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Conserved domains on  [gi|579108048|gb|EUR56896|]
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accessory Sec system glycosylation protein GtfA [Staphylococcus aureus M0008]

Protein Classification

TIGR02918 family protein( domain architecture ID 11495636)

TIGR02918 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TIGR02918 TIGR02918
accessory Sec system glycosylation protein GtfA; Members of this protein family are found only ...
1-499 0e+00

accessory Sec system glycosylation protein GtfA; Members of this protein family are found only in Gram-positive bacteria of the Firmicutes lineage, including several species of Staphylococcus, Streptococcus, and Lactobacillus. Members are associated with glycosylation of serine-rich glycoproteins exported by the accessory Sec system. [Protein fate, Protein modification and repair]


:

Pssm-ID: 131964  Cd Length: 500  Bit Score: 927.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048    1 MTIYNINFGIGWASSGVEYAQAYRAKLLRRTNQDTKFVFLDFIQSENIQTLTQNIGFKDQEVIWLYQYFSDISLAPTTYT 80
Cdd:TIGR02918   1 MTIYNINFGIGWASSGVEYAQAYRAQLFRKLNIEAKFIFLDFIQNENIQTLTANIGFKDDEIIWLYQYFTDIKIAPTTYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048   81 LDDIERELGHDISFRERNGKIVRLYFNGKSSFVTCYLQNEQKDIVDRAEFVINSMLVRKDFYSYTRIFSEYYAPADNKAK 160
Cdd:TIGR02918  81 VDDLEKELGLEITRREKNGKVLRLFFNNQSNFVTCYLKNENKDIVDRAEYVSNGKLIRKDFYSYTRYFSEYYAPADNKAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  161 LYMRQFYNQDGSIAYNEYIDGDSSIYVFEDAVLYNKTEFIAYFLQRLNLTRDDIVILDRASDIGQAVLQHKGDSKVGVVI 240
Cdd:TIGR02918 161 LYQRTFYNEDGSIAYDEYIDGKESVFVFKDKILYSKQEFIAYFLKQLNLTKSDIVILDRSTGIGQAVLENKGPAKLGVVV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  241 HADHYSNNMMSEQHILWNNYYEYQFSKAKYIDFFITATDIQNHMVCRQFEQYQGYRPRVYTIPVGSIDALSYPTLSRKPY 320
Cdd:TIGR02918 241 HAEHYSENATNETYILWNNYYEYQFSNADYIDFFITATDIQNQILQEQFKKYTNIEPKIYTIPVGSLDSLQYPEQERKPF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  321 AMISASRLANEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRKIIDTHRAQDYIRLLGHVKLDEIYNDYELFLSAS 400
Cdd:TIGR02918 321 SIITASRLAKEKHIDWLVKAVVKAKKSLPELTFDIYGEGGEKSKLRKIIAENQAEDYIQLKGHRNLSEIYKDYELYLSAS 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  401 TSEGFGLTLMEAVGSGLGMIGLNVNYGNPTFIRDGENGYLVPFDTDEDSVDDVIAKLAHAIVMYFN-NGPQTPHDISYEV 479
Cdd:TIGR02918 401 TSEGFGLTLMEAIGSGLGMIGFDVNYGNPTFIEDGQNGYLIPIDEEEDDEDQIITALAEKIVEYFNeNDLDAMHEYSYQI 480
                         490       500
                  ....*....|....*....|
gi 579108048  480 AQQFMTQDIILKWETLVQEV 499
Cdd:TIGR02918 481 AEGFLTKEIIEKWKKLVEEV 500
 
Name Accession Description Interval E-value
TIGR02918 TIGR02918
accessory Sec system glycosylation protein GtfA; Members of this protein family are found only ...
1-499 0e+00

accessory Sec system glycosylation protein GtfA; Members of this protein family are found only in Gram-positive bacteria of the Firmicutes lineage, including several species of Staphylococcus, Streptococcus, and Lactobacillus. Members are associated with glycosylation of serine-rich glycoproteins exported by the accessory Sec system. [Protein fate, Protein modification and repair]


