|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
1-370 |
0e+00 |
|
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: 648.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 1 MKIGITCYPSMGGSGIIATELGIKLAERGHEVHFITSNIPFRIRKPLPNMIFHQVEVNQYAVFQYPPYDITLSTKIAEVI 80
Cdd:cd04962 1 MKIGIVCYPSYGGSGVVATELGLELAERGHEVHFISSAIPFRLNLYSGNIFFHEVEVPNYPLFEYPPYTLALASKIVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 81 KEYDLDLLHMHYAVPHAICGILAREMSGKDIKIMTTLHGTDITVLGYDHSLQGAIKFGIEKSDIVTSVSKSLAQETHEII 160
Cdd:cd04962 81 KEHKLDVLHAHYAIPHASCAYLAREILGEKIPIVTTLHGTDITLVGYDPSLQPAVRFSINKSDRVTAVSSSLRQETYELF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 161 ETNKEIIPIYNFVRENEFPTKHNTALKSQFGIAPDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPSKLILLGDGPELVP 240
Cdd:cd04962 161 DVDKDIEVIHNFIDEDVFKRKPAGALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIPAKLLLVGDGPERVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 241 MRQLTKELNVEEDVLFLGKQDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDVG 320
Cdd:cd04962 241 AEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 616541834 321 DCDSASDYAIRLLEDKVLYNKLQKNMLADIAERFGSELITDQYEYYYQKM 370
Cdd:cd04962 321 DVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYYRRL 370
|
|
| thiol_BshA |
TIGR03999 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, ... |
1-371 |
0e+00 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, a glycosyltransferase required for bacillithiol biosynthesis. This enzyme combines UDP-GlcNAc and L-malate to form N-acetyl-alpha-D-glucosaminyl L-malate synthase. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
Pssm-ID: 274914 [Multi-domain] Cd Length: 374 Bit Score: 646.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 1 MKIGITCYPSMGGSGIIATELGIKLAERGHEVHFITSNIPFRIRKPLPNMIFHQVEVNQYAVFQYPPYDITLSTKIAEVI 80
Cdd:TIGR03999 1 MKIGITCYPTYGGSGVVATELGKALAERGHEVHFITSSQPFRLEKFHPNIFFHEVEVNQYPLFQYPPYDLALASKIAEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 81 KEYDLDLLHMHYAVPHAICGILAREMSGK---DIKIMTTLHGTDITVLGYDHSLQGAIKFGIEKSDIVTSVSKSLAQETH 157
Cdd:TIGR03999 81 KEEKLDLLHVHYAIPHAIAAYLARQMLGKegiDIPIVTTLHGTDITLVGADPSFKPAVRFSIEKSDGVTAVSESLKEETY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 158 EIIETNKEIIPIYNFVRENEFPTKHNTALKSQFGIAPDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPSKLILLGDGPE 237
Cdd:TIGR03999 161 ELFDIDKPIEVIPNFVDTDRYRRKNDPALKRKLGAPEDEKVLIHISNFRPVKRVEDVIEVFARVQQEVPAKLLLVGDGPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 238 LVPMRQLTKELNVEEDVLFLGKQDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVV 317
Cdd:TIGR03999 241 RSPAEQLVRELGLTDRVLFLGKQDDVAELLSISDLFLLPSEKESFGLAALEAMACGVPVIASNAGGIPEVVEHGVTGFLC 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 616541834 318 DVGDCDSASDYAIRLLEDKVLYNKLQKNMLADIAERFGSELITDQYEYYYQKML 371
Cdd:TIGR03999 321 DVGDVETMAEYAISLLEDEELLQRFSAAARERAKERFDSEKIVPQYEALYRRLL 374
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
9-368 |
2.45e-60 |
|
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: 198.92 E-value: 2.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 9 PSMGGSGIIATELGIKLAERGHEVHFITSNIPFRIRKPLPnmifHQVEVNQYAVFQYPPYDITLSTKIAEVIKEYDLDLL 88
Cdd:cd03801 11 PPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELE----DGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 89 HMHYAVPHAICGILARemsGKDIKIMTTLHGTDITVLGYDHSLQ----GAIKFGIEKSDIVTSVSKSLAQETHEI-IETN 163
Cdd:cd03801 87 HAHGLLAALLAALLAL---LLGAPLVVTLHGAEPGRLLLLLAAErrllARAEALLRRADAVIAVSEALRDELRALgGIPP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 164 KEIIPIYNFVRENEFPTkhntALKSQFGIAPDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPS-KLILLG-DGPELVPM 241
Cdd:cd03801 164 EKIVVIPNGVDLERFSP----PLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDvRLVIVGgDGPLRAEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 242 RQLtkELNVEEDVLFLGKQDC--VSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDV 319
Cdd:cd03801 240 EEL--ELGLGDRVRFLGFVPDeeLPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPP 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 616541834 320 GDCDSASDYAIRLLEDKVLYNKLQKNMLADIAERFGSELITDQYEYYYQ 368
