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Conserved domains on  [gi|705427975|ref|WP_033507954|]
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glycosyltransferase family 2 protein [Bifidobacterium pullorum]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11440371)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-180 7.39e-34

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 122.41  E-value: 7.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   1 MGNVSVVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDPaSVQVLDELeQADDITVVRQG-NAGPSAARNVGIRA 79
Cdd:COG1216    2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDG-TAELLAAL-AFPRVRVIRNPeNLGFAAARNLGLRA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  80 ARTDCVTVLDGDDRLLPTFLETtvglldgdasAVAASGWLrtfgvldavvkptggtiadflprnacpatftFRRTVWETC 159
Cdd:COG1216   80 AGGDYLLFLDDDTVVEPDWLER----------LLAAACLL-------------------------------IRREVFEEV 118
                        170       180
                 ....*....|....*....|.
gi 705427975 160 GGYDESMRCGFEDWDFCLSLL 180
Cdd:COG1216  119 GGFDERFFLYGEDVDLCLRLR 139
 
Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-180 7.39e-34

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 122.41  E-value: 7.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   1 MGNVSVVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDPaSVQVLDELeQADDITVVRQG-NAGPSAARNVGIRA 79
Cdd:COG1216    2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDG-TAELLAAL-AFPRVRVIRNPeNLGFAAARNLGLRA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  80 ARTDCVTVLDGDDRLLPTFLETtvglldgdasAVAASGWLrtfgvldavvkptggtiadflprnacpatftFRRTVWETC 159
Cdd:COG1216   80 AGGDYLLFLDDDTVVEPDWLER----------LLAAACLL-------------------------------IRREVFEEV 118
                        170       180
                 ....*....|....*....|.
gi 705427975 160 GGYDESMRCGFEDWDFCLSLL 180
Cdd:COG1216  119 GGFDERFFLYGEDVDLCLRLR 139
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-180 1.02e-31

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: 115.68  E-value: 1.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   6 VVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDpASVQVLDELEQADD--ITVVRQGNAGPSAARNVGIRAARTD 83
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTD-GTLEILEEYAKKDPrvIRVINEENQGLAAARNAGLKAARGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  84 CVTVLDGDDRLLPTFLETTVGLLDGDASAVAASGWlrtfgvldavvkptggtiadflprnacpATFTFRRTVWETCGGYD 163
Cdd:cd00761   80 YILFLDADDLLLPDWLERLVAELLADPEADAVGGP----------------------------GNLLFRRELLEEIGGFD 131
                        170
                 ....*....|....*..
gi 705427975 164 ESMRCGFEDWDFCLSLL 180
Cdd:cd00761  132 EALLSGEEDDDFLLRLL 148
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
5-126 3.67e-29

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: 109.02  E-value: 3.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975    5 SVVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDpASVQVLDELEQADD-ITVVRQG-NAGPSAARNVGIRAART 82
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTD-GTVEIAEEYAKKDPrVRVIRLPeNRGKAGARNAGLRAATG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 705427975   83 DCVTVLDGDDRLLPTFLETTVGLLDGDASAVAASGWLRTFGVLD 126
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETG 123
PRK10073 PRK10073
putative glycosyl transferase; Provisional
4-101 1.34e-17

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 81.63  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   4 VSVVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDpASVQVLDEL-EQADDITVVRQGNAGPSAARNVGIRAART 82
Cdd:PRK10073   8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTD-NSVEIAKHYaENYPHVRLLHQANAGVSVARNTGLAVATG 86
                         90
                 ....*....|....*....
gi 705427975  83 DCVTVLDGDDRLLPTFLET 101
Cdd:PRK10073  87 KYVAFPDADDVVYPTMYET 105
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
4-179 7.79e-04

