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Conserved domains on  [gi|2462626986|ref|XP_054220043|]
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alpha-1,3/1,6-mannosyltransferase ALG2 isoform X1 [Homo sapiens]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
14-314 4.78e-176

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


The actual alignment was detected with superfamily member cd03805:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 392  Bit Score: 492.87  E-value: 4.78e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  14 FGEKFKLFTL--VSACIPVFRLARRRKkILFYCHFPDLLLTKRDSFLKRLYRAPIDWIEEYTTGMADCILVNSQFTAAVF 91
Cdd:cd03805    91 SGEKYDVFIVdqVSACVPLLKLFRPSK-ILFYCHFPDQLLAQRKSLLKRLYRKPFDWLEEFTTGMADQIVVNSNFTAGVF 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  92 KETFKSLSHIDPDVLYPSLNVTSFDSVVPEK-LDDLVPKGKKFLLLSINRYERKKNLTLALEALVQLRGRLTSqdWERVH 170
Cdd:cd03805   170 KKTFPSLAKNPPEVLYPCVDTDSFDSTSEDPdPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQKLPE--FENVR 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 171 LIVAGGYDERVLENVEHYQELKKMVQQ-SDLGQYVTFLRSFSDKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVI 249
Cdd:cd03805   248 LVIAGGYDPRVAENVEYLEELQRLAEElLNVEDQVLFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPLEAMYAGKPVI 327
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462626986 250 AVNSGGPLESIDHSVTGFLCEPDPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQL 314
Cdd:cd03805   328 ACNSGGPLETVVEGVTGFLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAERL 392
 
Name Accession Description Interval E-value
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
14-314 4.78e-176

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 492.87  E-value: 4.78e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  14 FGEKFKLFTL--VSACIPVFRLARRRKkILFYCHFPDLLLTKRDSFLKRLYRAPIDWIEEYTTGMADCILVNSQFTAAVF 91
Cdd:cd03805    91 SGEKYDVFIVdqVSACVPLLKLFRPSK-ILFYCHFPDQLLAQRKSLLKRLYRKPFDWLEEFTTGMADQIVVNSNFTAGVF 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  92 KETFKSLSHIDPDVLYPSLNVTSFDSVVPEK-LDDLVPKGKKFLLLSINRYERKKNLTLALEALVQLRGRLTSqdWERVH 170
Cdd:cd03805   170 KKTFPSLAKNPPEVLYPCVDTDSFDSTSEDPdPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQKLPE--FENVR 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 171 LIVAGGYDERVLENVEHYQELKKMVQQ-SDLGQYVTFLRSFSDKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVI 249
Cdd:cd03805   248 LVIAGGYDPRVAENVEYLEELQRLAEElLNVEDQVLFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPLEAMYAGKPVI 327
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462626986 250 AVNSGGPLESIDHSVTGFLCEPDPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQL 314
Cdd:cd03805   328 ACNSGGPLETVVEGVTGFLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAERL 392
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
131-300 2.33e-32

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 117.76  E-value: 2.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 131 KKFLLLSINRYERKKNLTLALEALVQLRGRLtsqdwERVHLIVAGGYDERvlenvehyQELKKMVQQSDLGQYVTFLRSF 210
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKN-----PNLKLVIAGDGEEE--------KRLKKLAEKLGLGDNVIFLGFV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 211 SDKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEP-DPVHFSEAIEKFIREPSL 289
Cdd:pfam00534  68 SDEDLPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPnNAEALAEAIDKLLEDEEL 147
                         170
                  ....*....|.
gi 2462626986 290 KATMGLAGRAR 300
Cdd:pfam00534 148 RERLGENARKR 158
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
218-322 1.56e-26

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 101.22  E-value: 1.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 218 LLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEP-DPVHFSEAIEKFIREPSLKATMGLA 296
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPgDPEALAEAILRLLEDPELRRRLGEA 96
                          90       100
                  ....*....|....*....|....*.
gi 2462626986 297 GRARVKEKFSPEAFTEQLYRYVTKLL 322
Cdd:COG0438    97 ARERAEERFSWEAIAERLLALYEELL 122
PLN02949 PLN02949
transferase, transferring glycosyl groups
56-322 1.14e-16

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 80.17  E-value: 1.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  56 SFLKRLYRAPIDWIEEYTTGMADCILVNSQFTAAVFKETFKSLSHIDpdVLYPSLNVTSFDSVVPEKLDDlvpkGKKFLl 135
Cdd:PLN02949  200 STCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPERIK--RVYPPCDTSGLQALPLERSED----PPYII- 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 136 lSINRYERKKNLTLALEALVQLRGRLTSqDWERVHLIVAGG----YDERVLenvehyQELKKMVQQSDLGQYVTFLRSFS 211
Cdd:PLN02949  273 -SVAQFRPEKAHALQLEAFALALEKLDA-DVPRPKLQFVGScrnkEDEERL------QKLKDRAKELGLDGDVEFHKNVS 344
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 212 DKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGP-----LESIDHSvTGFLCEPDPvHFSEAIEKFIRE 286
Cdd:PLN02949  345 YRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPkmdivLDEDGQQ-TGFLATTVE-EYADAILEVLRM 422
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2462626986 287 PSlKATMGLAGRARVK-EKFSPEAFTEQLYRYVTKLL 322
Cdd:PLN02949  423 RE-TERLEIAAAARKRaNRFSEQRFNEDFKDAIRPIL 458
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
130-316 1.24e-15

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 76.69  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 130 GKKFLLLSINRYERKKNLTLALEALVQLRGRLtSQDWERVHLIVAGGYDERvlenvehyQELKKMVQQSDLGQYVTFLRS 209
Cdd:TIGR03088 192 DESVVVGTVGRLQAVKDQPTLVRAFALLVRQL-PEGAERLRLVIVGDGPAR--------GACEQMVRAAGLAHLVWLPGE 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 210 FSDkqkISLLHSCTCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEP-DPVHFSEAIEKFIREP 287
Cdd:TIGR03088 263 RDD---VPALMQALDLFVLPSlAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPgDAVALARALQPYVSDP 339
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462626986 288 SLKATMGLAGRARVKEKFSPEAFTEQ---LYR 316
Cdd:TIGR03088 340 AARRAHGAAGRARAEQQFSINAMVAAyagLYD 371
 