Cdd:cd03801 318 DDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
5-369 |
1.24e-50 |
|
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: 173.72 E-value: 1.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 5 ITCYP--SMGGSGIIATELGIKLAERGHEVHFITSNIPFRIRKPLPNMIFHQVEVNQYAVFQYPPY--DITLSTKIAE-- 78
Cdd:cd03798 5 TNIYPnaNSPGRGIFVRRQVRALSRRGVDVEVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKprLRLLAPLRAPsl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 79 -----VIKEYDLDLLHMHYAVPHAICGILAREMSGKDIKImtTLHGTDITVLGYDHSLQGAIKFGIEKSDIVTSVSKSLA 153
Cdd:cd03798 85 akllkRRRRGPPDLIHAHFAYPAGFAAALLARLYGVPYVV--TEHGSDINVFPPRSLLRKLLRWALRRAARVIAVSKALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 154 QETHEIIETNKEIIPIYNFVRENEFptkhnTALKSQFGIAPDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPS-KLILL 232
Cdd:cd03798 163 EELVALGVPRDRVDVIPNGVDPARF-----QPEDRGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDvVLLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 233 GDGPELVPMRQLTKELNVEEDVLFLG---KQDcVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIK 309
Cdd:cd03798 238 GDGPLREALRALAEDLGLGDRVTFTGrlpHEQ-VPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVG 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616541834 310 HGETGFVVDVGDCDSASDYAIRLLEDkvlyNKLQKNM---LADIAERFGSELITDQYEYYYQK 369
Cdd:cd03798 317 DPETGLLVPPGDADALAAALRRALAE----PYLRELGeaaRARVAERFSWVKAADRIAAAYRD 375
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
2-370 |
2.57e-44 |
|
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: 157.06 E-value: 2.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 2 KIGI---TCYPSMGGSGIIATELGIKLAERGHEVHFITSNIPfrirKPLPNMIFHQVEVNQYAVFQYPPYDITLSTKIA- 77
Cdd:cd03817 1 KIAIftdTYLPQVNGVATSVRNLARALEKRGHEVYVITPSDP----GAEDEEEVVRYRSFSIPIRKYHRQHIPFPFKKAv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 78 -EVIKEYDLDLLHMHyaVPHAICGILAREMSGKDIKIMTTLHgtditvLGYDHSLQGAIKFGIEKSDIVTSVSKSLAQET 156
Cdd:cd03817 77 iDRIKELGPDIIHTH--TPFSLGKLGLRIARKLKIPIVHTYH------TMYEDYLHYIPKGKLLVKAVVRKLVRRFYNHT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 157 HEII---------------ETNKEIIPiyNFVRENEFPTKHNTALKSQFGIAPDEKVLIHVSNFRQVKRIDTIIETFAKV 221
Cdd:cd03817 149 DAVIapsekikdtlreygvKGPIEVIP--NGIDLDKFEKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 222 RDKIPSKLILLGDGPELVPMRQLTKELNVEEDVLFLG--KQDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGS 299
Cdd:cd03817 227 KKEPNIKLVIVGDGPEREELKELARELGLADKVIFTGfvPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAA 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616541834 300 NAGGIKEVIKHGETGFVVDVGDcDSASDYAIRLLEDKVLYNKLQKNMLAdIAERFGselITDQYEYYYQKM 370
Cdd:cd03817 307 KDPAASELVEDGENGFLFEPND-ETLAEKLLHLRENLELLRKLSKNAEI-SAREFA---FAKSVEKLYEEV 372
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
7-354 |
1.84e-41 |
|
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: 149.05 E-value: 1.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 7 CYPSMGGSGI--IATELGIKLAERGHEVHFITSNIPFRIRKPLPNMIFHQVEVNQYaVFQYPPYDITLSTKIAEVIKEYD 84
Cdd:cd03811 5 VIPSLSGGGAerVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRV-LKLIKLGLLKAILKLKRILKRAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 85 LDLLH-MHYAVPHAICGILARemsgkDIKIMTTLHGtDITVLGYDHSLQGAIKFGIEKSDIVTSVSKSLAQETHEI-IET 162
Cdd:cd03811 84 PDVVIsFLGFATYIVAKLAAA-----RSKVIAWIHS-SLSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLgPSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 163 NKEIIPIYNFVRENEFPtkhNTALKSQFGIAPDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPS-KLILLGDGPELVPM 241
Cdd:cd03811 158 PEKIEVIYNPIDIDRIR---ALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDvKLVILGDGPLREEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 242 RQLTKELNVEEDVLFLGKQDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDVGD 321
Cdd:cd03811 235 EKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGD 314
|
330 340 350
....*....|....*....|....*....|...