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 39.80  E-value: 7.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975    4 VSVVITSYNQNEMIREAVDSVRRqkLRPDA-IIVVDDGSTDpASVQVLDELeqadDITVVrQGNAGPSAARNVGIRAART 82
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQA--LRGDAeVIVVDGGSTD-GTVEIARSL----GAKVI-HSPKGRARQMNAGAALAKG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   83 DCVTVLDGDDRLLPTFLETTVGLLDGDASAVAA--------SGWLRtfgVLDAVVK--------PTGgtiaDflprnacp 146
Cdd:TIGR04283  73 DILLFLHADTRLPKDFLEAIRRALAKPGYVAGAfdlrfdgpGLLLR---LIEWGVNlrsrltgiPYG----D-------- 137
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 705427975  147 ATFTFRRTVWETCGGYDES--MrcgfEDWDFCLSL 179
Cdd:TIGR04283 138 QGLFVRRSLFEQIGGFPDIplM----EDIELSRRL 168
 
Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-180 7.39e-34

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 122.41  E-value: 7.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   1 MGNVSVVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDPaSVQVLDELeQADDITVVRQG-NAGPSAARNVGIRA 79
Cdd:COG1216    2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDG-TAELLAAL-AFPRVRVIRNPeNLGFAAARNLGLRA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  80 ARTDCVTVLDGDDRLLPTFLETtvglldgdasAVAASGWLrtfgvldavvkptggtiadflprnacpatftFRRTVWETC 159
Cdd:COG1216   80 AGGDYLLFLDDDTVVEPDWLER----------LLAAACLL-------------------------------IRREVFEEV 118
                        170       180
                 ....*....|....*....|.
gi 705427975 160 GGYDESMRCGFEDWDFCLSLL 180
Cdd:COG1216  119 GGFDERFFLYGEDVDLCLRLR 139
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
4-175 3.12e-33

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 120.96  E-value: 3.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   4 VSVVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDpASVQVLDELEQAD-DITVVR-QGNAGPSAARNVGIRAAR 81
Cdd:COG0463    4 VSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTD-GTAEILRELAAKDpRIRVIRlERNRGKGAARNAGLAAAR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  82 TDCVTVLDGDDRLLPTFLETTVGLL-DGDASAVAASGWLRTFGVLDAVVKPTGGTIADFL---PRNACPATFtFRRTVWE 157
Cdd:COG0463   83 GDYIAFLDADDQLDPEKLEELVAALeEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLtnlPDSTSGFRL-FRREVLE 161
                        170
                 ....*....|....*...
gi 705427975 158 TCgGYDESMrcgFEDWDF 175
Cdd:COG0463  162 EL-GFDEGF---LEDTEL 175
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-180 1.02e-31

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: 115.68  E-value: 1.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   6 VVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDpASVQVLDELEQADD--ITVVRQGNAGPSAARNVGIRAARTD 83
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTD-GTLEILEEYAKKDPrvIRVINEENQGLAAARNAGLKAARGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  84 CVTVLDGDDRLLPTFLETTVGLLDGDASAVAASGWlrtfgvldavvkptggtiadflprnacpATFTFRRTVWETCGGYD 163
Cdd:cd00761   80 YILFLDADDLLLPDWLERLVAELLADPEADAVGGP----------------------------GNLLFRRELLEEIGGFD 131
                        170
                 ....*....|....*..
gi 705427975 164 ESMRCGFEDWDFCLSLL 180
Cdd:cd00761  132 EALLSGEEDDDFLLRLL 148
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
5-126 3.67e-29

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: 109.02  E-value: 3.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975    5 SVVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDpASVQVLDELEQADD-ITVVRQG-NAGPSAARNVGIRAART 82
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTD-GTVEIAEEYAKKDPrVRVIRLPeNRGKAGARNAGLRAATG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 705427975   83 DCVTVLDGDDRLLPTFLETTVGLLDGDASAVAASGWLRTFGVLD 126
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETG 123
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
4-180 5.32e-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: 104.44  E-value: 5.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   4 VSVVITSYNQNEMIREAVDSVRRQKLRPDA--IIVVDDGSTDPaSVQVLDEL-EQADDITVV-RQGNAGPSAARNVGIRA 79
Cdd:COG1215   31 VSVIIPAYNEEAVIEETLRSLLAQDYPKEKleVIVVDDGSTDE-TAEIARELaAEYPRVRVIeRPENGGKAAALNAGLKA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  80 ARTDCVTVLDGDDRLLPTFLETTVGLLDgdASAVAASGwlrtfgvldavvkptggtiadflprnacpATFTFRRTVWETC 159
Cdd:COG1215  110 ARGDIVVFLDADTVLDPDWLRRLVAAFA--DPGVGASG-----------------------------ANLAFRREALEEV 158
                        170       180
                 ....*....|....*....|.
gi 705427975 160 GGYDESMRCgfEDWDFCLSLL 180
Cdd:COG1215  159 GGFDEDTLG--EDLDLSLRLL 177
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-177 3.69e-23

