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Conserved domains on  [gi|2226658501|ref|WP_246341403|]
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glycosyltransferase family 4 protein [Simiduia aestuariiviva]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133453)

glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CAZY:  GT4
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3001586

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
1-335 1.41e-54

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: 183.12  E-value: 1.41e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501   1 MCQQGHRVKLVVLRHTPftETLTSFPCPIVDLDIHHVARPKTLQTLLR-FRRQLIQDQVDVLHAWLPESCLLAPLLLKHA 79
Cdd:cd03801    27 LAARGHDVTVLTPADPG--EPPEELEDGVIVPLLPSLAALLRARRLLReLRPLLRLRKFDVVHAHGLLAALLAALLALLL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  80 RLKVITSR-----RDMGLIYRGKPAWLYRMVR--RRTDTVISNSRAVAQHVSQQERLPATQSKVIYNGLDDFTPSATGTQ 152
Cdd:cd03801   105 GAPLVVTLhgaepGRLLLLLAAERRLLARAEAllRRADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSPPLRR 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 153 PIFNDTNAIKLILVANIKPVKRTLDAVNAVAALHAQGIAVELALVGepQDSAYVASIHNHIAaqQLASHIHWLGSV--NE 230
Cdd:cd03801   185 KLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVG--GDGPLRAELEELEL--GLGDRVRFLGFVpdEE 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 231 PRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQF 310
Cdd:cd03801   261 LPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARL 340
                         330       340
                  ....*....|....*....|....*
gi 2226658501 311 SERNKARIAADFTMANMIAKHLAAY 335
Cdd:cd03801   341 GRAARERVAERFSWERVAERLLDLY 365
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
1-335 1.41e-54

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: 183.12  E-value: 1.41e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501   1 MCQQGHRVKLVVLRHTPftETLTSFPCPIVDLDIHHVARPKTLQTLLR-FRRQLIQDQVDVLHAWLPESCLLAPLLLKHA 79
Cdd:cd03801    27 LAARGHDVTVLTPADPG--EPPEELEDGVIVPLLPSLAALLRARRLLReLRPLLRLRKFDVVHAHGLLAALLAALLALLL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  80 RLKVITSR-----RDMGLIYRGKPAWLYRMVR--RRTDTVISNSRAVAQHVSQQERLPATQSKVIYNGLDDFTPSATGTQ 152
Cdd:cd03801   105 GAPLVVTLhgaepGRLLLLLAAERRLLARAEAllRRADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSPPLRR 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 153 PIFNDTNAIKLILVANIKPVKRTLDAVNAVAALHAQGIAVELALVGepQDSAYVASIHNHIAaqQLASHIHWLGSV--NE 230
Cdd:cd03801   185 KLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVG--GDGPLRAELEELEL--GLGDRVRFLGFVpdEE 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 231 PRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQF 310
Cdd:cd03801   261 LPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARL 340
                         330       340
                  ....*....|....*....|....*
gi 2226658501 311 SERNKARIAADFTMANMIAKHLAAY 335
Cdd:cd03801   341 GRAARERVAERFSWERVAERLLDLY 365
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
100-337 2.47e-34

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: 129.46  E-value: 2.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 100 WLYRMVRRRTDTVISNSRAVAQHVSQQER----LPATQSKVIYNGLDD--FTPSATGTQPIFN-DTNAIKLIL---VANI 169
Cdd:TIGR03088 124 WKYRWLRRLYRPLIHHYVAVSRDLEDWLRgpvkVPPAKIHQIYNGVDTerFHPSRGDRSPILPpDFFADESVVvgtVGRL 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 170 KPVKRTLDAVNAVAALHAQGIAVE----LALVGepqDSAYVASIHNHIAAQQLAsHIHWL-GSVNEPRQLLSQADIGLLV 244
Cdd:TIGR03088 204 QAVKDQPTLVRAFALLVRQLPEGAerlrLVIVG---DGPARGACEQMVRAAGLA-HLVWLpGERDDVPALMQALDLFVLP 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 245 SESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSERNKARIAADFTM 324
Cdd:TIGR03088 280 SLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSI 359
                         250
                  ....*....|...
gi 2226658501 325 ANMIAKHLAAYDQ 337
Cdd:TIGR03088 360 NAMVAAYAGLYDQ 372
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
160-303 1.82e-32

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 118.00  E-value: 1.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 160 AIKLILVANI-KPVKRTLDAVNAVAALHAQGIAVELALVGEPQDSAYVAsihnhiAAQQLASHIHWLGSVNEPRQLLSQA 238
Cdd:pfam13692   1 RPVILFVGRLhPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELEE------LAAGLEDRVIFTGFVEDLAELLAAA 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2226658501 239 DIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIqHQHNGMLIEKGDVAELAQAIQTLHQN 303
Cdd:pfam13692  75 DVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLLED 138
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
234-338 5.24e-31

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 113.93  E-value: 5.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 234 LLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSER 313
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96
                          90       100
                  ....*....|....*....|....*
gi 2226658501 314 NKARIAADFTMANMIAKHLAAYDQA 338
Cdd:COG0438    97 ARERAEERFSWEAIAERLLALYEEL 121
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
59-336 1.79e-14

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 74.30  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  59 DVLHAWLPESCL---LAPLLLKHARLKVI------TSRRDMgliYRGKPAWLYR-MVRRRTDTVISNSRAVAQHVSQQER 128
Cdd:PRK15179  402 SVVHIWQDGSIFacaLAALLAGVPRIVLSvrtmppVDRPDR---YRVEYDIIYSeLLKMRGVALSSNSQFAAHRYADWLG 478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 129 LPATQSKVIYNGLDDF----TPSATGTQPIFNDTNAIKLILVANI---KPVKRTLDAVNAVAALHAQGIAVELALVGEpq 201
Cdd:PRK15179  479 VDERRIPVVYNGLAPLksvqDDACTAMMAQFDARTSDARFTVGTVmrvDDNKRPFLWVEAAQRFAASHPKVRFIMVGG-- 556
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 202 dsayvASIHNHIA--AQQL--ASHIHWLGSVNEPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQ 277
Cdd:PRK15179  557 -----GPLLESVRefAQRLgmGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQ 631
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2226658501 278 HQHNGMLIEKGDVA--ELAQAIQTLHQNPTLKTQFSERNKARIAADFTMANMIAKHLAAYD 336
Cdd:PRK15179  632 EGVTGLTLPADTVTapDVAEALARIHDMCAADPGIARKAADWASARFSLNQMIASTVRCYQ 692
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
166-335 1.58e-06

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 49.54  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 166 VANIKPVKRTLDAVNAVAAL--HAQGiavelALVG-EPQDSAYVASIHNHIAAQQLASHIHWLG--SVNEprqLLSQADI 240
Cdd:NF038011  315 VVPIKDIKTFIRAMRTVVRAmpEAEG-----WIVGpEEEDPAYAAECRSLVASLGLQDKVKFLGfqKIDD---LLPQVGL 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 241 GLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQ--------HNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSE 312
Cdd:NF038011  387 MVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQLIEGLdeedralgAAGEVVAIADPQALARAALDLLRDPQRWQAAQA 466
                         170       180
                  ....*....|....*....|...
gi 2226658501 313 RNKARIAADFTMANMIAKHLAAY 335
Cdd:NF038011  467 AGLARVERYYTEELMFDRYRELY 489
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
1-335 1.41e-54