gi 616541834 322 cDSASDYAIRLLEDKVLYNKLQKNMLADIAERF 354
Cdd:cd03811 315 -AAALAGILAALLQKKLDAALRERLAKAQEAVF 346
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
195-345 |
8.49e-39 |
|
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: 136.25 E-value: 8.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 195 DEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPS-KLILLGDGPELVPMRQLTKELNVEEDVLFLGKQD--CVSEFYQLSD 271
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNlKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSdeDLPELLKIAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616541834 272 LVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDVGDCDSASDYAIRLLEDKVLYNKLQKN 345
Cdd:pfam00534 81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGEN 154
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
25-364 |
1.36e-38 |
|
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: 141.58 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 25 LAERGHEVHFITSNIPFRIRKPLP-NMIFHQVEVNQYAVFqyPPYDITLSTKIAEVIKEYDLDLLHMHYAVPhAICGILA 103
Cdd:cd03808 23 LVKKGYEVHVIAPDGDKLSDELKElGVKVIDIPILRRGIN--PLKDLKALFKLYKLLKKEKPDIVHCHTPKP-GILGRLA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 104 REMSGKdIKIMTTLHGtditvLGYDHSLQGAIKFG---IEK-----SDIVTSVSKS---LAQETHEIIETNKEIIPiYNF 172
Cdd:cd03808 100 ARLAGV-PKVIYTVHG-----LGFVFTEGKLLRLLyllLEKlallfTDKVIFVNEDdrdLAIKKGIIKKKKTVLIP-GSG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 173 VRENEFPTKHNTALKSQFgiapdekVLIHVSNFRQVKRIDTIIETFAKVRDKIPS-KLILLGDGPELVPMRQLTKELNVE 251
Cdd:cd03808 173 VDLDRFQYSPESLPSEKV-------VFLFVARLLKDKGIDELIEAAKILKKKGPNvRFLLVGDGELENPSEILIEKLGLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 252 EDVLFLGKQDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDVGDCDSASDYAIR 331
Cdd:cd03808 246 GRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADAIEK 325
|
330 340 350
....*....|....*....|....*....|...
gi 616541834 332 LLEDKVLYNKLQKNMLADIAERFGSELITDQYE 364
Cdd:cd03808 326 LIEDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
75-367 |
3.89e-37 |
|
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: 137.45 E-value: 3.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 75 KIAEVIKEYDLDLLHMHYavPHA-ICGILAREMSGKdIKIMTTLHGTDItvLGYDHSLQGAIKFGIEKSDIVT-SVSKSL 152
Cdd:cd03807 70 RLAKLIRKRNPDVVHTWM--YHAdLIGGLAAKLAGG-VKVIWSVRSSNI--PQRLTRLVRKLCLLLSKFSPATvANSSAV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 153 AQETHEIIETNKEIIPIYNFVRENEF-PTKHNTA-LKSQFGIAPDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPS-KL 229
Cdd:cd03807 145 AEFHQEQGYAKNKIVVIYNGIDLFKLsPDDASRArARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDlRL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 230 ILLGDGPELVPMRQLTKELNVEEDVLFLGKQDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIK 309
Cdd:cd03807 225 LLVGRGPERPNLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVD 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 616541834 310 HGeTGFVVDVGDCDSASDYAIRLLEDKVLYNKLQKNMLADIAERFGSELITDQYEYYY 367
Cdd:cd03807 305 DG-TGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLY 361
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
5-354 |
4.25e-34 |
|
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: 129.01 E-value: 4.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 5 ITCYPSMGGSGIIATELGIKLAERGHEVHFITSNipFRIRKPLpnmifhQVEVNQYAVFQYPPYDITLSTK-IAEVIKEY 83
Cdd:cd03819 4 LTPALEIGGAETYILDLARALAERGHRVLVVTAG--GPLLPRL------RQIGIGLPGLKVPLLRALLGNVrLARLIRRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 84 DLDLLHMHYAVPHAICGILARemsGKDIKIMTTLHGTDI-TVLGYDHSLQgAIKFGieksDIVTSVSKSLAQETHEIIET 162
Cdd:cd03819 76 RIDLIHAHSRAPAWLGWLASR---LTGVPLVTTVHGSYLaTYHPKDFALA-VRARG----DRVIAVSELVRDHLIEALGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 163 NKEIIP-IYNFVRENEFPTKHNTALKSQFGIAPDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPSKLILLGDGPELVPM 241
Cdd:cd03819 148 DPERIRvIPNGVDTDRFPPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFRLLVAGDGPERDEI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 242 RQLTKELNVEEDVLFLGKQDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDVGD 321
Cdd:cd03819 228 RRLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGD 307
|
330 340 350
....*....|....*....|....*....|....
