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Conserved domains on  [gi|1736062551|gb|KAA0544282|]
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glycosyltransferase [Citrobacter portucalensis]

Protein Classification

glycosyltransferase family protein( domain architecture ID 1003037)

glycosyltransferase family protein belongs to a functionally diverse family, and may transfer sugar from sources such as UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose, or CDP-abequose, to one or more of a range of substrates

EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  9334165

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10073 super family cl32454
putative glycosyl transferase; Provisional
1-327 0e+00

putative glycosyl transferase; Provisional


The actual alignment was detected with superfamily member PRK10073:

Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 556.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   1 MQSKYKLSVIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYPHVRLLHQANQGVSVARNLGL 80
Cdd:PRK10073    2 MNSTPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551  81 DVAVGDYIAFVDADDEVYPEMYETLMGMALQDNLDVVQSNADWSSRETSRVWVSIPTDRLRSTGILSGPDWLRMGLASRR 160
Cdd:PRK10073   82 AVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNADWCFRDTGETWQSIPSDRLRSTGVLSGPDWLRMALSSRR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551 161 WTHVLWMGVYRNDLIKEHNIRFIPGLHHQDVMWSTVFMFNATRAKYTEKPLYKYYQHDGSISHMKRQGEANLNYQRHYIK 240
Cdd:PRK10073  162 WTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLHDTSVSRLPRQGNKNLNYQRHYIK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551 241 ITRLLDELNHSYANRITIYPEFKQQVIYEGLRVCHCIRKEPDPQIRQRMIAEVFVSGMFKRMVSNICSVKLGYQVLLWAI 320
Cdd:PRK10073  242 ITRMLEKLNRRYADKIKIYPAFHQQITKEALRVCHAVRKEPDILTRQRMIAEIFTSGMYKRIWKNARSVKLGYQLLLWSF 321

                  ....*..
gi 1736062551 321 RFSQWRD 327
Cdd:PRK10073  322 RLWQWRD 328
 
Name Accession Description Interval E-value
PRK10073 PRK10073
putative glycosyl transferase; Provisional
1-327 0e+00

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 556.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   1 MQSKYKLSVIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYPHVRLLHQANQGVSVARNLGL 80
Cdd:PRK10073    2 MNSTPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551  81 DVAVGDYIAFVDADDEVYPEMYETLMGMALQDNLDVVQSNADWSSRETSRVWVSIPTDRLRSTGILSGPDWLRMGLASRR 160
Cdd:PRK10073   82 AVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNADWCFRDTGETWQSIPSDRLRSTGVLSGPDWLRMALSSRR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551 161 WTHVLWMGVYRNDLIKEHNIRFIPGLHHQDVMWSTVFMFNATRAKYTEKPLYKYYQHDGSISHMKRQGEANLNYQRHYIK 240
Cdd:PRK10073  162 WTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLHDTSVSRLPRQGNKNLNYQRHYIK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551 241 ITRLLDELNHSYANRITIYPEFKQQVIYEGLRVCHCIRKEPDPQIRQRMIAEVFVSGMFKRMVSNICSVKLGYQVLLWAI 320
Cdd:PRK10073  242 ITRMLEKLNRRYADKIKIYPAFHQQITKEALRVCHAVRKEPDILTRQRMIAEIFTSGMYKRIWKNARSVKLGYQLLLWSF 321

                  ....*..
gi 1736062551 321 RFSQWRD 327
Cdd:PRK10073  322 RLWQWRD 328
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
6-222 4.49e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 142.92  E-value: 4.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   6 KLSVIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYPHVRLL-HQANQGVSVARNLGLDVAV 84
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIrLERNRGKGAARNAGLAAAR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551  85 GDYIAFVDADDEVYPEMYETLMGMALQDNLDVVQSNADWSSRETSRVWVSIPTDRLRStgilsgpdwlrmgLASRRWTHV 164
Cdd:COG0463    83 GDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVR-------------LLTNLPDST 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1736062551 165 LWMGVYRNDLIKEhnIRFIPGLHHQDVMwstvFMFNATRAKYTEKPlYKYYQHDGSIS 222
Cdd:COG0463   150 SGFRLFRREVLEE--LGFDEGFLEDTEL----LRALRHGFRIAEVP-VRYRAGESKLN 200
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
8-141 2.53e-38