Name Accession Description Interval E-value
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
14-314 4.78e-176

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 492.87  E-value: 4.78e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  14 FGEKFKLFTL--VSACIPVFRLARRRKkILFYCHFPDLLLTKRDSFLKRLYRAPIDWIEEYTTGMADCILVNSQFTAAVF 91
Cdd:cd03805    91 SGEKYDVFIVdqVSACVPLLKLFRPSK-ILFYCHFPDQLLAQRKSLLKRLYRKPFDWLEEFTTGMADQIVVNSNFTAGVF 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  92 KETFKSLSHIDPDVLYPSLNVTSFDSVVPEK-LDDLVPKGKKFLLLSINRYERKKNLTLALEALVQLRGRLTSqdWERVH 170
Cdd:cd03805   170 KKTFPSLAKNPPEVLYPCVDTDSFDSTSEDPdPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQKLPE--FENVR 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 171 LIVAGGYDERVLENVEHYQELKKMVQQ-SDLGQYVTFLRSFSDKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVI 249
Cdd:cd03805   248 LVIAGGYDPRVAENVEYLEELQRLAEElLNVEDQVLFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPLEAMYAGKPVI 327
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462626986 250 AVNSGGPLESIDHSVTGFLCEPDPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQL 314
Cdd:cd03805   328 ACNSGGPLETVVEGVTGFLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAERL 392
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
20-316 1.35e-38

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 139.98  E-value: 1.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  20 LFTLVSACIPVFRLARRRKKILFYCH-FPDLLLTKRDSFLKRLYRAPIDWIEEYTTgmadcILVNSQFTAAVFKETFKSL 98
Cdd:cd03801    88 AHGLLAALLAALLALLLGAPLVVTLHgAEPGRLLLLLAAERRLLARAEALLRRADA-----VIAVSEALRDELRALGGIP 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  99 SHiDPDVLYPSLNVTSFDSVVPEKLDdlvPKGKKFLLLSINRYERKKNLTLALEALVQLRGRltsqdWERVHLIVAGGYD 178
Cdd:cd03801   163 PE-KIVVIPNGVDLERFSPPLRRKLG---IPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRR-----GPDVRLVIVGGDG 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 179 ErvlenveHYQELKKMvqQSDLGQYVTFLRSFSDKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLE 258
Cdd:cd03801   234 P-------LRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPE 304
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462626986 259 SIDHSVTGFLCEPDPVH-FSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQLYR 316
Cdd:cd03801   305 VVEDGEGGLVVPPDDVEaLADALLRLLADPELRARLGRAARERVAERFSWERVAERLLD 363
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
131-300 2.33e-32

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 117.76  E-value: 2.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 131 KKFLLLSINRYERKKNLTLALEALVQLRGRLtsqdwERVHLIVAGGYDERvlenvehyQELKKMVQQSDLGQYVTFLRSF 210
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKN-----PNLKLVIAGDGEEE--------KRLKKLAEKLGLGDNVIFLGFV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 211 SDKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEP-DPVHFSEAIEKFIREPSL 289
Cdd:pfam00534  68 SDEDLPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPnNAEALAEAIDKLLEDEEL 147
                         170
                  ....*....|.
gi 2462626986 290 KATMGLAGRAR 300
Cdd:pfam00534 148 RERLGENARKR 158
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
21-310 7.82e-30

alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.


Pssm-ID: 340835 [Multi-domain]  Cd Length: 419  Bit Score: 117.32  E-value: 7.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  21 FTLvsaciPVFRLARRRKkILFYCHFP----DLL--------------LTKRDSFL---KRLYRAPIDWIEEYTTGMADC 79
Cdd:cd03806   119 FTY-----PLVRLLGGCP-VVAYVHYPtistDMLnkvrsreasynndsTIARSSVLsiaKLLYYRLFAFLYGLAGSFADV 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  80 ILVNSQFTAAVFKETFKSlsHIDPDVLYPSLNVTSFDSVvpekldDLVPKGKKFLLLSINRYERKKNLTLALEALVQLRG 159
Cdd:cd03806   193 VMVNSTWTYNHIRQLWKR--NIKPSIVYPPCDTEELTKL------PIDEKTRENQILSIAQFRPEKNHPLQLRAFAELLK 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 160 RLTSQDWERVHLIVAGG----YDErvlENVEhyqELKKMVQQSDLGQYVTFLR--SFSDKQKisLLHSCTCVLYTPSNEH 233
Cdd:cd03806   265 RLPESIRSNPKLVLIGScrneEDK---ERVE---ALKLLAKELILEDSVEFVVdaPYEELKE--LLSTASIGLHTMWNEH 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 234 FGIVPLEamYMQCPVIAV--NSGGPLESI----DHSVTGFLCEpDPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSP 307
Cdd:cd03806   337 FGIGVVE--YMAAGLIPLahASAGPLLDIvvpwDGGPTGFLAS-TPEEYAEAIEKILTLSEEERLQRREAARSSAERFSD 413

                  ...
gi 2462626986 308 EAF 310
Cdd:cd03806   414 EEF 416
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
59-314 2.25e-27