Pssm-ID: 131964  Cd Length: 500  Bit Score: 927.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048    1 MTIYNINFGIGWASSGVEYAQAYRAKLLRRTNQDTKFVFLDFIQSENIQTLTQNIGFKDQEVIWLYQYFSDISLAPTTYT 80
Cdd:TIGR02918   1 MTIYNINFGIGWASSGVEYAQAYRAQLFRKLNIEAKFIFLDFIQNENIQTLTANIGFKDDEIIWLYQYFTDIKIAPTTYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048   81 LDDIERELGHDISFRERNGKIVRLYFNGKSSFVTCYLQNEQKDIVDRAEFVINSMLVRKDFYSYTRIFSEYYAPADNKAK 160
Cdd:TIGR02918  81 VDDLEKELGLEITRREKNGKVLRLFFNNQSNFVTCYLKNENKDIVDRAEYVSNGKLIRKDFYSYTRYFSEYYAPADNKAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  161 LYMRQFYNQDGSIAYNEYIDGDSSIYVFEDAVLYNKTEFIAYFLQRLNLTRDDIVILDRASDIGQAVLQHKGDSKVGVVI 240
Cdd:TIGR02918 161 LYQRTFYNEDGSIAYDEYIDGKESVFVFKDKILYSKQEFIAYFLKQLNLTKSDIVILDRSTGIGQAVLENKGPAKLGVVV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  241 HADHYSNNMMSEQHILWNNYYEYQFSKAKYIDFFITATDIQNHMVCRQFEQYQGYRPRVYTIPVGSIDALSYPTLSRKPY 320
Cdd:TIGR02918 241 HAEHYSENATNETYILWNNYYEYQFSNADYIDFFITATDIQNQILQEQFKKYTNIEPKIYTIPVGSLDSLQYPEQERKPF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  321 AMISASRLANEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRKIIDTHRAQDYIRLLGHVKLDEIYNDYELFLSAS 400
Cdd:TIGR02918 321 SIITASRLAKEKHIDWLVKAVVKAKKSLPELTFDIYGEGGEKSKLRKIIAENQAEDYIQLKGHRNLSEIYKDYELYLSAS 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  401 TSEGFGLTLMEAVGSGLGMIGLNVNYGNPTFIRDGENGYLVPFDTDEDSVDDVIAKLAHAIVMYFN-NGPQTPHDISYEV 479
Cdd:TIGR02918 401 TSEGFGLTLMEAIGSGLGMIGFDVNYGNPTFIEDGQNGYLIPIDEEEDDEDQIITALAEKIVEYFNeNDLDAMHEYSYQI 480
                         490       500
                  ....*....|....*....|
gi 579108048  480 AQQFMTQDIILKWETLVQEV 499
Cdd:TIGR02918 481 AEGFLTKEIIEKWKKLVEEV 500
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
195-492 1.77e-109

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: 328.11  E-value: 1.77e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 195 NKTEFIAYFLQRLNLTRDDIVILDRASDIGQAVLQHKGDSKVGVVIHADHYSNNMMSEqHILWNNYYEYQFSKAKYIDFF 274
Cdd:cd04949   39 NEQELFAFFIEQLNLQKGDIFISDRPTLTGQVILNTKGPAKKGAVLHNEHVKNNDDPE-HSLIKNFYKYVFENLNKYDAI 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 275 ITATDIQNHMVCRQFEQYqgyrPRVYTIPVGSIDALSYP--TLSRKPYAMISASRLANEKHIDWLVKAVIVAKRQVPELT 352
Cdd:cd04949  118 IVSTEQQKQDLSERFNKY----PPIFTIPVGYVDQLDTAesNHERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEIT 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 353 FDIYGEGSEKTRLRKIIDTHRAQDYIRLLG-HVKLDEIYNDYELFLSASTSEGFGLTLMEAVGSGLGMIGLNVNYGNPTF 431
Cdd:cd04949  194 LDIYGYGEEREKLKKLIEELHLEDNVFLKGyHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKYGPSEL 273
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579108048 432 IRDGENGYLVPfdtdedsvDDVIAKLAHAIVMYFNN--GPQTPHDISYEVAQQFMTQDIILKW 492
Cdd:cd04949  274 IEDGENGYLIE--------KNNIDALADKIIELLNDpeKLQQFSEESYKIAEKYSTENVMEKW 328
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
318-454 1.56e-21

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: 91.18  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  318 KPYAMISASRLANEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRKIIDTHRAQDYIRLLGHV---KLDEIYNDYE 394
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVsdeDLPELLKIAD 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  395 LFLSASTSEGFGLTLMEAVGSGLGMIGLNVnYGNPTFIRDGENGYLVPFDTDEDSVDDVI 454
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDV-GGPPEVVKDGETGFLVKPNNAEALAEAID 139
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
386-500 1.34e-11

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 61.54  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 386 LDEIYNDYELFLSASTSEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDGENGYLVPFDTDEDsvddviakLAHAIVMYF 465
Cdd:COG0438   14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVG-GLPEVIEDGETGLLVPPGDPEA--------LAEAILRLL 84
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 579108048 466 NNgPQTPHDISYE----VAQQFMTQDIILKWETLVQEVL 500
Cdd:COG0438   85 ED-PELRRRLGEAarerAEERFSWEAIAERLLALYEELL 122
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
322-447 1.89e-03

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 40.85  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 322 MISASRLANEKHIDWLVKAVivakRQVPELTFDIYGEGSEKTRLRKIIDTHRAQdYIRLLGHVKLDEIYNDYELFLSAST 401
Cdd:PLN02871 266 IVYVGRLGAEKNLDFLKRVM----ERLPGARLAFVGDGPYREELEKMFAGTPTV-FTGMLQGDELSQAYASGDVFVMPSE 340
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 579108048 402 SEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRD---GENGYLV-PFDTDE 447
Cdd:PLN02871 341 SETLGFVVLEAMASGVPVVAARAG-GIPDIIPPdqeGKTGFLYtPGDVDD 389
 
