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Conserved domains on  [gi|1777466523|ref|XP_031533217|]
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alpha-1,3/1,6-mannosyltransferase ALG2 isoform X2 [Vicugna pacos]

Protein Classification

alpha-1,3/1,6-mannosyltransferase ALG2( domain architecture ID 10133515)

alpha-1,3/1,6-mannosyltransferase ALG2 mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate

CAZY:  GT4
Gene Symbol:  ALG2
Gene Ontology:  GO:0004378|GO:0006486
SCOP:  3001586

Graphical summary

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List of domain hits

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 ...
16-406 0e+00

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: 627.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  16 VLFLHPDLGVGGAERLVLDAALALQARGCSVKIWTAHYDPGHCFSESRE--LPVRCAGDWLPRSLGwgGR********** 93
Cdd:cd03805     3 VAFLHPDLGIGGAERLVVDAALALQSRGHEVTIYTSHHDPSHCFEETKDgtLPVRVRGDWLPRSIF--GRFHALCAYLRM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  94 ***ALYVLFLADEEFDVVVCDQVSACIPVFKLARRRKkILFYCHFPDLLLTRRDSFFKRLYRAPIDWVEEYTTGMADCIL 173
Cdd:cd03805    81 LYLALYLLLFSGEKYDVFIVDQVSACVPLLKLFRPSK-ILFYCHFPDQLLAQRKSLLKRLYRKPFDWLEEFTTGMADQIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 174 VNSRFTAAIFKETFKSLSHIDPDVLYPSLNITRFDSAIPEK-LDDLVPKGKKFLFLSINRYERKKNLTLALEALVKLRGR 252
Cdd:cd03805   160 VNSNFTAGVFKKTFPSLAKNPPEVLYPCVDTDSFDSTSEDPdPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 253 LTSqdWDKVHLIMAGGYDERVLENVQHYEELKKMVQ-LSDLGQYVTFLRSCSDEQKISLLRGCTCVLYTPSNEHFGIVPL 331
Cdd:cd03805   240 LPE--FENVRLVIAGGYDPRVAENVEYLEELQRLAEeLLNVEDQVLFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPL 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777466523 332 EAMYLQCPVIAVNSGGPLESVVHNVTGFLCEPDPVHFSEAMENFIHEPSLKATMGLAGRARVKEKFSPEAFTEQL 406
Cdd:cd03805   318 EAMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAERL 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 ...
16-406 0e+00

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: 627.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  16 VLFLHPDLGVGGAERLVLDAALALQARGCSVKIWTAHYDPGHCFSESRE--LPVRCAGDWLPRSLGwgGR********** 93
Cdd:cd03805     3 VAFLHPDLGIGGAERLVVDAALALQSRGHEVTIYTSHHDPSHCFEETKDgtLPVRVRGDWLPRSIF--GRFHALCAYLRM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  94 ***ALYVLFLADEEFDVVVCDQVSACIPVFKLARRRKkILFYCHFPDLLLTRRDSFFKRLYRAPIDWVEEYTTGMADCIL 173
Cdd:cd03805    81 LYLALYLLLFSGEKYDVFIVDQVSACVPLLKLFRPSK-ILFYCHFPDQLLAQRKSLLKRLYRKPFDWLEEFTTGMADQIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 174 VNSRFTAAIFKETFKSLSHIDPDVLYPSLNITRFDSAIPEK-LDDLVPKGKKFLFLSINRYERKKNLTLALEALVKLRGR 252
Cdd:cd03805   160 VNSNFTAGVFKKTFPSLAKNPPEVLYPCVDTDSFDSTSEDPdPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 253 LTSqdWDKVHLIMAGGYDERVLENVQHYEELKKMVQ-LSDLGQYVTFLRSCSDEQKISLLRGCTCVLYTPSNEHFGIVPL 331
Cdd:cd03805   240 LPE--FENVRLVIAGGYDPRVAENVEYLEELQRLAEeLLNVEDQVLFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPL 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777466523 332 EAMYLQCPVIAVNSGGPLESVVHNVTGFLCEPDPVHFSEAMENFIHEPSLKATMGLAGRARVKEKFSPEAFTEQL 406
Cdd:cd03805   318 EAMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAERL 392
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
223-392 1.81e-33

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: 122.77  E-value: 1.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 223 KKFLFLSINRYERKKNLTLALEALVKLRGRLtsqdwDKVHLIMAGGYDERvlenvqhyEELKKMVQLSDLGQYVTFLRSC 302
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKN-----PNLKLVIAGDGEEE--------KRLKKLAEKLGLGDNVIFLGFV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 303 SDEQKISLLRGCTCVLYTPSNEHFGIVPLEAMYLQCPVIAVNSGGPLESVVHNVTGFLCEP-DPVHFSEAMENFIHEPSL 381
Cdd:pfam00534  68 SDEDLPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPnNAEALAEAIDKLLEDEEL 147
                         170
                  ....*....|.
gi 1777466523 382 KATMGLAGRAR 392
Cdd:pfam00534 148 RERLGENARKR 158
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
310-414 2.10e-24

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 97.37  E-value: 2.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 310 LLRGCTCVLYTPSNEHFGIVPLEAMYLQCPVIAVNSGGPLESVVHNVTGFLCEP-DPVHFSEAMENFIHEPSLKATMGLA 388
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPgDPEALAEAILRLLEDPELRRRLGEA 96
                          90       100
                  ....*....|....*....|....*.
gi 1777466523 389 GRARVKEKFSPEAFTEQLYQYVTKLL 414
Cdd:COG0438    97 ARERAEERFSWEAIAERLLALYEELL 122
PLN02949 PLN02949
transferase, transferring glycosyl groups
148-414 1.46e-13

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 72.08  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 148 SFFKRLYRAPIDWVEEYTTGMADCILVNSRFTAAIFKETFKSLSHIDpdVLYPSLNITRFdSAIP-EKLDDlvpkgkKFL 226
Cdd:PLN02949  200 STCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPERIK--RVYPPCDTSGL-QALPlERSED------PPY 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 227 FLSINRYERKKNLTLALEALVKLRGRLTSqDWDKVHLIMAGG----YDERVLENvqhyeeLKKMVQLSDLGQYVTFLRSC 302
Cdd:PLN02949  271 IISVAQFRPEKAHALQLEAFALALEKLDA-DVPRPKLQFVGScrnkEDEERLQK------LKDRAKELGLDGDVEFHKNV 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 303 SDEQKISLLRGCTCVLYTPSNEHFGIVPLEAMYLQCPVIAVNSGGP-LESVVHNV---TGFLCEPDPvHFSEAMENFIHE 378
Cdd:PLN02949  344 SYRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPkMDIVLDEDgqqTGFLATTVE-EYADAILEVLRM 422
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1777466523 379 PSlKATMGLAGRARVK-EKFSPEAFTEQLYQYVTKLL 414
Cdd:PLN02949  423 RE-TERLEIAAAARKRaNRFSEQRFNEDFKDAIRPIL 458
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
222-408 1.78e-13

