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Conserved domains on  [gi|2502261507|ref|WP_281664475|]
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glycosyltransferase family 2 protein [Paraburkholderia fungorum]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11440371)

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

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  9445404|12691742

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
8-263 2.27e-20

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 86.97  E-value: 2.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507   8 KVSVIVPTYRRTADLARCLAALDAQERRADEVIVIARHNDYATLDWLRTCEVNRPdprRWIMLVRKPGVVAAYNLGIESA 87
Cdd:COG1216     4 KVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRV---RVIRNPENLGFAAARNLGLRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  88 LGDVLCFTGDDAAPHSDWIARIARAFesdpalgglggrdivhgcngiaqgrqppvglvrwygraignhhigcgaarkvqv 167
Cdd:COG1216    81 GGDYLLFLDDDTVVEPDWLERLLAAA------------------------------------------------------ 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507 168 lkgvNMAFRRDAIGTL-RFDRRLRGTGTqvhcEMAFSLKIERRGWALIYDPSLLVEHFPARAYHESPRLAF---NDAAFY 243
Cdd:COG1216   107 ----CLLIRREVFEEVgGFDERFFLYGE----DVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYYlgrNRLLFL 178
                         250       260
                  ....*....|....*....|
gi 2502261507 244 NASFNLRLIMCEYLTPPGRW 263
Cdd:COG1216   179 RKHGPRPLLRLALLRGLRLR 198
 
Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
8-263 2.27e-20

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 86.97  E-value: 2.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507   8 KVSVIVPTYRRTADLARCLAALDAQERRADEVIVIARHNDYATLDWLRTCEVNRPdprRWIMLVRKPGVVAAYNLGIESA 87
Cdd:COG1216     4 KVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRV---RVIRNPENLGFAAARNLGLRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  88 LGDVLCFTGDDAAPHSDWIARIARAFesdpalgglggrdivhgcngiaqgrqppvglvrwygraignhhigcgaarkvqv 167
Cdd:COG1216    81 GGDYLLFLDDDTVVEPDWLERLLAAA------------------------------------------------------ 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507 168 lkgvNMAFRRDAIGTL-RFDRRLRGTGTqvhcEMAFSLKIERRGWALIYDPSLLVEHFPARAYHESPRLAF---NDAAFY 243
Cdd:COG1216   107 ----CLLIRREVFEEVgGFDERFFLYGE----DVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYYlgrNRLLFL 178
                         250       260
                  ....*....|....*....|
gi 2502261507 244 NASFNLRLIMCEYLTPPGRW 263
Cdd:COG1216   179 RKHGPRPLLRLALLRGLRLR 198
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
11-124 3.09e-16

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: 74.46  E-value: 3.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  11 VIVPTYRRTADLARCLAALDAQERRADEVIVIARHNDYATLDWLRTCEVNRPDPRRWIMLvRKPGVVAAYNLGIESALGD 90
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINE-ENQGLAAARNAGLKAARGE 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2502261507  91 VLCFTGDDAAPHSDWIARIARAFESDPALGGLGG 124
Cdd:cd00761    80 YILFLDADDLLLPDWLERLVAELLADPEADAVGG 113
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
10-180 2.28e-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: 69.73  E-value: 2.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  10 SVIVPTYRRTADLARCLAALDAQERRADEVIVIarhNDY---ATLDWLRTCeVNRPDPRRWIMLVRKPGVVAAYNLGIES 86
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVV---DDGstdGTVEIAEEY-AKKDPRVRVIRLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  87 ALGDVLCFTGDDAAPHSDWIARIARAFESDPALGGLGGRDIVHGCNGIAQGRQPPVGLVRWYGRAIGNhhigcgAARKVQ 166
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRL------LGLNLP 150
                         170
                  ....*....|....
gi 2502261507 167 VLKGVNMAFRRDAI 180
Cdd:pfam00535 151 FLIGGFALYRREAL 164
 
Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
8-263 2.27e-20

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 86.97  E-value: 2.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507   8 KVSVIVPTYRRTADLARCLAALDAQERRADEVIVIARHNDYATLDWLRTCEVNRPdprRWIMLVRKPGVVAAYNLGIESA 87
Cdd:COG1216     4 KVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRV---RVIRNPENLGFAAARNLGLRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  88 LGDVLCFTGDDAAPHSDWIARIARAFesdpalgglggrdivhgcngiaqgrqppvglvrwygraignhhigcgaarkvqv 167
Cdd:COG1216    81 GGDYLLFLDDDTVVEPDWLERLLAAA------------------------------------------------------ 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507 168 lkgvNMAFRRDAIGTL-RFDRRLRGTGTqvhcEMAFSLKIERRGWALIYDPSLLVEHFPARAYHESPRLAF---NDAAFY 243
Cdd:COG1216   107 ----CLLIRREVFEEVgGFDERFFLYGE----DVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYYlgrNRLLFL 178
                         250       260
                  ....*....|....*....|
gi 2502261507 244 NASFNLRLIMCEYLTPPGRW 263
Cdd:COG1216   179 RKHGPRPLLRLALLRGLRLR 198
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
8-189 1.74e-19