Name Accession Description Interval E-value
TIGR02918 TIGR02918
accessory Sec system glycosylation protein GtfA; Members of this protein family are found only ...
1-499 0e+00

accessory Sec system glycosylation protein GtfA; Members of this protein family are found only in Gram-positive bacteria of the Firmicutes lineage, including several species of Staphylococcus, Streptococcus, and Lactobacillus. Members are associated with glycosylation of serine-rich glycoproteins exported by the accessory Sec system. [Protein fate, Protein modification and repair]


Pssm-ID: 131964  Cd Length: 500  Bit Score: 927.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048    1 MTIYNINFGIGWASSGVEYAQAYRAKLLRRTNQDTKFVFLDFIQSENIQTLTQNIGFKDQEVIWLYQYFSDISLAPTTYT 80
Cdd:TIGR02918   1 MTIYNINFGIGWASSGVEYAQAYRAQLFRKLNIEAKFIFLDFIQNENIQTLTANIGFKDDEIIWLYQYFTDIKIAPTTYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048   81 LDDIERELGHDISFRERNGKIVRLYFNGKSSFVTCYLQNEQKDIVDRAEFVINSMLVRKDFYSYTRIFSEYYAPADNKAK 160
Cdd:TIGR02918  81 VDDLEKELGLEITRREKNGKVLRLFFNNQSNFVTCYLKNENKDIVDRAEYVSNGKLIRKDFYSYTRYFSEYYAPADNKAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  161 LYMRQFYNQDGSIAYNEYIDGDSSIYVFEDAVLYNKTEFIAYFLQRLNLTRDDIVILDRASDIGQAVLQHKGDSKVGVVI 240
Cdd:TIGR02918 161 LYQRTFYNEDGSIAYDEYIDGKESVFVFKDKILYSKQEFIAYFLKQLNLTKSDIVILDRSTGIGQAVLENKGPAKLGVVV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  241 HADHYSNNMMSEQHILWNNYYEYQFSKAKYIDFFITATDIQNHMVCRQFEQYQGYRPRVYTIPVGSIDALSYPTLSRKPY 320
Cdd:TIGR02918 241 HAEHYSENATNETYILWNNYYEYQFSNADYIDFFITATDIQNQILQEQFKKYTNIEPKIYTIPVGSLDSLQYPEQERKPF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  321 AMISASRLANEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRKIIDTHRAQDYIRLLGHVKLDEIYNDYELFLSAS 400
Cdd:TIGR02918 321 SIITASRLAKEKHIDWLVKAVVKAKKSLPELTFDIYGEGGEKSKLRKIIAENQAEDYIQLKGHRNLSEIYKDYELYLSAS 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  401 TSEGFGLTLMEAVGSGLGMIGLNVNYGNPTFIRDGENGYLVPFDTDEDSVDDVIAKLAHAIVMYFN-NGPQTPHDISYEV 479
Cdd:TIGR02918 401 TSEGFGLTLMEAIGSGLGMIGFDVNYGNPTFIEDGQNGYLIPIDEEEDDEDQIITALAEKIVEYFNeNDLDAMHEYSYQI 480
                         490       500
                  ....*....|....*....|
gi 579108048  480 AQQFMTQDIILKWETLVQEV 499
Cdd:TIGR02918 481 AEGFLTKEIIEKWKKLVEEV 500
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
195-492 1.77e-109

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: 328.11  E-value: 1.77e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 195 NKTEFIAYFLQRLNLTRDDIVILDRASDIGQAVLQHKGDSKVGVVIHADHYSNNMMSEqHILWNNYYEYQFSKAKYIDFF 274
Cdd:cd04949   39 NEQELFAFFIEQLNLQKGDIFISDRPTLTGQVILNTKGPAKKGAVLHNEHVKNNDDPE-HSLIKNFYKYVFENLNKYDAI 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 275 ITATDIQNHMVCRQFEQYqgyrPRVYTIPVGSIDALSYP--TLSRKPYAMISASRLANEKHIDWLVKAVIVAKRQVPELT 352
Cdd:cd04949  118 IVSTEQQKQDLSERFNKY----PPIFTIPVGYVDQLDTAesNHERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEIT 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 353 FDIYGEGSEKTRLRKIIDTHRAQDYIRLLG-HVKLDEIYNDYELFLSASTSEGFGLTLMEAVGSGLGMIGLNVNYGNPTF 431
Cdd:cd04949  194 LDIYGYGEEREKLKKLIEELHLEDNVFLKGyHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKYGPSEL 273
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579108048 432 IRDGENGYLVPfdtdedsvDDVIAKLAHAIVMYFNN--GPQTPHDISYEVAQQFMTQDIILKW 492
Cdd:cd04949  274 IEDGENGYLIE--------KNNIDALADKIIELLNDpeKLQQFSEESYKIAEKYSTENVMEKW 328
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
203-494 4.07e-28