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: 93.39  E-value: 3.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   6 VVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDPaSVQVLDELEQadDITVVRQG-NAGPSAARNVGIRAARTDC 84
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDG-SVELLRELFP--EVRLIRNGeNLGFGAGNNQGIREAKGDY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  85 VTVLDGDDRLLPTFLETTVGLLDGDASAVAASGwlrtfgvldavvKPTGgtiadflprnACpatFTFRRTVWETCGGYDE 164
Cdd:cd04186   78 VLLLNPDTVVEPGALLELLDAAEQDPDVGIVGP------------KVSG----------AF---LLVRREVFEEVGGFDE 132
                        170
                 ....*....|...
gi 705427975 165 SMRCGFEDWDFCL 177
Cdd:cd04186  133 DFFLYYEDVDLCL 145
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
5-210 1.04e-18

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: 82.21  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   5 SVVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDpASVQVLDELEqaDDIT-VVRQGNAGPSAARNVGIRAARTD 83
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTD-GTVDIIKKYE--DKITyWISEPDKGIYDAMNKGIALATGD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  84 CVTVLDGDDRLLPTFLETTVGLLDGDASAVAASG---WLRTFGVLDAVVKPTGGTIADFL-PRNAC-PATFtFRRTVWET 158
Cdd:cd06433   78 IIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGdvlLVDENGRVIGRRRPPPFLDKFLLyGMPIChQATF-FRRSLFEK 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 705427975 159 CGGYDESMRCGFeDWDFCLSLLAaaataadttatgQEPRIAIAPEPLIEYRT 210
Cdd:cd06433  157 YGGFDESYRIAA-DYDLLLRLLL------------AGKIFKYLPEVLAAFRL 195
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
5-209 6.68e-18

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: 80.05  E-value: 6.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   5 SVVITSYNQN--EMIREAVDSVRRQKLRPDAIIVVDDGSTDPASVQVLDELEQADDITVVR-QGNAGPSAARNVGIRAAR 81
Cdd:cd04195    1 SVLMSVYIKEkpEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPlEKNRGLGKALNEGLKHCT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  82 TDCVTVLDGDDRLLPTFLETTVGLLDGDASAVAASGWLRTFG----VLDAVVKPTGGT-IADFlPRNACP---ATFTFRR 153
Cdd:cd04195   81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDsdgnDIGKRRLPTSHDdILKF-ARRRSPfnhPTVMFRK 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 705427975 154 TVWETCGGYDESMRcgFEDWDFCLSLLAAAAtaadttatgqepRIAIAPEPLIEYR 209
Cdd:cd04195  160 SKVLAVGGYQDLPL--VEDYALWARMLANGA------------RFANLPEILVKAR 201
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
4-175 1.24e-17

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: 80.35  E-value: 1.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   4 VSVVITSYNQNEMIREAVDSVRRQKLRPDA--IIVVDDGSTDpASVQVLDELEQADD-ITVVRQGNAGPSAARNVGIRAA 80
Cdd:cd02525    2 VSIIIPVRNEEKYIEELLESLLNQSYPKDLieIIVVDGGSTD-GTREIVQEYAAKDPrIRLIDNPKRIQSAGLNIGIRNS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  81 RTDCVTVLDGDDRLLPTFLETTVGLLdGDASAVAASGWLRTFG-------VLDAVVKPTGGTIADFlPRNACPATFT--- 150
Cdd:cd02525   81 RGDIIIRVDAHAVYPKDYILELVEAL-KRTGADNVGGPMETIGeskfqkaIAVAQSSPLGSGGSAY-RGGAVKIGYVdtv 158
                        170       180       190
                 ....*....|....*....|....*....|
gi 705427975 151 ----FRRTVWETCGGYDESM-RCgfEDWDF 175
Cdd:cd02525  159 hhgaYRREVFEKVGGFDESLvRN--EDAEL 186
PRK10073 PRK10073
putative glycosyl transferase; Provisional
4-101 1.34e-17