gi 616541834 322 CDSASDYAIRLLEDKVLYNKLQKN-MLADIAERF 354
Cdd:cd03819 308 AEALADAIRAAKLLPEAREKLQAAaALTEAVREL 341
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
2-364 |
1.41e-33 |
|
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: 127.74 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 2 KIGItCYPSMGGSGII---ATELGIKLAERGHEVHFITSnipFRIRKPlpnmIFHQV--EVNQYAVFQYPPYDITLSTKI 76
Cdd:cd03820 1 KIAI-VIPSISNAGGAervAINLANHLAKKGYDVTIISL---DSAEKP----PFYELddNIKIKNLGDRKYSHFKLLLKY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 77 AEVIKEydldlLHMHYAV--PHAICGILAREMS-----GKDIKIMTTLHgTDITVLGYDHSLQGAIKFGIEKSDIVTSVS 149
Cdd:cd03820 73 FKKVRR-----LRKYLKNnkPDVVISFRTSLLTflaliGLKSKLIVWEH-NNYEAYNKGLRRLLLRRLLYKRADKIVVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 150 KSLAQETHEIIETNkeIIPIYNFVreNEFPTKHNTALKSqfgiapdeKVLIHVSNFRQVKRIDTIIETFAKVRDKIPS-K 228
Cdd:cd03820 147 EADKLKKYKQPNSN--VVVIPNPL--SFPSEEPSTNLKS--------KRILAVGRLTYQKGFDLLIEAWALIAKKHPDwK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 229 LILLGDGPELVPMRQLTKELNVEEDVLFLGKQDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNA-GGIKEV 307
Cdd:cd03820 215 LRIYGDGPEREELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCpTGPSEI 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 616541834 308 IKHGETGFVVDVGDCDSASDYAIRLLEDKVLYNKLQKNMLADiAERFGSELITDQYE 364
Cdd:cd03820 295 IEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKN-AERFSIEKIIKQWE 350
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
12-364 |
5.55e-28 |
|
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: 113.49 E-value: 5.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 12 GGSGIIATELGIKLAERGHEV-------------------HFITSNIPFRIRKPLPNMifhqvevnqyavfQYPPYDITL 72
Cdd:cd03800 21 GGQNVYVLELARALAELGYQVdiftrrispadpevveiapGARVIRVPAGPPEYLPKE-------------ELWPYLEEF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 73 STKIAEVIKEYDL--DLLHMHYA----VphaicGILAREMSGkdIKIMTTLHGtditvLG---YDHSLQG-----AIKFG 138
Cdd:cd03800 88 ADGLLRFIAREGGryDLIHSHYWdsglV-----GALLARRLG--VPLVHTFHS-----LGrvkYRHLGAQdtyhpSLRIT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 139 IEK-----SDIVTSvskSLAQETHEIIETNK------EIIPiyNFVRENEF-PTKHNTALKSQFGIAPDEKVLIHVSNFR 206
Cdd:cd03800 156 AEEqileaADRVIA---STPQEADELISLYGadpsriNVVP--PGVDLERFfPVDRAEARRARLLLPPDKPVVLALGRLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 207 QVKRIDTIIETFAKVRDKIPSKLILLGDGPELVP-------MRQLTKELNVEEDVLFLG--KQDCVSEFYQLSDLVLLLS 277
Cdd:cd03800 231 PRKGIDTLVRAFAQLPELRELANLVLVGGPSDDPlsmdreeLAELAEELGLIDRVRFPGrvSRDDLPELYRAADVFVVPS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 278 EKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDVGDCDSASDYAIRLLEDKVLYNKLQKNMLADIAERFGSE 357
Cdd:cd03800 311 LYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWE 390
|
....*..