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: 114.64  E-value: 4.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 203 FLQRLNLTRDDIVILDRASDIG-QAVLQHKgdSKVGVVIHADHYSNNMMSEQHILWNNYYeyqfskaKYIDFFITATDIQ 281
Cdd:cd03820   79 LRKYLKNNKPDVVISFRTSLLTfLALIGLK--SKLIVWEHNNYEAYNKGLRRLLLRRLLY-------KRADKIVVLTEAD 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 282 nhmvcrQFEQYQGYRPRVYTIPvgsiDALSYPtLSRKPYAM-----ISASRLANEKHIDWLVKAVIVAKRQVPELTFDIY 356
Cdd:cd03820  150 ------KLKKYKQPNSNVVVIP----NPLSFP-SEEPSTNLkskriLAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIY 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 357 GEGSEKTRLRKIIDTHRAQDYIRLLGHVK-LDEIYNDYELFLSASTSEGFGLTLMEAVGSGLGMIGLNVNYGNPTFIRDG 435
Cdd:cd03820  219 GDGPEREELEKLIDKLGLEDRVKLLGPTKnIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCPTGPSEIIEDG 298
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579108048 436 ENGYLVPfdtDEDsvddvIAKLAHAIVMYFNNGP--QTPHDISYEVAQQFMTQDIILKWET 494
Cdd:cd03820  299 ENGLLVP---NGD-----VDALAEALLRLMEDEElrKKMGKNARKNAERFSIEKIIKQWEE 351
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
318-454 1.56e-21

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: 91.18  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  318 KPYAMISASRLANEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRKIIDTHRAQDYIRLLGHV---KLDEIYNDYE 394
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVsdeDLPELLKIAD 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  395 LFLSASTSEGFGLTLMEAVGSGLGMIGLNVnYGNPTFIRDGENGYLVPFDTDEDSVDDVI 454
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDV-GGPPEVVKDGETGFLVKPNNAEALAEAID 139
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
147-470 5.32e-21

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: 94.53  E-value: 5.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 147 IFSEYYAPADNKAKLYMRQFYNQ--------------DGSIAYNEYIDGDSSIYVFEDAVLYNKTEFIAYFLQRLNLTRD 212
Cdd:cd03801    4 LLSPELPPPVGGAERHVRELARAlaarghdvtvltpaDPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 213 DIVIL-DRASDIGQAVLQHKGDSKVGVVIH-ADHYSNNMMSEQHILWNNYYEYQFSKAkyiDFFITATDIQ-NHMVcrqf 289
Cdd:cd03801   84 DVVHAhGLLAALLAALLALLLGAPLVVTLHgAEPGRLLLLLAAERRLLARAEALLRRA---DAVIAVSEALrDELR---- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 290 EQYQGYRPRVYTIPVGSIDALSYPTLSRKPYA------MISASRLANEKHIDWLVKAVIVAKRQVPELTFDIYG-EGSEK 362
Cdd:cd03801  157 ALGGIPPEKIVVIPNGVDLERFSPPLRRKLGIppdrpvLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGgDGPLR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 363 TRLRKIIdtHRAQDYIRLLGHVK---LDEIYNDYELFLSASTSEGFGLTLMEAVGSGLGMIGLNVnYGNPTFIRDGENGY 439
Cdd:cd03801  237 AELEELE--LGLGDRVRFLGFVPdeeLPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDV-GGLPEVVEDGEGGL 313
                        330       340       350
                 ....*....|....*....|....*....|.
gi 579108048 440 LVPFDTDEDsvddviakLAHAIVMYFNNGPQ 470
Cdd:cd03801  314 VVPPDDVEA--------LADALLRLLADPEL 336
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
241-458 1.05e-20

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


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 93.50  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 241 HADHYSNNMMSeqHILWNNYYEYQFSKAKY--IDFFITATdiqnHMVCRQFEQYqGYRPRVYTIPVG----------SID 308
Cdd:cd03817  118 MYEDYLHYIPK--GKLLVKAVVRKLVRRFYnhTDAVIAPS----EKIKDTLREY-GVKGPIEVIPNGidldkfekplNTE 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 309 ALSYPTLSRKPYAMISASRLANEKHIDWLVKAVIVAKRQvPELTFDIYGEGSEKTRLRKIIDTHRAQDYIRLLGHVKLDE 388
Cdd:cd03817  191 ERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKE-PNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREE 269
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579108048 389 IYNDY---ELFLSASTSEGFGLTLMEAVGSGLGMIGLNvNYGNPTFIRDGENGYLvpFDTDEDSVDDVIAKLA 458
Cdd:cd03817  270 LPEYYkaaDLFVFASTTETQGLVYLEAMAAGLPVVAAK-DPAASELVEDGENGFL--FEPNDETLAEKLLHLR 339
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
323-462 1.88e-18