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: 134.06  E-value: 2.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   8 SVIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYPHVRLLHQA-NQGVSVARNLGLDVAVGD 86
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPeNRGKAGARNAGLRAATGD 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1736062551  87 YIAFVDADDEVYPEMYETLMGMALQDNLDVVQSNADWSSRETSRVWVSIPTDRLR 141
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSR 135
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
9-121 2.12e-35

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: 126.47  E-value: 2.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   9 VIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYPHV-RLLHQANQGVSVARNLGLDVAVGDY 87
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRViRVINEENQGLAAARNAGLKAARGEY 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1736062551  88 IAFVDADDEVYPEMYETLMGMALQD-NLDVVQSNA 121
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAELLADpEADAVGGPG 115
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
7-101 2.63e-10

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 60.58  E-value: 2.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   7 LSVIIPLYNAGSYFRDCMESLIAQ------TWkdlEIIIVNDGSTDCSVDIAQYYAEKYPH---VRLLHQANQGVSVARN 77
Cdd:NF038302    3 FTVAIPTYNGANRLPEVLERLRSQigteslSW---EIIVVDNNSTDNTAQVVQEYQKNWPSpypLRYCFEPQQGAAFARQ 79
                          90       100
                  ....*....|....*....|....
gi 1736062551  78 LGLDVAVGDYIAFVdaDDEVYPEM 101
Cdd:NF038302   80 RAIQEAKGELIGFL--DDDNLPAP 101
 
Name Accession Description Interval E-value
PRK10073 PRK10073
putative glycosyl transferase; Provisional
1-327 0e+00

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 556.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   1 MQSKYKLSVIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYPHVRLLHQANQGVSVARNLGL 80
Cdd:PRK10073    2 MNSTPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551  81 DVAVGDYIAFVDADDEVYPEMYETLMGMALQDNLDVVQSNADWSSRETSRVWVSIPTDRLRSTGILSGPDWLRMGLASRR 160
Cdd:PRK10073   82 AVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNADWCFRDTGETWQSIPSDRLRSTGVLSGPDWLRMALSSRR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551 161 WTHVLWMGVYRNDLIKEHNIRFIPGLHHQDVMWSTVFMFNATRAKYTEKPLYKYYQHDGSISHMKRQGEANLNYQRHYIK 240
Cdd:PRK10073  162 WTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLHDTSVSRLPRQGNKNLNYQRHYIK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551 241 ITRLLDELNHSYANRITIYPEFKQQVIYEGLRVCHCIRKEPDPQIRQRMIAEVFVSGMFKRMVSNICSVKLGYQVLLWAI 320
Cdd:PRK10073  242 ITRMLEKLNRRYADKIKIYPAFHQQITKEALRVCHAVRKEPDILTRQRMIAEIFTSGMYKRIWKNARSVKLGYQLLLWSF 321

                  ....*..
gi 1736062551 321 RFSQWRD 327
Cdd:PRK10073  322 RLWQWRD 328
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
6-222 4.49e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 142.92  E-value: 4.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   6 KLSVIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYPHVRLL-HQANQGVSVARNLGLDVAV 84
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIrLERNRGKGAARNAGLAAAR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551  85 GDYIAFVDADDEVYPEMYETLMGMALQDNLDVVQSNADWSSRETSRVWVSIPTDRLRStgilsgpdwlrmgLASRRWTHV 164
Cdd:COG0463    83 GDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVR-------------LLTNLPDST 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1736062551 165 LWMGVYRNDLIKEhnIRFIPGLHHQDVMwstvFMFNATRAKYTEKPlYKYYQHDGSIS 222
Cdd:COG0463   150 SGFRLFRREVLEE--LGFDEGFLEDTEL----LRALRHGFRIAEVP-VRYRAGESKLN 200
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
8-141 2.53e-38