gi 616541834 358 LITDQYE 364
Cdd:cd03800 391 SVADQLL 397
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
196-335 |
8.00e-28 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 106.44 E-value: 8.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 196 EKVLIHVSNF-RQVKRIDTIIETFAKVRDK-IPSKLILLGDGPElvpmRQLTKEL-NVEEDVLFLGKQDCVSEFYQLSDL 272
Cdd:pfam13692 1 RPVILFVGRLhPNVKGVDYLLEAVPLLRKRdNDVRLVIVGDGPE----EELEELAaGLEDRVIFTGFVEDLAELLAAADV 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616541834 273 VLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIkHGETGFVVDVGDCDSASDYAIRLLED 335
Cdd:pfam13692 77 FVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLLED 138
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
266-372 |
1.58e-26 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 102.38 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 266 FYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDVGDCDSASDYAIRLLEDKVLYNKLQKN 345
Cdd:COG0438 17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96
|
90 100
....*....|....*....|....*..
gi 616541834 346 MLADIAERFGSELITDQYEYYYQKMLN 372
Cdd:COG0438 97 ARERAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
10-369 |
6.02e-26 |
|
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: 107.15 E-value: 6.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 10 SMGGSGIIATELGIKLAERGHEVHFI--TSNIPFrirKPLPNMIFHQvevnqYAVFQYPPYDITLST-KIAEVIKEYDLD 86
Cdd:cd04951 10 GLGGAEKQTVLLADQMFIRGHDVNIVylTGEVEV---KPLNNNIIIY-----NLGMDKNPRSLLKALlKLKKIISAFKPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 87 LLHMHyaVPHAicGILAR--EMSGKDIKIMTTLHGTDItvlgydhslQGAIKFGIEK-----SDIVTSVSKSLAQE--TH 157
Cdd:cd04951 82 VVHSH--MFHA--NIFARflRMLYPIPLLICTAHNKNE---------GGRIRMFIYRltdflCDITTNVSREALDEfiAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 158 EIIETNKeIIPIYNFVRENEFPTKHNTALK--SQFGIAPDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPS-KLILLGD 234
Cdd:cd04951 149 KAFSKNK-SVPVYNGIDLNKFKKDINVRLKirNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDfKLLIAGD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 235 GPELVPMRQLTKELNVEEDVLFLGKQDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIkhGETG 314
Cdd:cd04951 228 GPLRNELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVV--GDHN 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 616541834 315 FVVDVGDCDSASDYAIRLLEDKVLYNKLQKNMLADIAERFGSELITDQYEYYYQK 369
Cdd:cd04951 306 YVVPVSDPQLLAEKIKEIFDMSDEERDILGNKNEYIAKNFSINTIVNEWERLYSG 360
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
190-355 |
1.34e-24 |
|
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: 103.55 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 190 FGIAPDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPS-KLILLG----DGPELVPMRQLTKEL-NVEED--VLFLGKQD 261
Cdd:cd03792 191 FVIDPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEpQLVICGhgavDDPEGSVVYEEVMEYaGDDHDihVLRLPPSD 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 262 -CVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDVGDCDSAsdYAIRLLEDKVLYN 340
Cdd:cd03792 271 qEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAV--RILRLLTDPELRR 348
|
170
....*....|....*
gi 616541834 341 KLQKNMLADIAERFG 355
Cdd:cd03792 349 KMGLAAREHVRDNFL 363
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
3-364 |
1.39e-23 |
|
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: 100.88 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 3 IGITCYPSMGGSGIIATELGIKLAERGHEVHFITS--NIPFRIRKPLPNMIFHQVEVnqYAVFQYPPYDITLSTKIAE-- 78