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 110.41  E-value: 2.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  59 KRLYRAPIDW--------IEEYTTGMADCILVNSQftaavfKETFKSLSHIDPD-----VLYPSLNVTSFdSVVPEKLDD 125
Cdd:cd03800   138 KYRHLGAQDTyhpslritAEEQILEAADRVIASTP------QEADELISLYGADpsrinVVPPGVDLERF-FPVDRAEAR 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 126 LVPKG---KKFLLLSINRYERKKNLTLALEALVQLRGRLtsqdwERVHLIVAGGYDERVLENVEhyQELKKMVQQSDLGQ 202
Cdd:cd03800   211 RARLLlppDKPVVLALGRLDPRKGIDTLVRAFAQLPELR-----ELANLVLVGGPSDDPLSMDR--EELAELAEELGLID 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 203 YVTFLRSFSDKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEP-DPVHFSEAIE 281
Cdd:cd03800   284 RVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPhDPEALAAALR 363
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2462626986 282 KFIREPSLKATMGLAGRARVKEKFSPEAFTEQL 314
Cdd:cd03800   364 RLLDDPALWQRLSRAGLERARAHYTWESVADQL 396
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
218-322 1.56e-26

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 101.22  E-value: 1.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 218 LLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEP-DPVHFSEAIEKFIREPSLKATMGLA 296
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPgDPEALAEAILRLLEDPELRRRLGEA 96
                          90       100
                  ....*....|....*....|....*.
gi 2462626986 297 GRARVKEKFSPEAFTEQLYRYVTKLL 322
Cdd:COG0438    97 ARERAEERFSWEAIAERLLALYEELL 122
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
32-314 2.98e-25

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 103.83  E-value: 2.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  32 RLARR---RKKILFYCHFPDLLLTKRdSFLKRLYRapidWIEEYTTGMADCILVNSQFTAAVFKEtfKSLSHIDPDVLYP 108
Cdd:cd03808    97 RLAARlagVPKVIYTVHGLGFVFTEG-KLLRLLYL----LLEKLALLFTDKVIFVNEDDRDLAIK--KGIIKKKKTVLIP 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 109 --SLNVTSFDSVVPeklddlVPKGKKFLLLSINRYERKKNLTLALEALVQLRGRLtsqdwERVHLIVAGGYDERvlenve 186
Cdd:cd03808   170 gsGVDLDRFQYSPE------SLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKG-----PNVRFLLVGDGELE------ 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 187 hyQELKKMVQQSDLGQYVTFLRSFSDKQkiSLLHSCTCVLYtPSN-EHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVT 265
Cdd:cd03808   233 --NPSEILIEKLGLEGRIEFLGFRSDVP--ELLAESDVFVL-PSYrEGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVN 307
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462626986 266 GFLCEP-DPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQL 314
Cdd:cd03808   308 GFLVPPgDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKL 357
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
31-314 8.45e-23

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 97.05  E-value: 8.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  31 FRLARRRKKILFYCHFPDLLLTKRDS-----------FLKRLYRAPIDWIEeYTTGM------ADCILVNSQFTAAVFKE 93
Cdd:cd03809    77 ILLPKKDKPDLLHSPHNTAPLLLKGCpqvvtihdlipLRYPEFFPKRFRLY-YRLLLpislrrADAIITVSEATRDDIIK 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  94 TFK-SLSHIDpdVLYPSlnvtsFDSVVPEKLDDLVPKGKKFL----LLSINRYERKKNLTLALEALVQLRGRLTsqdweR 168
Cdd:cd03809   156 FYGvPPEKIV--VIPLG-----VDPSFFPPESAAVLIAKYLLpepyFLYVGTLEPRKNHERLLKAFALLKKQGG-----D 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 169 VHLIVAGGYDERvlenvehYQELKKMVQQSDLGQYVTFLRSFSDKQKISLLHSCTCVLYtPS-NEHFGIVPLEAMYMQCP 247
Cdd:cd03809   224 LKLVIVGGKGWE-------DEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVF-PSlYEGFGLPVLEAMACGTP 295
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 248 VIAVNsGGPLESI--DHsvtGFLCEP-DPVHFSEAIEKFIREPSLKATMGLAGRARVKeKFSPEAFTEQL 314
Cdd:cd03809   296 VIASN-ISVLPEVagDA---ALYFDPlDPESIADAILRLLEDPSLREELIRKGLERAK-KFSWEKTAEKT 360
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
56-321 6.79e-21

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 91.96  E-value: 6.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  56 SFLKRLYRAPIDWIEEYTTGMADCILVNSQFTAAVFKE-----TFKSLSH-IDPDVLYPSLNvtsfdsvvPEKLDDLVPK 129
Cdd:cd03817   127 PKGKLLVKAVVRKLVRRFYNHTDAVIAPSEKIKDTLREygvkgPIEVIPNgIDLDKFEKPLN--------TEERRKLGLP 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 130 GKKFLLLSINRYERKKNLTLALEALVQLRGRltsqdwERVHLIVAG-GYDErvlenvehyQELKKMVQQSDLGQYVTFLR 208
Cdd:cd03817   199 PDEPILLYVGRLAKEKNIDFLLRAFAELKKE------PNIKLVIVGdGPER---------EELKELARELGLADKVIFTG 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 209 SFSDKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEPDPVHFSEAIEKFIREPS 288
Cdd:cd03817   264 FVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDETLAEKLLHLRENLE 343
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2462626986 289 LKATMGLAGRARVKEKfspeAFTEQLYRYVTKL 321
Cdd:cd03817   344 LLRKLSKNAEISAREF----AFAKSVEKLYEEV 372
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
25-314 2.02e-20

