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Conserved domains on  [gi|1926283267|ref|XP_036853525|]
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UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like protein 1 isoform X2 [Manis javanica]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 12-198 2.21e-124

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.


The actual alignment was detected with superfamily member cd06913:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 219  Bit Score: 360.62  E-value: 2.21e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  12 IILPVHNAEPWLDECLRSVLQQDFEGSMELSVFNDASKDKSMTIVEKWKEKLEGSGILVVIGGHDSPSPRGVGYSKNQAV 91
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  92 AQSSGPYLCFLDSDDVMMPQRVRLQHEAAVRCPAS--------------------------------VFTSNGPTVIMPT 139
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSiigcqvrripedsterytrwintltreqlltqVYTSHGPTVIMPT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1926283267 140 WFCSRAWFSHVGPFDEGGRGVPEDLLFFYNHLRKGGGVIRVDQSLLLYRYHPHAATHAV 198
Cdd:cd06913   161 WFCSREWFSHVGPFDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 181-395 4.67e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 4.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  181 DQSLLLYRYHPHAATHAVL--EKHSGVQKAEKQPHL-RADRDHPPGLSVPRAQSGPSCCPTHLPVGASPASTSCPSHHrP 257
Cdd:PHA03247  2565 DRSVPPPRPAPRPSEPAVTsrARRPDAPPQSARPRApVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHP-P 2643

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  258 WPAWQPTRGAHGAVPCGPRRHMLLPAFLPSLQRVAVLHPCQPPnCLPPGVGcrpppetPQCSFGKPVrcllPRPRTPLPR 337
Cdd:PHA03247  2644 PTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRR-AARPTVG-------SLTSLADPP----PPPPTPEPA 2711

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1926283267  338 SRPGGLVLPGDFVAHSSHEALPEPHPAPGTQARKHWLCCP-KPASPPSRLRPAGPGTPA 395
Cdd:PHA03247  2712 PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPgGPARPARPPTTAGPPAPA 2770
 
Name Accession Description Interval E-value
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 12-198 2.21e-124

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: 360.62  E-value: 2.21e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  12 IILPVHNAEPWLDECLRSVLQQDFEGSMELSVFNDASKDKSMTIVEKWKEKLEGSGILVVIGGHDSPSPRGVGYSKNQAV 91
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  92 AQSSGPYLCFLDSDDVMMPQRVRLQHEAAVRCPAS--------------------------------VFTSNGPTVIMPT 139
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSiigcqvrripedsterytrwintltreqlltqVYTSHGPTVIMPT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1926283267 140 WFCSRAWFSHVGPFDEGGRGVPEDLLFFYNHLRKGGGVIRVDQSLLLYRYHPHAATHAV 198
Cdd:cd06913   161 WFCSREWFSHVGPFDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 2-192 7.48e-22

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: 95.58  E-value: 7.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267   2 PARGDPARVSIILPVHNAEPWLDECLRSVLQQDF-EGSMELSVFNDASKDKSMTIVEKWKEKLegsGILVVIgghDSPSP 80
Cdd:COG1215    23 RAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYpKEKLEVIVVDDGSTDETAEIARELAAEY---PRVRVI---ERPEN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  81 RGVGYSKNQAVAQSSGPYLCFLDSDDVMMPQRVRLQHEAAVRCPASVFTSNGptvimptwFCSRAWFSHVGPFDEGGRGv 160
Cdd:COG1215    97 GGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGANL--------AFRREALEEVGGFDEDTLG- 167

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1926283267 161 pEDLLFFYnHLRKGGGVIRVDQSLLLYRYHPH 192
Cdd:COG1215   168 -EDLDLSL-RLLRAGYRIVYVPDAVVYEEAPE 197
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 11-172 7.08e-20

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: 86.29  E-value: 7.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  11 SIILPVHNAEPWLDECLRSVLQQDFEGsMELSVFNDASKDKSMTIVEKWKEKleGSGILVVIgghdSPSPRGVGYSKNQA 90
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPN-FEIIVVDDGSTDGTVEIAEEYAKK--DPRVRVIR----LPENRGKAGARNAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  91 VAQSSGPYLCFLDSDDVMMPQRVRLQHEAAVRCPASVFTSNGPTVIMPTWFCSRAWFSHV--GPFDEGGRGVPEDLLFFY 168
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLsrLPFFLGLRLLGLNLPFLI 153