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: 183.12  E-value: 1.41e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501   1 MCQQGHRVKLVVLRHTPftETLTSFPCPIVDLDIHHVARPKTLQTLLR-FRRQLIQDQVDVLHAWLPESCLLAPLLLKHA 79
Cdd:cd03801    27 LAARGHDVTVLTPADPG--EPPEELEDGVIVPLLPSLAALLRARRLLReLRPLLRLRKFDVVHAHGLLAALLAALLALLL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  80 RLKVITSR-----RDMGLIYRGKPAWLYRMVR--RRTDTVISNSRAVAQHVSQQERLPATQSKVIYNGLDDFTPSATGTQ 152
Cdd:cd03801   105 GAPLVVTLhgaepGRLLLLLAAERRLLARAEAllRRADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSPPLRR 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 153 PIFNDTNAIKLILVANIKPVKRTLDAVNAVAALHAQGIAVELALVGepQDSAYVASIHNHIAaqQLASHIHWLGSV--NE 230
Cdd:cd03801   185 KLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVG--GDGPLRAELEELEL--GLGDRVRFLGFVpdEE 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 231 PRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQF 310
Cdd:cd03801   261 LPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARL 340
                         330       340
                  ....*....|....*....|....*
gi 2226658501 311 SERNKARIAADFTMANMIAKHLAAY 335
Cdd:cd03801   341 GRAARERVAERFSWERVAERLLDLY 365
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
5-336 7.63e-54

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: 180.98  E-value: 7.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501   5 GHRVKLVVLRHT-PFTETLTSFPCPIVDLDIHHVARPKTLqtlLRFRRQLIQDQVDVLHAWLPESCLLAPLLLKHAR-LK 82
Cdd:cd03807    29 RFEHVVISLTGDgVLGEELLAAGVPVVCLGLSSGKDPGVL---LRLAKLIRKRNPDVVHTWMYHADLIGGLAAKLAGgVK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  83 VITSRRDMGLIYRGKP--AWLYRMVRRRTDTVISNSRAVAQhVSQQERLPATQSKVIYNGLD--DFTPSATGTQPIFN-- 156
Cdd:cd03807   106 VIWSVRSSNIPQRLTRlvRKLCLLLSKFSPATVANSSAVAE-FHQEQGYAKNKIVVIYNGIDlfKLSPDDASRARARRrl 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 157 --DTNAIKLILVANIKPVKRTLDAVNAVAALHAQGIAVELALVGE----PQDSAYVASIHnhiaaqqLASHIHWLGSVNE 230
Cdd:cd03807   185 glAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRgperPNLERLLLELG-------LEDRVHLLGERSD 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 231 PRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQhQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQF 310
Cdd:cd03807   258 VPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVD-DGTGFLVPAGDPQALADAIRALLEDPEKRARL 336
                         330       340
                  ....*....|....*....|....*.
gi 2226658501 311 SERNKARIAADFTMANMIAKHLAAYD 336
Cdd:cd03807   337 GRAARERIANEFSIDAMVRRYETLYY 362
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
43-319 3.47e-42

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: 149.82  E-value: 3.47e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  43 LQTLLRFRRQLIQDQVDVLHAWLPESCLLAPLLLKHARLKVITSRRDMGLIYRGKPAW-LYRMVRRRTDTVISNSRAVAQ 121
Cdd:cd03811    69 LKAILKLKRILKRAKPDVVISFLGFATYIVAKLAAARSKVIAWIHSSLSKLYYLKKKLlLKLKLYKKADKIVCVSKGIKE 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 122 HVSQQERLPATQSKVIYNGLD-DFTPSATGTQPIFNDTNAIKLILVANIKPVKRTLDAVNAVAALHAQGIAVELALVGEP 200
Cdd:cd03811   149 DLIRLGPSPPEKIEVIYNPIDiDRIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDG 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 201 QDSAYvasIHNHIAAQQLASHIHWLGSVNEPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQH 280
Cdd:cd03811   229 PLREE---LEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGE 305
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2226658501 281 NGMLIEKGDVAELAQAIQTLHQNPTLKTQFSERNKARIA 319
Cdd:cd03811   306 NGLLVPDGDAAALAGILAALLQKKLDAALRERLAKAQEA 344
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
41-332 1.19e-41

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: 148.90  E-value: 1.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  41 KTLQTLLRFRRQLIQDQVDVLHAWLPESCLLAPLLLKHAR-LKVITSRRDMGLIYRGKP------AWLYRMVRRRTDTVI 113
Cdd:cd03808    65 KDLKALFKLYKLLKKEKPDIVHCHTPKPGILGRLAARLAGvPKVIYTVHGLGFVFTEGKllrllyLLLEKLALLFTDKVI 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 114 SNSRAvAQHVSQQERLPATQSKVIYNG----LDDFTPsatgtQPIFNDTNAIKLILVANIKPVKRTLDAVNAVAALHAQG 189
Cdd:cd03808   145 FVNED-DRDLAIKKGIIKKKKTVLIPGsgvdLDRFQY-----SPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKG 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 190 IAVELALVGE-PQDSAYVASIHNhiaaQQLASHIHWLGSVNEPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATR 268
Cdd:cd03808   219 PNVRFLLVGDgELENPSEILIEK----LGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTD 294
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2226658501 269 VGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSERNKARIAADFTMANMIAKHL 332
Cdd:cd03808   295 VPGCRELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
100-337 2.47e-34

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: 129.46  E-value: 2.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 100 WLYRMVRRRTDTVISNSRAVAQHVSQQER----LPATQSKVIYNGLDD--FTPSATGTQPIFN-DTNAIKLIL---VANI 169
Cdd:TIGR03088 124 WKYRWLRRLYRPLIHHYVAVSRDLEDWLRgpvkVPPAKIHQIYNGVDTerFHPSRGDRSPILPpDFFADESVVvgtVGRL 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 170 KPVKRTLDAVNAVAALHAQGIAVE----LALVGepqDSAYVASIHNHIAAQQLAsHIHWL-GSVNEPRQLLSQADIGLLV 244
Cdd:TIGR03088 204 QAVKDQPTLVRAFALLVRQLPEGAerlrLVIVG---DGPARGACEQMVRAAGLA-HLVWLpGERDDVPALMQALDLFVLP 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 245 SESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSERNKARIAADFTM 324
Cdd:TIGR03088 280 SLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSI 359
                         250
                  ....*....|...
gi 2226658501 325 ANMIAKHLAAYDQ 337
Cdd:TIGR03088 360 NAMVAAYAGLYDQ 372
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
160-303 1.82e-32

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 118.00  E-value: 1.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 160 AIKLILVANI-KPVKRTLDAVNAVAALHAQGIAVELALVGEPQDSAYVAsihnhiAAQQLASHIHWLGSVNEPRQLLSQA 238
Cdd:pfam13692   1 RPVILFVGRLhPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELEE------LAAGLEDRVIFTGFVEDLAELLAAA 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2226658501 239 DIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIqHQHNGMLIEKGDVAELAQAIQTLHQN 303
Cdd:pfam13692  75 DVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLLED 138
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
234-338 5.24e-31