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 90.86  E-value: 2.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  25 SACIPVFRLARR-RKKILFYCH--FPDLLLTKRDSFLKRLYRApIDWIEEYTTGMADCILVNSQFTAAVFKETFKSLSHI 101
Cdd:cd03794   110 TLGLAALLLKKLrGAPFILDVRdlWPESLIALGVLKKGSLLKL-LKKLERKLYRLADAIIVLSPGLKEYLLRKGVPKEKI 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 102 DpdVLYPSLNVTSFDSVVPEKLDDLVPKGKKFLLL---SINRYErkkNLTLALEALVQLRGRltsqdwERVHLIVAGGYD 178
Cdd:cd03794   189 I--VIPNWADLEEFKPPPKDELRKKLGLDDKFVVVyagNIGKAQ---GLETLLEAAERLKRR------PDIRFLFVGDGD 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 179 ERvlenvehyQELKKMVQQSDLgQYVTFLRSFSDKQKISLLHSCTCVL--YTPSNEHFGIVP---LEAMYMQCPVIAVNS 253
Cdd:cd03794   258 EK--------ERLKELAKARGL-DNVTFLGRVPKEEVPELLSAADVGLvpLKDNPANRGSSPsklFEYMAAGKPILASDD 328
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462626986 254 GGPLESIDHSVTGFLCEP-DPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQL 314
Cdd:cd03794   329 GGSDLAVEINGCGLVVEPgDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRL 390
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
32-317 1.18e-19

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 88.12  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  32 RLARRRKKILF----YCHFPDLLLTKRDSFLKRLYRAPIDWIeeytTGMADCILVNSQFTAAVFKEtfkslsHIDPDVLY 107
Cdd:cd03814   101 LRAARRLGLPVvtsyHTDFPEYLSYYTLGPLSWLAWAYLRWF----HNPFDTTLVPSPSIARELEG------HGFERVRL 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 108 PSLNV--TSFDsvvPEKLDDLVPK----GKKFLLLSINRYERKKNLtlalEALVQLRGRLTSQDweRVHLIVAG-GYDER 180
Cdd:cd03814   171 WPRGVdtELFH---PSRRDAALRRrlgpPGRPLLLYVGRLAPEKNL----EALLDADLPLAASP--PVRLVVVGdGPARA 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 181 VLEnvehyqelKKMVQqsdlgqyVTFLRSFSDKQKISLLHSCTCVLYtPS-NEHFGIVPLEAMYMQCPVIAVNSGGPLES 259
Cdd:cd03814   242 ELE--------ARGPD-------VIFTGFLTGEELARAYASADVFVF-PSrTETFGLVVLEAMASGLPVVAADAGGPRDI 305
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462626986 260 IDHSVTGFLCEP-DPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQLYRY 317
Cdd:cd03814   306 VRPGGTGALVEPgDAAAFAAALRALLEDPELRRRMAARARAEAERYSWEAFLDNLLDYY 364
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
128-318 1.07e-18

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 85.03  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 128 PKGKKFLLLsINRYERKKNLTLALEALVQLRgrltsqdwerVHLIVAGGYDERvlenvEHYQELkkmvQQSDLGQYVTFL 207
Cdd:cd03802   166 PDPEDYLAF-LGRIAPEKGLEDAIRVARRAG----------LPLKIAGKVRDE-----DYFYYL----QEPLPGPRIEFI 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 208 RSFSDKQKISLLHSCTCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEPdpvhFSEAIEKFIRE 286
Cdd:cd03802   226 GEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDS----VEEMAEAIANI 301
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462626986 287 PSLKatmGLAGRARVKEKFSPEAFTEQ---LYRYV 318
Cdd:cd03802   302 DRID---RAACRRYAEDRFSAARMADRyeaLYRKV 333
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
23-292 2.58e-18

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 84.33  E-value: 2.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  23 LVSACIPVFRLARRRKKILFYCH-FPDLLLTKRDSFLKRLYRAPidwieeyttgMADCILVNSQFTAAVFKETFKSL-SH 100
Cdd:cd03811    91 LGFATYIVAKLAAARSKVIAWIHsSLSKLYYLKKKLLLKLKLYK----------KADKIVCVSKGIKEDLIRLGPSPpEK 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 101 IDpdVLYpslNVTSFDSVVPE-KLDDLVPKGKKFLLLSINRYERKKNLTLALEALVQLRGRLTSqdwerVHLIVAGGYDE 179
Cdd:cd03811   161 IE--VIY---NPIDIDRIRALaKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPD-----VKLVILGDGPL 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 180 RvlenvehyQELKKMVQQSDLGQYVTFLrsfsDKQK--ISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPL 257
Cdd:cd03811   231 R--------EELEKLAKELGLAERVIFL----GFQSnpYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPR 298
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2462626986 258 ESIDHSVTGFLCEPDPVHFSEAIEKFIREPSLKAT 292
Cdd:cd03811   299 EILDDGENGLLVPDGDAAALAGILAALLQKKLDAA 333
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
188-311 4.55e-18

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 83.48  E-value: 4.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 188 YQELKKMVQQSdLGQYVTFLRSFSDKQKISLLHSCTCVLYtPS---NEHFGIVPLEAMYMQCPVIA--VNSGGPLESIdH 262
Cdd:cd03795   229 KPDLEAQIELN-LLDNVKFLGRVDDEEKVIYLHLCDVFVF-PSvlrSEAFGIVLLEAMMCGKPVIStnIGTGVPYVNN-N 305
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462626986 263 SVTGFLCEP-DPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFT 311
Cdd:cd03795   306 GETGLVVPPkDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEKMK 355
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
132-285 2.97e-17

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 76.78  E-value: 2.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 132 KFLLLSINR-YERKKNLTLALEALVQLRGRLtsqdwERVHLIVAGGYDERVLENvehyqelkkmvQQSDLGQYVTFLRSF 210
Cdd:pfam13692   1 RPVILFVGRlHPNVKGVDYLLEAVPLLRKRD-----NDVRLVIVGDGPEEELEE-----------LAAGLEDRVIFTGFV 64
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626986 211 SDKQKisLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHsVTGFLCEP-DPVHFSEAIEKFIR 285
Cdd:pfam13692  65 EDLAE--LLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDG-ENGLLVPPgDPEALAEAILRLLE 137
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
69-315 9.19e-17

