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Conserved domains on  [gi|914776607|ref|WP_050719329|]
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glycosyltransferase family 2 protein [Aeromonas tecta]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10118426)

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

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  9445404|12691742
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 5-234 4.68e-89

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: 263.38  E-value: 4.68e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   5 TLAAVLIVKNEADNLRACLASLGDLVDEIVILDSGSQDETPSIAAEFGARFFVNKeWPGFGRQRRLAQSHVQSQWVLWLD 84
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRW-WDGFGAQRNFALELATNDWVLSLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607  85 ADERLTPELKAAITTVMANPAKDtIYSLPRLSWVFGRFIRHSGWYPDRVLRLYPKALTGYNEALVHEKVEVRANMQIVnL 164
Cdd:cd02511   80 ADERLTPELADEILALLATDDYD-GYYVPRRNFFLGRWIRHGGWYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGIV-L 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914776607 165 HGDLLHFTYRDLEHYLVKSAGYARAWADQRTARGKKGSLGQGLVHA--LGCFLKMYLLKAGFLDGKQGLLLA 234
Cdd:cd02511  158 KGDILHYGYKSLEEFLEKHNRYSSLEAKDLAAKGKKRSLLKGLLLGrpLLAFLKMYILKRGFLDGRAGFILA 229
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 5-234 4.68e-89

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: 263.38  E-value: 4.68e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   5 TLAAVLIVKNEADNLRACLASLGDLVDEIVILDSGSQDETPSIAAEFGARFFVNKeWPGFGRQRRLAQSHVQSQWVLWLD 84
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRW-WDGFGAQRNFALELATNDWVLSLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607  85 ADERLTPELKAAITTVMANPAKDtIYSLPRLSWVFGRFIRHSGWYPDRVLRLYPKALTGYNEALVHEKVEVRANMQIVnL 164
Cdd:cd02511   80 ADERLTPELADEILALLATDDYD-GYYVPRRNFFLGRWIRHGGWYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGIV-L 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914776607 165 HGDLLHFTYRDLEHYLVKSAGYARAWADQRTARGKKGSLGQGLVHA--LGCFLKMYLLKAGFLDGKQGLLLA 234
Cdd:cd02511  158 KGDILHYGYKSLEEFLEKHNRYSSLEAKDLAAKGKKRSLLKGLLLGrpLLAFLKMYILKRGFLDGRAGFILA 229
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 3-144 1.21e-22

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 92.07  E-value: 1.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   3 KPTLAAVLIVKNEADNLRACLASL---GDLVDEIVILDSGSQDETPSIAAEFGA-----RFFVNKEWPGFGRQRRLAQSH 74
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLlaqTYPDFEIIVVDDGSTDGTAEILRELAAkdpriRVIRLERNRGKGAARNAGLAA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914776607  75 VQSQWVLWLDADERLTPELKAAITTVMANPAKDTIYS--LPRLSWVFGRFIRHSGWYPDRVLRLYPKALTGY 144
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGsrLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGF 152
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 9-150 1.01e-19

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: 83.21  E-value: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607    9 VLIVKNEADNLRACLASL---GDLVDEIVILDSGSQDETPSIAAEF-----GARFFVNKEWPGFGRQRRLAQSHVQSQWV 80
Cdd:pfam00535   3 IIPTYNEEKYLLETLESLlnqTYPNFEIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLPENRGKAGARNAGLRAATGDYI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914776607   81 LWLDADERLTPE-LKAAITTVMANPAKDTIYSLPRLSWVFGRFIRHSGWYPDRVLRLYPKALTGYNEALVH 150
Cdd:pfam00535  83 AFLDADDEVPPDwLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 5-54 6.31e-07

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 49.53  E-value: 6.31e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914776607   5 TLAAVLIVKNE----ADNLRACLASLGD-LVDEIVILDSGSQDETPSIAAEFGAR 54
Cdd:PRK13915  32 TVSVVLPALNEeetvGKVVDSIRPLLMEpLVDELIVIDSGSTDATAERAAAAGAR 86
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 5-234 4.68e-89