                  ....
gi 1926283267 169 NHLR 172
Cdd:pfam00535 154 GGFA 157
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 9-111 6.63e-13

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 69.30  E-value: 6.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267   9 RVSIILPVHNAEPWLDECLRSVLQQDFEgSMELSVFNDASKDKSMTIVEKWKEKLEGSGILVVIGGhdspsprGVGYSKN 88
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWT-ALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANA-------GVSVARN 78

                          90       100
                  ....*....|....*....|...
gi 1926283267  89 QAVAQSSGPYLCFLDSDDVMMPQ 111
Cdd:PRK10073   79 TGLAVATGKYVAFPDADDVVYPT 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
 181-395 4.67e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 4.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  181 DQSLLLYRYHPHAATHAVL--EKHSGVQKAEKQPHL-RADRDHPPGLSVPRAQSGPSCCPTHLPVGASPASTSCPSHHrP 257
Cdd:PHA03247  2565 DRSVPPPRPAPRPSEPAVTsrARRPDAPPQSARPRApVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHP-P 2643

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  258 WPAWQPTRGAHGAVPCGPRRHMLLPAFLPSLQRVAVLHPCQPPnCLPPGVGcrpppetPQCSFGKPVrcllPRPRTPLPR 337
Cdd:PHA03247  2644 PTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRR-AARPTVG-------SLTSLADPP----PPPPTPEPA 2711

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1926283267  338 SRPGGLVLPGDFVAHSSHEALPEPHPAPGTQARKHWLCCP-KPASPPSRLRPAGPGTPA 395
Cdd:PHA03247  2712 PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPgGPARPARPPTTAGPPAPA 2770
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 220-417 3.71e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 39.75  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267 220 HPPGLsvpRAQSGPSCCPTHLPVGASPASTSCPSHHRPWPAWQPTRgahgAVPCGPRRHMLLPAFLPSLQRVAVLHPCQP 299
Cdd:pfam03154 170 QPPVL---QAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSP----ATSQPPNQTQSTAAPHTLIQQTPTLHPQRL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267 300 PNCLPPGVGCRPPPETPQCSFGKPVRCLLPRPRTPLPRSRPGGlvlpgdfVAHSSHEALPEPHPAPGTQARKHWLCCPKP 379
Cdd:pfam03154 243 PSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTG-------PSHMQHPVPPQPFPLTPQSSQSQVPPGPSP 315

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1926283267 380 ASP-PSRLRPAGPGTPALRQRGRiwpvpRGRCRELPPWP 417
Cdd:pfam03154 316 AAPgQSQQRIHTPPSQSQLQSQQ-----PPREQPLPPAP 349
 
Name Accession Description Interval E-value
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 12-198 2.21e-124

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: 360.62  E-value: 2.21e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  12 IILPVHNAEPWLDECLRSVLQQDFEGSMELSVFNDASKDKSMTIVEKWKEKLEGSGILVVIGGHDSPSPRGVGYSKNQAV 91
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  92 AQSSGPYLCFLDSDDVMMPQRVRLQHEAAVRCPAS--------------------------------VFTSNGPTVIMPT 139
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSiigcqvrripedsterytrwintltreqlltqVYTSHGPTVIMPT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1926283267 140 WFCSRAWFSHVGPFDEGGRGVPEDLLFFYNHLRKGGGVIRVDQSLLLYRYHPHAATHAV 198
Cdd:cd06913   161 WFCSREWFSHVGPFDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 12-179 1.04e-27

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: 107.98  E-value: 1.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  12 IILPVHNAEPWLDECLRSVLQQDFEgSMELSVFNDASKDKSMTIVEKWKEKlegsGILVVIggHDSPSPRGVGYSKNQAV 91
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYP-NFEVIVVDDGSTDGTLEILEEYAKK----DPRVIR--VINEENQGLAAARNAGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  92 AQSSGPYLCFLDSDDVMMPQRVRLQHEAAVRCPASVFTSngptvIMPTWFCSRAWFSHVGPFDEGGRGVPEDLLFFYNHL 171
Cdd:cd00761    74 KAARGEYILFLDADDLLLPDWLERLVAELLADPEADAVG-----GPGNLLFRRELLEEIGGFDEALLSGEEDDDFLLRLL 148


                  ....*...
gi 1926283267 172 RKGGGVIR 179
Cdd:cd00761   149 RGGKVAFR 156
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 2-192 7.48e-22