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: 71.29  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 222 GKKFLFLSINRYERKKNLTLALEALVKLRGRLtSQDWDKVHLIMAGGYDERvlenvqhyEELKKMVQLSDLGQYVTFLRS 301
Cdd:TIGR03088 192 DESVVVGTVGRLQAVKDQPTLVRAFALLVRQL-PEGAERLRLVIVGDGPAR--------GACEQMVRAAGLAHLVWLPGE 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 302 CSDEQkiSLLRGCTCVLYTPSNEHFGIVPLEAMYLQCPVIAVNSGGPLESVVHNVTGFLCEP-DPVHFSEAMENFIHEPS 380
Cdd:TIGR03088 263 RDDVP--ALMQALDLFVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPgDAVALARALQPYVSDPA 340
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1777466523 381 LKATMGLAGRARVKEKFSPEAFTEQ---LYQ 408
Cdd:TIGR03088 341 ARRAHGAAGRARAEQQFSINAMVAAyagLYD 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 ...
16-406 0e+00

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: 627.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  16 VLFLHPDLGVGGAERLVLDAALALQARGCSVKIWTAHYDPGHCFSESRE--LPVRCAGDWLPRSLGwgGR********** 93
Cdd:cd03805     3 VAFLHPDLGIGGAERLVVDAALALQSRGHEVTIYTSHHDPSHCFEETKDgtLPVRVRGDWLPRSIF--GRFHALCAYLRM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  94 ***ALYVLFLADEEFDVVVCDQVSACIPVFKLARRRKkILFYCHFPDLLLTRRDSFFKRLYRAPIDWVEEYTTGMADCIL 173
Cdd:cd03805    81 LYLALYLLLFSGEKYDVFIVDQVSACVPLLKLFRPSK-ILFYCHFPDQLLAQRKSLLKRLYRKPFDWLEEFTTGMADQIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 174 VNSRFTAAIFKETFKSLSHIDPDVLYPSLNITRFDSAIPEK-LDDLVPKGKKFLFLSINRYERKKNLTLALEALVKLRGR 252
Cdd:cd03805   160 VNSNFTAGVFKKTFPSLAKNPPEVLYPCVDTDSFDSTSEDPdPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 253 LTSqdWDKVHLIMAGGYDERVLENVQHYEELKKMVQ-LSDLGQYVTFLRSCSDEQKISLLRGCTCVLYTPSNEHFGIVPL 331
Cdd:cd03805   240 LPE--FENVRLVIAGGYDPRVAENVEYLEELQRLAEeLLNVEDQVLFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPL 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777466523 332 EAMYLQCPVIAVNSGGPLESVVHNVTGFLCEPDPVHFSEAMENFIHEPSLKATMGLAGRARVKEKFSPEAFTEQL 406
Cdd:cd03805   318 EAMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSREAFAERL 392
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
16-408 1.92e-45

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: 160.78  E-value: 1.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  16 VLFLHPDL--GVGGAERLVLDAALALQARGCSVKIWTahYDPGHCFSESRELPVRCAGDWLPRSLGWGGR********** 93
Cdd:cd03801     2 ILLLSPELppPVGGAERHVRELARALAARGHDVTVLT--PADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRP--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  94 ***alyvlFLADEEFDVVVC-DQVSACIPVFKLARRRKKILFYCHFPDLLLTRRDSFFKR--LYRApidwveEYTTGMAD 170
Cdd:cd03801    77 --------LLRLRKFDVVHAhGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERrlLARA------EALLRRAD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 171 CILVNSRFTAAIFKETFKSLSHiDPDVLYPSLNITRFDSAIPEKLDdlvPKGKKFLFLSINRYERKKNLTLALEALVKLR 250
Cdd:cd03801   143 AVIAVSEALRDELRALGGIPPE-KIVVIPNGVDLERFSPPLRRKLG---IPPDRPVLLFVGRLSPRKGVDLLLEALAKLL 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 251 GRltsqdWDKVHLIMAGGYDErvlenvqHYEELKKMvqLSDLGQYVTFLRSCSDEQKISLLRGCTCVLYTPSNEHFGIVP 330
Cdd:cd03801   219 RR-----GPDVRLVIVGGDGP-------LRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVV 284
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1777466523 331 LEAMYLQCPVIAVNSGGPLESVVHNVTGFLCEPDPVH-FSEAMENFIHEPSLKATMGLAGRARVKEKFSPEAFTEQLYQ 408
Cdd:cd03801   285 LEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEaLADALLRLLADPELRARLGRAARERVAERFSWERVAERLLD 363
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
223-392 1.81e-33

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: 122.77  E-value: 1.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 223 KKFLFLSINRYERKKNLTLALEALVKLRGRLtsqdwDKVHLIMAGGYDERvlenvqhyEELKKMVQLSDLGQYVTFLRSC 302
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKN-----PNLKLVIAGDGEEE--------KRLKKLAEKLGLGDNVIFLGFV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 303 SDEQKISLLRGCTCVLYTPSNEHFGIVPLEAMYLQCPVIAVNSGGPLESVVHNVTGFLCEP-DPVHFSEAMENFIHEPSL 381
Cdd:pfam00534  68 SDEDLPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPnNAEALAEAIDKLLEDEEL 147
                         170
                  ....*....|.
gi 1777466523 382 KATMGLAGRAR 392
Cdd:pfam00534 148 RERLGENARKR 158
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
16-384 1.42e-31

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: 123.24  E-value: 1.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  16 VLFLHPDLGVGGAERLVLDAALALQARGCSVKIWTaHYDPGHCFSESRELPVRCAGDWLPRSLGWGGR************ 95
Cdd:cd03811     2 ILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVL-LRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILK------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  96 *alYVLFLADEEFDVVVCDQVSACIPVFKLARRRKKILFYCH-FPDLLLTRRDSFFKRLYRAPidwveeyttgMADCILV 174
Cdd:cd03811    75 ---LKRILKRAKPDVVISFLGFATYIVAKLAAARSKVIAWIHsSLSKLYYLKKKLLLKLKLYK----------KADKIVC 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 175 NSRFTAAIFKETFKSL-SHIDpdVLYpslNITRFDSAIPE-KLDDLVPKGKKFLFLSINRYERKKNLTLALEALVKLRGR 252
Cdd:cd03811   142 VSKGIKEDLIRLGPSPpEKIE--VIY---NPIDIDRIRALaKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKK 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 253 LTsqdwdKVHLIMAGGYDERvlenvqhyEELKKMVQLSDLGQYVTFLRSCSDeqkI-SLLRGCTCVLYTPSNEHFGIVPL 331
Cdd:cd03811   217 YP-----DVKLVILGDGPLR--------EELEKLAKELGLAERVIFLGFQSN---PyPYLKKADLFVLSSRYEGFPNVLL 280
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1777466523 332 EAMYLQCPVIAVNSGGPLESVVHNVTGFLCEPDPVHFSEAMENFIHEPSLKAT 384
Cdd:cd03811   281 EAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQKKLDAA 333
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
167-402 6.92e-29

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: 116.94  E-value: 6.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 167 GMADCILVNSRFTAAIFKETFKSlsHIDPDVLYPSLNITRFdSAIPEKlddlvPKGKKFLFLSINRYERKKNLTLALEAL 246
Cdd:cd03806   188 SFADVVMVNSTWTYNHIRQLWKR--NIKPSIVYPPCDTEEL-TKLPID-----EKTRENQILSIAQFRPEKNHPLQLRAF 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 247 VKLRGRLTSQDWDKVHLIMAGG----YDE-RVlenvqhyEELKKMVQLSDLGQYVTFLRSCSDEQKISLLRGCTCVLYTP 321
Cdd:cd03806   260 AELLKRLPESIRSNPKLVLIGScrneEDKeRV-------EALKLLAKELILEDSVEFVVDAPYEELKELLSTASIGLHTM 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 322 SNEHFGIVPLEAMYLQCPVIAVNSGGPLESVV----HNVTGFLCEpDPVHFSEAMENFIHEPSLKATMGLAGRARVKEKF 397
Cdd:cd03806   333 WNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVvpwdGGPTGFLAS-TPEEYAEAIEKILTLSEEERLQRREAARSSAERF 411