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: 263.38  E-value: 4.68e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   5 TLAAVLIVKNEADNLRACLASLGDLVDEIVILDSGSQDETPSIAAEFGARFFVNKeWPGFGRQRRLAQSHVQSQWVLWLD 84
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRW-WDGFGAQRNFALELATNDWVLSLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607  85 ADERLTPELKAAITTVMANPAKDtIYSLPRLSWVFGRFIRHSGWYPDRVLRLYPKALTGYNEALVHEKVEVRANMQIVnL 164
Cdd:cd02511   80 ADERLTPELADEILALLATDDYD-GYYVPRRNFFLGRWIRHGGWYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGIV-L 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914776607 165 HGDLLHFTYRDLEHYLVKSAGYARAWADQRTARGKKGSLGQGLVHA--LGCFLKMYLLKAGFLDGKQGLLLA 234
Cdd:cd02511  158 KGDILHYGYKSLEEFLEKHNRYSSLEAKDLAAKGKKRSLLKGLLLGrpLLAFLKMYILKRGFLDGRAGFILA 229
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 3-144 1.21e-22

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 92.07  E-value: 1.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   3 KPTLAAVLIVKNEADNLRACLASL---GDLVDEIVILDSGSQDETPSIAAEFGA-----RFFVNKEWPGFGRQRRLAQSH 74
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLlaqTYPDFEIIVVDDGSTDGTAEILRELAAkdpriRVIRLERNRGKGAARNAGLAA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914776607  75 VQSQWVLWLDADERLTPELKAAITTVMANPAKDTIYS--LPRLSWVFGRFIRHSGWYPDRVLRLYPKALTGY 144
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGsrLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGF 152
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 9-150 1.01e-19

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: 83.21  E-value: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607    9 VLIVKNEADNLRACLASL---GDLVDEIVILDSGSQDETPSIAAEF-----GARFFVNKEWPGFGRQRRLAQSHVQSQWV 80
Cdd:pfam00535   3 IIPTYNEEKYLLETLESLlnqTYPNFEIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLPENRGKAGARNAGLRAATGDYI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914776607   81 LWLDADERLTPE-LKAAITTVMANPAKDTIYSLPRLSWVFGRFIRHSGWYPDRVLRLYPKALTGYNEALVH 150
Cdd:pfam00535  83 AFLDADDEVPPDwLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 8-115 1.26e-14

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: 69.46  E-value: 1.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   8 AVLIVKNEADNLRACLASL---GDLVDEIVILDSGSQDETPSIAAEFGA-----RFFVNKEWPGFGRQRRLAQSHVQSQW 79
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLlaqTYPNFEVIVVDDGSTDGTLEILEEYAKkdprvIRVINEENQGLAAARNAGLKAARGEY 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 914776607  80 VLWLDADERLTPE-LKAAITTVMANPAKDTIYSLPRL 115
Cdd:cd00761   81 ILFLDADDLLLPDwLERLVAELLADPEADAVGGPGNL 117
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
3-92 3.01e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 69.25  E-value: 3.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   3 KPTLAAVLIVKNEADNLRACLASLG---DLVDEIVILDSGSQDETPSIAAEF---GARFFVNKEWPGFGRQRRLAQSHVQ 76
Cdd:COG1216    2 RPKVSVVIPTYNRPELLRRCLESLLaqtYPPFEVIVVDNGSTDGTAELLAALafpRVRVIRNPENLGFAAARNLGLRAAG 81

                         90
                 ....*....|....*.
gi 914776607  77 SQWVLWLDADERLTPE 92
Cdd:COG1216   82 GDYLLFLDDDTVVEPD 97
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 4-154 1.47e-12