Cdd:cd03794 5 ISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPspNYPLGRIFAGATETKDGIRV--IRVKLGPIKKNGLIRRLLNyl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 79 ----------VIKEYDLDLLHmHYAVPH--AICGILAREMSGK----DIKIMTTLHGTDITVLGYDHSLQGAIKFgiEK- 141
Cdd:cd03794 83 sfalaallklLVREERPDVII-AYSPPItlGLAALLLKKLRGApfilDVRDLWPESLIALGVLKKGSLLKLLKKL--ERk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 142 ----SDIVTSVSKSLAQETHEIIETNKEIIPIYNFVRENEFPTKHNTALKSQFGiAPDEKVLIHVSNFRQVKRIDTIIET 217
Cdd:cd03794 160 lyrlADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPKDELRKKLG-LDDKFVVVYAGNIGKAQGLETLLEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 218 FAKVRDKIPSKLILLGDGPELVPMRQLTKELNVEeDVLFLGKQ--DCVSEFYQLSDLVLL-LSEKESFGLT----LLEAM 290
Cdd:cd03794 239 AERLKRRPDIRFLFVGDGDEKERLKELAKARGLD-NVTFLGRVpkEEVPELLSAADVGLVpLKDNPANRGSspskLFEYM 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616541834 291 KTGVVPIGSNAGGIKEVIKHGETGFVVDVGDCDSASDYAIRLLEDKVLYNKLQKNMLADIAERFGSELITDQYE 364
Cdd:cd03794 318 AAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRLL 391
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
128-363 |
1.47e-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: 99.68 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 128 DHSL-QGAIKFGIEKSDIVTSVSKSLAQETHEIIETNKEIIPIYN----FVRENEFPTKHntalksqfgIAPDEKVLIHV 202
Cdd:cd04949 96 EHSLiKNFYKYVFENLNKYDAIIVSTEQQKQDLSERFNKYPPIFTipvgYVDQLDTAESN---------HERKSNKIITI 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 203 SNFRQVKRIDTIIETFAKVRDKIPS-KLILLGDGPELVPMRQLTKELNVEEDVLFLGKQDCVSEFYQLSDLVLLLSEKES 281
Cdd:cd04949 167 SRLAPEKQLDHLIEAVAKAVKKVPEiTLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLSLLTSQMEG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 282 FGLTLLEAMKTGVVPIGSNAG-GIKEVIKHGETGFVVDVGDCDSASDYAIRLLEDKVLYNKLQKNMLAdIAERFGSELIT 360
Cdd:cd04949 247 FGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYK-IAEKYSTENVM 325
|
...
gi 616541834 361 DQY 363
Cdd:cd04949 326 EKW 328
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
193-367 |
1.06e-22 |
|
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: 97.75 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 193 APDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPSKLILLGDGPEL-VPMRQLTkelnveeDVLFLGKQD--CVSEFYQL 269
Cdd:cd03814 195 PPGRPLLLYVGRLAPEKNLEALLDADLPLAASPPVRLVVVGDGPARaELEARGP-------DVIFTGFLTgeELARAYAS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 270 SDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDVGDCDSASDYAIRLLEDKVLYNKLQKNMLAD 349
Cdd:cd03814 268 ADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAE 347
|
170
....*....|....*...
gi 616541834 350 iAERFGSELITDQYEYYY 367
Cdd:cd03814 348 -AERYSWEAFLDNLLDYY 364
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
85-338 |
1.73e-22 |
|
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: 97.52 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 85 LDLLHMHYAVPHAICGILAREMsgkDIKIMTTLHGTDITVlgydhSLQGAIKFGIEKSdiVTSVSKSLAQeTHEIIetnk 164
Cdd:cd05844 82 PALVHAHFGRDGVYALPLARAL---GVPLVVTFHGFDITT-----SRAWLAASPGWPS--QFQRHRRALQ-RPAAL---- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 165 eIIPIYNFVRENE----FPTKH--------NTALKSQFGIAPDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPS-KLIL 231
Cdd:cd05844 147 -FVAVSGFIRDRLlargLPAERihvhyigiDPAKFAPRDPAERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTaRLVI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 232 LGDGPELVPMRQLTKELNveeDVLFLGKQ--DCVSEFYQLSDLVLLLS------EKESFGLTLLEAMKTGVVPIGSNAGG 303