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 84.75  E-value: 1.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507   8 KVSVIVPTYRRTADLARCLAALDAQERRADEVIVIarhNDY---ATLDWLRtcEVNRPDPR-RWIMLVRKPGVVAAYNLG 83
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVV---DDGstdGTAEILR--ELAAKDPRiRVIRLERNRGKGAARNAG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  84 IESALGDVLCFTGDDAAPHSDWIARIARAFESDPAlgglggrDIVHGC----NGIAQGRQPPVGLVRWYGRAIGNHHIGC 159
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPA-------DLVYGSrlirEGESDLRRLGSRLFNLVRLLTNLPDSTS 150
                         170       180       190
                  ....*....|....*....|....*....|
gi 2502261507 160 GAarkvqvlkgvnMAFRRDAIGTLRFDRRL 189
Cdd:COG0463   151 GF-----------RLFRREVLEELGFDEGF 169
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
11-124 3.09e-16

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: 74.46  E-value: 3.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  11 VIVPTYRRTADLARCLAALDAQERRADEVIVIARHNDYATLDWLRTCEVNRPDPRRWIMLvRKPGVVAAYNLGIESALGD 90
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINE-ENQGLAAARNAGLKAARGE 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2502261507  91 VLCFTGDDAAPHSDWIARIARAFESDPALGGLGG 124
Cdd:cd00761    80 YILFLDADDLLLPDWLERLVAELLADPEADAVGG 113
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
2-313 4.13e-16

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: 77.09  E-value: 4.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507   2 PREPCVKVSVIVPTYRRTADLARCLAALDAQERRAD--EVIVIARHNDYATLDWLRtcEVNRPDPRrwIMLVRKP---GV 76
Cdd:COG1215    24 APADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEklEVIVVDDGSTDETAEIAR--ELAAEYPR--VRVIERPengGK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  77 VAAYNLGIESALGDVLCFTGDDAAPHSDWIARIARAFESDpalgglggrdivhgcngiaqgrqppvglvrwygraignhh 156
Cdd:COG1215   100 AAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADP---------------------------------------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507 157 iGCGAArkvqvlkGVNMAFRRDAIgtlrfdRRLRGTGTQVHCE-MAFSLKIERRGWALIYDPSLLVEHFP---------- 225
Cdd:COG1215   140 -GVGAS-------GANLAFRREAL------EEVGGFDEDTLGEdLDLSLRLLRAGYRIVYVPDAVVYEEApetlralfrq 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507 226 -ARAYHESPRLAFNDAAFYNASFNLRLIMcEYLTPPGRWAFVVYSTLIGERADPGFLRALSQVFEVGGMALALRKWRVGL 304
Cdd:COG1215   206 rRRWARGGLQLLLKHRPLLRPRRLLLFLL-LLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGL 284

                  ....*....
gi 2502261507 305 RAMRGAWRA 313
Cdd:COG1215   285 LLLLAALRG 293
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
11-180 1.19e-14

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: 70.72  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  11 VIVPTYRRTADLARCLAALDAQERRADEVIVIARHNDYATLDWLRTCEVNRPDPRRWIMLVRKPGVVAAYNLGIESALGD 90
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRHAKGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  91 VLCFTGDDAAPHSDWIARIARAFESDPALGGLGGRDIVH-GCNGIaqgrqppvgLVRW----YGRAIGNHHIGCGAARKV 165
Cdd:cd06423    81 IVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRnGSENL---------LTRLqaieYLSIFRLGRRAQSALGGV 151
                         170
                  ....*....|....*
gi 2502261507 166 QVLKGVNMAFRRDAI 180
Cdd:cd06423   152 LVLSGAFGAFRREAL 166
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
10-180 2.28e-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: 69.73  E-value: 2.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  10 SVIVPTYRRTADLARCLAALDAQERRADEVIVIarhNDY---ATLDWLRTCeVNRPDPRRWIMLVRKPGVVAAYNLGIES 86
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVV---DDGstdGTVEIAEEY-AKKDPRVRVIRLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  87 ALGDVLCFTGDDAAPHSDWIARIARAFESDPALGGLGGRDIVHGCNGIAQGRQPPVGLVRWYGRAIGNhhigcgAARKVQ 166
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRL------LGLNLP 150
                         170
                  ....*....|....
gi 2502261507 167 VLKGVNMAFRRDAI 180
Cdd:pfam00535 151 FLIGGFALYRREAL 164
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
9-227 2.39e-12