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: 64.90  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   4 PTLaavlivkNEADNLRACLASL---GDLVDEIVILDSGSQDETPSIAAEFGARFFVNKewPGFGRQRRLAQSHVQSQWV 80
Cdd:cd02522    6 PTL-------NEAENLPRLLASLrrlNPLPLEIIVVDGGSTDGTVAIARSAGVVVISSP--KGRARQMNAGAAAARGDWL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607  81 LWLDADERLTPELKAAITTVMANPA-----------KDTIYSLPRLSWVFGRFiRHSGW-YPDRVL----RLYpKALTGY 144
Cdd:cd02522   77 LFLHADTRLPPDWDAAIIETLRADGavagafrlrfdDPGPRLRLLELGANLRS-RLFGLpYGDQGLfirrELF-EELGGF 154

                        170
                 ....*....|
gi 914776607 145 NEALVHEKVE 154
Cdd:cd02522  155 PELPLMEDVE 164
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 4-91 1.67e-11

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: 63.22  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   4 PTLAAVLIVKNEADNLRACLASLGDL-----VDEIVILDSGSQDETPSIAAEFGA-----RFFVNKEWPGFGRQRRLAQS 73
Cdd:COG1215   29 PRVSVIIPAYNEEAVIEETLRSLLAQdypkeKLEVIVVDDGSTDETAEIARELAAeyprvRVIERPENGGKAAALNAGLK 108

                         90
                 ....*....|....*...
gi 914776607  74 HVQSQWVLWLDADERLTP 91
Cdd:COG1215  109 AARGDIVVFLDADTVLDP 126
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 9-104 2.45e-07

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: 49.53  E-value: 2.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   9 VLI-VKNEADNLRACLASLGDL---VDEIVILDSGSQDETPSIAAEFGARFFVNK----EWPGFGRQRRLAQ--SHVQSQ 78
Cdd:cd06423    1 IIVpAYNEEAVIERTIESLLALdypKLEVIVVDDGSTDDTLEILEELAALYIRRVlvvrDKENGGKAGALNAglRHAKGD 80

                         90       100
                 ....*....|....*....|....*..
gi 914776607  79 WVLWLDADERLTPE-LKAAITTVMANP 104
Cdd:cd06423   81 IVVVLDADTILEPDaLKRLVVPFFADP 107
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 9-86 5.36e-07

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: 48.72  E-value: 5.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   9 VLI-VKNEADNLRACLASL-----GDLVDEIVILDSGSQDETPSIAAEFGARFFVNKEWP-----GFGRQRRLAQSHVQS 77
Cdd:cd04179    1 VVIpAYNEEENIPELVERLlavleEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRlsrnfGKGAAVRAGFKAARG 80


                 ....*....
gi 914776607  78 QWVLWLDAD 86
Cdd:cd04179   81 DIVVTMDAD 89
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 5-54 6.31e-07

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 49.53  E-value: 6.31e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914776607   5 TLAAVLIVKNE----ADNLRACLASLGD-LVDEIVILDSGSQDETPSIAAEFGAR 54
Cdd:PRK13915  32 TVSVVLPALNEeetvGKVVDSIRPLLMEpLVDELIVIDSGSTDATAERAAAAGAR 86
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 9-55 1.61e-06

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: 48.00  E-value: 1.61e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 914776607   9 VLIVKNEADNLRACLASL------GDLVdEIVILDSGSQDETPSIAAEFGARF 55
Cdd:cd02525    5 IIPVRNEEKYIEELLESLlnqsypKDLI-EIIVVDGGSTDGTREIVQEYAAKD 56
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 9-91 4.46e-06

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 45.63  E-value: 4.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   9 VLIVKNEADNLRACLASLGDLVD---EIVILDSGSQDETPSIAAEFGARFFV--NKEWPGFGRQRRLAQSHVQSQWVLWL 83
Cdd:cd04186    2 IIVNYNSLEYLKACLDSLLAQTYpdfEVIVVDNASTDGSVELLRELFPEVRLirNGENLGFGAGNNQGIREAKGDYVLLL 81


                 ....*...
gi 914776607  84 DADERLTP 91
Cdd:cd04186   82 NPDTVVEP 89
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
 13-87 9.13e-05

