSGSTDNTLHICQSYG--LSPVY-----KKYGwHGEQMNHAVS 70
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYpdfEIIVVDDGSTDGTAEILRELAakDPRIRvirleRNRG-KGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  71 LASHDWVLCIDSDEILDSDTVDAILKLKRSDEPDPVMAWRICRHWYVLGEK--------VRTLYPVSSPDFPVRLFNR-- 140
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRlgsrlfnlVRLLTNLPDSTSGFRLFRRev 159

                         170       180
                  ....*....|....*....|....*.
gi 1737379504 141 -KQARFNNRPVDDK--VEGFRHSERI 163
Cdd:COG0463   160 lEELGFDEGFLEDTelLRALRHGFRI 185
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-158 1.93e-14

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: 69.35  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   5 TVCLLTFNSERLLRDVIPPLLKI---ADEIIIVDSGSTDNTLHICQSY-----GLSPVYKKYGW-HGEQMNHAVSLASHD 75
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQtypNFEIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLPENRgKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  76 WVLCIDSDEILDSDTVDAILKLKRSDEPDPVMAWRICRhwyvlgEKVRTLYPVSSPDFPVRLFNRKQARFNNRPVDDKVE 155
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVI------FGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIG 154


                  ...
gi 1737379504 156 GFR 158
Cdd:pfam00535 155 GFA 157
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 3-83 4.33e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 44.14  E-value: 4.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   3 KITVCLLTFNSER--------LLRDVIPPLLkiaDEIIIVDSGSTDNTLHICQSYG------------LSPVYKKygwhG 62
Cdd:PRK13915   32 TVSVVLPALNEEEtvgkvvdsIRPLLMEPLV---DELIVIDSGSTDATAERAAAAGarvvsreeilpeLPPRPGK----G 104

                          90       100
                  ....*....|....*....|.
gi 1737379504  63 EQMNHAVSLASHDWVLCIDSD 83
Cdd:PRK13915  105 EALWRSLAATTGDIVVFVDAD 125
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
2-91 3.63e-03

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 38.24  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   2 FKITVCLLTFNSERLLRDVIPPLL------KIADEIIIVDSGSTDNTLHICQSY---GLSPVYKKYGWHGEQ-----MNH 67
Cdd:NF038302    1 LDFTVAIPTYNGANRLPEVLERLRsqigteSLSWEIIVVDNNSTDNTAQVVQEYqknWPSPYPLRYCFEPQQgaafaRQR 80

                          90       100
                  ....*....|....*....|....
gi 1737379504  68 AVSLASHDWVLCIDSDEILDSDTV 91
Cdd:NF038302   81 AIQEAKGELIGFLDDDNLPAPNWV 104
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 3-226 4.87e-56

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: 179.41  E-value: 4.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   3 KITVCLLTFNSERLLRDVIPPLLKIADEIIIVDSGSTDNTLHICQSYGLSPVYKKYGWHGEQMNHAVSLASHDWVLCIDS 82
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRWWDGFGAQRNFALELATNDWVLSLDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  83 DEILDSDTVDAILKLKRSDEPDpvmAWRICRHWYVLGEKVRtlYPVSSPDFPVRLFNRKQARFNNRPVDDKVEGFRHSER 162
Cdd:cd02511    81 DERLTPELADEILALLATDDYD---GYYVPRRNFFLGRWIR--HGGWYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGI 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504 163 -IPGYVRHDTFHTLHELFSKLNGYTTRLV-----QYQTIRPSIGRGVISAIGAFFKWYLFSGAWRQGRVG 226
Cdd:cd02511   156 vLKGDILHYGYKSLEEFLEKHNRYSSLEAkdlaaKGKKRSLLKGLLLGRPLLAFLKMYILKRGFLDGRAG 225
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-163 1.63e-21

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 89.38  E-value: 1.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   1 MFKITVCLLTFNSERLLRDVIPPLLKIAD---EIIIVDSGSTDNTLHICQSYG--LSPVY-----KKYGwHGEQMNHAVS 70
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYpdfEIIVVDDGSTDGTAEILRELAakDPRIRvirleRNRG-KGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  71 LASHDWVLCIDSDEILDSDTVDAILKLKRSDEPDPVMAWRICRHWYVLGEK--------VRTLYPVSSPDFPVRLFNR-- 140
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRlgsrlfnlVRLLTNLPDSTSGFRLFRRev 159

                         170       180
                  ....*....|....*....|....*.
gi 1737379504 141 -KQARFNNRPVDDK--VEGFRHSERI 163
Cdd:COG0463   160 lEELGFDEGFLEDTelLRALRHGFRI 185
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-158 1.93e-14