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 81.63  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   4 VSVVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDpASVQVLDEL-EQADDITVVRQGNAGPSAARNVGIRAART 82
Cdd:PRK10073   8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTD-NSVEIAKHYaENYPHVRLLHQANAGVSVARNTGLAVATG 86
                         90
                 ....*....|....*....
gi 705427975  83 DCVTVLDGDDRLLPTFLET 101
Cdd:PRK10073  87 KYVAFPDADDVVYPTMYET 105
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
6-166 2.04e-17

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: 78.04  E-value: 2.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   6 VVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDpASVQVLDELEQADD---ITVVRQGNAGPSAARNVGIRAART 82
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTD-DTLEILEELAALYIrrvLVVRDKENGGKAGALNAGLRHAKG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  83 DCVTVLDGDDRLLPTFLETTVGLLDGDASAVAASG-------------------WLRTFGVLDAVVKPTGGTIAdflprn 143
Cdd:cd06423   80 DIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGrvrvrngsenlltrlqaieYLSIFRLGRRAQSALGGVLV------ 153
                        170       180
                 ....*....|....*....|....
gi 705427975 144 aCPATFT-FRRTVWETCGGYDESM 166
Cdd:cd06423  154 -LSGAFGaFRREALREVGGWDEDT 176
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
6-123 1.26e-15

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: 73.38  E-value: 1.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   6 VVITSYNQNEMIREAVDSVRRQKLRPDA--IIVVDDGSTDpASVQVLDELEQAD--DITVVRQGNAGPSAARNVGIRAAR 81
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGYDyeIIVVDDGSTD-GTAEIARELAARVprVRVIRLSRNFGKGAAVRAGFKAAR 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 705427975  82 TDCVTVLDGDD----RLLPTFLETtvgLLDGDASAVAAS----------GWLRTFG 123
Cdd:cd04179   80 GDIVVTMDADLqhppEDIPKLLEK---LLEGGADVVIGSrfvrgggagmPLLRRLG 132
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
4-96 2.06e-13

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: 67.61  E-value: 2.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   4 VSVVITSYNQNE-MIREAVDSVRRQKLRPDAIIVVDDGSTDPASVQVLDELEQADD-ITVVRQG-NAGPSAARNVGIRAA 80
Cdd:cd04184    3 ISIVMPVYNTPEkYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDPrIKVVFREeNGGISAATNSALELA 82
                         90
                 ....*....|....*.
gi 705427975  81 RTDCVTVLDGDDRLLP 96
Cdd:cd04184   83 TGEFVALLDHDDELAP 98
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
6-100 2.63e-12

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: 64.14  E-value: 2.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   6 VVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDpASVQVLDELEQADDITV--VRQGNAG--PSAARNVGIRAAR 81
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTE-ETKELIEEFKSQFPIPIkhVWQEDEGfrKAKIRNKAIAAAK 79
                         90
                 ....*....|....*....
gi 705427975  82 TDCVTVLDGDDRLLPTFLE 100
Cdd:cd06420   80 GDYLIFIDGDCIPHPDFIA 98
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
2-179 3.92e-12

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


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 64.70  E-value: 3.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975    2 GNVSVVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDPAsVQVLDELE---QADDITVVRQ----GNAGPSAARN 74
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAET-LDVAEEIAarfPDVRLRVIRNarllGPTGKSRGLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   75 VGIRAARTDCVTVLDGDDRLLPTFLETTVGLLDG-DASAVAASGWLRTFGVLDAVV-----------KPTGGTIADFLPR 142
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSpKVGAVGTPVFSLNRSTMLSALgalefalrhlrMMSLRLALGVLPL 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 705427975  143 NacPATFTFRRTVWETCGGYDESMrCGFEDWDFCLSL 179
Cdd:pfam13641 161 S--GAGSAIRREVLKELGLFDPFF-LLGDDKSLGRRL 194
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
3-96 5.32e-12