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: 134.06  E-value: 2.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   8 SVIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYPHVRLLHQA-NQGVSVARNLGLDVAVGD 86
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPeNRGKAGARNAGLRAATGD 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1736062551  87 YIAFVDADDEVYPEMYETLMGMALQDNLDVVQSNADWSSRETSRVWVSIPTDRLR 141
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSR 135
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
9-121 2.12e-35

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: 126.47  E-value: 2.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   9 VIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYPHV-RLLHQANQGVSVARNLGLDVAVGDY 87
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRViRVINEENQGLAAARNAGLKAARGEY 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1736062551  88 IAFVDADDEVYPEMYETLMGMALQD-NLDVVQSNA 121
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAELLADpEADAVGGPG 115
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
3-109 4.58e-26

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 103.15  E-value: 4.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   3 SKYKLSVIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQyyAEKYPHVRLLHQ-ANQGVSVARNLGLD 81
Cdd:COG1216     1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLA--ALAFPRVRVIRNpENLGFAAARNLGLR 78
                          90       100
                  ....*....|....*....|....*...
gi 1736062551  82 VAVGDYIAFVDADDEVYPEMYETLMGMA 109
Cdd:COG1216    79 AAGGDYLLFLDDDTVVEPDWLERLLAAA 106
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
6-117 9.20e-26

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: 104.82  E-value: 9.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   6 KLSVIIPLYNAGSYFRDCMESLIAQTW--KDLEIIIVNDGSTDCSVDIAQYYAEKYPHVRLLHQ-ANQGVSVARNLGLDV 82
Cdd:COG1215    30 RVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERpENGGKAAALNAGLKA 109
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1736062551  83 AVGDYIAFVDADDEVYPEMYETLMGMALQDNLDVV 117
Cdd:COG1215   110 ARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS 144
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
8-117 2.71e-25

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: 102.31  E-value: 2.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   8 SVIIPLYNAGSYFRDCMESLIAQTW--KDLEIIIVNDGSTDCSVDIAQYYAEKYPHVRLLHQANQGVSVARNLGLDVAVG 85
Cdd:cd02525     3 SIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKRIQSAGLNIGIRNSRG 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1736062551  86 DYIAFVDAdDEVYPEMY-ETLMGMALQDNLDVV 117
Cdd:cd02525    83 DIIIRVDA-HAVYPKDYiLELVEALKRTGADNV 114
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
9-117 8.00e-23

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: 93.79  E-value: 8.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   9 VIIPLYNAGSYFRDCMESLIA--QTWKDLEIIIVNDGSTDCSVDIAQYYAEKYPHVRLL-HQANQGVSVARNLGLDVAVG 85
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIrLSRNFGKGAAVRAGFKAARG 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1736062551  86 DYIAFVDADDEVYPEMYETLMGMALQDNLDVV 117
Cdd:cd04179    81 DIVVTMDADLQHPPEDIPKLLEKLLEGGADVV 112
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
8-141 2.48e-21

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: 90.30  E-value: 2.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   8 SVIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKypHVRLLHQANQGVSVARNLGLDVAVGDY 87
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDK--ITYWISEPDKGIYDAMNKGIALATGDI 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1736062551  88 IAFVDADDEVYPEMYETLMGMAL-QDNLDVVQSNADWSSRETSRVWVSIPTDRLR 141
Cdd:cd06433    79 IGFLNSDDTLLPGALLAVVAAFAeHPEVDVVYGDVLLVDENGRVIGRRRPPPFLD 133
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
9-120 3.87e-21