                  ....*
gi 1777466523 398 SPEAF 402
Cdd:cd03806   412 SDEEF 416
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
151-406 1.29e-25

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: 107.33  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 151 KRLYRAPIDWVEEYTTGMADCILVNS--RFTAAIFKETFKSLSHIDPD-----VLYPSLNITRFdSAIPEKLDDLVPKG- 222
Cdd:cd03800   138 KYRHLGAQDTYHPSLRITAEEQILEAadRVIASTPQEADELISLYGADpsrinVVPPGVDLERF-FPVDRAEARRARLLl 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 223 --KKFLFLSINRYERKKNLTLALEALVKLRGRLTsqdwdKVHLIMAGGYDERVLENVQhyEELKKMVQLSDLGQYVTFLR 300
Cdd:cd03800   217 ppDKPVVLALGRLDPRKGIDTLVRAFAQLPELRE-----LANLVLVGGPSDDPLSMDR--EELAELAEELGLIDRVRFPG 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 301 SCSDEQKISLLRGCTCVLYTPSNEHFGIVPLEAMYLQCPVIAVNSGGPLESVVHNVTGFLCEP-DPVHFSEAMENFIHEP 379
Cdd:cd03800   290 RVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPhDPEALAAALRRLLDDP 369
                         250       260
                  ....*....|....*....|....*..
gi 1777466523 380 SLKATMGLAGRARVKEKFSPEAFTEQL 406
Cdd:cd03800   370 ALWQRLSRAGLERARAHYTWESVADQL 396
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
97-406 2.13e-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: 106.14  E-value: 2.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  97 ALYVL--FLADEEFDVVVCDQVSACI---PVFKLARRRKKIL----FYCHFPDLLLTRRdsFFKRLYRapidwveeYTTG 167
Cdd:cd03808    69 ALFKLykLLKKEKPDIVHCHTPKPGIlgrLAARLAGVPKVIYtvhgLGFVFTEGKLLRL--LYLLLEK--------LALL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 168 MADCILVNSRFTAAIFKEtfKSLSHIDPDVLYP--SLNITRFDSAIPeklddlVPKGKKFLFLSINRYERKKNLTLALEA 245
Cdd:cd03808   139 FTDKVIFVNEDDRDLAIK--KGIIKKKKTVLIPgsGVDLDRFQYSPE------SLPSEKVVFLFVARLLKDKGIDELIEA 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 246 --LVKLRGrltsqdwDKVHLIMAGGYDERvLENVQHYEELkkmvQLSDLgqyVTFLRSCSDeqKISLLRGCTCVLYtPSN 323
Cdd:cd03808   211 akILKKKG-------PNVRFLLVGDGELE-NPSEILIEKL----GLEGR---IEFLGFRSD--VPELLAESDVFVL-PSY 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 324 -EHFGIVPLEAMYLQCPVIAVNSGGPLESVVHNVTGFLCEP-DPVHFSEAMENFIHEPSLKATMGLAGRARVKEKFSPEA 401
Cdd:cd03808   273 rEGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPgDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEK 352

                  ....*
gi 1777466523 402 FTEQL 406
Cdd:cd03808   353 VVNKL 357
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
125-406 2.54e-25

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: 105.91  E-value: 2.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 125 LARRRKKILFYCH--FPDLLLTRRDSFFKRLYRAPIDWVEEYttgmADCILVNSRFTAA-IFKETFKSLSHIDpdVLYps 201
Cdd:cd03809    97 LLLKGCPQVVTIHdlIPLRYPEFFPKRFRLYYRLLLPISLRR----ADAIITVSEATRDdIIKFYGVPPEKIV--VIP-- 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 202 LNITRFDSaIPEKLDDLVPKG--KKFLFLSINRYERKKNLTLALEALVKLRGRltsqdWDKVHLIMAGGYDERvlenvqh 279
Cdd:cd03809   169 LGVDPSFF-PPESAAVLIAKYllPEPYFLYVGTLEPRKNHERLLKAFALLKKQ-----GGDLKLVIVGGKGWE------- 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 280 YEELKKMVQLSDLGQYVTFLRSCSDEQKISLLRGCTCVLYtPS-NEHFGIVPLEAMYLQCPVIAVNSggpleSVVHNVTG 358
Cdd:cd03809   236 DEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVF-PSlYEGFGLPVLEAMACGTPVIASNI-----SVLPEVAG 309
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1777466523 359 ---FLCEP-DPVHFSEAMENFIHEPSLKATMGLAGRARVKeKFSPEAFTEQL 406
Cdd:cd03809   310 daaLYFDPlDPESIADAILRLLEDPSLREELIRKGLERAK-KFSWEKTAEKT 360
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
310-414 2.10e-24

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 97.37  E-value: 2.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 310 LLRGCTCVLYTPSNEHFGIVPLEAMYLQCPVIAVNSGGPLESVVHNVTGFLCEP-DPVHFSEAMENFIHEPSLKATMGLA 388
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPgDPEALAEAILRLLEDPELRRRLGEA 96
                          90       100
                  ....*....|....*....|....*.
gi 1777466523 389 GRARVKEKFSPEAFTEQLYQYVTKLL 414
Cdd:COG0438    97 ARERAEERFSWEAIAERLLALYEELL 122
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
15-406 8.97e-22