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


Pssm-ID: 433416 [Multi-domain]  Cd Length: 97  Bit Score: 40.31  E-value: 9.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   13 KNEADNLRACLA---SLGdlVDEIVILDSGSQDETPSIAAEFGA-RFFVNKEwpGFGRQRR-------LAQSHVQSQWVL 81
Cdd:pfam13704   1 RNEADILPQWLAhhlALG--FDHIYVYDNGSDDGTAEILARLPDvSILRSDL--SYKDARFqvdwrnaLLARYAEADWVL 76


                  ....*.
gi 914776607   82 WLDADE 87
Cdd:pfam13704  77 VVDADE 82
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 14-95 1.11e-04

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: 42.17  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607  14 NEADNLRACLASLGDLVD-------EIVILDSGSQDETPSIAAEFGARFFVNKEWPGFGRQR------RLAQSHVQSQWV 80
Cdd:cd04188    7 NEEKRLPPTLEEAVEYLEerpsfsyEIIVVDDGSKDGTAEVARKLARKNPALIRVLTLPKNRgkggavRAGMLAARGDYI 86

                         90       100
                 ....*....|....*....|...
gi 914776607  81 LWLDAD--------ERLTPELKA 95
Cdd:cd04188   87 LFADADlatpfeelEKLEEALKT 109
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 14-86 2.44e-04

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 41.36  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607  14 NEADNLRACLASLGDLVD----EIVILDSGSQDETPSIAAEFGARFF-----VNKEWPGFGRQRRLAQSHVQSQWVLWLD 84
Cdd:cd06442    7 NERENIPELIERLDAALKgidyEIIVVDDNSPDGTAEIVRELAKEYPrvrliVRPGKRGLGSAYIEGFKAARGDVIVVMD 86


                 ..
gi 914776607  85 AD 86
Cdd:cd06442   87 AD 88
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 4-104 2.46e-03

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: 38.12  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607    4 PTLAAVLIVKNEADNLRACLASLGDLV---DEIVILDSGSQDETPSIAAEFGARFFVNKEW-------PGFGRQRRL--- 70
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPyppVEVVVVVNPSDAETLDVAEEIAARFPDVRLRvirnarlLGPTGKSRGlnh 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 914776607   71 AQSHVQSQWVLWLDADERLTPELKAAITTVMANP 104
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSP 115
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 3-93 4.19e-03

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 38.10  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   3 KPTLAAVLIVKNEADNLRACLASLGD--LVD-EIVILDSGSQDETPSIAAEFGARF----FVNKEWPGFGRQRRLAQSHV 75
Cdd:PRK10073   5 TPKLSIIIPLYNAGKDFRAFMESLIAqtWTAlEIIIVNDGSTDNSVEIAKHYAENYphvrLLHQANAGVSVARNTGLAVA 84

                         90
                 ....*....|....*...
gi 914776607  76 QSQWVLWLDADERLTPEL 93
Cdd:PRK10073  85 TGKYVAFPDADDVVYPTM 102
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 14-86 4.55e-03

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: 37.17  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607  14 NEADNLRACLASL---GDLVDEIVILDSGSQDETPSIAAEFGARFFVN-----KEWPGF--GRQRRLAQSHVQSQWVLWL 83
Cdd:cd06420    7 NRPEALELVLKSVlnqSILPFEVIIADDGSTEETKELIEEFKSQFPIPikhvwQEDEGFrkAKIRNKAIAAAKGDYLIFI 86


                 ...
gi 914776607  84 DAD 86
Cdd:cd06420   87 DGD 89
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 9-110 7.50e-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: 36.88  E-value: 7.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914776607   9 VLI-VKNEADNLRACLASLGDLvD------EIVILDSGSQDETPSIAAEFGA--RFFV----NKEWPGFGRQRRLAQ--S 73
Cdd:cd04192    1 VVIaARNEAENLPRLLQSLSAL-DypkekfEVILVDDHSTDGTVQILEFAAAkpNFQLkilnNSRVSISGKKNALTTaiK 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 914776607  74 HVQSQWVLWLDADERLTPELkaaITTVMANPAKDTIY 110
Cdd:cd04192   80 AAKGDWIVTTDADCVVPSNW---LLTFVAFIQKEQIG 113
 
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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