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: 95.58  E-value: 7.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267   2 PARGDPARVSIILPVHNAEPWLDECLRSVLQQDF-EGSMELSVFNDASKDKSMTIVEKWKEKLegsGILVVIgghDSPSP 80
Cdd:COG1215    23 RAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYpKEKLEVIVVDDGSTDETAEIARELAAEY---PRVRVI---ERPEN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  81 RGVGYSKNQAVAQSSGPYLCFLDSDDVMMPQRVRLQHEAAVRCPASVFTSNGptvimptwFCSRAWFSHVGPFDEGGRGv 160
Cdd:COG1215    97 GGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGANL--------AFRREALEEVGGFDEDTLG- 167

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1926283267 161 pEDLLFFYnHLRKGGGVIRVDQSLLLYRYHPH 192
Cdd:COG1215   168 -EDLDLSL-RLLRAGYRIVYVPDAVVYEEAPE 197
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 9-131 1.58e-21

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 92.46  E-value: 1.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267   9 RVSIILPVHNAEPWLDECLRSVLQQDFEgSMELSVFNDASKDKSMTIVEKWKEKLegSGILVVigghDSPSPRGVGYSKN 88
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYP-DFEIIVVDDGSTDGTAEILRELAAKD--PRIRVI----RLERNRGKGAARN 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1926283267  89 QAVAQSSGPYLCFLDSDDVMMPQRVRLQHEAAVRCPASVFTSN 131
Cdd:COG0463    76 AGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGS 118
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
9-196 3.82e-21

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 91.21  E-value: 3.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267   9 RVSIILPVHNAEPWLDECLRSVLQQDFeGSMELSVFNDASKDKSMTIVEKWKekleGSGILVVigghDSPSPRGVGYSKN 88
Cdd:COG1216     4 KVSVVIPTYNRPELLRRCLESLLAQTY-PPFEVIVVDNGSTDGTAELLAALA----FPRVRVI----RNPENLGFAAARN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  89 QAVAQSSGPYLCFLDSDDVMMPQRVrlqhEAAVRCPAsvftsngptvimptWFCSRAWFSHVGPFDEGGRGVPEDLLFFY 168
Cdd:COG1216    75 LGLRAAGGDYLLFLDDDTVVEPDWL----ERLLAAAC--------------LLIRREVFEEVGGFDERFFLYGEDVDLCL 136

                         170       180
                  ....*....|....*....|....*...
gi 1926283267 169 NHLRKGGGVIRVDQSLLlyrYHPHAATH 196
Cdd:COG1216   137 RLRKAGYRIVYVPDAVV---YHLGGASS 161
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 11-172 7.08e-20

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: 86.29  E-value: 7.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  11 SIILPVHNAEPWLDECLRSVLQQDFEGsMELSVFNDASKDKSMTIVEKWKEKleGSGILVVIgghdSPSPRGVGYSKNQA 90
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPN-FEIIVVDDGSTDGTVEIAEEYAKK--DPRVRVIR----LPENRGKAGARNAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  91 VAQSSGPYLCFLDSDDVMMPQRVRLQHEAAVRCPASVFTSNGPTVIMPTWFCSRAWFSHV--GPFDEGGRGVPEDLLFFY 168
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLsrLPFFLGLRLLGLNLPFLI 153


                  ....
gi 1926283267 169 NHLR 172
Cdd:pfam00535 154 GGFA 157
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 9-111 6.63e-13

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 69.30  E-value: 6.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267   9 RVSIILPVHNAEPWLDECLRSVLQQDFEgSMELSVFNDASKDKSMTIVEKWKEKLEGSGILVVIGGhdspsprGVGYSKN 88
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWT-ALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANA-------GVSVARN 78

                          90       100
                  ....*....|....*....|...
gi 1926283267  89 QAVAQSSGPYLCFLDSDDVMMPQ 111
Cdd:PRK10073   79 TGLAVATGKYVAFPDADDVVYPT 101
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 1-115 2.87e-11

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: 63.37  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267   1 MPARGDPARVSIILPVHNAEPWLDECLRSVLQQDFEGS-MELSVFNDASKDKSMTIVEKWKEKlegsGILVviggHDSPS 79
Cdd:cd06439    22 LPDPAYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRDrLEIIVVSDGSTDGTAEIAREYADK----GVKL----LRFPE 93