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: 96.26  E-value: 8.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  15 SVLFLHPD--LGVGGAERLVLDAALALQARGCSVKI--WTAHYDPGHCFSESRE-------LPVRCagdwlpRSLGWGGR 83
Cdd:cd03794     1 KILLISQYypPPKGAAAARVYELAKELVRRGHEVTVltPSPNYPLGRIFAGATEtkdgirvIRVKL------GPIKKNGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  84 *************ALYVLFLADEEFDVVVC--DQVSACIPVFKLARR-RKKILFYCH--FPDLLLTRRDSFFKRLYRApI 158
Cdd:cd03794    75 IRRLLNYLSFALAALLKLLVREERPDVIIAysPPITLGLAALLLKKLrGAPFILDVRdlWPESLIALGVLKKGSLLKL-L 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 159 DWVEEYTTGMADCILVNSRFTAAIFKETFKSLSHIDpdVLYPSLNITRFDSAIPEKLDDLVPKGKKFLFL---SINRYEr 235
Cdd:cd03794   154 KKLERKLYRLADAIIVLSPGLKEYLLRKGVPKEKII--VIPNWADLEEFKPPPKDELRKKLGLDDKFVVVyagNIGKAQ- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 236 kkNLTLALEALVKLRGRltsqdwDKVHLIMAGGYDERvlenvqhyEELKKMVQLSDLgQYVTFLRSCSDEQKISLLRGCT 315
Cdd:cd03794   231 --GLETLLEAAERLKRR------PDIRFLFVGDGDEK--------ERLKELAKARGL-DNVTFLGRVPKEEVPELLSAAD 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 316 CVL--YTPSNEHFGIVP---LEAMYLQCPVIAVNSGGPLESVVHNVTGFLCEP-DPVHFSEAMENFIHEPSLKATMGLAG 389
Cdd:cd03794   294 VGLvpLKDNPANRGSSPsklFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPgDPEALADAILELLDDPELRRAMGENG 373
                         410
                  ....*....|....*..
gi 1777466523 390 RARVKEKFSPEAFTEQL 406
Cdd:cd03794   374 RELAEEKFSREKLADRL 390
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
36-410 6.66e-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: 93.50  E-value: 6.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  36 ALALQARGCSVKIWTAHYdPGHcfsESRELPVRCagdwlpRSLGWGGR*************AlYVLFLADEEFDVV-VCD 114
Cdd:cd03817    24 ARALEKRGHEVYVITPSD-PGA---EDEEEVVRY------RSFSIPIRKYHRQHIPFPFKKA-VIDRIKELGPDIIhTHT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 115 QVSACIPVFKLARRRK------------KILFYCHFPDLLL-TRRDSFFKRLYRapidwveeyttgMADCILVNSRFTaa 181
Cdd:cd03817    93 PFSLGKLGLRIARKLKipivhtyhtmyeDYLHYIPKGKLLVkAVVRKLVRRFYN------------HTDAVIAPSEKI-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 182 ifKETFKSLSHIDP-DVLYPSLNITRF-DSAIPEKLDDLVPKGKKFLFLSINRYERKKNLTLALEALVKLRGRltsqdwD 259
Cdd:cd03817   159 --KDTLREYGVKGPiEVIPNGIDLDKFeKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKE------P 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 260 KVHLIMAG-GYDErvlenvqhyEELKKMVQLSDLGQYVTFLRSCSDEQKISLLRGCTCVLYTPSNEHFGIVPLEAMYLQC 338
Cdd:cd03817   231 NIKLVIVGdGPER---------EELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGL 301
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777466523 339 PVIAVNSGGPLESVVHNVTGFLCEPDPVHFSEAMENFIHEPSLKATMGLAGRARVKEKFSPEAfTEQLYQYV 410
Cdd:cd03817   302 PVVAAKDPAASELVEDGENGFLFEPNDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAKS-VEKLYEEV 372
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
21-408 1.59e-19

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: 89.36  E-value: 1.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  21 PDLGVGGAERLVLDAALALQARGCSVKIWTahydPGHCFSESRELPVRCAGDWLP-----RSLGWGGR************ 95
Cdd:cd03798     9 PNANSPGRGIFVRRQVRALSRRGVDVEVLA----PAPWGPAAARLLRKLLGEAVPprdgrRLLPLKPRLRLLAPLRAPSL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  96 *ALYvLFLADEEFDVVVCDQVSACIPVFKLARRRKKI--LFYCHFPDLLLTRRDSFFKRLYRapidwveeYTTGMADCIL 173
Cdd:cd03798    85 AKLL-KRRRRGPPDLIHAHFAYPAGFAAALLARLYGVpyVVTEHGSDINVFPPRSLLRKLLR--------WALRRAARVI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 174 VNSRFTAAIFKETFKSLSHIDpdVLYPSLNITRFdsAIPEKLDDLVPKGkkFLFLSINRYERKKNLTLALEALVKLRGRl 253
Cdd:cd03798   156 AVSKALAEELVALGVPRDRVD--VIPNGVDPARF--QPEDRGLGLPLDA--FVILFVGRLIPRKGIDLLLEAFARLAKA- 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 254 tSQDwdkVHLIMAGGYDERvlenvqhyEELKKMVQLSDLGQYVTFLRSCSDEQKISLLRGCTC-VLytPS-NEHFGIVPL 331
Cdd:cd03798   229 -RPD---VVLLIVGDGPLR--------EALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVfVL--PSrHEGFGLVLL 294
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777466523 332 EAMYLQCPVIAVNSGGPLESVVHNVTGFLCEP-DPVHFSEAMENFIHEPsLKATMGLAGRARVKEKFSPEAFTEQLYQ 408
Cdd:cd03798   295 EAMACGLPVVATDVGGIPEVVGDPETGLLVPPgDADALAAALRRALAEP-YLRELGEAARARVAERFSWVKAADRIAA 371
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
221-403 1.83e-19

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: 88.87  E-value: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 221 KGKKFlFLSINRYERKKNLTLALEALVKLrgrltsqdwdKVHLIMAGGYDERvlenvqhyEELKKMVQLSdLGQYVTFLR 300
Cdd:cd03795   189 KGKKI-FLFIGRLVYYKGLDYLIEAAQYL----------NYPIVIGGEGPLK--------PDLEAQIELN-LLDNVKFLG 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 301 SCSDEQKISLLRGCTCVLYtPS---NEHFGIVPLEAMYLQCPVIAVNSGGPLESVV-HNVTGFLCEP-DPVHFSEAMENF 375
Cdd:cd03795   249 RVDDEEKVIYLHLCDVFVF-PSvlrSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNnNGETGLVVPPkDPDALAEAIDKL 327
                         170       180
                  ....*....|....*....|....*...
gi 1777466523 376 IHEPSLKATMGLAGRARVKEKFSPEAFT 403
Cdd:cd03795   328 LSDEELRESYGENAKKRFEELFTAEKMK 355
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
197-410 6.03e-19

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: 86.96  E-value: 6.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 197 VLYPSLNITRFDSAipeklddlVPKGKKFLFLSinRYERKKNLTLALEALVKLrgrltsqdwdKVHLIMAGGYDErvlen 276
Cdd:cd03802   152 VVHNGLDPADYRFQ--------PDPEDYLAFLG--RIAPEKGLEDAIRVARRA----------GLPLKIAGKVRD----- 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 277 vQHYEElkkMVQLSDLGQYVTFLRSCSDEQKISLLRGCTCVLYTPS-NEHFGIVPLEAMYLQCPVIAVNSGGPLESVVHN 355
Cdd:cd03802   207 -EDYFY---YLQEPLPGPRIEFIGEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHG 282
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1777466523 356 VTGFLCEPdpvhfSEAMENFIHE-PSLKatmGLAGRARVKEKFSPEAFTEQ---LYQYV 410
Cdd:cd03802   283 ETGFLVDS-----VEEMAEAIANiDRID---RAACRRYAEDRFSAARMADRyeaLYRKV 333
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
16-390 7.38e-19

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: 87.03  E-value: 7.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  16 VLFLHPDLGVGGAERLVLDAALALQARGCSVKIWTAHyDPGHCFSESRELPVRCA-GDWLPRSLGWggr*********** 94
Cdd:cd03819     1 ILMLTPALEIGGAETYILDLARALAERGHRVLVVTAG-GPLLPRLRQIGIGLPGLkVPLLRALLGN-------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  95 **ALYVLfLADEEFDVVVCdQVSACIPVFKLARRRK--KILFYCHfpdlLLTRRDSFFKRLYRAPIDWVEEyttgmadCI 172
Cdd:cd03819    66 -VRLARL-IRRERIDLIHA-HSRAPAWLGWLASRLTgvPLVTTVH----GSYLATYHPKDFALAVRARGDR-------VI 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 173 LVnSRFTaaifKETFKSLSHIDPD---VLYPSLNITRFD-SAIPEKLDDLVPKGKKFLFLSINRYERKKNLTLALEALVK 248
Cdd:cd03819   132 AV-SELV----RDHLIEALGVDPErirVIPNGVDTDRFPpEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAE 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 249 LRGRLTsqdwdkVHLIMAGGYDERvlenvqhyEELKKMVQLSDLGQYVTFLRSCSDeqKISLLRGCTCVLYTPSNEHFGI 328
Cdd:cd03819   207 LKDEPD------FRLLVAGDGPER--------DEIRRLVERLGLRDRVTFTGFRED--VPAALAASDVVVLPSLHEEFGR 270
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777466523 329 VPLEAMYLQCPVIAVNSGGPLESVVHNVTGFLCEP-DPVHFSEAMENFIHEPSLKATMGLAGR 390
Cdd:cd03819   271 VALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPgDAEALADAIRAAKLLPEAREKLQAAAA 333
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
125-414 4.02e-18