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 80.12  E-value: 9.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  69 IEEYTTGMADCILVNSQFTAAVFKETFKSLSHIDpdVLYPSLNVTSFDsvvPEkLDDLVPKGKKFLLLSINRYERKKNLT 148
Cdd:cd03798   143 LLRWALRRAARVIAVSKALAEELVALGVPRDRVD--VIPNGVDPARFQ---PE-DRGLGLPLDAFVILFVGRLIPRKGID 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 149 LALEALVQLRgrltsQDWERVHLIVAGGYDERvlenvehyQELKKMVQQSDLGQYVTFLRSFSDKQKISLLHSCTC-VLy 227
Cdd:cd03798   217 LLLEAFARLA-----KARPDVVLLIVGDGPLR--------EALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVfVL- 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 228 tPS-NEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEP-DPVHFSEAIEKFIREPsLKATMGLAGRARVKEKF 305
Cdd:cd03798   283 -PSrHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPgDADALAAALRRALAEP-YLRELGEAARARVAERF 360
                         250
                  ....*....|
gi 2462626986 306 SPEAFTEQLY 315
Cdd:cd03798   361 SWVKAADRIA 370
PLN02949 PLN02949
transferase, transferring glycosyl groups
56-322 1.14e-16

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 80.17  E-value: 1.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  56 SFLKRLYRAPIDWIEEYTTGMADCILVNSQFTAAVFKETFKSLSHIDpdVLYPSLNVTSFDSVVPEKLDDlvpkGKKFLl 135
Cdd:PLN02949  200 STCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPERIK--RVYPPCDTSGLQALPLERSED----PPYII- 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 136 lSINRYERKKNLTLALEALVQLRGRLTSqDWERVHLIVAGG----YDERVLenvehyQELKKMVQQSDLGQYVTFLRSFS 211
Cdd:PLN02949  273 -SVAQFRPEKAHALQLEAFALALEKLDA-DVPRPKLQFVGScrnkEDEERL------QKLKDRAKELGLDGDVEFHKNVS 344
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 212 DKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGP-----LESIDHSvTGFLCEPDPvHFSEAIEKFIRE 286
Cdd:PLN02949  345 YRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPkmdivLDEDGQQ-TGFLATTVE-EYADAILEVLRM 422
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2462626986 287 PSlKATMGLAGRARVK-EKFSPEAFTEQLYRYVTKLL 322
Cdd:PLN02949  423 RE-TERLEIAAAARKRaNRFSEQRFNEDFKDAIRPIL 458
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
126-322 2.89e-16

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 78.55  E-value: 2.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 126 LVPKGKKfLLLSINRYERKKNLTLALEALVQLRGRLTSQdwervhLIVAGGYDERVlenvehyqELKKMVQQSDLGQYVT 205
Cdd:cd04962   191 LAPPDEK-VVIHVSNFRPVKRIDDVVRVFARVRRKIPAK------LLLVGDGPERV--------PAEELARELGVEDRVL 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 206 FLRSFSDKQKIslLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEPDPVH-FSEAIEKFI 284
Cdd:cd04962   256 FLGKQDDVEEL--LSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDaMAKSALSIL 333
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462626986 285 REPSLKATMGLAGRARVKEKFSPEAFTEQlYRYVTKLL 322
Cdd:cd04962   334 EDDELYNRMGRAARKRAAERFDPERIVPQ-YEAYYRRL 370
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
2-317 3.70e-16

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 77.78  E-value: 3.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986   2 PLLKlvHGSPLVFGEKFKLFTLVSACIPVFRLARRRKKI---LFYCHF--PDLLltkrdSFL-KRLYRAPI-------DW 68
Cdd:cd03819    39 PLLP--RLRQIGIGLPGLKVPLLRALLGNVRLARLIRREridLIHAHSraPAWL-----GWLaSRLTGVPLvttvhgsYL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  69 IEEYTTGMADCILVNSQFTAAV---FKETFKSLSHIDPD---VLYPSLNVTSFD-SVVPEKLDDLVPKGKKFLLLSINRY 141
Cdd:cd03819   112 ATYHPKDFALAVRARGDRVIAVselVRDHLIEALGVDPErirVIPNGVDTDRFPpEAEAEERAQLGLPEGKPVVGYVGRL 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 142 ERKKNLTLALEALVQLrgrltsQDWERVHLIVAGGYDERvlenvehyQELKKMVQQSDLGQYVTFLrSFSDKQKiSLLHS 221
Cdd:cd03819   192 SPEKGWLLLVDAAAEL------KDEPDFRLLVAGDGPER--------DEIRRLVERLGLRDRVTFT-GFREDVP-AALAA 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 222 CTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEP-DPVHFSEAIEKFIREPSLKATMGLAGRAR 300
Cdd:cd03819   256 SDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPgDAEALADAIRAAKLLPEAREKLQAAAALT 335
                         330
                  ....*....|....*..
gi 2462626986 301 vkekfspEAFTEQLYRY 317
Cdd:cd03819   336 -------EAVRELLLRV 345
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
128-313 5.39e-16

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 77.66  E-value: 5.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 128 PKGKKFLllSINRYERKKNLTLALEALVQLRGRLtsQDWErvhLIVAGGYDERvlenvehyQELKKMVQQSDLGQYVTFL 207
Cdd:cd03820   179 LKSKRIL--AVGRLTYQKGFDLLIEAWALIAKKH--PDWK---LRIYGDGPER--------EELEKLIDKLGLEDRVKLL 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 208 RSFSDKQKISLLHSCTCVlyTPSNEHFGIVPLEAMYMQCPVIAVNS-GGPLESIDHSVTGFLCEP-DPVHFSEAIEKFIR 285
Cdd:cd03820   244 GPTKNIAEEYANSSIFVL--SSRYEGFPMVLLEAMAYGLPIISFDCpTGPSEIIEDGENGLLVPNgDVDALAEALLRLME 321
                         170       180
                  ....*....|....*....|....*...
gi 2462626986 286 EPSLKATMGLAGRARVkEKFSPEAFTEQ 313
Cdd:cd03820   322 DEELRKKMGKNARKNA-ERFSIEKIIKQ 348
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
130-316 1.24e-15