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1926283267  80 PRGVGYSKNQAVAQSSGPYLCFLDSDDVMMPQRVRL 115
Cdd:cd06439    94 RRGKAAALNRALALATGEIVVFTDANALLDPDALRL 129
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 11-197 4.33e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 62.26  E-value: 4.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  11 SIILPVHNAEPWLDECLRSVLQQDFEGSmELSVFNDASKDKSMTIVEKWKEKlEGSGILVVIGGHdspsprGVGYSKN-- 88
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKND-ELIISDDGSTDGTVEIIKEYIDK-DPFIIILIRNGK------NLGVARNfe 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  89 QAVAQSSGPYLCFLDSDDVMMPQRVrlqhEAAVRcpaSVFTSNGPTVImptwfCSRAWF-------SHVGPFDEGGRGVP 161
Cdd:cd04196    73 SLLQAADGDYVFFCDQDDIWLPDKL----ERLLK---AFLKDDKPLLV-----YSDLELvdengnpIGESFFEYQKIKPG 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1926283267 162 EDL--LFFYN----------------------------------HLRKGGGVIRVDQSLLLYRYHPHAATHA 197
Cdd:cd04196   141 TSFnnLLFQNvvtgctmafnrellelalpfpdadvimhdwwlalLASAFGKVVFLDEPLILYRQHGNNVVGA 212
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 12-190 1.17e-10

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: 59.88  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  12 IILPVHNAEPWLDECLRSVLQQDFEgSMELSVFNDASKDKSmtiVEKWKEKLEGsgilVVIggHDSPSPRGVGYSKNQAV 91
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYP-DFEVIVVDNASTDGS---VELLRELFPE----VRL--IRNGENLGFGAGNNQGI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  92 AQSSGPYLCFLDSDDVMMPQRVRLQHEAAVRCP-ASVFTSNGPTVIMptwFCSRAWFSHVGPFDEGGRGVPEDLLFFYnH 170
Cdd:cd04186    71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDPdVGIVGPKVSGAFL---LVRREVFEEVGGFDEDFFLYYEDVDLCL-R 146

                         170       180
                  ....*....|....*....|
gi 1926283267 171 LRKGGGVIRVDQSLLLYRYH 190
Cdd:cd04186   147 ARLAGYRVLYVPQAVIYHHG 166
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 11-190 1.88e-10

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 60.25  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  11 SIILPVHNAEPWLDECLRSVLQQDFEgSMELSVFNDASKDKSMTIVEKWKEKlegsgILVVIGGHDspspRGVGYSKNQA 90
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYP-NIEYIVIDGGSTDGTVDIIKKYEDK-----ITYWISEPD----KGIYDAMNKG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  91 VAQSSGPYLCFLDSDDVMMP----QRVRLQHEA----AVRCPASVFTSNGPTVIM-------------------PTWFCS 143
Cdd:cd06433    71 IALATGDIIGFLNSDDTLLPgallAVVAAFAEHpevdVVYGDVLLVDENGRVIGRrrpppfldkfllygmpichQATFFR 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1926283267 144 RAWFSHVGPFDEGGRgVPEDLLFFYNHLRKGGGVIRVDQSLLLYRYH 190
Cdd:cd06433   151 RSLFEKYGGFDESYR-IAADYDLLLRLLLAGKIFKYLPEVLAAFRLG 196
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 12-108 2.22e-10

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: 59.55  E-value: 2.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  12 IILPVHNAEPWLDECLRSVLQQDFEgSMELSVFNDASKDKSMTIVEKWKEKLEGSGILVVIGGHdspspRGVGYSKNQAV 91
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYP-KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEN-----GGKAGALNAGL 74

                          90
                  ....*....|....*..
gi 1926283267  92 AQSSGPYLCFLDSDDVM 108
Cdd:cd06423    75 RHAKGDIVVVLDADTIL 91
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 9-105 1.44e-09

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: 58.40  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267   9 RVSIILPVHNAEPWLDECLRSVLQQDFE-GSMELSVFNDASKDKSMTIVEKWKEKLEgsgILVVIgghDSPSpRGVGYSK 87
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYPkDLIEIIVVDGGSTDGTREIVQEYAAKDP---RIRLI---DNPK-RIQSAGL 73

                          90
                  ....*....|....*...
gi 1926283267  88 NQAVAQSSGPYLCFLDSD 105
Cdd:cd02525    74 NIGIRNSRGDIIIRVDAH 91
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 9-110 4.32e-09