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: 85.10  E-value: 4.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 125 LAR----RRKKILFYCHFPDLLLTRRDSFFKRLYRAPIDWVEEYTTgmadcilvNSRFTAAifkETFkslSHIDPD---- 196
Cdd:cd04962   102 LAReilgEKIPIVTTLHGTDITLVGYDPSLQPAVRFSINKSDRVTA--------VSSSLRQ---ETY---ELFDVDkdie 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 197 VLYPSLNITRF--DSAIPEKLDDLVPKGKKFLfLSINRYERKKNLTLALEALVKLRGRLtsqdwdKVHLIMAGGYDERVl 274
Cdd:cd04962   168 VIHNFIDEDVFkrKPAGALKRRLLAPPDEKVV-IHVSNFRPVKRIDDVVRVFARVRRKI------PAKLLLVGDGPERV- 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 275 envqhyeELKKMVQLSDLGQYVTFLRSCSDEQKIslLRGCTCVLYTPSNEHFGIVPLEAMYLQCPVIAVNSGGPLESVVH 354
Cdd:cd04962   240 -------PAEELARELGVEDRVLFLGKQDDVEEL--LSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKH 310
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1777466523 355 NVTGFLCEPDPVH-FSEAMENFIHEPSLKATMGLAGRARVKEKFSPEAFTEQlYQYVTKLL 414
Cdd:cd04962   311 GETGFLSDVGDVDaMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQ-YEAYYRRL 370
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
103-411 2.51e-17

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: 82.75  E-value: 2.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 103 LADEEFDVVVC-DQVSACIPVFKlARRRKKILFYCHFpDLlltrRDSFFKRLYRApIDWVEEYTtgmadcilvnSRFTAA 181
Cdd:cd03792    83 LLDGDADVVVIhDPQPALLPKIK-KKRDRKWIWRCHI-DI----STPLTEPQPRV-WDFLWNYI----------EGYDLF 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 182 IF--KETFKSLSHIDPDVLYPS------LNITRFDSAIP---EKLDDLVPKgkKFLFLSINRYERKKNLTLALEALVKLR 250
Cdd:cd03792   146 VFhpPEFVPPQVPPPKFYIPPSidplsgKNKDLSPADIRyylEKPFVIDPE--RPYILQVARFDPSKDPLGVIDAYKLFK 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 251 GRLtsqdwDKVHLIMAGGYDERVLENVQHYEELKKMVQLSDLgqyVTFLRSCSDEQKIS-LLRGCTCVLYTPSNEHFGIV 329
Cdd:cd03792   224 RRA-----EEPQLVICGHGAVDDPEGSVVYEEVMEYAGDDHD---IHVLRLPPSDQEINaLQRAATVVLQLSTREGFGLT 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 330 PLEAMYLQCPVIAVNSGG-PLEsVVHNVTGFLC---EPDPVHFseamENFIHEPSLKATMGLAGRARVKEKFSPeafTEQ 405
Cdd:cd03792   296 VSEALWKGKPVIATPAGGiPLQ-VIDGETGFLVnsvEGAAVRI----LRLLTDPELRRKMGLAAREHVRDNFLI---TGN 367

                  ....*.
gi 1777466523 406 LYQYVT 411
Cdd:cd03792   368 LRAWLY 373
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
19-406 4.27e-17

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: 81.99  E-value: 4.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  19 LHPDLGVGGAERLVLDAALALQARGCSVKIWTAHYDPGHCFSESRELPVRCAGDWLPRSLGWGGR*************AL 98
Cdd:cd03823     8 LYPPQRVGGAEISVHDLAEALVAEGHEVAVLTAGVGPPGQATVARSVVRYRRAPDETLPLALKRRGYELFETYNPGLRRL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  99 YVLFLADEEFDVVV--CDQVSACIPVFKLARRRKKILFYCHfpDLLLTR-RDSFFKRLYRApidwveeyttgmadcILVN 175
Cdd:cd03823    88 LARLLEDFRPDVVHthNLSGLGASLLDAARDLGIPVVHTLH--DYWLLCpRQFLFKKGGDA---------------VLAP 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 176 SRFTAAIFKETFKSLSHIDpdVLYPSLnitRFDSAIPEKLddlVPKGKKFLFLSINRYERKKNLTLALEALvklrGRLTS 255
Cdd:cd03823   151 SRFTANLHEANGLFSARIS--VIPNAV---EPDLAPPPRR---RPGTERLRFGYIGRLTEEKGIDLLVEAF----KRLPR 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 256 QDWdkvHLIMAGGYDErvlenvQHYEELKKMVQLSDLGQYVT-----FLrscsdeQKISllrgctcVLYTPS--NEHFGI 328
Cdd:cd03823   219 EDI---ELVIAGHGPL------SDERQIEGGRRIAFLGRVPTddikdFY------EKID-------VLVVPSiwPEPFGL 276
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1777466523 329 VPLEAMYLQCPVIAVNSGGPLESVVHNVTGFLCEP-DPVHFSEAMENFIHEPSLKATMGLAGRARVKEKFSPEAFTEQL 406
Cdd:cd03823   277 VVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPgDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAEEYLKLY 355
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
126-409 1.63e-16