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 113.93  E-value: 5.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 234 LLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSER 313
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96
                          90       100
                  ....*....|....*....|....*
gi 2226658501 314 NKARIAADFTMANMIAKHLAAYDQA 338
Cdd:COG0438    97 ARERAEERFSWEAIAERLLALYEEL 121
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
10-333 7.31e-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: 103.60  E-value: 7.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  10 LVVLRHTPFTETLTSFPCPIVDLDIHHVARPKTLQTLLRFRRQLI-QDQVDVLHAwlpeSCLLAPLLLKHARLKV----- 83
Cdd:cd03809    36 VLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPkKDKPDLLHS----PHNTAPLLLKGCPQVVtihdl 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  84 --ITSRRDMGLIYRGKPAWLYRMVRRRTDTVISNSRAVAQHVSQQERLPATQSKVIYNGLDDFTPSATGTQPIFNDTNAI 161
Cdd:cd03809   112 ipLRYPEFFPKRFRLYYRLLLPISLRRADAIITVSEATRDDIIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLP 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 162 K--LILVANIKPVKRTLDAVNAVAALHAQGIAVELALVGEPQDsaYVASIHNHIAAQQLASHIHWLGSVNEP--RQLLSQ 237
Cdd:cd03809   192 EpyFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGW--EDEELLDLVKKLGLGGRVRFLGYVSDEdlPALYRG 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 238 ADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIqhQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSERNKAR 317
Cdd:cd03809   270 ARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVA--GDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLER 347
                         330
                  ....*....|....*.
gi 2226658501 318 iAADFTMANMIAKHLA 333
Cdd:cd03809   348 -AKKFSWEKTAEKTLE 362
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
57-320 1.20e-24

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: 102.43  E-value: 1.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  57 QVDVLHAWLPESCLLAPLLLKHARLKVITSRRDMGLIYRGKPAWLYRmVRRRTDTVISNSRAVAQHVSQQERLPATQSKV 136
Cdd:cd03819    76 RIDLIHAHSRAPAWLGWLASRLTGVPLVTTVHGSYLATYHPKDFALA-VRARGDRVIAVSELVRDHLIEALGVDPERIRV 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 137 IYNGLDD--FTPSATGTQPIFN--DTNAIKLILVANIKPVKRTLDAVNAVAALHAQGiAVELALVGEPQDSAYvasIHNH 212
Cdd:cd03819   155 IPNGVDTdrFPPEAEAEERAQLglPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEP-DFRLLVAGDGPERDE---IRRL 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 213 IAAQQLASHIHWLGSVNEPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAE 292
Cdd:cd03819   231 VERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEA 310
                         250       260
                  ....*....|....*....|....*...
gi 2226658501 293 LAQAIQTLHQNPtlktqfSERNKARIAA 320
Cdd:cd03819   311 LADAIRAAKLLP------EAREKLQAAA 332
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
2-330 1.22e-24

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: 102.70  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501   2 CQQGHRVKLVVL---RHTPFtetltsFP-------CPIVDLDIHHVARP-KTLQTLLRFRRQLIQDQVDVLHAWLPES-C 69
Cdd:cd03820    27 AKKGYDVTIISLdsaEKPPF------YElddnikiKNLGDRKYSHFKLLlKYFKKVRRLRKYLKNNKPDVVISFRTSLlT 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  70 LLAPLLLKharLKVI----TSRRDMGLIYRgkPAWLYRMVRRRTDTVISNSRAVAQHvsqQERLPATQSKVIYNGLDDFT 145
Cdd:cd03820   101 FLALIGLK---SKLIvwehNNYEAYNKGLR--RLLLRRLLYKRADKIVVLTEADKLK---KYKQPNSNVVVIPNPLSFPS 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 146 PSATGTQpifndtNAIKLILVANIKPVK---RTLDAVNAVAALHAqgiAVELALVGEPQDSAyvaSIHNHIAAQQLASHI 222
Cdd:cd03820   173 EEPSTNL------KSKRILAVGRLTYQKgfdLLIEAWALIAKKHP---DWKLRIYGDGPERE---ELEKLIDKLGLEDRV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 223 HWLGSVNEPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVAT-RVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLH 301
Cdd:cd03820   241 KLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFdCPTGPSEIIEDGENGLLVPNGDVDALAEALLRLM 320
                         330       340
                  ....*....|....*....|....*....
gi 2226658501 302 QNPTLKTQFSERNKARiAADFTMANMIAK 330
Cdd:cd03820   321 EDEELRKKMGKNARKN-AERFSIEKIIKQ 348
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
5-338 1.80e-24

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: 102.46  E-value: 1.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501   5 GHRVKLVVLRHTP-----FTETLTSFPCPIVDLDIHHVARPKTLQ-------TLLRFRRQLIQDQVDVLHA-WLPESCLL 71
Cdd:cd03798    31 GVDVEVLAPAPWGpaaarLLRKLLGEAVPPRDGRRLLPLKPRLRLlaplrapSLAKLLKRRRRGPPDLIHAhFAYPAGFA 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  72 AplLLKHARLK---VITSRRDMGLIYRGKPaWLYRMVR---RRTDTVISNSRAVAQHVsQQERLPATQSKVIYNGLDDFT 145
Cdd:cd03798   111 A--ALLARLYGvpyVVTEHGSDINVFPPRS-LLRKLLRwalRRAARVIAVSKALAEEL-VALGVPRDRVDVIPNGVDPAR 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 146 PSATGTQPIFNDtNAIKLILVANIKPVKRTLDAVNAVAALHAQGIAVELALVGEPQDSAYVASIHnhiAAQQLASHIHWL 225
Cdd:cd03798   187 FQPEDRGLGLPL-DAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALA---EDLGLGDRVTFT 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 226 GSVnePRQLLSQ----ADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLH 301
Cdd:cd03798   263 GRL--PHEQVPAyyraCDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRAL 340
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2226658501 302 QNPTlKTQFSERNKARIAADFTMANMIAKHLAAYDQA 338
Cdd:cd03798   341 AEPY-LRELGEAARARVAERFSWVKAADRIAAAYRDV 376
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
3-330 2.40e-24

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: 102.42  E-value: 2.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501   3 QQGHRVKLVvlrHTPFTETLTSFPCPIVD----LDIHHVARP--------KTLQTLLRFRRQLI------QDQVDVLHAW 64
Cdd:cd03794    29 RRGHEVTVL---TPSPNYPLGRIFAGATEtkdgIRVIRVKLGpikkngliRRLLNYLSFALAALlkllvrEERPDVIIAY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  65 LP--ESCLLAPLLLKHARLKVI--------TSRRDMGLIYRGKP----AWLYRMVRRRTDTVISNSRAVAQHVSQQErLP 130
Cdd:cd03794   106 SPpiTLGLAALLLKKLRGAPFIldvrdlwpESLIALGVLKKGSLlkllKKLERKLYRLADAIIVLSPGLKEYLLRKG-VP 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 131 ATQSKVIYNGLDDFT---PSATGTQPIFNDTNAIKLILVANIkPVKRTLDAVNAVAALHAQGIAVELALVGEPQDSAYVa 207
Cdd:cd03794   185 KEKIIVIPNWADLEEfkpPPKDELRKKLGLDDKFVVVYAGNI-GKAQGLETLLEAAERLKRRPDIRFLFVGDGDEKERL- 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 208 sihNHIAAQQLASHIHWLGSVnePRQ----LLSQADIGLL-----VSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQH 278
Cdd:cd03794   263 ---KELAKARGLDNVTFLGRV--PKEevpeLLSAADVGLVplkdnPANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEI 337
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2226658501 279 QHNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSERNKARIAADFTMANMIAK 330
Cdd:cd03794   338 NGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADR 389
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
161-317 3.50e-24