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: 56.06  E-value: 4.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267   9 RVSIILPVHNA-EPWLDECLRSVLQQDFEgSMELSVFNDASKDKSMTIVEKWKEKLEgSGILVVIgghdSPSPRGVGYSK 87
Cdd:cd04184     2 LISIVMPVYNTpEKYLREAIESVRAQTYP-NWELCIADDASTDPEVKRVLKKYAAQD-PRIKVVF----REENGGISAAT 75

                          90       100
                  ....*....|....*....|...
gi 1926283267  88 NQAVAQSSGPYLCFLDSDDVMMP 110
Cdd:cd04184    76 NSALELATGEFVALLDHDDELAP 98
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 12-105 1.31e-07

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: 51.80  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  12 IILPVHNAE----PWLDEcLRSVLQQDFEGSMELSVFNDASKDKSMTIVEKWKEKLegSGILVVIgghDSPSPRGVGYSK 87
Cdd:cd04188     1 VVIPAYNEEkrlpPTLEE-AVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKN--PALIRVL---TLPKNRGKGGAV 74

                          90
                  ....*....|....*...
gi 1926283267  88 NQAVAQSSGPYLCFLDSD 105
Cdd:cd04188    75 RAGMLAARGDYILFADAD 92
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 12-175 2.64e-06

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


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 47.57  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  12 IILPVHNAEPWLDECLRSVLQQ---DFEgsmeLSVFNDASKDKSMTIVEKWKeklegsgilvviggHDSPSP------RG 82
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQsilPFE----VIIADDGSTEETKELIEEFK--------------SQFPIPikhvwqED 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  83 VGYSK----NQAVAQSSGPYLCFLDSDDVMMPQRVRLQHEAAVRcpaSVFTSnGPTVIMPTWF-----------CSRAWF 147
Cdd:cd06420    63 EGFRKakirNKAIAAAKGDYLIFIDGDCIPHPDFIADHIELAEP---GVFLS-GSRVLLNEKLtergirgcnmsFWKKDL 138

                         170       180
                  ....*....|....*....|....*....
gi 1926283267 148 SHVGPFDEGGRG-VPEDLLFFYNHLRKGG 175
Cdd:cd06420   139 LAVNGFDEEFTGwGGEDSELVARLLNSGI 167
PHA03247 PHA03247
large tegument protein UL36; Provisional
 181-395 4.67e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 4.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  181 DQSLLLYRYHPHAATHAVL--EKHSGVQKAEKQPHL-RADRDHPPGLSVPRAQSGPSCCPTHLPVGASPASTSCPSHHrP 257
Cdd:PHA03247  2565 DRSVPPPRPAPRPSEPAVTsrARRPDAPPQSARPRApVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHP-P 2643

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  258 WPAWQPTRGAHGAVPCGPRRHMLLPAFLPSLQRVAVLHPCQPPnCLPPGVGcrpppetPQCSFGKPVrcllPRPRTPLPR 337
Cdd:PHA03247  2644 PTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRR-AARPTVG-------SLTSLADPP----PPPPTPEPA 2711

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1926283267  338 SRPGGLVLPGDFVAHSSHEALPEPHPAPGTQARKHWLCCP-KPASPPSRLRPAGPGTPA 395
Cdd:PHA03247  2712 PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPgGPARPARPPTTAGPPAPA 2770
PHA03247 PHA03247
large tegument protein UL36; Provisional
 208-433 1.26e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  208 AEKQPHLRADRDHPPGLSVPRAQSGPSCCPTHLPVGAS--PASTSCPSHHRPWPAWQPTRGAHGAVPCGPRRHMLLPAFL 285
Cdd:PHA03247  2753 GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASlsESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT 2832

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  286 PSLQRVAVLHPCQPPNCLPPGVGC------------RPPPETPQCSFGKPVRCL---------LPRPRTPLPRSRPGGLV 344
Cdd:PHA03247  2833 SAQPTAPPPPPGPPPPSLPLGGSVapggdvrrrppsRSPAAKPAAPARPPVRRLarpavsrstESFALPPDQPERPPQPQ 2912

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  345 LPGDFVAHSSHEALPEPHPAPGTQARKhwlccPKPASPPSRLRPAGPGTPALRQR-------GRIwPVPRGRC------R 411
Cdd:PHA03247  2913 APPPPQPQPQPPPPPQPQPPPPPPPRP-----QPPLAPTTDPAGAGEPSGAVPQPwlgalvpGRV-AVPRFRVpqpapsR 2986