Cdd:cd05844 226 AGDGPLRPALQALAAALG---RVRFLGALphAEVQDWMRRAEIFCLPSvtaasgDSEGLGIVLLEAAACGVPVVSSRHGG 302
|
250 260 270
....*....|....*....|....*....|....*
gi 616541834 304 IKEVIKHGETGFVVDVGDCDSASDYAIRLLEDKVL 338
Cdd:cd05844 303 IPEAILDGETGFLVPEGDVDALADALQALLADRAL 337
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
9-317 |
4.29e-22 |
|
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: 93.62 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 9 PSMGGSGIIATELGIKLAERGHEVHFITSNIPFRIRkplpnmifhqvevnqyavfqyppyditlstkIAEVIKEYDLDLL 88
Cdd:cd01635 10 PLRGGLELHVRALARALAALGHEVTVLALLLLALRR-------------------------------ILKKLLELKPDVV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 89 HMHYAVPHAICGILAREMSGkdIKIMTTLHGtditvlgydhslqgaikfgieksdivtSVSKSLAQETHEIIETNKEIIP 168
Cdd:cd01635 59 HAHSPHAAALAALLAARLLG--IPIVVTVHG---------------------------PDSLESTRSELLALARLLVSLP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 169 IYNFVrenefptkhntalksqfgiapdekvliHVSNFRQVKRIDTIIETFAKVRDKIPS-KLILLGDGPELVPMRQLTKE 247
Cdd:cd01635 110 LADKV---------------------------SVGRLVPEKGIDLLLEALALLKARLPDlVLVLVGGGGEREEEEALAAA 162
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616541834 248 LNVEEDVLFLGKQDC---VSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVV 317
Cdd:cd01635 163 LGLLERVVIIGGLVDdevLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
6-364 |
2.06e-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: 94.32 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 6 TCYP--SMGGSGIIATELGIKLAERGHEV-HFITSNIP----------FRIRKPLPNMIFHQVEVNQYAVFQYppYDITL 72
Cdd:cd03823 7 SLYPpqRVGGAEISVHDLAEALVAEGHEVaVLTAGVGPpgqatvarsvVRYRRAPDETLPLALKRRGYELFET--YNPGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 73 STKIAEVIKEYDLDLLHMH------YAVPHAicgilAREMSgkdIKIMTTLHgtDITVLGYDHSLQGAikfgieKSDIVT 146
Cdd:cd03823 85 RRLLARLLEDFRPDVVHTHnlsglgASLLDA-----ARDLG---IPVVHTLH--DYWLLCPRQFLFKK------GGDAVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 147 SVSKSLAqETHE---IIETNKEIIPiyNFVRENEFPTKH--NTALKSQFG-IAPDEKVlihvsnfrqvKRIDTIIETFAK 220
Cdd:cd03823 149 APSRFTA-NLHEangLFSARISVIP--NAVEPDLAPPPRrrPGTERLRFGyIGRLTEE----------KGIDLLVEAFKR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 221 VRDKiPSKLILLGDGPELVPmrqltKELNVEEDVLFLGK--QDCVSEFYQLSDLVLLLSE-KESFGLTLLEAMKTGVVPI 297
Cdd:cd03823 216 LPRE-DIELVIAGHGPLSDE-----RQIEGGRRIAFLGRvpTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVI 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616541834 298 GSNAGGIKEVIKHGETGFVVDVGDCDSASDYAIRLLEDKVLYNKLQKNMLADIAERFGSELITDQYE 364
Cdd:cd03823 290 ASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAEEYLKLYR 356
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
137-369 |
3.19e-20 |
|
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: 90.85 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 137 FGIEKSDIVtSVSKSLAQETHE-IIETNKEIIPIYNFVRENEFPTKHNTALKSQFGIAPDEKVLIHVSN--FRQVKRIDT 213
Cdd:cd03825 134 LAKKRLTIV-APSRWLADMVRRsPLLKGLPVVVIPNGIDTEIFAPVDKAKARKRLGIPQDKKVILFGAEsvTKPRKGFDE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 214 IIETFAKVRDKIPSKLILLG-DGPELVPMRQLTKELNVEEDVLFLgkqdcvSEFYQLSDLVLLLSEKESFGLTLLEAMKT 292
Cdd:cd03825 213 LIEALKLLATKDDLLLVVFGkNDPQIVILPFDIISLGYIDDDEQL------VDIYSAADLFVHPSLADNLPNTLLEAMAC 286
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616541834 293 GVVPIGSNAGGIKEVIKHGETGFVVDVGDCDSASDYAIRLLEDKVLYNKLQKNMLADIAERFGSELITDQYEYYYQK 369
Cdd:cd03825 287 GTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYKD 363