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: 96.57  E-value: 3.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 161 IKLILVANIKPVKRTLDAVNAVAALHAQGIAVELALVGepqDSAYVASIHNHIAAQQLASHIHWLGSVN--EPRQLLSQA 238
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAG---DGEEEKRLKKLAEKLGLGDNVIFLGFVSdeDLPELLKIA 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2226658501 239 DIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSERNKAR 317
Cdd:pfam00534  80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
111-337 4.06e-24

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: 101.25  E-value: 4.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 111 TVISNSRAVAQHVSQQERLPATQSKVIYNGLDD--FTPSATG-TQPIFN-DTNAIKLILVAN--IKPVKRTLDAVNAVAA 184
Cdd:cd03825   140 TIVAPSRWLADMVRRSPLLKGLPVVVIPNGIDTeiFAPVDKAkARKRLGiPQDKKVILFGAEsvTKPRKGFDELIEALKL 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 185 LHAQGIaVELALVGepqdsayvasiHNHIAAQQLASHIHWLGSVNEPRQL---LSQADIGLLVSESEGLSNTLMEYMQAG 261
Cdd:cd03825   220 LATKDD-LLLVVFG-----------KNDPQIVILPFDIISLGYIDDDEQLvdiYSAADLFVHPSLADNLPNTLLEAMACG 287
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2226658501 262 LPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSERNKARIAADFTMANMIAKHLAAYDQ 337
Cdd:cd03825   288 TPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYKD 363
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
162-330 3.35e-23

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: 98.14  E-value: 3.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 162 KLILVANIKPVKRTLDAVNAVAALHAQGIAVELALVGEPQDSAyvaSIHNHIAAQQLASHIHWLGSVNEPRQLLSQADIG 241
Cdd:cd04949   162 KIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEERE---KLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLS 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 242 LLVSESEGLSNTLMEYMQAGLPVVATRVG-GNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSErnKAR-IA 319
Cdd:cd04949   239 LLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSE--ESYkIA 316
                         170
                  ....*....|.
gi 2226658501 320 ADFTMANMIAK 330
Cdd:cd04949   317 EKYSTENVMEK 327
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
6-328 2.19e-21

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: 93.55  E-value: 2.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501   6 HRVKLVVLRHTPFTETLTSFPcpivdlDIHHVARPKTlQTLLRFRRQLIQD-QVDVLHAwlpeSCL--LAPLLLKHARLK 82
Cdd:cd03823    51 ARSVVRYRRAPDETLPLALKR------RGYELFETYN-PGLRRLLARLLEDfRPDVVHT----HNLsgLGASLLDAARDL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  83 ----VITSRrDMGLI-YRGKpawlyrMVRRRTDTVISNSRAVAQhVSQQERLPATQSKVIYNGLddfTPSATGTQPIFND 157
Cdd:cd03823   120 gipvVHTLH-DYWLLcPRQF------LFKKGGDAVLAPSRFTAN-LHEANGLFSARISVIPNAV---EPDLAPPPRRRPG 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 158 TNAIKLILVANIKPVKRTLDAVNAVAALHAQGIavELALVGEPQDSAYvasihnhiAAQQLASHIHWLGSVN--EPRQLL 235
Cdd:cd03823   189 TERLRFGYIGRLTEEKGIDLLVEAFKRLPREDI--ELVIAGHGPLSDE--------RQIEGGRRIAFLGRVPtdDIKDFY 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 236 SQADIGLLVS---ESEGLsnTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSE 312
Cdd:cd03823   259 EKIDVLVVPSiwpEPFGL--VVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRA 336
                         330
                  ....*....|....*.
gi 2226658501 313 RNKARIAADFTMANMI 328
Cdd:cd03823   337 GAEPPRSTESQAEEYL 352
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
58-335 1.80e-20

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: 91.26  E-value: 1.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  58 VDVLHAW--LPE--SCLLAPLLLKHaRLKVITSRR--DMGLIYRGKPawLYRMVR---RRTDTVISNSRAVAQHVsqQER 128
Cdd:cd04962    85 LDVLHAHyaIPHasCAYLAREILGE-KIPIVTTLHgtDITLVGYDPS--LQPAVRfsiNKSDRVTAVSSSLRQET--YEL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 129 LPATQS-KVIYNGLDD--FTP-SATGTQPIFNDTNAIKLIL-VANIKPVKRTLDAVnAVAALHAQGIAVELALVGEPQDs 203
Cdd:cd04962   160 FDVDKDiEVIHNFIDEdvFKRkPAGALKRRLLAPPDEKVVIhVSNFRPVKRIDDVV-RVFARVRRKIPAKLLLVGDGPE- 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 204 ayVASIHNHIAAQQLASHIHWLGSVNEPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGM 283
Cdd:cd04962   238 --RVPAEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGF 315
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2226658501 284 LIEKGDVAELAQ-AIQTLHqNPTLKTQFSERNKARIAADFTMANMIAKHLAAY 335
Cdd:cd04962   316 LSDVGDVDAMAKsALSILE-DDELYNRMGRAARKRAAERFDPERIVPQYEAYY 367
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
76-336 2.56e-19

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: 88.55  E-value: 2.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  76 LKHARLKVITSRRDMGLIyrgKPAW------LYRMVRRRTDTVIS----NSRavaqhvsQQERL--PATQSKVIYNGLD- 142
Cdd:cd03813   209 TRERKIEILQSTWIMGYI---KKLWirfferLGKLAYQQADKIISlyegNRR-------RQIRLgaDPDKTRVIPNGIDi 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 143 -DFTPSatGTQPIFNDTNAIKLIL-VANIKPVKrTLdaVNAVAALHAQGIAVELALVG-EPQDSAYVASIHNHIAAQQLA 219
Cdd:cd03813   279 qRFAPA--REERPEKEPPVVGLVGrVVPIKDVK-TF--IRAFKLVRRAMPDAEGWLIGpEDEDPEYAQECKRLVASLGLE 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 220 SHIHWLGSVNEpRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHN-----GMLIEKGDVAELA 294
Cdd:cd03813   354 NKVKFLGFQNI-KEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELIYGADDalgqaGLVVPPADPEALA 432
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2226658501 295 QAIQTLHQNPTLKTQFSERNKARIAADFTMANMIAKHLAAYD 336
Cdd:cd03813   433 EALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
3-336 5.53e-19

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


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 86.96  E-value: 5.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501   3 QQGHRVKLVVLRHTPFTE-------TLTSFPCPIV-DLDIHHVARPKTLQTLLRFrrqliqdQVDVLHAWLPESCLLAPL 74
Cdd:cd03814    29 RRGHEVRVVAPGPFDEAEsaegrvvSVPSFPLPFYpEYRLALPLPRRVRRLIKEF-------QPDIIHIATPGPLGLAAL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  75 LLK-----------HARLKVITSRRDMGLIYRGKPAWLyRMVRRRTDTVISNSRAVAQHVsqqERLPATQSKVIYNGLD- 142
Cdd:cd03814   102 RAArrlglpvvtsyHTDFPEYLSYYTLGPLSWLAWAYL-RWFHNPFDTTLVPSPSIAREL---EGHGFERVRLWPRGVDt 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 143 -DFTPSA--TGTQPIFNDTNAIKLILVANIKPVKRtLDAVNAVAALHAQGIAVELALVGEPQDSAYVASIHnhiaaqqla 219
Cdd:cd03814   178 eLFHPSRrdAALRRRLGPPGRPLLLYVGRLAPEKN-LEALLDADLPLAASPPVRLVVVGDGPARAELEARG--------- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 220 SHIHWLGSVN--EPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAI 297
Cdd:cd03814   248 PDVIFTGFLTgeELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAAL 327
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2226658501 298 QTLHQNPTLKTQFSERNKARiAADFTMANMIAKHLAAYD 336
Cdd:cd03814   328 RALLEDPELRRRMAARARAE-AERYSWEAFLDNLLDYYA 365
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
91-285 1.66e-18