                          250       260
                   ....*....|....*....|....*..
gi 1926283267  412 ELP-----PWPHAACPRGSGWGVLMAL 433
Cdd:PHA03247  2987 EAPasstpPLTGHSLSRVSSWASSLAL 3013
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
10-118 5.27e-05

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 44.98  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  10 VSIILPVHNAEPWLDECLRSVLQQDFEgSMELSVFNDASKdkSMTIVEKWKEKLEGSGILVVIGGHDSpsprGVGYSKNQ 89
Cdd:PRK10018    7 ISIYMPTWNRQQLAIRAIKSVLRQDYS-NWEMIIVDDCST--SWEQLQQYVTALNDPRITYIHNDINS----GACAVRNQ 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1926283267  90 AVAQSSGPYLCFLDSDDVMMPQR--VRLQHE 118
Cdd:PRK10018   80 AIMLAQGEYITGIDDDDEWTPNRlsVFLAHK 110
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 7-110 9.37e-05

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: 43.51  E-value: 9.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267   7 PARVSIILPVHNAEPWLDECLRSVLQQDFeGSMELSVFNDASKDKSMTIVEKWKEKLEGSGILVVIGGHDsPSPRGVGYS 86
Cdd:pfam13641   1 PPDVSVVVPAFNEDSVLGRVLEAILAQPY-PPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARL-LGPTGKSRG 78

                          90       100
                  ....*....|....*....|....
gi 1926283267  87 KNQAVAQSSGPYLCFLDSDDVMMP 110
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDSVLHP 102
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 12-117 1.18e-04

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: 42.95  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  12 IILPVHNAEPWLDECLRSVLQQDFEG-SMELSVFNDASKDKSMTIVEKWKEKLEGSGILVvigghdSPSPRGVGYSKNQA 90
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGyDYEIIVVDDGSTDGTAEIARELAARVPRVRVIR------LSRNFGKGAAVRAG 74

                          90       100
                  ....*....|....*....|....*..
gi 1926283267  91 VAQSSGPYLCFLDSDdvmmpqrvrLQH 117
Cdd:cd04179    75 FKAARGDIVVTMDAD---------LQH 92
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 208-425 1.37e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  208 AEKQPHLRADRDHPPGLSVPRAQSGPSCCPTHLPVGASPASTSCPSHHRPWPAWQPTRGAHGAVPCGPRRHMLLPAFLPS 287
Cdd:PHA03307    99 SPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSS 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  288 LQRVA--VLHPCQPPNCLPPGVGCRPPPETPQCSFGKPVRCLLPRP----RTPLPRSRPGGLVLPGDFVAHSSHEALPEP 361
Cdd:PHA03307   179 PEETAraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPgrsaADDAGASSSDSSSSESSGCGWGPENECPLP 258

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1926283267  362 HPAPGTQARKHWlcCPKPASPPSRLRPAGPGTPALRQRGRIWPVPRGRCRELPPWPHAACPRGS 425
Cdd:PHA03307   259 RPAPITLPTRIW--EASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSS 320
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 10-166 3.72e-04

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: 41.79  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  10 VSIILPVHNAEPWLDECLRSvLQQDFEGSMELSVFNDASKDKSMTIVEKwkeklegSGILVVigghdsPSPRGVGYSKNQ 89
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLAS-LRRLNPLPLEIIVVDGGSTDGTVAIARS-------AGVVVI------SSPKGRARQMNA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  90 AVAQSSGPYLCFLDSdDVMMPQRVRLQHEAAVRCPASV-------FTSNGPTV----IMPTW--------------FCSR 144
Cdd:cd02522    67 GAAAARGDWLLFLHA-DTRLPPDWDAAIIETLRADGAVagafrlrFDDPGPRLrlleLGANLrsrlfglpygdqglFIRR 145