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: 89.21  E-value: 3.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   9 VIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKY--PHVRLLHQANQGVSVARNLGLDVAVGD 86
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYirRVLVVRDKENGGKAGALNAGLRHAKGD 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1736062551  87 YIAFVDADDEVYPEMYETLMGMALQD-NLDVVQSN 120
Cdd:cd06423    81 IVVVLDADTILEPDALKRLVVPFFADpKVGAVQGR 115
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
8-121 2.58e-19

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: 84.99  E-value: 2.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   8 SVIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYPHVRLLHQANQGVSVARN--LGLDVAVG 85
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNLGVARNfeSLLQAADG 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1736062551  86 DYIAFVDADDEVYPEMYETLMGMALQDNL-DVVQSNA 121
Cdd:cd04196    81 DYVFFCDQDDIWLPDKLERLLKAFLKDDKpLLVYSDL 117
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
9-116 3.14e-19

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: 83.38  E-value: 3.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   9 VIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAqyyAEKYPHVRLLHQA-NQGVSVARNLGLDVAVGDY 87
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELL---RELFPEVRLIRNGeNLGFGAGNNQGIREAKGDY 77
                          90       100
                  ....*....|....*....|....*....
gi 1736062551  88 IAFVDADDEVYPEMYETLMGmALQDNLDV 116
Cdd:cd04186    78 VLLLNPDTVVEPGALLELLD-AAEQDPDV 105
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
6-122 6.50e-19

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 83.41  E-value: 6.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   6 KLSVIIPLYNA-GSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSV-DIAQYYAEKYPHVRLLHQA-NQGVSVARNLGLDV 82
Cdd:cd04184     2 LISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTDPEVkRVLKKYAAQDPRIKVVFREeNGGISAATNSALEL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1736062551  83 AVGDYIAFVDADDEVYPE-MYETLMGMALQDNLDVVQSNAD 122
Cdd:cd04184    82 ATGEFVALLDHDDELAPHaLYEVVKALNEHPDADLIYSDED 122
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
9-117 2.69e-17

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: 79.15  E-value: 2.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   9 VIIPLYNA----GSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYP-HVRLLHQ-ANQGVSVARNLGLDV 82
Cdd:cd04188     1 VVIPAYNEekrlPPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPaLIRVLTLpKNRGKGGAVRAGMLA 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1736062551  83 AVGDYIAFVDADDEVYPEMYETLMGMALQDNLDVV 117
Cdd:cd04188    81 ARGDYILFADADLATPFEELEKLEEALKTSGYDIA 115
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
9-117 5.67e-17

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: 77.52  E-value: 5.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   9 VIIPLYNAGSYFRDCMESL---IAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYPHVRLLHQA-NQGVSVARNLGLDVAV 84
Cdd:cd04187     1 IVVPVYNEEENLPELYERLkavLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSrNFGQQAALLAGLDHAR 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1736062551  85 GDYIAFVDAD--D--EVYPEMYEtlmgmALQDNLDVV 117
Cdd:cd04187    81 GDAVITMDADlqDppELIPEMLA-----KWEEGYDVV 112
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
6-100 1.21e-14

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: 72.32  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   6 KLSVIIPLYNAGSYFRDCMESLiaQTWKDlEIIIVNDGSTDCSVDIAQYYAekyphVRLLHQANQGVSVARNLGLDVAVG 85
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESV--KWAVD-EIIVVDSGSTDRTVEIAKEYG-----AKVYQRWWDGFGAQRNFALELATN 72
                          90
                  ....*....|....*
gi 1736062551  86 DYIAFVDADDEVYPE 100
Cdd:cd02511    73 DWVLSLDADERLTPE 87
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
6-94 5.96e-12