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 81.79  E-value: 1.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048  323 ISASRLA-NEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKtRLRKIIdtHRAQDYIRLLGHVK-LDEIYNDYELFLSAS 400
Cdd:pfam13692   5 LFVGRLHpNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEE-ELEELA--AGLEDRVIFTGFVEdLAELLAAADVFVLPS 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579108048  401 TSEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIrDGENGYLVPFDTDEDsvddviakLAHAIV 462
Cdd:pfam13692  82 LYEGFGLKLLEAMAAGLPVVATDVG-GIPELV-DGENGLLVPPGDPEA--------LAEAIL 133
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
238-441 7.04e-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: 82.84  E-value: 7.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 238 VVIHADHYSNNMMSEQHILWNNYYEYQFSKAKY----IDFFItATDIQNHMVCRQFEQYQGYRPRVYTI--------PVG 305
Cdd:cd01635   18 HVRALARALAALGHEVTVLALLLLALRRILKKLlelkPDVVH-AHSPHAAALAALLAARLLGIPIVVTVhgpdslesTRS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 306 SIDALSYPTLSRKPYAMISASRLANEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRKIIDTHRAQDYIRLLGHV- 384
Cdd:cd01635   97 ELLALARLLVSLPLADKVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLv 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 385 ---KLDEIYNDYELFLSASTSEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDGENGYLV 441
Cdd:cd01635  177 ddeVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVG-GIPEFVVDGENGLLV 235
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
295-499 2.23e-16

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


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 80.89  E-value: 2.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 295 YRPRVYTIPVGsID-ALSYPTLSRKPYA-----MISASRLANEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRKI 368
Cdd:cd03798  171 PRDRVDVIPNG-VDpARFQPEDRGLGLPldafvILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRAL 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 369 IDTHRAQDYIRLLGHVKLDEI---YNDYELFLSASTSEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDGENGYLVPfDT 445
Cdd:cd03798  250 AEDLGLGDRVTFTGRLPHEQVpayYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVG-GIPEVVGDPETGLLVP-PG 327
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 579108048 446 DEDSVDDVIAKLAHAivmyfNNGPQTPHDISYEVAQQFMTQDIILKWETLVQEV 499
Cdd:cd03798  328 DADALAAALRRALAE-----PYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
272-457 2.22e-15

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: 78.05  E-value: 2.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 272 DFFITAT-DIQNHMVcrqfEQYQGYRPRVYTIPVGSIDALSYPT---------LSRKPYAMI--SASRLANEKHIDWLVK 339
Cdd:cd03800  165 DRVIASTpQEADELI----SLYGADPSRINVVPPGVDLERFFPVdraearrarLLLPPDKPVvlALGRLDPRKGIDTLVR 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 340 AV--IVAKRQVPELTF---DIYGEGSEKT-RLRKIIDTHRAQDYIRLLGHVK---LDEIYNDYELFLSASTSEGFGLTLM 410
Cdd:cd03800  241 AFaqLPELRELANLVLvggPSDDPLSMDReELAELAEELGLIDRVRFPGRVSrddLPELYRAADVFVVPSLYEPFGLTAI 320
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 579108048 411 EAVGSGLGMIGLNVNyGNPTFIRDGENGYLVPfDTDEDSVDDVIAKL 457
Cdd:cd03800  321 EAMACGTPVVATAVG-GLQDIVRDGRTGLLVD-PHDPEALAAALRRL 365
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
311-459 4.58e-15

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: 76.48  E-value: 4.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 311 SYPTLSRKPYAMISASRLANEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRKIIDTHRAQDYIRLLGHVK-LDEI 389
Cdd:cd03808  181 SPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFRSdVPEL 260
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 390 YNDYELFLSASTSEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDGENGYLVPFDtDEDSVDDVIAKLAH 459
Cdd:cd03808  261 LAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVP-GCRELVIDGVNGFLVPPG-DVEALADAIEKLIE 328
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
171-461 9.91e-15

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: 75.47  E-value: 9.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 171 GSIAYNEYIDGDSSIYVFEDAVLYNKTEFIAYFLQRL----NLTRDDIVILDRASDIGQAVLQHKGDSKVGVVIHadhys 246
Cdd:cd03811   39 DEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLkrilKRAKPDVVISFLGFATYIVAKLAAARSKVIAWIH----- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 247 nNMMSEQHILWNNYYE--YQFSKAKYIdFFITaTDIQNHMVcrqfEQYQGYRPRVYTIPVGsIDALSYPTLSRKPYA--- 321
Cdd:cd03811  114 -SSLSKLYYLKKKLLLklKLYKKADKI-VCVS-KGIKEDLI----RLGPSPPEKIEVIYNP-IDIDRIRALAKEPILnep 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 322 -----MISASRLANEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRKIIDTHRAQDYIRLLGHVklDEIYNDYE-- 394
Cdd:cd03811  186 edgpvILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKELGLAERVIFLGFQ--SNPYPYLKka 263
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579108048 395 -LFLSASTSEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDGENGYLVPFDtDEDSVDDVIAKLAHAI 461
Cdd:cd03811  264 dLFVLSSRYEGFPNVLLEAMALGTPVVSTDCP-GPREILDDGENGLLVPDG-DAAALAGILAALLQKK 329
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
296-448 1.21e-12