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: 83.22  E-value: 1.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  91 GLIYRGKPAWLYRMVRRRTDTVISNS-RAVAQHVSQQERLPATQSKVIYNGLDDFTPSATGTQPIFNDTNAIKL---ILV 166
Cdd:cd01635    37 ALLLLALRRILKKLLELKPDVVHAHSpHAAALAALLAARLLGIPIVVTVHGPDSLESTRSELLALARLLVSLPLadkVSV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 167 ANIKPVKRTLDAVNAVAALHAQGIAVELALVGEPQDSAYVASihnHIAAQQLASHIHWLG--SVNEPRQLLSQ-ADIGLL 243
Cdd:cd01635   117 GRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEA---LAAALGLLERVVIIGglVDDEVLELLLAaADVFVL 193
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2226658501 244 VSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLI 285
Cdd:cd01635   194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
89-330 3.26e-18

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: 84.64  E-value: 3.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  89 DMGLIYRGKPAWLYRMVRRRTDTVISNSRAVAQHVsqQERLPATQSKVIYNGLD-DFTPSATGTQPI---FNDTNAIKLI 164
Cdd:cd03817   128 KGKLLVKAVVRKLVRRFYNHTDAVIAPSEKIKDTL--REYGVKGPIEVIPNGIDlDKFEKPLNTEERrklGLPPDEPILL 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 165 LVANIKPVKRTLDAVNAVAALHAQgIAVELALVGepqDSAYVASIHNHIAAQQLASHIHWLGSVnEPRQL---LSQADIG 241
Cdd:cd03817   206 YVGRLAKEKNIDFLLRAFAELKKE-PNIKLVIVG---DGPEREELKELARELGLADKVIFTGFV-PREELpeyYKAADLF 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 242 LLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVaELAQAIQTLHQNPTLKTQFSeRNKARIAAD 321
Cdd:cd03817   281 VFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDE-TLAEKLLHLRENLELLRKLS-KNAEISARE 358

                  ....*....
gi 2226658501 322 FTMANMIAK 330
Cdd:cd03817   359 FAFAKSVEK 367
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
3-336 1.15e-16

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: 79.64  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501   3 QQGHRVKLV--------VLRHTPFTETLTSFPCPIVDLDIHHvarpktlqtLLRFRRQLIQDQVDVLHAWLPescLLAPL 74
Cdd:cd03802    33 RRGHEVTLFapgdshtsAPLVAVIPRALRLDPIPQESKLAEL---------LEALEVQLRASDFDVIHNHSY---DWLPP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  75 LLKHARLKVIT-----SRRDMGLIYRGKPAWLYrmvrrrtdtvISNSRAvaqhvSQQERLPATQSKVIYNGLDD----FT 145
Cdd:cd03802   101 FAPLIGTPFVTtlhgpSIPPSLAIYAAEPPVNY----------VSISDA-----QRAATPPIDYLTVVHNGLDPadyrFQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 146 PSATGtqpifndtnaiKLILVANIKPVKRTLDAVNAVAALhaqGIAVELALVGEPQDSAYvasihnHIAAQQLASHIHWL 225
Cdd:cd03802   166 PDPED-----------YLAFLGRIAPEKGLEDAIRVARRA---GLPLKIAGKVRDEDYFY------YLQEPLPGPRIEFI 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 226 GSVNEPR--QLLSQAdIGLLVSE--SEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEkgDVAELAQAIQTLh 301
Cdd:cd03802   226 GEVGHDEkqELLGGA-RALLFPInwDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVD--SVEEMAEAIANI- 301
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2226658501 302 qnptlkTQFSERNKARIAAD-FTMANMIAKHLAAYD 336
Cdd:cd03802   302 ------DRIDRAACRRYAEDrFSAARMADRYEALYR 331
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
178-324 2.65e-16

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: 79.03  E-value: 2.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 178 AVNAVAALHAQGIAVELALVGepqDSAYVASIHNHIAAQQLASHIHWLGSVNEPR--QLLSQADIGLLVS------ESEG 249
Cdd:cd03799   192 AIEAVAKLAQKYPNIEYQIIG---DGDLKEQLQQLIQELNIGDCVKLLGWKPQEEiiEILDEADIFIAPSvtaadgDQDG 268
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2226658501 250 LSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSERNKARIAADFTM 324
Cdd:cd03799   269 PPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDI 343
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
59-336 1.79e-14

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 74.30  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  59 DVLHAWLPESCL---LAPLLLKHARLKVI------TSRRDMgliYRGKPAWLYR-MVRRRTDTVISNSRAVAQHVSQQER 128
Cdd:PRK15179  402 SVVHIWQDGSIFacaLAALLAGVPRIVLSvrtmppVDRPDR---YRVEYDIIYSeLLKMRGVALSSNSQFAAHRYADWLG 478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 129 LPATQSKVIYNGLDDF----TPSATGTQPIFNDTNAIKLILVANI---KPVKRTLDAVNAVAALHAQGIAVELALVGEpq 201
Cdd:PRK15179  479 VDERRIPVVYNGLAPLksvqDDACTAMMAQFDARTSDARFTVGTVmrvDDNKRPFLWVEAAQRFAASHPKVRFIMVGG-- 556
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 202 dsayvASIHNHIA--AQQL--ASHIHWLGSVNEPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQ 277
Cdd:PRK15179  557 -----GPLLESVRefAQRLgmGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQ 631
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2226658501 278 HQHNGMLIEKGDVA--ELAQAIQTLHQNPTLKTQFSERNKARIAADFTMANMIAKHLAAYD 336
Cdd:PRK15179  632 EGVTGLTLPADTVTapDVAEALARIHDMCAADPGIARKAADWASARFSLNQMIASTVRCYQ 692
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
1-142 2.41e-12

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 64.48  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501   1 MCQQGHRVKLVVLRHTPFTETLTSFPCPIVDLDIHHVARPK-TLQTLLRFRRQLIQDQVDVLHAWLPESCLLAPLLLKHA 79
Cdd:pfam13439  14 LARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLrSLAFLRRLRRLLRRERPDVVHAHSPFPLGLAALAARLR 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2226658501  80 -RLKVITS----------RRDMGLIYRGKPAWLYRMVRRRTDTVISNSRAVAQHVSQQERLPATQSKVIYNGLD 142
Cdd:pfam13439  94 lGIPLVVTyhglfpdykrLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVPPEKIRVIPNGVD 167
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
107-323 2.51e-12