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: 80.42  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 126 ARRRKKILF----YCHFPDLLLTRRDSFFKRLYRAPIDWVeeytTGMADCILVNSRFTAAIFKET-FKSLSH----IDPD 196
Cdd:cd03814   103 AARRLGLPVvtsyHTDFPEYLSYYTLGPLSWLAWAYLRWF----HNPFDTTLVPSPSIARELEGHgFERVRLwprgVDTE 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 197 VLYPSlnitRFDSAIPEKLDDlvpkGKKFLFLSINRYERKKNLTLALEALVKLrgrltsQDWDKVHLIMAGGYDERvlen 276
Cdd:cd03814   179 LFHPS----RRDAALRRRLGP----PGRPLLLYVGRLAPEKNLEALLDADLPL------AASPPVRLVVVGDGPAR---- 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 277 vqhyEELKKMvqLSDlgqyVTFLRSCSDEQKISLLRGCTCVLYtPS-NEHFGIVPLEAMYLQCPVIAVNSGGPLESVVHN 355
Cdd:cd03814   241 ----AELEAR--GPD----VIFTGFLTGEELARAYASADVFVF-PSrTETFGLVVLEAMASGLPVVAADAGGPRDIVRPG 309
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1777466523 356 VTGFLCEP-DPVHFSEAMENFIHEPSLKATMGLAGRARVKEKFSPEAFTEQLYQY 409
Cdd:cd03814   310 GTGALVEPgDAAAFAAALRALLEDPELRRRMAARARAEAERYSWEAFLDNLLDYY 364
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
15-405 1.85e-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: 79.97  E-value: 1.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  15 SVLFLHPDLG-VGGAERLVLDAALALQARGCSVKIWTAHYDPGHCFSEsrelpvrcagdwLPRSLGWGGR********** 93
Cdd:cd03820     1 KIAIVIPSISnAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYE------------LDDNIKIKNLGDRKYSHFKL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  94 ***ALYVL-----FLADEEFDVVVCDQVS--ACIPVFKLArrrKKILFYCHFP---DLLLTRRDSFFKRLYRApidwvee 163
Cdd:cd03820    69 LLKYFKKVrrlrkYLKNNKPDVVISFRTSllTFLALIGLK---SKLIVWEHNNyeaYNKGLRRLLLRRLLYKR------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 164 yttgmADCILVNSRFTAAIFKETFKSlshidpdvlypslNITRFDSAIPEKLDDLVPKGKKFLFLSINRYERKKNLTLAL 243
Cdd:cd03820   139 -----ADKIVVLTEADKLKKYKQPNS-------------NVVVIPNPLSFPSEEPSTNLKSKRILAVGRLTYQKGFDLLI 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 244 EALVKLRGRLtsQDWDkvhLIMAGGYDERvlenvqhyEELKKMVQLSDLGQYVTFLrsCSDEQKISLLRGCTCVLYTPSN 323
Cdd:cd03820   201 EAWALIAKKH--PDWK---LRIYGDGPER--------EELEKLIDKLGLEDRVKLL--GPTKNIAEEYANSSIFVLSSRY 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 324 EHFGIVPLEAMYLQCPVIAVNS-GGPLESVVHNVTGFLCEP-DPVHFSEAMENFIHEPSLKATMGLAGRARVkEKFSPEA 401
Cdd:cd03820   266 EGFPMVLLEAMAYGLPIISFDCpTGPSEIIEDGENGLLVPNgDVDALAEALLRLMEDEELRKKMGKNARKNA-ERFSIEK 344

                  ....
gi 1777466523 402 FTEQ 405
Cdd:cd03820   345 IIKQ 348
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
222-377 2.37e-16

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 75.24  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 222 GKKFLFLSiNRYERKKNLTLALEALVKLRGRLtsqdwDKVHLIMAGGYDERVLENvqhyeelkkmvQLSDLGQYVTFLRS 301
Cdd:pfam13692   1 RPVILFVG-RLHPNVKGVDYLLEAVPLLRKRD-----NDVRLVIVGDGPEEELEE-----------LAAGLEDRVIFTGF 63
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777466523 302 CSDeqKISLLRGCTCVLYTPSNEHFGIVPLEAMYLQCPVIAVNSGGPLEsVVHNVTGFLCEP-DPVHFSEAMENFIH 377
Cdd:pfam13692  64 VED--LAELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPE-LVDGENGLLVPPgDPEALAEAILRLLE 137
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
26-406 5.08e-15

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: 75.87  E-value: 5.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  26 GGAERLVLDAALALQARGCSVKIWTahYDPGHcfsesRELPVRCAGDWLPRSLGWGgR*************AL---YVLF 102
Cdd:cd03821    14 GGPVKVVLRLAAALAALGHEVTIVS--TGDGY-----ESLVVEENGRYIPPQDGFA-SIPLLRQGAGRTDFSPglpNWLR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 103 LADEEFDVV----VCDQVSAciPVFKLARRRKkiLFYCHFP----DLLLTRRDSFFKRLYRapiDWVEEYTTGMADCIlv 174
Cdd:cd03821    86 RNLREYDVVhihgVWTYTSL--AACKLARRRG--IPYVVSPhgmlDPWALQQKHWKKRIAL---HLIERRNLNNAALV-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 175 nsRFTAAIFKETFKSLSHIDPDVLYP-SLNITRFDSAIPEKLDDLVPKGKK-FLFLSinRYERKKNLTLALEALVKLrgr 252
Cdd:cd03821   157 --HFTSEQEADELRRFGLEPPIAVIPnGVDIPEFDPGLRDRRKHNGLEDRRiILFLG--RIHPKKGLDLLIRAARKL--- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 253 ltSQDWDKVHLIMAGgYDERvlenvqhyEELKKMVQLSD--LGQYVTFLRSCSDEQKISLLRGCTC-VLytPS-NEHFGI 328
Cdd:cd03821   230 --AEQGRDWHLVIAG-PDDG--------AYPAFLQLQSSlgLGDRVTFTGPLYGEAKWALYASADLfVL--PSySENFGN 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 329 VPLEAMYLQCPVIaVNSGGPLESVVHNVTGFLCEPDPVHFSEAMENFIHEPSLKATMGLAGRA--RVKEKFSPEAFTEQL 406
Cdd:cd03821   297 VVAEALACGLPVV-ITDKCGLSELVEAGCGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRarQVEENFSWEAVAGQL 375
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
170-402 7.19e-15

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: 75.40  E-value: 7.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 170 DCILVNSRFTAAIFKETFkslsHIDPDVLYPSLNITRFDSAiPEKLDDlvpkgkkflFLSINRYERKKNLTLALEALVKL 249
Cdd:cd03804   159 DLFIANSQFVARRIKKFY----GRESTVIYPPVDTDAFAPA-ADKEDY---------YLTASRLVPYKRIDLAVEAFNEL 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 250 RGRLtsqdwdkvhlIMAG-GYDErvlenvqhyEELKKMvqlsdLGQYVTFLRSCSDEQKISLLRGCTCVLYtPSNEHFGI 328
Cdd:cd03804   225 PKRL----------VVIGdGPDL---------DRLRAM-----ASPNVEFLGYQPDEVLKELLSKARAFVF-AAEEDFGI 279
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777466523 329 VPLEAMYLQCPVIAVNSGGPLESVVHNVTGFL-CEPDPVHFSEAMENFIHEPSLKATMGLAGRArvkEKFSPEAF 402
Cdd:cd03804   280 VPVEAQACGTPVIAFGKGGALETVRPGPTGILfGEQTVESLKAAVEEFEQNFDRFKPQAIRANA---ERFSRARF 351
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
223-361 2.07e-14

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: 72.44  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 223 KKFLFLSINRYERKKNLTLALEALVKLRgrltSQDWDKVHLIMAGGYDERVLENVQHYEELKKMVQLsdLGQYVtflrsc 302
Cdd:cd01635   109 PLADKVSVGRLVPEKGIDLLLEALALLK----ARLPDLVLVLVGGGGEREEEEALAAALGLLERVVI--IGGLV------ 176
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1777466523 303 SDEQKISLLRGCTCVLYTPSNEHFGIVPLEAMYLQCPVIAVNSGGPLESVVHNVTGFLC 361
Cdd:cd01635   177 DDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
PLN02949 PLN02949
transferase, transferring glycosyl groups
148-414 1.46e-13