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: 64.91  E-value: 5.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   6 KLSVIIPLYNAGSYFRDCMESLIAQTWKD--LEIIIVNDGSTDCSVDIAQYYAEKypHVRLLHQ-ANQGVSVARNLGLDV 82
Cdd:cd06439    30 TVTIIIPAYNEEAVIEAKLENLLALDYPRdrLEIIVVSDGSTDGTAEIAREYADK--GVKLLRFpERRGKAAALNRALAL 107
                          90
                  ....*....|..
gi 1736062551  83 AVGDYIAFVDAD 94
Cdd:cd06439   108 ATGEIVVFTDAN 119
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
9-106 1.09e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 63.85  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   9 VIIPLYNAGSYFRDCMESLIAQTWKD--LEIIIVNDGSTDCSVDIAQ-YYAEKYPHVRLLHQA---NQGVSVARNLGLDV 82
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPKekFEVILVDDHSTDGTVQILEfAAAKPNFQLKILNNSrvsISGKKNALTTAIKA 80
                          90       100
                  ....*....|....*....|....
gi 1736062551  83 AVGDYIAFVDADDEVYPEMYETLM 106
Cdd:cd04192    81 AKGDWIVTTDADCVVPSNWLLTFV 104
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
9-117 2.55e-11

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: 62.55  E-value: 2.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   9 VIIPLYNAgsyfRDCMESLIAQ-----TWKDLEIIIVNDGSTDCSVDIAQYYAEKYPHVRLLHQANQ-GVSVARNLGLDV 82
Cdd:cd06442     1 IIIPTYNE----RENIPELIERldaalKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKrGLGSAYIEGFKA 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1736062551  83 AVGDYIAFVDAD----DEVYPEMYETlmgmALQDNLDVV 117
Cdd:cd06442    77 ARGDVIVVMDADlshpPEYIPELLEA----QLEGGADLV 111
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
9-100 4.32e-11

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: 61.70  E-value: 4.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   9 VIIPLYNAGSYFRDCMESLIAQTWKD-LEIIIVNDGSTDCSVDIAQYYAEKYPHVRLL-----HQANQ--GVSVARNLGL 80
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKWRKKLEDSGVIvlvgsHNSPSpkGVGYAKNQAI 80
                          90       100
                  ....*....|....*....|
gi 1736062551  81 DVAVGDYIAFVDADDEVYPE 100
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQ 100
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
7-130 5.01e-11

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: 61.62  E-value: 5.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   7 LSVIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYPH--VRLLHQANQ----GVSVARNLGL 80
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDvrLRVIRNARLlgptGKSRGLNHGF 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1736062551  81 DVAVGDYIAFVDADDEVYPEMYETLMGMALQDNLDVVQSNADWSSRETSR 130
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRSTML 133
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
9-94 9.44e-11

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: 59.90  E-value: 9.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   9 VIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYP----HVRllhQANQG--VSVARNLGLDV 82
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPipikHVW---QEDEGfrKAKIRNKAIAA 77
                          90
                  ....*....|..
gi 1736062551  83 AVGDYIAFVDAD 94
Cdd:cd06420    78 AKGDYLIFIDGD 89
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
7-101 2.63e-10

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 60.58  E-value: 2.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   7 LSVIIPLYNAGSYFRDCMESLIAQ------TWkdlEIIIVNDGSTDCSVDIAQYYAEKYPH---VRLLHQANQGVSVARN 77
Cdd:NF038302    3 FTVAIPTYNGANRLPEVLERLRSQigteslSW---EIIVVDNNSTDNTAQVVQEYQKNWPSpypLRYCFEPQQGAAFARQ 79
                          90       100
                  ....*....|....*....|....
gi 1736062551  78 LGLDVAVGDYIAFVdaDDEVYPEM 101
Cdd:NF038302   80 RAIQEAKGELIGFL--DDDNLPAP 101
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
8-104 1.06e-09