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: 69.35  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   5 TVCLLTFNSERLLRDVIPPLLKI---ADEIIIVDSGSTDNTLHICQSY-----GLSPVYKKYGW-HGEQMNHAVSLASHD 75
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQtypNFEIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLPENRgKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  76 WVLCIDSDEILDSDTVDAILKLKRSDEPDPVMAWRICRhwyvlgEKVRTLYPVSSPDFPVRLFNRKQARFNNRPVDDKVE 155
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVI------FGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIG 154


                  ...
gi 1737379504 156 GFR 158
Cdd:pfam00535 155 GFA 157
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-96 9.26e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 68.10  E-value: 9.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   1 MFKITVCLLTFNSERLLRDVIPPLLK---IADEIIIVDSGSTDNTLHICQSYGLSPV----YKKYGWHGEQMNHAVSLAS 73
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESLLAqtyPPFEVIVVDNGSTDGTAELLAALAFPRVrvirNPENLGFAAARNLGLRAAG 81

                          90       100
                  ....*....|....*....|...
gi 1737379504  74 HDWVLCIDSDEILDSDTVDAILK 96
Cdd:COG1216    82 GDYLLFLDDDTVVEPDWLERLLA 104
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-145 1.89e-13

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: 66.38  E-value: 1.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   6 VCLLTFNSERLLRDVIPPLLKI---ADEIIIVDSGSTDNTLHICQSYGLSP------VYKKYGWHGEQMNHAVSLASHDW 76
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQtypNFEVIVVDDGSTDGTLEILEEYAKKDprvirvINEENQGLAAARNAGLKAARGEY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737379504  77 VLCIDSDEILDSDTVDAILK-LKRSDEPDPVMAWRIC---RHWY--VLGEKVRTLYPVSSPDFPVRLFNRKQARF 145
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAeLLADPEADAVGGPGNLlfrRELLeeIGGFDEALLSGEEDDDFLLRLLRGGKVAF 155
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 3-96 1.30e-10

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: 60.53  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   3 KITVCLLTFNSERLLRDVIPPLLKI-----ADEIIIVDSGSTDNTLHICQSYG-----LSPVYKKYGWH-GEQMNHAVSL 71
Cdd:COG1215    30 RVSVIIPAYNEEAVIEETLRSLLAQdypkeKLEVIVVDDGSTDETAEIARELAaeyprVRVIERPENGGkAAALNAGLKA 109

                          90       100
                  ....*....|....*....|....*
gi 1737379504  72 ASHDWVLCIDSDEILDSDTVDAILK 96
Cdd:COG1215   110 ARGDIVVFLDADTVLDPDWLRRLVA 134
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 4-163 3.38e-10

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 57.94  E-value: 3.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   4 ITVClltFNSERLLRDVI--------PPLlkiadEIIIVDSGSTDNTLHICQSYGLSPVYkkygWHGEQ-------MNHA 68
Cdd:cd06433     3 ITPT---YNQAETLEETIdsvlsqtyPNI-----EYIVIDGGSTDGTVDIIKKYEDKITY----WISEPdkgiydaMNKG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  69 VSLASHDWVLCIDSDEILDSDTVDAILKLKRsDEPDPVMawrICRHWYVLGEKVRTLYPVSSPDFPVRLFNRK-----QA 143
Cdd:cd06433    71 IALATGDIIGFLNSDDTLLPGALLAVVAAFA-EHPEVDV---VYGDVLLVDENGRVIGRRRPPPFLDKFLLYGmpichQA 146

                         170       180
                  ....*....|....*....|
gi 1737379504 144 RFNNRPVDDKVEGFRHSERI 163
Cdd:cd06433   147 TFFRRSLFEKYGGFDESYRI 166
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 10-103 1.18e-09

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: 56.81  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  10 TFNSE----RLLRDVIPpLLKIADEIIIVDSGSTDNTLHICQSYGLSPVYKKYGwHGEQMNHAVSLASHDWVLCIDSDEI 85
Cdd:cd02522     7 TLNEAenlpRLLASLRR-LNPLPLEIIVVDGGSTDGTVAIARSAGVVVISSPKG-RARQMNAGAAAARGDWLLFLHADTR 84

                          90
                  ....*....|....*...
gi 1737379504  86 LDSDTVDAILKLKRSDEP 103
Cdd:cd02522    85 LPPDWDAAIIETLRADGA 102
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 10-158 1.18e-09