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: 64.23  E-value: 5.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   3 NVSVVITSYNQNEMIREAVDSVRRQklrPDAIIVVDDGSTDpASVqvldELEQADDITVVRQGNAGPSAARNVGIRAART 82
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWA---VDEIIVVDSGSTD-RTV----EIAKEYGAKVYQRWWDGFGAQRNFALELATN 72
                         90
                 ....*....|....
gi 705427975  83 DCVTVLDGDDRLLP 96
Cdd:cd02511   73 DWVLSLDADERLTP 86
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
6-100 9.69e-12

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: 62.49  E-value: 9.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   6 VVITSYNQNEMIREAVDSVRR--QKLRPDA-IIVVDDGSTDpASVQVLDELEQADD-ITVVR-QGNAGPSAARNVGIRAA 80
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAvlESLGYDYeIIFVDDGSTD-RTLEILRELAARDPrVKVIRlSRNFGQQAALLAGLDHA 79
                         90       100
                 ....*....|....*....|....
gi 705427975  81 RTDCVTVLDGD--D--RLLPTFLE 100
Cdd:cd04187   80 RGDAVITMDADlqDppELIPEMLA 103
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-139 3.99e-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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 61.11  E-value: 3.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   6 VVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDpASVQVLDELEQADDITVVRQG-NAGPSAARNVGIR-AARTD 83
Cdd:cd04185    1 AVVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTD-GTAEWLTSLGDLDNIVYLRLPeNLGGAGGFYEGVRrAYELG 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705427975  84 C--VTVLDGDDRLLPTFLETTVGLLDGDASAVAASgwLR-----TF-GVL--DAVVKPTGGTIADF 139
Cdd:cd04185   80 YdwIWLMDDDAIPDPDALEKLLAYADKDNPQFLAP--LVldpdgSFvGVLisRRVVEKIGLPDKEF 143
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-145 3.27e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 58.80  E-value: 3.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   5 SVVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDpASVQVLDELEQADD---ITVVRQGNAGPsaARNV--GIRA 79
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTD-GTVEIIKEYIDKDPfiiILIRNGKNLGV--ARNFesLLQA 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705427975  80 ARTDCVTVLDGDDRLLPTFLETTVGLLDGDASAVAASGWLRTFgvlDAVVKPTGGTIADFLPRNAC 145
Cdd:cd04196   78 ADGDYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELV---DENGNPIGESFFEYQKIKPG 140
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
5-180 5.11e-10

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: 58.83  E-value: 5.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975    5 SVVITSYN--QNEMIREAVDSVRRQKLRPDAIIVVDDGSTDPASVQV--------LDELEQADDITVvrqgnaGPSAARN 74
Cdd:pfam10111   1 SVVIPVYNgeKTHWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVssikdhnlQVYYPNAPDTTY------SLAASRN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   75 VGIRAARTDCVTVLDGDDRLLPTFLETTVGLLDG-------DASAV--------AASGWLRTFG-------VLDAVVKPT 132
Cdd:pfam10111  75 RGTSHAIGEYISFIDGDCLWSPDKFEKQLKIATSlalqeniQAAVVlpvtdlndESSNFLRRGGdltasgdVLRDLLVFY 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 705427975  133 GGTIADFLPRNacpATFTFRRTVWETCGGYDESMRC-GFEDWDFCLSLL 180
Cdd:pfam10111 155 SPLAIFFAPNS---SNALINRQAFIEVGGFDESFRGhGAEDFDIFLRLA 200
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
6-116 1.39e-09