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 76.69  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 130 GKKFLLLSINRYERKKNLTLALEALVQLRGRLtSQDWERVHLIVAGGYDERvlenvehyQELKKMVQQSDLGQYVTFLRS 209
Cdd:TIGR03088 192 DESVVVGTVGRLQAVKDQPTLVRAFALLVRQL-PEGAERLRLVIVGDGPAR--------GACEQMVRAAGLAHLVWLPGE 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 210 FSDkqkISLLHSCTCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEP-DPVHFSEAIEKFIREP 287
Cdd:TIGR03088 263 RDD---VPALMQALDLFVLPSlAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPgDAVALARALQPYVSDP 339
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462626986 288 SLKATMGLAGRARVKEKFSPEAFTEQ---LYR 316
Cdd:TIGR03088 340 AARRAHGAAGRARAEQQFSINAMVAAyagLYD 371
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
78-310 2.48e-14

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 72.70  E-value: 2.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  78 DCILVNSQFTAAVFKETFkslsHIDPDVLYPSLNVTSFDsVVPEKLDDlvpkgkkFLLLSinRYERKKNLTLALEALVQL 157
Cdd:cd03804   159 DLFIANSQFVARRIKKFY----GRESTVIYPPVDTDAFA-PAADKEDY-------YLTAS--RLVPYKRIDLAVEAFNEL 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 158 RGRLtsqdwervhlIVAG-GYDErvlenvehyQELKKMVQQSdlgqyVTFLRSFSDKQKISLLHSCTCVLYtPSNEHFGI 236
Cdd:cd03804   225 PKRL----------VVIGdGPDL---------DRLRAMASPN-----VEFLGYQPDEVLKELLSKARAFVF-AAEEDFGI 279
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462626986 237 VPLEAMYMQCPVIAVNSGGPLESIDHSVTGFL-CEPDPVHFSEAIEKFIREPSLKATMGLAGRArvkEKFSPEAF 310
Cdd:cd03804   280 VPVEAQACGTPVIAFGKGGALETVRPGPTGILfGEQTVESLKAAVEEFEQNFDRFKPQAIRANA---ERFSRARF 351
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
30-316 7.18e-14

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 71.58  E-value: 7.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  30 VFRLARRRKKI---LFYCHFPDLLLTKRdsFLKRLYRAP-------IDWIEEYTTGMA-----------DCILVNSQFTA 88
Cdd:cd03807    68 LLRLAKLIRKRnpdVVHTWMYHADLIGG--LAAKLAGGVkviwsvrSSNIPQRLTRLVrklclllskfsPATVANSSAVA 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  89 AVFKETfkslsHIDPDVLYPSLNVTSFDSVVPEKLDDLVPK------GKKFLLLSINRYERKKNLTLALEALVQLRgrlt 162
Cdd:cd03807   146 EFHQEQ-----GYAKNKIVVIYNGIDLFKLSPDDASRARARrrlglaEDRRVIGIVGRLHPVKDHSDLLRAAALLV---- 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 163 sQDWERVHLIVAGGYDERvlenvehyQELKKMVQQSDLGQYVTFLRSFSDKQkiSLLHSCTCVLYTPSNEHFGIVPLEAM 242
Cdd:cd03807   217 -ETHPDLRLLLVGRGPER--------PNLERLLLELGLEDRVHLLGERSDVP--ALLPAMDIFVLSSRTEGFPNALLEAM 285
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462626986 243 YMQCPVIAVNSGGPLESIDHSvTGFLCEP-DPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFT---EQLYR 316
Cdd:cd03807   286 ACGLPVVATDVGGAAELVDDG-TGFLVPAgDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVrryETLYY 362
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
136-269 1.92e-13

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 68.58  E-value: 1.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 136 LSINRYERKKNLTLALEALVQLRgrltsQDWERVHLIVAGGYDERvlenvehyQELKKMVQQSDLGQYVTFLRSFSDKQK 215
Cdd:cd01635   114 VSVGRLVPEKGIDLLLEALALLK-----ARLPDLVLVLVGGGGER--------EEEEALAAALGLLERVVIIGGLVDDEV 180
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462626986 216 ISLLHSCTCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLC 269
Cdd:cd01635   181 LELLLAAADVFVLPSrSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
26-319 3.61e-12

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 66.58  E-value: 3.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  26 ACIPVFRlARRRKKILFYCHFpDLlltkRDSFLKRLYRApIDWIEEYTtgmadcilvnSQFTAAVF--KETFKSLSHIDP 103
Cdd:cd03792    99 ALLPKIK-KKRDRKWIWRCHI-DI----STPLTEPQPRV-WDFLWNYI----------EGYDLFVFhpPEFVPPQVPPPK 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 104 DVLYPS------LNVTSFDSVVP---EKLDDLVPKgkKFLLLSINRYERKKNLTLALEALvqlrgRLTSQDWERVHLIVA 174
Cdd:cd03792   162 FYIPPSidplsgKNKDLSPADIRyylEKPFVIDPE--RPYILQVARFDPSKDPLGVIDAY-----KLFKRRAEEPQLVIC 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 175 GGY------DERVLENVEHYQELKKMVqqsdlgqyvTFLR-SFSDKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCP 247
Cdd:cd03792   235 GHGavddpeGSVVYEEVMEYAGDDHDI---------HVLRlPPSDQEINALQRAATVVLQLSTREGFGLTVSEALWKGKP 305
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626986 248 VIAVNSGG-PLEsIDHSVTGFLC---EPDPVHfseaIEKFIREPSLKATMGLAGRARVKEKFSPeafTEQLYRYVT 319
Cdd:cd03792   306 VIATPAGGiPLQ-VIDGETGFLVnsvEGAAVR----ILRLLTDPELRRKMGLAAREHVRDNFLI---TGNLRAWLY 373
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
20-314 6.51e-12