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: 56.43  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  10 TFNSERLLRDVIPPLLK-----IADEIIIVDSGSTDNTLHICQSYGLSPVY-------KKYGwHGEQMNHAVSLASHDWV 77
Cdd:cd04179     5 AYNEEENIPELVERLLAvleegYDYEIIVVDDGSTDGTAEIARELAARVPRvrvirlsRNFG-KGAAVRAGFKAARGDIV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  78 LCIDSDeilDSDTVDAILKL---KRSDEPDPVMAWRICRHWYVLGEKVRTlypvsspdFPVRLFNRKQARFNNRPVDDKV 154
Cdd:cd04179    84 VTMDAD---LQHPPEDIPKLlekLLEGGADVVIGSRFVRGGGAGMPLLRR--------LGSRLFNFLIRLLLGVRISDTQ 152


                  ....
gi 1737379504 155 EGFR 158
Cdd:cd04179   153 SGFR 156
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 10-103 2.20e-09

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: 55.31  E-value: 2.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  10 TFNSERLLRDVIPPLLKI---ADEIIIVDSGSTDNTLHICQSYGLSPVYKKYGWHGEQ-------MNHAVSLASHDWVLC 79
Cdd:cd06423     5 AYNEEAVIERTIESLLALdypKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEnggkagaLNAGLRHAKGDIVVV 84

                          90       100
                  ....*....|....*....|....
gi 1737379504  80 IDSDEILDSDTVDAILKLKRSDEP 103
Cdd:cd06423    85 LDADTILEPDALKRLVVPFFADPK 108
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 3-102 2.03e-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: 53.77  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   3 KITVCLLTFNSERLLRDVIPPLL-----KIADEIIIVDSGSTDNTLHICQSY-GLSPVYKKYgwHGEQ------MNHAVS 70
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLnqsypKDLIEIIVVDGGSTDGTREIVQEYaAKDPRIRLI--DNPKriqsagLNIGIR 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1737379504  71 LASHDWVLCIDSDEILDSDTVDAILK-LKRSDE 102
Cdd:cd02525    79 NSRGDIIIRVDAHAVYPKDYILELVEaLKRTGA 111
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 8-101 7.82e-07

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: 47.94  E-value: 7.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   8 LLTFNSERLLRDVIPPLLKIAD---EIIIVDSGSTDNTLHICQSYGLSPVY----KKYGWhGEQMNHAVSLASHDWVLCI 80
Cdd:cd04186     3 IVNYNSLEYLKACLDSLLAQTYpdfEVIVVDNASTDGSVELLRELFPEVRLirngENLGF-GAGNNQGIREAKGDYVLLL 81

                          90       100
                  ....*....|....*....|.
gi 1737379504  81 DSDEILDSDTVDAILKLKRSD 101
Cdd:cd04186    82 NPDTVVEPGALLELLDAAEQD 102
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-107 3.59e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 46.47  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   5 TVCLLTFNSERLLRDVIPPLLK---IADEIIIVDSGSTDNTLHICQSYG---LSPVY-----KKYGWHGeqmN--HAVSL 71
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAqtyKNDELIISDDGSTDGTVEIIKEYIdkdPFIIIlirngKNLGVAR---NfeSLLQA 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1737379504  72 ASHDWVLCIDSDEILDSDTVDAILKlKRSDEPDPVM 107
Cdd:cd04196    78 ADGDYVFFCDQDDIWLPDKLERLLK-AFLKDDKPLL 112
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 10-91 4.31e-06

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 46.03  E-value: 4.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  10 TFNSERLLRDVIPPLLK---IADEIIIVDSGSTDNTLHICQSYG-LSPVYKKYGWHGEQ-------MNHAVSLASHDWVL 78
Cdd:cd06420     5 TYNRPEALELVLKSVLNqsiLPFEVIIADDGSTEETKELIEEFKsQFPIPIKHVWQEDEgfrkakiRNKAIAAAKGDYLI 84

                          90
                  ....*....|...
gi 1737379504  79 CIDSDEILDSDTV 91
Cdd:cd06420    85 FIDGDCIPHPDFI 97
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
 28-90 7.56e-06

Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative glucosyltransferases,


Pssm-ID: 433416 [Multi-domain]  Cd Length: 97  Bit Score: 43.39  E-value: 7.56e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  28 ADEIIIVDSGSTDNTLHICQSY---GLSPV---YKKYGWHGEQMNHAVSLASH-DWVLCIDSDEILDSDT 90
Cdd:pfam13704  19 FDHIYVYDNGSDDGTAEILARLpdvSILRSdlsYKDARFQVDWRNALLARYAEaDWVLVVDADEFLVYPP 88
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 3-83 4.33e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 44.14  E-value: 4.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   3 KITVCLLTFNSER--------LLRDVIPPLLkiaDEIIIVDSGSTDNTLHICQSYG------------LSPVYKKygwhG 62
Cdd:PRK13915   32 TVSVVLPALNEEEtvgkvvdsIRPLLMEPLV---DELIVIDSGSTDATAERAAAAGarvvsreeilpeLPPRPGK----G 104