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: 57.32  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   8 SVIIPLYNAGS--YFRDCMESLIAQTWKDLEIIIVNDGSTDCSVD-IAQYYAEKYPHVRLLHQANQGVSVARNLGLDVAV 84
Cdd:cd04195     1 SVLMSVYIKEKpeFLREALESILKQTLPPDEVVLVKDGPVTQSLNeVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80
                          90       100
                  ....*....|....*....|
gi 1736062551  85 GDYIAFVDADDEVYPEMYET 104
Cdd:cd04195    81 YDWVARMDTDDISLPDRFEK 100
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
7-94 3.77e-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: 56.04  E-value: 3.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   7 LSVIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQyyaekYPHVRLLHqANQGVSVARNLGLDVAVGD 86
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIAR-----SAGVVVIS-SPKGRARQMNAGAAAARGD 74

                  ....*...
gi 1736062551  87 YIAFVDAD 94
Cdd:cd02522    75 WLLFLHAD 82
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
8-97 1.08e-08

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: 55.67  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   8 SVIIPLYN-AGSYFRDCMESLIAQTWKDL--EIIIVNDGSTDCSVDIA-QYYAEKYPH-VRLLH-QANQGVSVARNLGLD 81
Cdd:cd02510     1 SVIIIFHNeALSTLLRTVHSVINRTPPELlkEIILVDDFSDKPELKLLlEEYYKKYLPkVKVLRlKKREGLIRARIAGAR 80
                          90
                  ....*....|....*.
gi 1736062551  82 VAVGDYIAFVDADDEV 97
Cdd:cd02510    81 AATGDVLVFLDSHCEV 96
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
8-114 3.03e-08

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 54.21  E-value: 3.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   8 SVIIPLYNA--GSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDIAQYYAEKYPHVRLLH--QANQGVSVARNLGLDVA 83
Cdd:pfam10111   1 SVVIPVYNGekTHWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNapDTTYSLAASRNRGTSHA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1736062551  84 VGDYIAFVDADDEVYPEMYETLMGMALQDNL 114
Cdd:pfam10111  81 IGEYISFIDGDCLWSPDKFEKQLKIATSLAL 111
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
3-94 4.27e-08

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 54.00  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   3 SKYKLSVIIPLYNA----GSYFRDCMESLIAQTWKDL----EIIIVNDGSTDCSVDIAQYYAEKYPH----VRLL-HQAN 69
Cdd:PTZ00260   68 SDVDLSIVIPAYNEedrlPKMLKETIKYLESRSRKDPkfkyEIIIVNDGSKDKTLKVAKDFWRQNINpnidIRLLsLLRN 147
                          90       100
                  ....*....|....*....|....*
gi 1736062551  70 QGVSVARNLGLDVAVGDYIAFVDAD 94
Cdd:PTZ00260  148 KGKGGAVRIGMLASRGKYILMVDAD 172
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-117 4.64e-07

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 50.08  E-value: 4.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   1 MQSKYKLSVIIPLYN-----------AGSYFRDCmesliaqtwKDLEIIIVNDGSTDCSVDIAQYYAEKY--PHVRLLHQ 67
Cdd:PLN02726    5 GEGAMKYSIIVPTYNerlnialivylIFKALQDV---------KDFEIIVVDDGSPDGTQDVVKQLQKVYgeDRILLRPR 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1736062551  68 ANQ-GVSVARNLGLDVAVGDYIAFVDADDEVYPEMYETLMGMALQDNLDVV 117
Cdd:PLN02726   76 PGKlGLGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIV 126
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
6-117 3.05e-06

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 48.19  E-value: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   6 KLSVIIPLYNAGSYFRDCMESLIA---QTWKDLEIIIVNDGSTDCSVDI--AQYYAEKYPHVRLLHQANQGVSVARNLGL 80
Cdd:PRK10714    7 KVSVVIPVYNEQESLPELIRRTTAaceSLGKEYEILLIDDGSSDNSAEMlvEAAQAPDSHIVAILLNRNYGQHSAIMAGF 86
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1736062551  81 DVAVGDYIAFVDADDEVYPEMYETLMGMAlQDNLDVV 117
Cdd:PRK10714   87 SHVTGDLIITLDADLQNPPEEIPRLVAKA-DEGYDVV 122
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
7-99 1.40e-05