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: 65.47  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507   9 VSVIVPTYRRTADLARCLAALDAQERRADEVIVIARHNDYATLDWLRTCEVNRPDPRRW-IMLVRKPGV---VAAYNLGI 84
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRvIRNARLLGPtgkSRGLNHGF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  85 ESALGDVLCFTGDDAAPHSDWIARIARAFESDPAlGGLGGRDIVHgcngiaqgrQPPVGLVRWYGRAIGNHHIGCGAARK 164
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKV-GAVGTPVFSL---------NRSTMLSALGALEFALRHLRMMSLRL 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2502261507 165 ---VQVLKGVNMAFRRDAIgtLRFDRRLRGTGTQVHCEMAFSLKieRRGWALIYDPSLLVEHFPAR 227
Cdd:pfam13641 154 algVLPLSGAGSAIRREVL--KELGLFDPFFLLGDDKSLGRRLR--RHGWRVAYAPDAAVRTVFPT 215
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
8-225 6.29e-12

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: 64.56  E-value: 6.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507   8 KVSVIVPTYRRTADLARCLAALDAQERRAD--EVIVIARHNDYATLDWLRtcEVNRPDPRrwIMLVRKPG--VVAAYNLG 83
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYPKDliEIIVVDGGSTDGTREIVQ--EYAAKDPR--IRLIDNPKriQSAGLNIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  84 IESALGDVLCFTGDDAAPHSDWIARIARAFESDPAlGGLGG--RDIVHGCNGIAqgrqppVGLVRWYGRAIGNHHIGCGA 161
Cdd:cd02525    77 IRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGA-DNVGGpmETIGESKFQKA------IAVAQSSPLGSGGSAYRGGA 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2502261507 162 ARKVQVLKGVNMAFRRD---AIGTlrFDRRLrgtgtqVHCEMA-FSLKIERRGWALIYDPSLLVEHFP 225
Cdd:cd02525   150 VKIGYVDTVHHGAYRREvfeKVGG--FDESL------VRNEDAeLNYRLRKAGYKIWLSPDIRVYYYP 209
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
11-224 2.03e-11

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: 61.42  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  11 VIVPTYRRTADLARCLAALDAQERRADEVIVIARHNDYATLDWLRTCEVNrpdprrwIMLVRKP---GVVAAYNLGIESA 87
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPE-------VRLIRNGenlGFGAGNNQGIREA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  88 LGDVLCFTGDDAAPHSDWIARIARAFESDPALGGLGGRdivhgcngiaqgrqppvglvrwygraignhhiGCGAArkvqv 167
Cdd:cd04186    74 KGDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIVGPK--------------------------------VSGAF----- 116
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507 168 lkgvnMAFRRDAIgtlrfdRRLRG--TGTQVHCE-MAFSLKIERRGWALIYDPSLLVEHF 224
Cdd:cd04186   117 -----LLVRREVF------EEVGGfdEDFFLYYEdVDLCLRARLAGYRVLYVPQAVIYHH 165
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
11-132 1.51e-07

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: 50.65  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  11 VIVPTYRRTADLARCLAALDAQERRADEVIVIARHNDYATLDWLRTCEVNRPDPRRWIML----VRKPGVVaayNLGIES 86
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPIPIKHVWQedegFRKAKIR---NKAIAA 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2502261507  87 ALGDVLCFTGDDAAPHSDWIARIARAFESDPALGG-------LGGRDIVHGCN 132
Cdd:cd06420    78 AKGDYLIFIDGDCIPHPDFIADHIELAEPGVFLSGsrvllneKLTERGIRGCN 130
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
8-233 3.19e-06