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 65.47  E-value: 6.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  20 LFTLVSAciPVFRLARRRKkiLFYCHFP--DLLLTKRDS--FLKRLYRapiDWIEEYTTGMADCILVNS-QFTAAVFKET 94
Cdd:cd03821    99 VWTYTSL--AACKLARRRG--IPYVVSPhgMLDPWALQQkhWKKRIAL---HLIERRNLNNAALVHFTSeQEADELRRFG 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  95 FKSlshidPDVLYP-SLNVTSFDSVVPEKLDDLVPKGKKFLL-LSinRYERKKNLTLALEALVQLrgrltSQDWERVHLI 172
Cdd:cd03821   172 LEP-----PIAVIPnGVDIPEFDPGLRDRRKHNGLEDRRIILfLG--RIHPKKGLDLLIRAARKL-----AEQGRDWHLV 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 173 VAGgYDERvlenvehyQELKKMVQQSD--LGQYVTFLRSFSDKQKISLLHSCTC-VLytPS-NEHFGIVPLEAMYMQCPV 248
Cdd:cd03821   240 IAG-PDDG--------AYPAFLQLQSSlgLGDRVTFTGPLYGEAKWALYASADLfVL--PSySENFGNVVAEALACGLPV 308
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462626986 249 IAVNSGGPLESIDHSvTGFLCEPDPVHFSEAIEKFIREPSLKATMGLAGRA--RVKEKFSPEAFTEQL 314
Cdd:cd03821   309 VITDKCGLSELVEAG-CGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRarQVEENFSWEAVAGQL 375
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
135-314 1.14e-11

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 64.78  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 135 LLSINRYERKKNLTLALEALVQLRGRLTSqdwerVHLIVAGGYDERvlenvehyQELKKMVqqSDLGQyVTFLRSFSDKQ 214
Cdd:cd05844   192 ILFVGRLVEKKGCDVLIEAFRRLAARHPT-----ARLVIAGDGPLR--------PALQALA--AALGR-VRFLGALPHAE 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 215 KISLLHSCTcVLYTPS-------NEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLC-EPDPVHFSEAIEKFIRE 286
Cdd:cd05844   256 VQDWMRRAE-IFCLPSvtaasgdSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVpEGDVDALADALQALLAD 334
                         170       180
                  ....*....|....*....|....*...
gi 2462626986 287 PSLKATMGLAGRARVKEKFSPEAFTEQL 314
Cdd:cd05844   335 RALADRMGGAARAFVCEQFDIRVQTAKL 362
PLN00142 PLN00142
sucrose synthase
131-321 2.46e-11

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 64.61  E-value: 2.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 131 KKFLLLSINRYERKKNLTlaleALVQLRG---RLTsqdwERVHLIVAGGY-DERVLENVEHYQELKKM---VQQSDLGQY 203
Cdd:PLN00142  572 KKPIIFSMARLDRVKNLT----GLVEWYGknkRLR----ELVNLVVVGGFiDPSKSKDREEIAEIKKMhslIEKYNLKGQ 643
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 204 VTFLRSFSDKQKISLLHSCTC---------VLYtpsnEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCepDPV 274
Cdd:PLN00142  644 FRWIAAQTNRVRNGELYRYIAdtkgafvqpALY----EAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHI--DPY 717
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462626986 275 HFSEA-------IEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQL---------YRYVTKL 321
Cdd:PLN00142  718 HGDEAankiadfFEKCKEDPSYWNKISDAGLQRIYECYTWKIYAERLltlggvygfWKYVSKL 780
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
102-316 4.62e-11

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 63.51  E-value: 4.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 102 DPD---VLYPSLNVTSFDSVVPEKlddlvPKGKKFLLLSINRYERKKNLTLALEALVQLRGRL-TSQDWervhliVAGGY 177
Cdd:cd03813   265 DPDktrVIPNGIDIQRFAPAREER-----PEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMpDAEGW------LIGPE 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 178 DErvleNVEHYQELKKMVQQSDLGQYVTFLrsfsDKQKIS-LLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGP 256
Cdd:cd03813   334 DE----DPEYAQECKRLVASLGLENKVKFL----GFQNIKeYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSC 405
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626986 257 LESI-----DHSVTGFLCEP-DPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQlYR 316
Cdd:cd03813   406 RELIygaddALGQAGLVVPPaDPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDS-YR 470
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
128-314 1.50e-10

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 61.31  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 128 PKGKKFLLLSINRYERKKNLTLALEALVQLrgrltSQDWERVHLIVAGGYDervLENvehyqELKKMVQQSDLGQYVTFL 207
Cdd:cd03799   170 PLDGKIRILTVGRLTEKKGLEYAIEAVAKL-----AQKYPNIEYQIIGDGD---LKE-----QLQQLIQELNIGDCVKLL 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 208 RSFSDKQKISLLHScTCVLYTPS------NEHFGIVPL-EAMYMQCPVIAVNSGGPLESIDHSVTGFLC-EPDPVHFSEA 279
Cdd:cd03799   237 GWKPQEEIIEILDE-ADIFIAPSvtaadgDQDGPPNTLkEAMAMGLPVISTEHGGIPELVEDGVSGFLVpERDAEAIAEK 315
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462626986 280 IEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQL 314
Cdd:cd03799   316 LTYLIEHPAIWPEMGKAGRARVEEEYDINKLNDEL 350
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
78-316 3.14e-09

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 57.34  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986  78 DCILVNSQFTAAVFKETFKSLSHIDpdVLYPSLnvtSFDSVVPEKLddlVPKGKKFLLLSINRYERKKNLTLALEALvql 157
Cdd:cd03823   145 DAVLAPSRFTANLHEANGLFSARIS--VIPNAV---EPDLAPPPRR---RPGTERLRFGYIGRLTEEKGIDLLVEAF--- 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 158 rGRLTSQDWErvhLIVAGGYDErvlenveHYQElkkmvqQSDLGQYVTFLRSFSDKQKISLLHSCTCVLyTPS--NEHFG 235
Cdd:cd03823   214 -KRLPREDIE---LVIAGHGPL-------SDER------QIEGGRRIAFLGRVPTDDIKDFYEKIDVLV-VPSiwPEPFG 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 236 IVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEP-DPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFtEQL 314
Cdd:cd03823   276 LVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPgDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAEEY-LKL 354