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: 67.27  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 107 RRTDTVISNSRAVAQHVSQQERLPATQSKVIYNGLDD--FTPSATGTQPIF---NDTNAIKLILVANIKPVKRTLDAVNA 181
Cdd:cd03800   162 EAADRVIASTPQEADELISLYGADPSRINVVPPGVDLerFFPVDRAEARRArllLPPDKPVVLALGRLDPRKGIDTLVRA 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 182 VAALHAQGIAVELALVGEPQDSAyvaSIHNHIAAQQLAsHIHWL-GSVNEPRQLlSQADIGLL-----------VSESEG 249
Cdd:cd03800   242 FAQLPELRELANLVLVGGPSDDP---LSMDREELAELA-EELGLiDRVRFPGRV-SRDDLPELyraadvfvvpsLYEPFG 316
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2226658501 250 LsnTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSERNKARIAADFT 323
Cdd:cd03800   317 L--TAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYT 388
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
84-322 5.61e-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: 65.94  E-value: 5.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  84 ITSRRDMGLIYRGKPAW---LYRMVRRRTDTVISNSRAVaqhvsqQERL-----PATQSKVIYNGLD--DFTPSATGTQp 153
Cdd:cd05844   116 ITTSRAWLAASPGWPSQfqrHRRALQRPAALFVAVSGFI------RDRLlarglPAERIHVHYIGIDpaKFAPRDPAER- 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 154 ifndtnAIKLILVANIKPVKRTLDAVNAVAALHAQGIAVELALVGepqDSAYVASIHNHIAAqqlASHIHWLGSVNEPR- 232
Cdd:cd05844   189 ------APTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAG---DGPLRPALQALAAA---LGRVRFLGALPHAEv 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 233 -QLLSQADIGLLVS------ESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPT 305
Cdd:cd05844   257 qDWMRRAEIFCLPSvtaasgDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRA 336
                         250
                  ....*....|....*..
gi 2226658501 306 LKTQFSERNKARIAADF 322
Cdd:cd05844   337 LADRMGGAARAFVCEQF 353
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
97-313 5.92e-12

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


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 66.24  E-value: 5.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  97 KPAWLYRMVRR---RTDTVISNSRAVAQHVSQqeRLPATQSKVIYNGLD-DFTPSATGTQPIFNDTNAIKLIL-VANIKP 171
Cdd:cd03821   138 KRIALHLIERRnlnNAALVHFTSEQEADELRR--FGLEPPIAVIPNGVDiPEFDPGLRDRRKHNGLEDRRIILfLGRIHP 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 172 VKRTLDAVNAVAALHAQGIAVELALVGePQDSAYVASIHNhIAAQQLASHIHWLGSVNEPRQ--LLSQADIGLLVSESEG 249
Cdd:cd03821   216 KKGLDLLIRAARKLAEQGRDWHLVIAG-PDDGAYPAFLQL-QSSLGLGDRVTFTGPLYGEAKwaLYASADLFVLPSYSEN 293
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2226658501 250 LSNTLMEYMQAGLPVVATRVGGNPELIQHQhNGMLIEKgDVAELAQAIQTLHQNPTLKTQFSER 313
Cdd:cd03821   294 FGNVVAEALACGLPVVITDKCGLSELVEAG-CGVVVDP-NVSSLAEALAEALRDPADRKRLGEM 355
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
1-140 1.68e-10

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 58.95  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501   1 MCQQGHRVKLVVLRHTPFTETLTSFPCPIVDLDI-HHVARPKTLQTLLRFRRQLIQDQVDVLHAWLPESCLLAPLLLKHA 79
Cdd:pfam13579  14 LAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPVpPRPSPLADLAALRRLRRLLRAERPDVVHAHSPTAGLAARLARRRR 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2226658501  80 RLKVITSRRDMGLIYRGKPA-WLYRMVRRRT----DTVISNSRAVAQHVSQQeRLPATQSKVIYNG 140
Cdd:pfam13579  94 GVPLVVTVHGLALDYGSGWKrRLARALERRLlrraDAVVVVSEAEAELLRAL-GVPAARVVVVPNG 158
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
54-304 2.68e-10

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


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 61.32  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  54 IQDQVDVLHA-WLPESCLLAPLLLKHARLKVITSRRDMGLIYRGKPAWLYRMVRRRTDTVISNSRAVAQH--VSQQERLP 130
Cdd:cd04946   118 IFGQGTVVYSyWLNHTALGLGLLKDEYYRDVVISRAHRYDLYEDQYGSYYLPLREYLVSYLDAVFLISKEgkDYLQKCYP 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 131 ATQSKVIYNGLDDFTPSAtGTQPIFNDTnaIKLILVANIKPVKRT---LDAVNAVAALHAQgIAVELALVGepqDSAYVA 207
Cdd:cd04946   198 AYKEKIFVSRLGVSDKEQ-YSKVKKEGD--LRLVSCSSIVPVKRIdliIETLNSLCVAHPS-ICISWTHIG---GGPLKE 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 208 SIHNHIAAQQLASHIHWLGSV--NEPRQLLSQ--ADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGM 283
Cdd:cd04946   271 RLEKLAENKLENVKVNFTGEVsnKEVKQLYKEndVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGL 350
                         250       260
                  ....*....|....*....|..
gi 2226658501 284 LIEKG-DVAELAQAIQTLHQNP 304
Cdd:cd04946   351 LLDKDpTPNEIVSSIMKFYLDG 372
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
235-309 2.81e-10

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 61.27  E-value: 2.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 235 LSQA----DIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELI---QHQHNGMLIEKGDVAELAQAIQTLHQNPTLK 307
Cdd:PLN02871  325 LSQAyasgDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPELR 404

                  ..
gi 2226658501 308 TQ 309
Cdd:PLN02871  405 ER 406
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
222-328 2.94e-10

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: 60.75  E-value: 2.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 222 IHWLGSVN--EPRQLLSQADIGLLVS--ESEGLSNTLMEYMQAGLPVVATRVG-GNPELIQHQHNGMLIEKGDVAELAQA 296
Cdd:cd03795   244 VKFLGRVDdeEKVIYLHLCDVFVFPSvlRSEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVVPPKDPDALAEA 323
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2226658501 297 IQTLHQNPTLKTQFSERNKARIAADFTMANMI 328
Cdd:cd03795   324 IDKLLSDEELRESYGENAKKRFEELFTAEKMK 355
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
141-335 2.43e-09

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: 58.10  E-value: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 141 LDDFTPSATGTQPIFNDTNAIKLILVANIKPVKRTLDAVNAVAALHAQGIAVELALVGEPQDSAYVAS-IHNHI-AAQQL 218
Cdd:cd03792   178 LSPADIRYYLEKPFVIDPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGAVDDPEGSvVYEEVmEYAGD 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 219 ASHIHWL---GSVNEPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDvaELAQ 295
Cdd:cd03792   258 DHDIHVLrlpPSDQEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVE--GAAV 335
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2226658501 296 AIQTLHQNPTLKTQFSERNKARIAADFTmanmIAKHLAAY 335
Cdd:cd03792   336 RILRLLTDPELRRKMGLAAREHVRDNFL----ITGNLRAW 371
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
1-330 4.19e-09

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: 57.45  E-value: 4.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501   1 MCQQGHRVKLVVLrhtpfteTLTSFPCPIVDLDIHH-VARPKTLQTLLR--FR-RQLIQD-QVDVLHAWLPESCLLA--- 72
Cdd:cd04951    25 MFIRGHDVNIVYL-------TGEVEVKPLNNNIIIYnLGMDKNPRSLLKalLKlKKIISAfKPDVVHSHMFHANIFArfl 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  73 ------PLLLKHARLKVITSRRDMgliyrgkpaWLYRMVRRRTDTVISNSRAVAQHVSQQERLPATQSKVIYNG--LDDF 144
Cdd:cd04951    98 rmlypiPLLICTAHNKNEGGRIRM---------FIYRLTDFLCDITTNVSREALDEFIAKKAFSKNKSVPVYNGidLNKF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 145 TPSATGTQPI---FNDTNAIKLIL-VANIKPVKRTLDAVNAVAALHAQGIAVELALVGepqDSAYVASIHNHIAAQQLAS 220
Cdd:cd04951   169 KKDINVRLKIrnkLNLKNDEFVILnVGRLTEAKDYPNLLLAISELILSKNDFKLLIAG---DGPLRNELERLICNLNLVD 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 221 HIHWLGSVNEPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQhQHNgMLIEKGDVAELAQAI-QT 299
Cdd:cd04951   246 RVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVG-DHN-YVVPVSDPQLLAEKIkEI 323
                         330       340       350
                  ....*....|....*....|....*....|.
gi 2226658501 300 LHQNPTLKTQFSERNKARiAADFTMaNMIAK 330
Cdd:cd04951   324 FDMSDEERDILGNKNEYI-AKNFSI-NTIVN 352
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
240-326 1.04e-07