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 46.14  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   7 LSVIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTdcSVDIAQYYAEKY--PHVRLLHQA-NQGVSVARNLGLDVA 83
Cdd:PRK10018    7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCST--SWEQLQQYVTALndPRITYIHNDiNSGACAVRNQAIMLA 84
                          90
                  ....*....|....*.
gi 1736062551  84 VGDYIAFVDADDEVYP 99
Cdd:PRK10018   85 QGEYITGIDDDDEWTP 100
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
9-123 1.48e-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: 45.32  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   9 VIIPLYNAGSYFRDCMESLIAQTWKDLEIIIVNDGSTDCSVDI-AQYYAEKYPHVRLLHQaNQGVSVARNLGLDVAVG-- 85
Cdd:cd04185     1 AVVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWlTSLGDLDNIVYLRLPE-NLGGAGGFYEGVRRAYElg 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1736062551  86 -DYIAFVDADDEVYPEMYETLMGMALQDNLDVVQSNADW 123
Cdd:cd04185    80 yDWIWLMDDDAIPDPDALEKLLAYADKDNPQFLAPLVLD 118
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
7-102 2.50e-05

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: 44.94  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   7 LSVIIPLYNA-GSYFRDCMESLIAQtwKDLEIIIVNDGS--TDCSVDIAQyyaEKYPHVRLLHQANQGVSVARNLGLDVA 83
Cdd:cd06434     2 VTVIIPVYDEdPDVFRECLRSILRQ--KPLEIIVVTDGDdePYLSILSQT---VKYGGIFVITVPHPGKRRALAEGIRHV 76
                          90
                  ....*....|....*....
gi 1736062551  84 VGDYIAFVDaDDEVYPEMY 102
Cdd:cd06434    77 TTDIVVLLD-SDTVWPPNA 94
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
8-94 1.20e-04

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 42.68  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   8 SVIIPLYNAgsyfRDCMESLIAQT----W-KDLEIIIVNDGSTDCSVDIAQYYAEKYP----HVRLLHQANQGVSVARNL 78
Cdd:cd06437     4 TVQLPVFNE----KYVVERLIEAAcaldYpKDRLEIQVLDDSTDETVRLAREIVEEYAaqgvNIKHVRRADRTGYKAGAL 79
                          90
                  ....*....|....*...
gi 1736062551  79 --GLDVAVGDYIAFVDAD 94
Cdd:cd06437    80 aeGMKVAKGEYVAIFDAD 97
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
9-116 1.21e-04

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 43.04  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736062551   9 VIIPLYN-AGSYFRDCMESLIAQTWKdleIIIVNDGSTdcsVDIAQYYAEKYPHVRLLHQ-ANQGVSVARNLGLDVAVG- 85
Cdd:cd02526     1 AVVVTYNpDLSKLKELLAALAEQVDK---VVVVDNSSG---NDIELRLRLNSEKIELIHLgENLGIAKALNIGIKAALEn 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1736062551  86 --DYIAFVDADDEVYPEMYETL--MGMALQDNLDV 116
Cdd:cd02526    75 gaDYVLLFDQDSVPPPDMVEKLlaYKILSDKNSNI 109
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
36-94 3.78e-03

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


Pssm-ID: 433416 [Multi-domain]  Cd Length: 97  Bit Score: 36.45  E-value: 3.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1736062551  36 EIIIVNDGSTDCSVDIAQyyaeKYPHVRLLH------QANQGVSVARNLGLDVAVGDYIAFVDAD 94
Cdd:pfam13704  21 HIYVYDNGSDDGTAEILA----RLPDVSILRsdlsykDARFQVDWRNALLARYAEADWVLVVDAD 81
 
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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