                          90       100
                  ....*....|....*....|.
gi 1737379504  63 EQMNHAVSLASHDWVLCIDSD 83
Cdd:PRK13915  105 EALWRSLAATTGDIVVFVDAD 125
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 10-83 3.08e-04

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: 40.98  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  10 TFNsER-----LLRDVIPPLLKIADEIIIVDSGSTDNTLHICQSY----------------GLSPVYKkygwhgeqmnHA 68
Cdd:cd06442     5 TYN-ERenipeLIERLDAALKGIDYEIIVVDDNSPDGTAEIVRELakeyprvrlivrpgkrGLGSAYI----------EG 73

                          90
                  ....*....|....*
gi 1737379504  69 VSLASHDWVLCIDSD 83
Cdd:cd06442    74 FKAARGDVIVVMDAD 88
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 3-99 6.17e-04

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: 40.26  E-value: 6.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   3 KITVCLLTFNSERLLRDVIPPLLKI---AD--EIIIVDSGSTDNTLHICQSYgLSPVYKKYGWHGEQ-----MNHAVSLA 72
Cdd:cd06439    30 TVTIIIPAYNEEAVIEAKLENLLALdypRDrlEIIVVSDGSTDGTAEIAREY-ADKGVKLLRFPERRgkaaaLNRALALA 108

                          90       100
                  ....*....|....*....|....*..
gi 1737379504  73 SHDWVLCIDSDEILDSdtvDAILKLKR 99
Cdd:cd06439   109 TGEIVVFTDANALLDP---DALRLLVR 132
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 4-106 7.94e-04

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: 39.66  E-value: 7.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   4 ITVCLLTFNSERLLRDVIPPLLKIA---DEIIIVDSGSTDNTLHICQ---------SYGLSPVYKKYGWHG--EQMNHAV 69
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPyppVEVVVVVNPSDAETLDVAEeiaarfpdvRLRVIRNARLLGPTGksRGLNHGF 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1737379504  70 SLASHDWVLCIDSDEILDSDTVDAILKLKRSDEPDPV 106
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAV 120
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 9-104 1.30e-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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 38.77  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   9 LTFNSERLLRDVIPPLLKI---ADEIIIVDSGSTDNTLHICQSYGLSPVYKKY----------GWHgEQMNHAVSLAsHD 75
Cdd:cd04185     4 VTYNRLDLLKECLDALLAQtrpPDHIIVIDNASTDGTAEWLTSLGDLDNIVYLrlpenlggagGFY-EGVRRAYELG-YD 81

                          90       100
                  ....*....|....*....|....*....
gi 1737379504  76 WVLCIDSDEILDSDTVDAILKLKRSDEPD 104
Cdd:cd04185    82 WIWLMDDDAIPDPDALEKLLAYADKDNPQ 110
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
2-91 3.63e-03

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 38.24  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504   2 FKITVCLLTFNSERLLRDVIPPLL------KIADEIIIVDSGSTDNTLHICQSY---GLSPVYKKYGWHGEQ-----MNH 67
Cdd:NF038302    1 LDFTVAIPTYNGANRLPEVLERLRsqigteSLSWEIIVVDNNSTDNTAQVVQEYqknWPSPYPLRYCFEPQQgaafaRQR 80

                          90       100
                  ....*....|....*....|....
gi 1737379504  68 AVSLASHDWVLCIDSDEILDSDTV 91
Cdd:NF038302   81 AIQEAKGELIGFLDDDNLPAPNWV 104
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 11-114 8.28e-03

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: 36.30  E-value: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379504  11 FNSERLLRDVIPPLLKIAD------EIIIVDSGSTDNTLHICQSygLSPVYKK---------YGwHGEQMNHAVSLASHD 75
Cdd:cd04187     6 YNEEENLPELYERLKAVLEslgydyEIIFVDDGSTDRTLEILRE--LAARDPRvkvirlsrnFG-QQAALLAGLDHARGD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1737379504  76 WVLCIDSDeiLdSDTVDAILKL--KRSDEPDPVMAWRICRH 114
Cdd:cd04187    83 AVITMDAD--L-QDPPELIPEMlaKWEEGYDVVYGVRKNRK 120
 
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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