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 49.14  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 240 IGLLVSES-EGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEkgDVAELAQAIQTLHQNPTLKTQFSERNKARI 318
Cdd:pfam13524   1 IVLNPSRRpDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERV 78

                  ....*...
gi 2226658501 319 AADFTMAN 326
Cdd:pfam13524  79 LAEHTYAH 86
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
52-339 5.61e-07

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 51.24  E-value: 5.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  52 QLIQDQVDVLHAWLPESCLLAPLllkhARLKVITSRRDMGLiyRGKPAwlyrMVRRRTDT-----------------VIS 114
Cdd:PRK15490  275 HLCERKLDYLSVWQDGACLMIAL----AALIAGVPRIQLGL--RGLPP----VVRKRLFKpeyeplyqalavvpgvdFMS 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 115 NSRAVAQHVSQQERLPATQSKVIYNGL--DDFTPSATGTQPIFNDTNAIKLILVANIKPVKRTLDAVNAVAALH------ 186
Cdd:PRK15490  345 NNHCVTRHYADWLKLEAKHFQVVYNGVlpPSTEPSSEVPHKIWQQFTQKTQDADTTIGGVFRFVGDKNPFAWIDfaaryl 424
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 187 AQGIAVELALVGepqDSAYVASIHNHIAAQQLASHIHWLGSVNEPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVA 266
Cdd:PRK15490  425 QHHPATRFVLVG---DGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVIS 501
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2226658501 267 TRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNPTL---KTQFSERNKARIAADFTMANMIAKHLAAYDQAP 339
Cdd:PRK15490  502 TPAGGSAECFIEGVSGFILDDAQTVNLDQACRYAEKLVNLwrsRTGICQQTQSFLQERFTVEHMVGTFVKTIASQP 577
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
58-335 6.03e-07

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 50.85  E-value: 6.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  58 VDVLHAWLPES-----CLLAPL-LLKHARLKVITSRRD-MGLIYRGK--PAWLYRMVRRRTdtvisnsrAVAQHVSQQER 128
Cdd:cd03822    76 PDVVHIQHEFGifggkYGLYALgLLLHLRIPVITTLHTvLDLSDPGKqaLKVLFRIATLSE--------RVVVMAPISRF 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 129 L-------PATQSKVIYNG-LDDFTPSATGTQPIFNDTNAIKLILVANIKPVKRTLDAVNAVAALHAQGIAVELALVGEP 200
Cdd:cd03822   148 LlvrikliPAVNIEVIPHGvPEVPQDPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGEL 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 201 QDS-AYVASIHNHIAAQQ---LASHIHWlgsvnePRQLLSQADIGLLVSES-----------EGLSNTLMEYMQAGLPVV 265
Cdd:cd03822   228 HPSlARYEGERYRKAAIEelgLQDHVDF------HNNFLPEEEVPRYISAAdvvvlpylnteQSSSGTLSYAIACGKPVI 301
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 266 ATRVGGNPELIqHQHNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSERNkARIAADFTMANMIAKHLAAY 335
Cdd:cd03822   302 STPLRHAEELL-ADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERA-YAYARAMTWESIADRYLRLF 369
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
166-335 1.58e-06

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 49.54  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 166 VANIKPVKRTLDAVNAVAAL--HAQGiavelALVG-EPQDSAYVASIHNHIAAQQLASHIHWLG--SVNEprqLLSQADI 240
Cdd:NF038011  315 VVPIKDIKTFIRAMRTVVRAmpEAEG-----WIVGpEEEDPAYAAECRSLVASLGLQDKVKFLGfqKIDD---LLPQVGL 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 241 GLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQ--------HNGMLIEKGDVAELAQAIQTLHQNPTLKTQFSE 312
Cdd:NF038011  387 MVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQLIEGLdeedralgAAGEVVAIADPQALARAALDLLRDPQRWQAAQA 466
                         170       180
                  ....*....|....*....|...
gi 2226658501 313 RNKARIAADFTMANMIAKHLAAY 335
Cdd:NF038011  467 AGLARVERYYTEELMFDRYRELY 489
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
135-265 2.32e-06

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: 48.82  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 135 KVIYNGLDDftpsatgTQPIFNDT------------NAIKLILVANIKPVKRTLDAVNAVAALHAQGIAVELALVGEPQD 202
Cdd:cd03812   161 KVIPNGIDI-------EKYKFNKEkrrkrrkllileDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGEL 233
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2226658501 203 sayVASIHNHIAAQQLASHIHWLGSVNEPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVV 265
Cdd:cd03812   234 ---KEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCL 293
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
222-333 5.30e-06

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


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 47.74  E-value: 5.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 222 IHWLGSVN--EPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQT 299
Cdd:cd03818   283 VHFVGKVPydQYVRLLQLSDAHVYLTYPFVLSWSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLE 362
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2226658501 300 LHQNPTLKTQFSERNKARIAADFTMANMIAKHLA 333
Cdd:cd03818   363 LLEDPDRAAALRRAARRTVERSDSLDVCLARYLA 396
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
99-275 7.72e-06

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: 47.22  E-value: 7.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  99 AWLYRMVRRRTDTVISNSRAVAQHVSQQERLPaTQSKVIYN--GLDDFTPSatgtqPIFNDTNAIKLILVANIKPVKR-- 174
Cdd:cd03806   180 AFLYGLAGSFADVVMVNSTWTYNHIRQLWKRN-IKPSIVYPpcDTEELTKL-----PIDEKTRENQILSIAQFRPEKNhp 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 175 -TLDAVNAVAALHAQGI--AVELALVG---EPQDSAYVASIHNHIAAQQLASHIHWlgSVNEP----RQLLSQADIGLLV 244
Cdd:cd03806   254 lQLRAFAELLKRLPESIrsNPKLVLIGscrNEEDKERVEALKLLAKELILEDSVEF--VVDAPyeelKELLSTASIGLHT 331
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2226658501 245 SESEGLSNTLMEYMQAGLPVVATRVGGnPEL 275
Cdd:cd03806   332 MWNEHFGIGVVEYMAAGLIPLAHASAG-PLL 361
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
87-304 8.19e-06

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: 47.28  E-value: 8.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  87 RRDMGLIyRGKPAWLYRMV-----------RRRTDTVISNSRAVAQHVSQQERLPATqskVIYN--GLDDFTPSATGtqp 153
Cdd:cd03804   126 LAESGLG-KGIKSLLASLFlhylrlwdvrtAQRVDLFIANSQFVARRIKKFYGREST---VIYPpvDTDAFAPAADK--- 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 154 ifNDTNAIKLILVanikPVKRTLDAVNAVAALhaqgiAVELALVGEPQDSAYVASIhnhiaaqqLASHIHWLG--SVNEP 231
Cdd:cd03804   199 --EDYYLTASRLV----PYKRIDLAVEAFNEL-----PKRLVVIGDGPDLDRLRAM--------ASPNVEFLGyqPDEVL 259
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2226658501 232 RQLLSQADIGLLVSEsEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTLHQNP 304
Cdd:cd03804   260 KELLSKARAFVFAAE-EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEFEQNF 331
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
136-298 2.84e-05