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: 47.58  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507   8 KVSVIVPTYRRTADLARCLAALDAQERRAD--EVIVIarhNDYATlDwlRTCEVNRPDPRRWIMLVRKP---GVVAAYNL 82
Cdd:cd06439    30 TVTIIIPAYNEEAVIEAKLENLLALDYPRDrlEIIVV---SDGST-D--GTAEIAREYADKGVKLLRFPerrGKAAALNR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  83 GIESALGDVLCFTGDDAAPHSDWIARIARAFeSDPALGGLGGRDIVHGCNGIAQGrqppVGLVRWYGRAI----GNHH-- 156
Cdd:cd06439   104 ALALATGEIVVFTDANALLDPDALRLLVRHF-ADPSVGAVSGELVIVDGGGSGSG----EGLYWKYENWLkraeSRLGst 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2502261507 157 IGC-GAArkvqvlkgvnMAFRRDAIGTLRFDrrlrgtgtQVHCEMAFSLKIERRGWALIYDPSllvehfpARAYHESP 233
Cdd:cd06439   179 VGAnGAI----------YAIRRELFRPLPAD--------TINDDFVLPLRIARQGYRVVYEPD-------AVAYEEVA 231
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
10-148 5.46e-06

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: 46.38  E-value: 5.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  10 SVIVPTYRRTADLARCLAALDAQERRADEVIVIarhnDYA----TLDWLRTCEvnrPDPRRWImlvRKP--GVVAAYNLG 83
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVI----DGGstdgTVDIIKKYE---DKITYWI---SEPdkGIYDAMNKG 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2502261507  84 IESALGDVLCFTGDDAAPHSDWIARIARAFESDPALGGLGGRDIVHGCNGIAQGRQPPVGLVRWY 148
Cdd:cd06433    71 IALATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKF 135
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
11-116 4.52e-05

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: 43.78  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  11 VIVPTYRRTADLARCLAALDAQERRADEVIVIARHNDYATLDWLRTCevnrpDPRRWIMLVRKP---GVVAAYNLGIESA 87
Cdd:cd04185     1 AVVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSL-----GDLDNIVYLRLPenlGGAGGFYEGVRRA 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2502261507  88 LG---DVLCFTGDDAAPHSDWIARIARAFESD 116
Cdd:cd04185    76 YElgyDWIWLMDDDAIPDPDALEKLLAYADKD 107
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
9-121 9.36e-05

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: 42.94  E-value: 9.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507   9 VSVIVPTYRRTADLARCLAALDAQERRADEVIVIARHNDYATLDWLRTcevnrpdpRRWIMLVRKPGVVAAYNLGIESAL 88
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARS--------AGVVVISSPKGRARQMNAGAAAAR 72
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2502261507  89 GDVLCFTGDDAAPHSDWIARIARAFESDPALGG 121
Cdd:cd02522    73 GDWLLFLHADTRLPPDWDAAIIETLRADGAVAG 105
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
9-125 1.07e-04

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: 43.01  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507   9 VSVIVPTYRRTAD-LARCLAALDAQERraDEVIVIARHNDYATLDWLrtcEVNRPDPRRWIMLVRKPGVVAAYNLGIESA 87
Cdd:cd06434     2 VTVIIPVYDEDPDvFRECLRSILRQKP--LEIIVVTDGDDEPYLSIL---SQTVKYGGIFVITVPHPGKRRALAEGIRHV 76
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2502261507  88 LGDVLCFTGDDAAPHSDWIARIARAFEsDPALGGLGGR 125
Cdd:cd06434    77 TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTN 113
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
11-191 4.59e-03

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: 37.55  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  11 VIVPTYRRTADLARCLAALDA--QERRADEVIVIarhNDY---ATLDWLRTCEVNRPDPRRWImLVRKPGVVAAYNLGIE 85
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVV---DDGstdGTAEIARELAARVPRVRVIR-LSRNFGKGAAVRAGFK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  86 SALGDVLCFT-GDDAAPHSDwIARIARAFESDPAlgglggrDIVHGCngiaqgRQPPVGLVRWYG-RAIGNHhigcGAAR 163
Cdd:cd04179    77 AARGDIVVTMdADLQHPPED-IPKLLEKLLEGGA-------DVVIGS------RFVRGGGAGMPLlRRLGSR----LFNF 138
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2502261507 164 KVQVLKGVNM--------AFRRDAIGTLRFDRRLRG 191
Cdd:cd04179   139 LIRLLLGVRIsdtqsgfrLFRREVLEALLSLLESNG 174
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
11-124 5.36e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 37.65  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261507  11 VIVPtYRRTAD-LARCLAALDAQERRAD--EVIVIARHNDYATLDWLRTCEvNRPDPRRWIMLVRKPGVV---AAYNLGI 84
Cdd:cd04192     1 VVIA-ARNEAEnLPRLLQSLSALDYPKEkfEVILVDDHSTDGTVQILEFAA-AKPNFQLKILNNSRVSISgkkNALTTAI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2502261507  85 ESALGDVLCFTGDDAAPHSDWIARIARAFESDPALGGLGG 124
Cdd:cd04192    79 KAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGP 118
 
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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