                         170       180
                  ....*....|....*....|....
gi 1926283267 145 AWFSHVGPFDEggrgVP--EDLLF 166
Cdd:cd02522   146 ELFEELGGFPE----LPlmEDVEL 165
PHA03378 PHA03378
EBNA-3B; Provisional
 218-414 8.23e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.98  E-value: 8.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267 218 RDHPPGLSVPRAQSGPSCCPTHLPVGASPASTSCPSHHRP-WP------AWQPTRGAHGAVPCGPR----RHMLLPAFLP 286
Cdd:PHA03378  612 QSHIPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPhQPpqveitPYKPTWTQIGHIPYQPSptgaNTMLPIQWAP 691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267 287 SLQrvavlhpcQPPNCLPpgvGCRPPPETPqcsfgkPVRclLPRPRTPLPRSRPGGLVLPGDFVAHSSHEALPEPHPAPG 366
Cdd:PHA03378  692 GTM--------QPPPRAP---TPMRPPAAP------PGR--AQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPG 752

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1926283267 367 TQARkhwlccpkPASPPSRLRP--AGPGTPALRQRGRIWPVPRGRCRELP 414
Cdd:PHA03378  753 RARP--------PAAAPGRARPpaAAPGAPTPQPPPQAPPAPQQRPRGAP 794
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 11-105 1.46e-03

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 40.52  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  11 SIILPVHNAEPWLDECLRSVLQ-----QDFEGSM--ELSVFNDASKDKSMTIVEK-WKEKL-EGSGILVVigghDSPSPR 81
Cdd:PTZ00260   73 SIVIPAYNEEDRLPKMLKETIKylesrSRKDPKFkyEIIIVNDGSKDKTLKVAKDfWRQNInPNIDIRLL----SLLRNK 148

                          90       100
                  ....*....|....*....|....
gi 1926283267  82 GVGYSKNQAVAQSSGPYLCFLDSD 105
Cdd:PTZ00260  149 GKGGAVRIGMLASRGKYILMVDAD 172
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 12-111 1.96e-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: 39.58  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  12 IILPVHNAEPWLDECLRSVLQQDF-EGSMELSVFNDASKDKSMTIVEKWKEKleGSGILVVIgghdSPSPRGVGYSKN-- 88
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYpKEKFEVILVDDHSTDGTVQILEFAAAK--PNFQLKIL----NNSRVSISGKKNal 74

                          90       100
                  ....*....|....*....|....
gi 1926283267  89 -QAVAQSSGPYLCFLDSDDVMMPQ 111
Cdd:cd04192    75 tTAIKAAKGDWIVTTDADCVVPSN 98
PHA03247 PHA03247
large tegument protein UL36; Provisional
 221-422 2.67e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 2.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  221 PPGLSVPRA-QSGPSCCPTHLPVGasPASTScpSHHRPWPAWQPTRGAHGAVPCGPRRHMLLPAFLPSLQrvavlHPCQP 299
Cdd:PHA03247  2556 PPAAPPAAPdRSVPPPRPAPRPSE--PAVTS--RARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDT-----HAPDP 2626

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267  300 P--------NCLPPGVGCRPPPETPQCSFGKPVRCLLPR----------PRTPLPRSRPGGLVLPGDFVAHSSHEALPEP 361
Cdd:PHA03247  2627 PppspspaaNEPDPHPPPTVPPPERPRDDPAPGRVSRPRrarrlgraaqASSPPQRPRRRAARPTVGSLTSLADPPPPPP 2706

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1926283267  362 HPAPGTQARKHWLCCP------------KPASPPSRLRPAGPGTPALRQRGRIWPVPRGRCRELPPWPHAACP 422
Cdd:PHA03247  2707 TPEPAPHALVSATPLPpgpaaarqaspaLPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP 2779
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 220-417 3.71e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 39.75  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267 220 HPPGLsvpRAQSGPSCCPTHLPVGASPASTSCPSHHRPWPAWQPTRgahgAVPCGPRRHMLLPAFLPSLQRVAVLHPCQP 299
Cdd:pfam03154 170 QPPVL---QAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSP----ATSQPPNQTQSTAAPHTLIQQTPTLHPQRL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926283267 300 PNCLPPGVGCRPPPETPQCSFGKPVRCLLPRPRTPLPRSRPGGlvlpgdfVAHSSHEALPEPHPAPGTQARKHWLCCPKP 379
Cdd:pfam03154 243 PSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTG-------PSHMQHPVPPQPFPLTPQSSQSQVPPGPSP 315

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1926283267 380 ASP-PSRLRPAGPGTPALRQRGRiwpvpRGRCRELPPWP 417
Cdd:pfam03154 316 AAPgQSQQRIHTPPSQSQLQSQQ-----PPREQPLPPAP 349
 
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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