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 45.47  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 136 VIYNglddftPSATGTQ--PIFNDTNAIKLILVANIK--PVKRTLDAVNAVAALHAQgiaVELALVGEPQDSAYVASIhn 211
Cdd:PRK09922  160 VIYN------PVEIKTIiiPPPERDKPAVFLYVGRLKfeGQKNVKELFDGLSQTTGE---WQLHIIGDGSDFEKCKAY-- 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 212 hiaAQQL--ASHIHWLGSVNEPRQLLSQaDIG-----LLVSESEGLSNTLMEYMQAGLPVVATRVGGNPE-LIQHQHNGM 283
Cdd:PRK09922  229 ---SRELgiEQRIIWHGWQSQPWEVVQQ-KIKnvsalLLTSKFEGFPMTLLEAMSYGIPCISSDCMSGPRdIIKPGLNGE 304
                         170
                  ....*....|....*
gi 2226658501 284 LIEKGDVAELAQAIQ 298
Cdd:PRK09922  305 LYTPGNIDEFVGKLN 319
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
218-327 4.87e-05

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: 44.89  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 218 LASHIHWLGSVN--EPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKgDVAELAQ 295
Cdd:cd03805   278 VEDQVLFLRSISdsQKEQLLSSALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TPEAFAE 356
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2226658501 296 AIQTLHQNPTLKTQFSERNKARIAADFTMANM 327
Cdd:cd03805   357 AMLKLANDPDLADRMGAAGRKRVKEKFSREAF 388
GT4_TuaH-like cd04950
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this ...
107-298 8.48e-05

teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. 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.


Pssm-ID: 340856 [Multi-domain]  Cd Length: 373  Bit Score: 43.90  E-value: 8.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 107 RRTDTVISNSRAVaqhvsQQERLPATQSKVIY-NGLD--DF--TPSATGTQPIFNDTNAIKLILVANIKPvKRTLDAVNA 181
Cdd:cd04950   152 KRADVVFTTSPAL-----YEAKRPLHENVHPIpNGVDveHFaaARQPLDDPIDLREIPGPVLGFFGAIDE-KLDFDLIEE 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 182 VAALHAQgiaVELALVGePQDSAYVASIHNHiaaqqlaSHIHWLGSV--NEPRQLLSQADIGLLVSESEGLSNT-----L 254
Cdd:cd04950   226 LAKARPQ---WNFVFIG-PVVKIDPSSLPRA-------PNIHWLGPKpyKELPAYLAGFDVALLPFALNEYTRFisplkL 294
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2226658501 255 MEYMQAGLPVVATRVggnPELIQHQHNGMLIEKgDVAELAQAIQ 298
Cdd:cd04950   295 FEYLAAGKPVVATSI---PSVVRFYGEAVLCGD-DPDEFSAAIE 334
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
225-316 1.07e-04

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 43.77  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 225 LGSV--NEPRQLLSQADIGLLVSESEGLSNTLMEYMQAGLPVVATRVGGNPELIQHqhnGMLI-----EKGDVAELAQAI 297
Cdd:cd03796   255 LGAVphEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPP---DMILlaepdPEDIVRKLEEAI 331
                          90
                  ....*....|....*....
gi 2226658501 298 QTLHQNPTLKTQFSERNKA 316
Cdd:cd03796   332 SILRTGKHDPWSFHNRVKK 350
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
126-306 3.42e-04

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 42.08  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 126 QERLPATQSKVIYNGLDDFTPSATGTQPIFNDTN---AIKLILVAN-IKPVKRTLDAVNAVAALHAQGIAVELALVGEPQ 201
Cdd:PRK15484  155 EERLPNADISIVPNGFCLETYQSNPQPNLRQQLNispDETVLLYAGrISPDKGILLLMQAFEKLATAHSNLKLVVVGDPT 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 202 DS------AYVASIHNhiAAQQLASHIHWLGSVnEPRQL---LSQADIGLLVSE-SEGLSNTLMEYMQAGLPVVATRVGG 271
Cdd:PRK15484  235 ASskgekaAYQKKVLE--AAKRIGDRCIMLGGQ-PPEKMhnyYPLADLVVVPSQvEEAFCMVAVEAMAAGKPVLASTKGG 311
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2226658501 272 NPELIQHQHNGM-LIEKGDVAELAQAIQTLHQNPTL 306
Cdd:PRK15484  312 ITEFVLEGITGYhLAEPMTSDSIISDINRTLADPEL 347
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
253-300 3.03e-03

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 39.76  E-value: 3.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2226658501  253 TLMEYMQAGLPVVATRVGGNPELIQHQHNGMLIEKGDVAELAQAIQTL 300
Cdd:TIGR02468  587 TLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALLKL 634
PLN02275 PLN02275
transferase, transferring glycosyl groups
200-294 7.41e-03

transferase, transferring glycosyl groups


Pssm-ID: 215155 [Multi-domain]  Cd Length: 371  Bit Score: 38.12  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 200 PQDSAYVASIH----NHIAAQQLashihWLGSVNEPRqLLSQADIGL-LVSESEGLS--NTLMEYMQAGLPVVATRVGGN 272
Cdd:PLN02275  271 PQKAMYEEKISrlnlRHVAFRTM-----WLEAEDYPL-LLGSADLGVsLHTSSSGLDlpMKVVDMFGCGLPVCAVSYSCI 344
                          90       100
                  ....*....|....*....|..
gi 2226658501 273 PELIQHQHNGMLIEKGDvaELA 294
Cdd:PLN02275  345 GELVKDGKNGLLFSSSS--ELA 364
PLN02949 PLN02949
transferase, transferring glycosyl groups
92-317 9.16e-03

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 37.79  E-value: 9.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501  92 LIYRGKPAWLYRMVRRRTDTVISNSRAVAQHVSQQERLPATqSKVIY-----NGLDDFtpsatgtqPIFNDTNAIKLILV 166
Cdd:PLN02949  204 ILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPER-IKRVYppcdtSGLQAL--------PLERSEDPPYIISV 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 167 ANIKPVKR---TLDAVN-AVAALHAQGIAVELALVG---EPQDSAYVASIHNHIAAQQLASHI--HWLGSVNEPRQLLSQ 237
Cdd:PLN02949  275 AQFRPEKAhalQLEAFAlALEKLDADVPRPKLQFVGscrNKEDEERLQKLKDRAKELGLDGDVefHKNVSYRDLVRLLGG 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2226658501 238 ADIGL--LVSESEGLSntLMEYMQAG-LPVVATRVGGNPELIQHQHN---GMLIEkgDVAELAQAI-QTLHQNPTLKTQF 310
Cdd:PLN02949  355 AVAGLhsMIDEHFGIS--VVEYMAAGaVPIAHNSAGPKMDIVLDEDGqqtGFLAT--TVEEYADAIlEVLRMRETERLEI 430

                  ....*..
gi 2226658501 311 SERNKAR 317
Cdd:PLN02949  431 AAAARKR 437
 
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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