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 72.08  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 148 SFFKRLYRAPIDWVEEYTTGMADCILVNSRFTAAIFKETFKSLSHIDpdVLYPSLNITRFdSAIP-EKLDDlvpkgkKFL 226
Cdd:PLN02949  200 STCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPERIK--RVYPPCDTSGL-QALPlERSED------PPY 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 227 FLSINRYERKKNLTLALEALVKLRGRLTSqDWDKVHLIMAGG----YDERVLENvqhyeeLKKMVQLSDLGQYVTFLRSC 302
Cdd:PLN02949  271 IISVAQFRPEKAHALQLEAFALALEKLDA-DVPRPKLQFVGScrnkEDEERLQK------LKDRAKELGLDGDVEFHKNV 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 303 SDEQKISLLRGCTCVLYTPSNEHFGIVPLEAMYLQCPVIAVNSGGP-LESVVHNV---TGFLCEPDPvHFSEAMENFIHE 378
Cdd:PLN02949  344 SYRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPkMDIVLDEDgqqTGFLATTVE-EYADAILEVLRM 422
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1777466523 379 PSlKATMGLAGRARVK-EKFSPEAFTEQLYQYVTKLL 414
Cdd:PLN02949  423 RE-TERLEIAAAARKRaNRFSEQRFNEDFKDAIRPIL 458
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
222-408 1.78e-13

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: 71.29  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 222 GKKFLFLSINRYERKKNLTLALEALVKLRGRLtSQDWDKVHLIMAGGYDERvlenvqhyEELKKMVQLSDLGQYVTFLRS 301
Cdd:TIGR03088 192 DESVVVGTVGRLQAVKDQPTLVRAFALLVRQL-PEGAERLRLVIVGDGPAR--------GACEQMVRAAGLAHLVWLPGE 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 302 CSDEQkiSLLRGCTCVLYTPSNEHFGIVPLEAMYLQCPVIAVNSGGPLESVVHNVTGFLCEP-DPVHFSEAMENFIHEPS 380
Cdd:TIGR03088 263 RDDVP--ALMQALDLFVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPgDAVALARALQPYVSDPA 340
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1777466523 381 LKATMGLAGRARVKEKFSPEAFTEQ---LYQ 408
Cdd:TIGR03088 341 ARRAHGAAGRARAEQQFSINAMVAAyagLYD 371
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
26-187 1.81e-12

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 65.25  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  26 GGAERLVLDAALALQARGCSVKIWTAHYDPGHCFSESRELPVRCAGDWLPRSLGWGGR*************alYVLFLAD 105
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRR-----------LRRLLRR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 106 EEFDVVVCDQVSACIPVFKLARRRKKI--LFYCHFPDLLLTRRDsFFKRLYRAPIDWVEEYTTGMADCILVNSRFTAAIF 183
Cdd:pfam13439  70 ERPDVVHAHSPFPLGLAALAARLRLGIplVVTYHGLFPDYKRLG-ARLSPLRRLLRRLERRLLRRADRVIAVSEAVADEL 148

                  ....
gi 1777466523 184 KETF 187
Cdd:pfam13439 149 RRLY 152
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
16-407 1.89e-12

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: 68.11  E-value: 1.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  16 VLFLHPDLGVGGAERLVLDAA--LALQARGCSVKIWTahyDPGHCFSESRELPVR--CAGDWLPRSLGwggr******** 91
Cdd:cd03807     2 VAHVITGLNVGGAETMLLRLLehMDKSRFEHVVISLT---GDGVLGEELLAAGVPvvCLGLSSGKDPG------------ 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  92 *****ALYVL--FLADEEFDVVVCDQVSACI---PVFKLARRRKKILfychfpdlllTRRDSffkrlyrapidWVEEYTT 166
Cdd:cd03807    67 -----VLLRLakLIRKRNPDVVHTWMYHADLiggLAAKLAGGVKVIW----------SVRSS-----------NIPQRLT 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 167 GMAdcILVN------SRFTAAIFKETFKSL--SHIDPDVLYPSLN-ITRFDSAIPEKLDD-----LVPKGKKFLFLSINR 232
Cdd:cd03807   121 RLV--RKLClllskfSPATVANSSAVAEFHqeQGYAKNKIVVIYNgIDLFKLSPDDASRArarrrLGLAEDRRVIGIVGR 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 233 YERKKNLTLALEALVKLRgrltsQDWDKVHLIMAGGYDERvlenvqhyEELKKMVQLSDLGQYVTFLRSCSDeqkISLLR 312
Cdd:cd03807   199 LHPVKDHSDLLRAAALLV-----ETHPDLRLLLVGRGPER--------PNLERLLLELGLEDRVHLLGERSD---VPALL 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 313 GCTCVLYTPS-NEHFGIVPLEAMYLQCPVIAVNSGGPLESVVhNVTGFLCEP-DPVHFSEAMENFIHEPSLKATMGLAGR 390
Cdd:cd03807   263 PAMDIFVLSSrTEGFPNALLEAMACGLPVVATDVGGAAELVD-DGTGFLVPAgDPQALADAIRALLEDPEKRARLGRAAR 341
                         410       420
                  ....*....|....*....|
gi 1777466523 391 ARVKEKFSPEAFT---EQLY 407
Cdd:cd03807   342 ERIANEFSIDAMVrryETLY 361
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
227-406 4.95e-12

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: 66.71  E-value: 4.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 227 FLSINRYERKKNLTLALEALVKLRGRLTSqdwdkVHLIMAGGYDERvlenvqhyeelKKMVQLSDLGQYVTFLRSCSDEQ 306
Cdd:cd05844   192 ILFVGRLVEKKGCDVLIEAFRRLAARHPT-----ARLVIAGDGPLR-----------PALQALAAALGRVRFLGALPHAE 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 307 KISLLRGCTcVLYTPS-------NEHFGIVPLEAMYLQCPVIAVNSGGPLESVVHNVTGFLC-EPDPVHFSEAMENFIHE 378
Cdd:cd05844   256 VQDWMRRAE-IFCLPSvtaasgdSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVpEGDVDALADALQALLAD 334
                         170       180
                  ....*....|....*....|....*...
gi 1777466523 379 PSLKATMGLAGRARVKEKFSPEAFTEQL 406
Cdd:cd05844   335 RALADRMGGAARAFVCEQFDIRVQTAKL 362
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
26-183 1.07e-10

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 59.72  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523  26 GGAERLVLDAALALQARGCSVKIWTAHYDPGHCFSESRELPVRCAgdWLPRSLGWGGR*************ALYVL--FL 103
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRL--PVPPRPSPLAD-----------LAALRRLrrLL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 104 ADEEFDVVVCDQVSACIPVfKLARRRKKILFYCHFPDLLLTRRDSFFKRLYRapidWVEEYTTGMADCILVNSRFTAAIF 183
Cdd:pfam13579  68 RAERPDVVHAHSPTAGLAA-RLARRRRGVPLVVTVHGLALDYGSGWKRRLAR----ALERRLLRRADAVVVVSEAEAELL 142
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
220-406 2.29e-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: 61.70  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 220 PKGKKFLFLSINRYERKKNLTLALEALVKLRGRLTSQDWDKVhlimagGYDErvLEnvqhyEELKKMVQLSDLGQYVTFL 299
Cdd:cd03799   170 PLDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQII------GDGD--LK-----EQLQQLIQELNIGDCVKLL 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 300 RSCSDEQKISLLRGcTCVLYTPS------NEHFGIVPL-EAMYLQCPVIAVNSGGPLESVVHNVTGFLC-EPDPVHFSEA 371
Cdd:cd03799   237 GWKPQEEIIEILDE-ADIFIAPSvtaadgDQDGPPNTLkEAMAMGLPVISTEHGGIPELVEDGVSGFLVpERDAEAIAEK 315
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1777466523 372 MENFIHEPSLKATMGLAGRARVKEKFSPEAFTEQL 406
Cdd:cd03799   316 LTYLIEHPAIWPEMGKAGRARVEEEYDINKLNDEL 350
PLN00142 PLN00142
sucrose synthase
205-413 3.91e-08