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: 57.16  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   6 VVITSYNQNEMIREAVDSVRRQKLRPDA-IIVVDDGSTDpASVQVLDELEQAD--DITVVRQGNAGPSAARNVGIRAART 82
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGIDYeIIVVDDNSPD-GTAEIVRELAKEYprVRLIVRPGKRGLGSAYIEGFKAARG 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 705427975  83 DCVTVLDGD----DRLLPTFLETtvgLLDGDASAVAAS 116
Cdd:cd06442   80 DVIVVMDADlshpPEYIPELLEA---QLEGGADLVIGS 114
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
6-179 5.84e-08

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: 52.67  E-value: 5.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   6 VVITSYNQN-EMIREAVDSVRRQKlrpDAIIVVDDGSTdpaSVQVLDELEQADDITVVRQG-NAGPSAARNVGIRAART- 82
Cdd:cd02526    1 AVVVTYNPDlSKLKELLAALAEQV---DKVVVVDNSSG---NDIELRLRLNSEKIELIHLGeNLGIAKALNIGIKAALEn 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  83 --DCVTVLDGDDRLLPTFLET---TVGLLDGDASAVAA------------SGWLRTFGVLDAVVKPTGGTIADflprnaC 145
Cdd:cd02526   75 gaDYVLLFDQDSVPPPDMVEKllaYKILSDKNSNIGAVgpriidrrtgenSPGVRKSGYKLRIQKEGEEGLKE------V 148
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 705427975 146 PATFT----FRRTVWETCGGYDESMRCGFEDWDFCLSL 179
Cdd:cd02526  149 DFLITsgslISLEALEKVGGFDEDLFIDYVDTEWCLRA 186
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
6-122 1.18e-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: 51.41  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   6 VVITSYNQNE----MIREAVDSVRRQKLRPDAIIVVDDGSTDpASVQVLDEL--EQADDITVVRQ-GNAGPSAARNVGIR 78
Cdd:cd04188    1 VVIPAYNEEKrlppTLEEAVEYLEERPSFSYEIIVVDDGSKD-GTAEVARKLarKNPALIRVLTLpKNRGKGGAVRAGML 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 705427975  79 AARTDCVTVLDGD--------DRLLPTFLETTVGLLDG-----DASAVAASGWLRTF 122
Cdd:cd04188   80 AARGDYILFADADlatpfeelEKLEEALKTSGYDIAIGsrahlASAAVVKRSWLRNL 136
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-177 2.71e-07

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 50.36  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   6 VVITSYNQNEMIREAVDSVRRQKLRPDA--IIVVDDGSTDpASVQVLDELEQADD-----ITVVRQGNAGPSAARNVGIR 78
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYPKEKfeVILVDDHSTD-GTVQILEFAAAKPNfqlkiLNNSRVSISGKKNALTTAIK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  79 AARTDCVTVLDGDDRLLPTFLETTV--------GLLDGDASAVAASGWLRTFGVLDAVVkpTGGTIADFL----PRNACP 146
Cdd:cd04192   80 AAKGDWIVTTDADCVVPSNWLLTFVafiqkeqiGLVAGPVIYFKGKSLLAKFQRLDWLS--LLGLIAGSFglgkPFMCNG 157
                        170       180       190
                 ....*....|....*....|....*....|.
gi 705427975 147 ATFTFRRTVWETCGGYDESMRCGFEDWDFCL 177
Cdd:cd04192  158 ANMAYRKEAFFEVGGFEGNDHIASGDDELLL 188
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
4-114 3.01e-07

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 50.26  E-value: 3.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   4 VSVVITSYNQN-EMIREAVDSVRRQKLRPDA--IIVVDDGsTDPASVQVLDELEQADDIT-VVRQGNAGPSAAR-NVGIR 78
Cdd:cd06421    3 VDVFIPTYNEPlEIVRKTLRAALAIDYPHDKlrVYVLDDG-RRPELRALAAELGVEYGYRyLTRPDNRHAKAGNlNNALA 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 705427975  79 AARTDCVTVLDGDDRLLPTFLETTVGLLDgDASAVA 114
Cdd:cd06421   82 HTTGDFVAILDADHVPTPDFLRRTLGYFL-DDPKVA 116
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
4-97 4.49e-07