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: 69.28  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 296 RPRVYTIPVGsIDALSYPTLSRKPYA----MISASRLANEKHIDWLVKAVIVAKRQVPELTfdIYGEGSEKtrlrkIIDT 371
Cdd:cd03823  165 SARISVIPNA-VEPDLAPPPRRRPGTerlrFGYIGRLTEEKGIDLLVEAFKRLPREDIELV--IAGHGPLS-----DERQ 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 372 HRAQDYIRLLGHVKLDEIYNDYE----LFLSASTSEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDGENGYLVPFDTDE 447
Cdd:cd03823  237 IEGGRRIAFLGRVPTDDIKDFYEkidvLVVPSIWPEPFGLVVREAIAAGLPVIASDLG-GIAELIQPGVNGLLFAPGDAE 315

                 .
gi 579108048 448 D 448
Cdd:cd03823  316 D 316
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
325-460 1.49e-12

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: 68.92  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 325 ASRLANEKHIDWLVKAVIVAKRQVPeLTFDIYGEGSEKTRLRKIIDTHRAQDYIRLLGHV-KLDEIYNDYELFLSASTSE 403
Cdd:cd03819  188 VGRLSPEKGWLLLVDAAAELKDEPD-FRLLVAGDGPERDEIRRLVERLGLRDRVTFTGFReDVPAALAASDVVVLPSLHE 266
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 579108048 404 GFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDGENGYLVPFDTDEDSVDDVIAKLAHA 460
Cdd:cd03819  267 EFGRVALEAMACGTPVVATDVG-GAREIVVHGRTGLLVPPGDAEALADAIRAAKLLP 322
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
315-459 2.75e-12

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


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 68.11  E-value: 2.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 315 LSRKPYAMISASRLANEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRKIIDTHRAQDYIRLLGHVK-LDEIYNDY 393
Cdd:cd03807  186 LAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERLLLELGLEDRVHLLGERSdVPALLPAM 265
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579108048 394 ELFLSASTSEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDGeNGYLVPFDtDEDSVDDVIAKLAH 459
Cdd:cd03807  266 DIFVLSSRTEGFPNALLEAMACGLPVVATDVG-GAAELVDDG-TGFLVPAG-DPQALADAIRALLE 328
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
386-500 1.34e-11

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 61.54  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 386 LDEIYNDYELFLSASTSEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDGENGYLVPFDTDEDsvddviakLAHAIVMYF 465
Cdd:COG0438   14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVG-GLPEVIEDGETGLLVPPGDPEA--------LAEAILRLL 84
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 579108048 466 NNgPQTPHDISYE----VAQQFMTQDIILKWETLVQEVL 500
Cdd:COG0438   85 ED-PELRRRLGEAarerAEERFSWEAIAERLLALYEELL 122
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
357-461 1.67e-11

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: 65.84  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 357 GEGSEKTRLRKIIDTHRAQDYIRLLGHV-KLDEIYNDYELFLSASTSEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDG 435
Cdd:cd04962  233 GDGPERVPAEELARELGVEDRVLFLGKQdDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAG-GIPEVVKHG 311
                         90       100
                 ....*....|....*....|....*.
gi 579108048 436 ENGYLVPfdtdedsVDDVIAKLAHAI 461
Cdd:cd04962  312 ETGFLSD-------VGDVDAMAKSAL 330
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
322-461 9.55e-11

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: 63.24  E-value: 9.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 322 MISASRLANEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRKIIDTHRAQDYIRLLGHVKLDEI--YNDY-ELFLS 398
Cdd:cd03799  177 ILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIieILDEaDIFIA 256
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579108048 399 ASTS------EGFGLTLMEAVGSGLGMIGlNVNYGNPTFIRDGENGYLVPfdtdEDSVDDVIAKLAHAI 461
Cdd:cd03799  257 PSVTaadgdqDGPPNTLKEAMAMGLPVIS-TEHGGIPELVEDGVSGFLVP----ERDAEAIAEKLTYLI 320
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
298-500 1.74e-10

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: 62.64  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 298 RVYTIP--VGSIDALSYPTLSRKPYAMI-SASRLANEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRKIIDTHRA 374
Cdd:cd03796  169 IVSVIPnaVDSSDFTPDPSKPDPNKITIvVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMREKYQL 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 375 QDYIRLLG---HVKLDEIYNDYELFLSASTSEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDGENGYLVPfdtdedSVD 451
Cdd:cd03796  249 QDRVELLGavpHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVG-GIPEVLPPDMILLAEP------DPE 321
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 579108048 452 DVIAKLAHAIVMYFNNGPQtPHDISYEVAQQFMTQDIILKWETLVQEVL 500
Cdd:cd03796  322 DIVRKLEEAISILRTGKHD-PWSFHNRVKKMYSWEDVARRTEKVYDRIL 369
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
325-459 1.66e-09