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 55.37  E-value: 3.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 205 TRFDSAIPEKLDD----------LVPKGKKFLFlSINRYERKKNLTlaleALVKLRG---RLTsqdwDKVHLIMAGGY-D 270
Cdd:PLN00142  545 TSLHPSIEELLYSpeqndehigyLKDRKKPIIF-SMARLDRVKNLT----GLVEWYGknkRLR----ELVNLVVVGGFiD 615
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 271 ERVLENVQHYEELKKMVQLSDL----GQYvTFLRSCSDEQKISLLRGCTC---------VLYtpsnEHFGIVPLEAMYLQ 337
Cdd:PLN00142  616 PSKSKDREEIAEIKKMHSLIEKynlkGQF-RWIAAQTNRVRNGELYRYIAdtkgafvqpALY----EAFGLTVVEAMTCG 690
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 338 CPVIAVNSGGPLESVVHNVTGFLCEP-DPVHFSEAMENFI----HEPSLKATMGLAGRARVKEKFSPEAFTEQL------ 406
Cdd:PLN00142  691 LPTFATCQGGPAEIIVDGVSGFHIDPyHGDEAANKIADFFekckEDPSYWNKISDAGLQRIYECYTWKIYAERLltlggv 770
                         250
                  ....*....|
gi 1777466523 407 ---YQYVTKL 413
Cdd:PLN00142  771 ygfWKYVSKL 780
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
169-398 5.51e-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: 5.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 169 ADCILVN-SRFTAAIFKETFkSLSHIDPDVLYPSLNITRF---DSAIPEKLDDLVPKGKKFLFLSINRYERKKNLTLALE 244
Cdd:cd03825   137 KRLTIVApSRWLADMVRRSP-LLKGLPVVVIPNGIDTEIFapvDKAKARKRLGIPQDKKVILFGAESVTKPRKGFDELIE 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 245 ALVKLrgrltsQDWDKVHLIMAGGYDERVLE---NVQHYEELKKMVQLSDLgqyvtflRSCSDeqkisllrgctcVLYTP 321
Cdd:cd03825   216 ALKLL------ATKDDLLLVVFGKNDPQIVIlpfDIISLGYIDDDEQLVDI-------YSAAD------------LFVHP 270
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1777466523 322 S-NEHFGIVPLEAMYLQCPVIAVNSGGPLESVVHNVTGFLCEP-DPVHFSEAMENFIHEPSLKATMGLAGRARVKEKFS 398
Cdd:cd03825   271 SlADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPgDVQALAEAIEWLLANPKERESLGERARALAENHFD 349
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
317-406 3.49e-07

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 52.02  E-value: 3.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 317 VLYTPS-NEHFGIVPLEAMYLQCPVIAVNSGG-P--LESVVHNVTGFLCEP-DPVHFSEAMENFIHEPSLKATMGLAGRA 391
Cdd:PLN02871  334 VFVMPSeSETLGFVVLEAMASGVPVVAARAGGiPdiIPPDQEGKTGFLYTPgDVDDCVEKLETLLADPELRERMGAAARE 413
                          90
                  ....*....|....*
gi 1777466523 392 RVkEKFSPEAFTEQL 406
Cdd:PLN02871  414 EV-EKWDWRAATRKL 427
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
198-408 7.48e-07

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: 50.91  E-value: 7.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 198 LYPSLNITRFDSAIPEKL---DDLVPKGKKFLFLSINRYERKKNLTLALEALVKLrgrltSQDWDKVHLIMAGgydERVL 274
Cdd:cd04951   159 VYNGIDLNKFKKDINVRLkirNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISEL-----ILSKNDFKLLIAG---DGPL 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 275 ENvqhyeELKKMVQLSDLGQYVTFLRSCSDeqkIS-LLRGCTCVLYTPSNEHFGIVPLEAMYLQCPVIAVNSGGPLEsVV 353
Cdd:cd04951   231 RN-----ELERLICNLNLVDRVILLGQISN---ISeYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAE-VV 301
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777466523 354 HNVTGFLCEPDPVHFSEAM-ENFIHEPSLKATMGLAGRARVKeKFSPEAFTEQLYQ 408
Cdd:cd04951   302 GDHNYVVPVSDPQLLAEKIkEIFDMSDEERDILGNKNEYIAK-NFSINTIVNEWER 356
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
223-405 2.19e-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: 49.22  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 223 KKFLFLSINRYERKKNLTLALEALVKLRGRLTSQdwdKVHLImagGYDErvlenvqHYEELKKMVQLSDLGQYVT---FL 299
Cdd:cd04949   159 KSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEI---TLDIY---GYGE-------EREKLKKLIEELHLEDNVFlkgYH 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 300 RSCSDEQKISLLrgctcVLYTPSNEHFGIVPLEAMYLQCPVIAVNSG-GPLESVVHNVTGFLCEPDPVH-FSEAMENFIH 377
Cdd:cd04949   226 SNLDQEYQDAYL-----SLLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDaLADKIIELLN 300
                         170       180
                  ....*....|....*....|....*...
gi 1777466523 378 EPSLKATMGLAGRArVKEKFSPEAFTEQ 405
Cdd:cd04949   301 DPEKLQQFSEESYK-IAEKYSTENVMEK 327
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
194-405 1.36e-05

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: 46.94  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 194 DPD---VLYPSLNITRFDSAIPEKlddlvPKGKKFLFLSINRYERKKNLTLALEAL-VKLRGRLTSQDWdkvhLImaGGY 269
Cdd:cd03813   265 DPDktrVIPNGIDIQRFAPAREER-----PEKEPPVVGLVGRVVPIKDVKTFIRAFkLVRRAMPDAEGW----LI--GPE 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 270 DErvleNVQHYEELKKMVQLSDLGQYVTFLrscsDEQKIS-LLRGCTCVLYTPSNEHFGIVPLEAMYLQCPVIAVNSGGP 348
Cdd:cd03813   334 DE----DPEYAQECKRLVASLGLENKVKFL----GFQNIKeYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSC 405
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777466523 349 LESV-----VHNVTGFLCEP-DPVHFSEAMENFIHEPSLKATMGLAGRARVKEKFSPEAFTEQ 405
Cdd:cd03813   406 RELIygaddALGQAGLVVPPaDPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDS 468
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
223-378 2.67e-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: 39.58  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 223 KKFLFLSINRYERKKNLTLALEALVKLRGRLTSQ---------------DWDKVHLIMAGGYDERvlenvqhyEELKKMV 287
Cdd:cd03812   170 EKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQknhsflidifeelkkKNPNVKLVLVGEGELK--------EKIKEKV 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777466523 288 QLSDLGQYVTFLRSCSDEQKI-SLLRgctcVLYTPSN-EHFGIVPLEAMYLQCPVIAVNSGGPLESVVHNVTGFLCEPDP 365
Cdd:cd03812   242 KELGLEDKVIFLGFRNDVSEIlSAMD----VFLFPSLyEGLPLVAVEAQASGLPCLLSDTITKECDITNNVEFLPLNETP 317
                         170
                  ....*....|...
gi 1777466523 366 VHFSEAMENFIHE 378
Cdd:cd03812   318 STWAEKILKLIKR 330
 
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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