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: 49.95  E-value: 4.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   4 VSVVITSYNQNEMI-REAVDSVRRQKlrPDAIIVVDDGSTDPaSVQVLDELEQADDITVVRQGNAGPSAARNVGIRAART 82
Cdd:cd06434    2 VTVIIPVYDEDPDVfRECLRSILRQK--PLEIIVVTDGDDEP-YLSILSQTVKYGGIFVITVPHPGKRRALAEGIRHVTT 78
                         90
                 ....*....|....*
gi 705427975  83 DCVTVLDgDDRLLPT 97
Cdd:cd06434   79 DIVVLLD-SDTVWPP 92
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
4-88 9.16e-07

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: 49.12  E-value: 9.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   4 VSVVITSYNQNEMIREAVDSVRRQKLRPDA--IIVVDDGSTDpASVQVLDELEQaDDITVVRQ-GNAGPSAARNVGIRAA 80
Cdd:cd06439   31 VTIIIPAYNEEAVIEAKLENLLALDYPRDRleIIVVSDGSTD-GTAEIAREYAD-KGVKLLRFpERRGKAAALNRALALA 108

                 ....*...
gi 705427975  81 RTDcVTVL 88
Cdd:cd06439  109 TGE-IVVF 115
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
4-179 1.58e-06

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: 47.95  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   4 VSVVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDpASVQVLDELEqaddiTVVRQGNAGPSAARNVGIRAARTD 83
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTD-GTVAIARSAG-----VVVISSPKGRARQMNAGAAAARGD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975  84 CVTVLDGDDRLLPTFLETTVGLLDGDAsAVAASGWLRTfgvldavvkpTGGTIADFLPRNA----CPATFT--------F 151
Cdd:cd02522   75 WLLFLHADTRLPPDWDAAIIETLRADG-AVAGAFRLRF----------DDPGPRLRLLELGanlrSRLFGLpygdqglfI 143
                        170       180       190
                 ....*....|....*....|....*....|
gi 705427975 152 RRTVWETCGGYDES--MrcgfEDWDFCLSL 179
Cdd:cd02522  144 RRELFEELGGFPELplM----EDVELVRRL 169
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
4-99 6.50e-06

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 46.91  E-value: 6.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   4 VSVVITSYNQNEMIREAVDSVRRQKLRPDAIIVVDDGSTDPASVQVLDELEQADDITVVRQG-NAGPSAARNVGIRAART 82
Cdd:PRK10018   7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCSTSWEQLQQYVTALNDPRITYIHNDiNSGACAVRNQAIMLAQG 86
                         90
                 ....*....|....*..
gi 705427975  83 DCVTVLDGDDRLLPTFL 99
Cdd:PRK10018  87 EYITGIDDDDEWTPNRL 103
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
4-124 2.05e-05

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 45.07  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   4 VSVVITSYNQNE-------MIREAVDSVRRQKlrpdaIIVVDDGSTDpASVQVLDELEQA---DDITVV-RQGNAGPSAA 72
Cdd:PLN02726  11 YSIIVPTYNERLnialivyLIFKALQDVKDFE-----IIVVDDGSPD-GTQDVVKQLQKVygeDRILLRpRPGKLGLGTA 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 705427975  73 RNVGIRAARTDCVTVLDGD----DRLLPTFLEttvGLLDGDASAVAASGWLRTFGV 124
Cdd:PLN02726  85 YIHGLKHASGDFVVIMDADlshhPKYLPSFIK---KQRETGADIVTGTRYVKGGGV 137
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
5-90 2.45e-05

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: 44.89  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   5 SVVITSYN-QNEMIREAVDSVR----RQKLRpdAIIVVDDGSTDPASVQVLDELEQA--DDITVVR-QGNAGPSAARNVG 76
Cdd:cd02510    1 SVIIIFHNeALSTLLRTVHSVInrtpPELLK--EIILVDDFSDKPELKLLLEEYYKKylPKVKVLRlKKREGLIRARIAG 78
                         90
                 ....*....|....
gi 705427975  77 IRAARTDCVTVLDG 90
Cdd:cd02510   79 ARAATGDVLVFLDS 92
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
3-91 1.17e-04