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: 59.62  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 325 ASRLANEKHIDWLVKAVIVAKRQVPeLTFDIYGEGSEKTRLRKII-DTHraqdYIRLLGHVKLDEIYNDYELFLSASTSE 403
Cdd:cd03814  204 VGRLAPEKNLEALLDADLPLAASPP-VRLVVVGDGPARAELEARGpDVI----FTGFLTGEELARAYASADVFVFPSRTE 278
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 579108048 404 GFGLTLMEAVGSGLGMIGlnVNYGNPT-FIRDGENGYLVPfDTDEDSVDDVIAKLAH 459
Cdd:cd03814  279 TFGLVVLEAMASGLPVVA--ADAGGPRdIVRPGGTGALVE-PGDAAAFAAALRALLE 332
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
290-457 6.29e-09

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: 57.67  E-value: 6.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 290 EQYQGYRPRVYTIPVGsIDALSY--PTLSR--------KPYAMISASRLANEKHIDWLVKAvivAKRQVPELTfdIYGEG 359
Cdd:cd03795  153 PTLREFKNKVRVIPLG-IDKNVYniPRVDFenikrekkGKKIFLFIGRLVYYKGLDYLIEA---AQYLNYPIV--IGGEG 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 360 SEKTRLRKIIDTHRaQDYIRLLGHVKLDEIYNDYEL-----FLSASTSEGFGLTLMEAVGSGLGMIGLNVNYGNPTFIRD 434
Cdd:cd03795  227 PLKPDLEAQIELNL-LDNVKFLGRVDDEEKVIYLHLcdvfvFPSVLRSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNN 305
                        170       180
                 ....*....|....*....|...
gi 579108048 435 GENGYLVPfDTDEDSVDDVIAKL 457
Cdd:cd03795  306 GETGLVVP-PKDPDALAEAIDKL 327
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
290-453 2.62e-08

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: 55.93  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 290 EQYQGYRPRVYTIPVGSIDA--LSYPTLSRKPYaMISASRLANEKHIDWLVKAV--IVAKRQVPELTFDIYGEGSEKTRL 365
Cdd:cd04946  194 KCYPAYKEKIFVSRLGVSDKeqYSKVKKEGDLR-LVSCSSIVPVKRIDLIIETLnsLCVAHPSICISWTHIGGGPLKERL 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 366 RKIIDTHRAQDYIRLLGHVKLDEIY-----NDYELFLSASTSEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDGENGYL 440
Cdd:cd04946  273 EKLAENKLENVKVNFTGEVSNKEVKqlykeNDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVG-GTREIVENETNGLL 351
                        170
                 ....*....|....
gi 579108048 441 VPFD-TDEDSVDDV 453
Cdd:cd04946  352 LDKDpTPNEIVSSI 365
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
254-417 5.25e-07

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: 51.60  E-value: 5.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 254 HILWNNYYEYQFSKAKYIDFFITATDIQNHMVCRQFeqyqGYRPRVYTIPVGSI---------DALSYPTLSRKPYaMIS 324
Cdd:cd03821  135 HWKKRIALHLIERRNLNNAALVHFTSEQEADELRRF----GLEPPIAVIPNGVDipefdpglrDRRKHNGLEDRRI-ILF 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 325 ASRLANEKHIDWLVKAV--IVAKRQVPELTFDIYGEGSEkTRLRKIIDTHRAQDYIRLLGHV---KLDEIYNDYELFLSA 399
Cdd:cd03821  210 LGRIHPKKGLDLLIRAArkLAEQGRDWHLVIAGPDDGAY-PAFLQLQSSLGLGDRVTFTGPLygeAKWALYASADLFVLP 288
                        170
                 ....*....|....*...
gi 579108048 400 STSEGFGLTLMEAVGSGL 417
Cdd:cd03821  289 SYSENFGNVVAEALACGL 306
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
298-442 1.39e-06

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: 50.53  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 298 RVYTIPVGSIDALSYPTLSRKPYAMI-SASRLANEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRkiiDTHRAQD 376
Cdd:cd05844  167 RIHVHYIGIDPAKFAPRDPAERAPTIlFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQ---ALAAALG 243
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579108048 377 YIRLLG---HVKLDEIYNDYELFLSAST------SEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDGENGYLVP 442
Cdd:cd05844  244 RVRFLGalpHAEVQDWMRRAEIFCLPSVtaasgdSEGLGIVLLEAAACGVPVVSSRHG-GIPEAILDGETGFLVP 317
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
332-420 3.28e-06

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: 49.28  E-value: 3.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 332 KHIDWLVKAVIVAKRQVPELTFDIYGE-GSEKTRLRKIIDTHRAQDYIRLLGHV---KLDEIYNDYELFLSASTSEGFGL 407
Cdd:cd03809  205 KNHERLLKAFALLKKQGGDLKLVIVGGkGWEDEELLDLVKKLGLGGRVRFLGYVsdeDLPALYRGARAFVFPSLYEGFGL 284
                         90
                 ....*....|...
gi 579108048 408 TLMEAVGSGLGMI 420
Cdd:cd03809  285 PVLEAMACGTPVI 297
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
384-461 4.59e-06