                  ..
gi 2462626986 315 YR 316
Cdd:cd03823   355 YR 356
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
232-306 3.03e-08

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 54.26  E-value: 3.03e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626986 232 EHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEP-DPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFS 306
Cdd:cd03825   274 DNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPgDVQALAEAIEWLLANPKERESLGERARALAENHFD 349
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
225-314 4.01e-08

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 54.33  E-value: 4.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 225 VLYTPS-NEHFGIVPLEAMYMQCPVIAVNSGGPLESI---DHSVTGFLCEP-DPVHFSEAIEKFIREPSLKATMGLAGRA 299
Cdd:PLN02871  334 VFVMPSeSETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPgDVDDCVEKLETLLADPELRERMGAAARE 413
                          90
                  ....*....|....*
gi 2462626986 300 RVkEKFSPEAFTEQL 314
Cdd:PLN02871  414 EV-EKWDWRAATRKL 427
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
131-313 8.52e-06

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 46.91  E-value: 8.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 131 KKFLLLSINRYERKKNLTLALEALVQLRGRLTSQdweRVHLIvagGYDErvlenveHYQELKKMVQQSDLGQYVtFLRSF 210
Cdd:cd04949   159 KSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEI---TLDIY---GYGE-------EREKLKKLIEELHLEDNV-FLKGY 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 211 SDK-----QKISLLhsctcvLYTPSNEHFGIVPLEAMYMQCPVIAVNSG-GPLESIDHSVTGFLCEPDPVH-FSEAIEKF 283
Cdd:cd04949   225 HSNldqeyQDAYLS------LLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDaLADKIIEL 298
                         170       180       190
                  ....*....|....*....|....*....|
gi 2462626986 284 IREPSLKATMGLAGRArVKEKFSPEAFTEQ 313
Cdd:cd04949   299 LNDPEKLQQFSEESYK-IAEKYSTENVMEK 327
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
133-316 2.49e-05

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 45.51  E-value: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 133 FLLLSINRYERKK---NLTLALEALVQLRgrltsqdwERVHLIVAGgydERVLENvehyqELKKMVQQSDLGQYVTFLRS 209
Cdd:cd04951   189 FVILNVGRLTEAKdypNLLLAISELILSK--------NDFKLLIAG---DGPLRN-----ELERLICNLNLVDRVILLGQ 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 210 FSDkqkISLLHS-CTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSvTGFLCEPDPVHFSEAI-EKFIREP 287
Cdd:cd04951   253 ISN---ISEYYNaADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDH-NYVVPVSDPQLLAEKIkEIFDMSD 328
                         170       180
                  ....*....|....*....|....*....
gi 2462626986 288 SLKATMGLAGRARVKeKFSPEAFTEQLYR 316
Cdd:cd04951   329 EERDILGNKNEYIAK-NFSINTIVNEWER 356
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
157-306 3.87e-05

Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 45.05  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 157 LRGRLTSQ---DWERVHliVAGgydeRVlenveHYQELKKMVQQSDLGQYVT--FLRSFSdkqkisllhsctcvlytpsn 231
Cdd:cd03818   268 WKQKMLAElgvDLERVH--FVG----KV-----PYDQYVRLLQLSDAHVYLTypFVLSWS-------------------- 316
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626986 232 ehfgivPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCE-PDPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFS 306
Cdd:cd03818   317 ------LLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDfFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDS 386
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
29-89 7.34e-04

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 39.69  E-value: 7.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462626986  29 PVFRLARRRKKILFYCHFPDLLLTKRDSFLKRLYRapidWIEEYTTGMADCILVNSQFTAA 89
Cdd:pfam13579  84 LAARLARRRRGVPLVVTVHGLALDYGSGWKRRLAR----ALERRLLRRADAVVVVSEAEAE 140
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
234-314 1.59e-03

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 37.20  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 234 FGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEpDPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQ 313
Cdd:pfam13524  12 PNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYR-DPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHTYAHRAEQ 90

                  .
gi 2462626986 314 L 314
Cdd:pfam13524  91 L 91
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
239-316 2.15e-03

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 39.37  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 239 LEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEPDPV--HFSEAIEKFIREPSLKATMGLAGRARVKEKFSpeafTEQLYR 316
Cdd:cd04946   322 MEAISFGIPVIATNVGGTREIVENETNGLLLDKDPTpnEIVSSIMKFYLDGGDYKTMKISARECWEERFN----AEVNYS 397
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
110-284 3.51e-03

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 38.81  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 110 LNVTSFDSVVPEKLDDLVPKGKKFLLLSINRYERKKNLTLALEALVQLRGRltsqdWERVHLIVAGgydervleNVEHYQ 189
Cdd:cd03812   169 IEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKK-----NPNVKLVLVG--------EGELKE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626986 190 ELKKMVQQSDLGQYVTFLRSFSDkqkISLLHSCTCVLYTPSN-EHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFL 268
Cdd:cd03812   236 KIKEKVKELGLEDKVIFLGFRND---VSEILSAMDVFLFPSLyEGLPLVAVEAQASGLPCLLSDTITKECDITNNVEFLP 312
                         170
                  ....*....|....*.
gi 2462626986 269 CEPDPVHFSEAIEKFI 284
Cdd:cd03812   313 LNETPSTWAEKILKLI 328
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
33-95 3.84e-03

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 37.51  E-value: 3.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462626986  33 LARRRKKILFYCHFPDLLlTKRDSFLKRLYRAPIDWIEEYTTGMADCILVNSQFTAAVFKETF 95
Cdd:pfam13439  91 RLRLGIPLVVTYHGLFPD-YKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLY 152
 
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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