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 43.19  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   3 NVSVVITSYNQNEMIREAV---DSVRRQKLRPDAIIVVDDGSTDpASVQVLDELEQADD---ITVVRQGNAGPSAARNVG 76
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIrrtTAACESLGKEYEILLIDDGSSD-NSAEMLVEAAQAPDshiVAILLNRNYGQHSAIMAG 85
                         90
                 ....*....|....*
gi 705427975  77 IRAARTDCVTVLDGD 91
Cdd:PRK10714  86 FSHVTGDLIITLDAD 100
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
4-179 7.79e-04

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 39.80  E-value: 7.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975    4 VSVVITSYNQNEMIREAVDSVRRqkLRPDA-IIVVDDGSTDpASVQVLDELeqadDITVVrQGNAGPSAARNVGIRAART 82
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQA--LRGDAeVIVVDGGSTD-GTVEIARSL----GAKVI-HSPKGRARQMNAGAALAKG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   83 DCVTVLDGDDRLLPTFLETTVGLLDGDASAVAA--------SGWLRtfgVLDAVVK--------PTGgtiaDflprnacp 146
Cdd:TIGR04283  73 DILLFLHADTRLPKDFLEAIRRALAKPGYVAGAfdlrfdgpGLLLR---LIEWGVNlrsrltgiPYG----D-------- 137
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 705427975  147 ATFTFRRTVWETCGGYDES--MrcgfEDWDFCLSL 179
Cdd:TIGR04283 138 QGLFVRRSLFEQIGGFPDIplM----EDIELSRRL 168
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
4-118 1.67e-03

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: 39.22  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   4 VSVVITSYNQNEMIREAVDSVR-----RQKLRpdaIIVVDDgSTDPaSVQVLDELE-----QADDITVVRQGN-----AG 68
Cdd:cd06437    3 VTVQLPVFNEKYVVERLIEAACaldypKDRLE---IQVLDD-STDE-TVRLAREIVeeyaaQGVNIKHVRRADrtgykAG 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 705427975  69 PSAArnvGIRAARTDCVTVLDGDDRLLPTFLETTVGLLDGDASAVAASGW 118
Cdd:cd06437   78 ALAE---GMKVAKGEYVAIFDADFVPPPDFLQKTPPYFADPKLGFVQTRW 124
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
5-122 1.69e-03

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 39.37  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   5 SVVITSYNQ----NEMIREAVDSVRRqKLRPDA-----IIVVDDGSTDPASVQVLDELEQAD----DITVVR-QGNAGPS 70
Cdd:PTZ00260  73 SIVIPAYNEedrlPKMLKETIKYLES-RSRKDPkfkyeIIIVNDGSKDKTLKVAKDFWRQNInpniDIRLLSlLRNKGKG 151
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705427975  71 AARNVGIRAARTDCVTVLDGD--------DRLLPTFLET-------TVG----LLDGDasAVAASGWLRTF 122
Cdd:PTZ00260 152 GAVRIGMLASRGKYILMVDADgatdiddfDKLEDIMLKIeqnglgiVFGsrnhLVDSD--VVAKRKWYRNI 220
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
6-96 2.75e-03

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 38.21  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705427975   6 VVITSYNQNEMIREAVDSVRRQKLR-PDAIIVVDDGSTDPASVQVLD---ELEQADDITVVRQGNA----GPSAARNVGI 77
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDFEgTLELSVFNDASTDKSAEIIEKwrkKLEDSGVIVLVGSHNSpspkGVGYAKNQAI 80
                         90
                 ....*....|....*....
gi 705427975  78 RAARTDCVTVLDGDDRLLP 96
Cdd:cd06913   81 AQSSGRYLCFLDSDDVMMP 99
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
4-43 3.22e-03

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 38.36  E-value: 3.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 705427975   4 VSVVITSYNQNEMIREAVDSVRRQKLRP--DAIIVVDDGSTD 43
Cdd:PRK13915  33 VSVVLPALNEEETVGKVVDSIRPLLMEPlvDELIVIDSGSTD 74
 
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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