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: 48.87  E-value: 4.59e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579108048 384 VKLDEIYNDYELFLSASTSEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDGENGYLV-PFDTDEdsvddviakLAHAI 461
Cdd:cd03825  255 EQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTG-GSPEIVQHGVTGYLVpPGDVQA---------LAEAI 323
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
197-442 6.70e-06

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: 48.47  E-value: 6.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 197 TEFIAYFL-QRLNLTRD-------DIVILDRASDIGQAVLQHKGDSKVGVVIHADhYSNNMMSEQHILWNnyyeYQFSKA 268
Cdd:cd03792   65 EDKEIYLEwIEENASRYplldgdaDVVVIHDPQPALLPKIKKKRDRKWIWRCHID-ISTPLTEPQPRVWD----FLWNYI 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 269 KYIDFFITatdiqnHMVcrQFEQYQGYRPRVYtIPVgSIDALSY------PTLSR------------KPYaMISASRLAN 330
Cdd:cd03792  140 EGYDLFVF------HPP--EFVPPQVPPPKFY-IPP-SIDPLSGknkdlsPADIRyylekpfvidpeRPY-ILQVARFDP 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 331 EKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRKII--DTHRAQDYIRLLgHVkLDEIYNDYEL--FLSA------- 399
Cdd:cd03792  209 SKDPLGVIDAYKLFKRRAEEPQLVICGHGAVDDPEGSVVyeEVMEYAGDDHDI-HV-LRLPPSDQEInaLQRAatvvlql 286
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 579108048 400 STSEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRDGENGYLVP 442
Cdd:cd03792  287 STREGFGLTVSEALWKGKPVIATPAG-GIPLQVIDGETGFLVN 328
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
322-423 5.86e-04

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: 42.05  E-value: 5.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 322 MISASRLANEKHIDWLVKAVIVAKRQVPELTFDIYGEGSEKTRLRKIIDTHRAQDYIRLLG-HVKLDEIYNDYELFLSAS 400
Cdd:cd04951  191 ILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDGPLRNELERLICNLNLVDRVILLGqISNISEYYNAADLFVLSS 270
                         90       100
                 ....*....|....*....|...
gi 579108048 401 TSEGFGLTLMEAVGSGLGMIGLN 423
Cdd:cd04951  271 EWEGFGLVVAEAMACERPVVATD 293
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
357-417 1.63e-03

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


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 40.74  E-value: 1.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579108048 357 GEGSEKTRLRKIIDTHRAQDYIRLLGHVK-LDEIYNDYELFLSASTSEGFGLTLMEAVGSGL 417
Cdd:cd03812  229 GEGELKEKIKEKVKELGLEDKVIFLGFRNdVSEILSAMDVFLFPSLYEGLPLVAVEAQASGL 290
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
322-447 1.89e-03

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 40.85  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 322 MISASRLANEKHIDWLVKAVivakRQVPELTFDIYGEGSEKTRLRKIIDTHRAQdYIRLLGHVKLDEIYNDYELFLSAST 401
Cdd:PLN02871 266 IVYVGRLGAEKNLDFLKRVM----ERLPGARLAFVGDGPYREELEKMFAGTPTV-FTGMLQGDELSQAYASGDVFVMPSE 340
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 579108048 402 SEGFGLTLMEAVGSGLGMIGLNVNyGNPTFIRD---GENGYLV-PFDTDE 447
Cdd:PLN02871 341 SETLGFVVLEAMASGVPVVAARAG-GIPDIIPPdqeGKTGFLYtPGDVDD 389
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
389-458 6.62e-03

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: 38.88  E-value: 6.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 389 IYNDYELFLSAStsegfgltLMEAVGSGLGMIGLNVNyGNPTFIRDGENGYLVPFDTDEDSVDDVIAKLA 458
Cdd:cd03818  305 VYLTYPFVLSWS--------LLEAMACGCPVIGSDTA-PVREVIRDGRNGLLVDFFDPDALAAAVLELLE 365
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
246-424 9.36e-03

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: 38.47  E-value: 9.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 246 SNNMMSEQHILWNNYYeYQFSKAKYIdffiTATDI-----QNhmvcRQFEQYQGYRP-RVYTIPVGsIDALSYPTLSRK- 318
Cdd:cd03813  219 STWIMGYIKKLWIRFF-ERLGKLAYQ----QADKIislyeGN----RRRQIRLGADPdKTRVIPNG-IDIQRFAPAREEr 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579108048 319 ----PYAMISASRLANEKHIDWLVKAVIVAKRQVPELTFDIYG--EGSEK--TRLRKIIDTHRAQDYIRLLGHVKLDEIY 390
Cdd:cd03813  289 pekePPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIGpeDEDPEyaQECKRLVASLGLENKVKFLGFQNIKEYY 368
                        170       180       190
                 ....*....|....*....|....*....|....
gi 579108048 391 NDYELFLSASTSEGFGLTLMEAVGSGLGMIGLNV 424
Cdd:cd03813  369 PKLGLLVLTSISEGQPLVILEAMASGVPVVATDV 402
 
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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