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
208-367 |
9.81e-20 |
|
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: 90.47 E-value: 9.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 208 VKRIDTIIETFAKVRDKIP-SKLILLG---DGPELVP-MRQLTKELNVEEDVLFLGKQDcVSEFYQLSDLVLLLSEKESF 282
Cdd:cd03813 305 IKDVKTFIRAFKLVRRAMPdAEGWLIGpedEDPEYAQeCKRLVASLGLENKVKFLGFQN-IKEYYPKLGLLVLTSISEGQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 283 GLTLLEAMKTGVVPIGSNAGGIKEVI-----KHGETGFVVDVGDCDSASDYAIRLLEDKVLYNKLQKNMLADIAERFGSE 357
Cdd:cd03813 384 PLVILEAMASGVPVVATDVGSCRELIygaddALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLE 463
|
170
....*....|
gi 616541834 358 LITDQYEYYY 367
Cdd:cd03813 464 GMIDSYRKLY 473
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
12-173 |
2.57e-19 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 84.12 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 12 GGSGIIATELGIKLAERGHEVHFITSNIPFRIRKPLPNmiFHQVEVNQYAVFQYPPYDITLSTKIAEVIKEYDLDLLHMH 91
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVR--VVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 92 YAVPHAICGILARemSGKDIKIMTTLHGTDI--TVLGYDHSLQGAIKFGIEK-----SDIVTSVSKSLAQETHEIIETNK 164
Cdd:pfam13439 79 SPFPLGLAALAAR--LRLGIPLVVTYHGLFPdyKRLGARLSPLRRLLRRLERrllrrADRVIAVSEAVADELRRLYGVPP 156
|
170
....*....|
gi 616541834 165 E-IIPIYNFV 173
Cdd:pfam13439 157 EkIRVIPNGV 166
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
75-349 |
6.66e-18 |
|
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: 83.88 E-value: 6.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 75 KIAEVIKEYDLDLLHMHYAVPHAICGILAREMsGKDIKIMTTlHGTDITVLGYDHSLQGAIKFGIEK-SDIVTSVSKSlA 153
Cdd:cd03812 71 KLLKLIKKEKYDIVHVHGSSSNGIILLLAAKA-GVPVRIAHS-HNTKDSSIKLRKIRKNVLKKLIERlSTKYLACSED-A 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 154 QETHEIIETNKEIIPIYNFVRENEF-PTKHNTALKSQFGIAPDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIP-SKLIL 231
Cdd:cd03812 148 GEWLFGEVENGKFKVIPNGIDIEKYkFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPnVKLVL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 232 LGDGPELVPMRQLTKELNVEEDVLFLGKQDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHG 311
Cdd:cd03812 228 VGEGELKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITNN 307
|
250 260 270
....*....|....*....|....*....|....*...
gi 616541834 312 ETGFVVDVGDcDSASDYAIRLLEDKVLYNKLQKNMLAD 349
Cdd:cd03812 308 VEFLPLNETP-STWAEKILKLIKRKRRINKEINKEKKE 344
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
2-354 |
1.65e-17 |
|
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: 82.80 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 2 KIGI-TCYPSMGGSGI------IATELgikLAERGHEVHFITSNIPFRIRKPLPNmifhqvevnqYAVFQYPPYDITLST 74
Cdd:cd03809 1 KILIdGRSLAQRLTGIgrytreLLKAL---AKNDPDESVLAVPPLPGELLRLLRE----------YPELSLGVIKIKLWR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 75 KIAEVIKEYDLDLLHMHYAVPHAICGILAREMSGkdIKIMTTLHgtDITVL--------GYDHSLQGAIKFGIEKSDIVT 146
Cdd:cd03809 68 ELALLRWLQILLPKKDKPDLLHSPHNTAPLLLKG--CPQVVTIH--DLIPLrypeffpkRFRLYYRLLLPISLRRADAII 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 147 SVSKSLAQEtheIIET----NKEIIPIYNFVRENEFPTKHNTALKSQFGIapDEKVLIHVSNFRQVKRIDTIIETFAKVR 222
Cdd:cd03809 144 TVSEATRDD---IIKFygvpPEKIVVIPLGVDPSFFPPESAAVLIAKYLL--PEPYFLYVGTLEPRKNHERLLKAFALLK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 223 DKIPS-KLILLG-DGPELVPMRQLTKELNVEEDVLFLGK--QDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIG 298
Cdd:cd03809 219 KQGGDlKLVIVGgKGWEDEELLDLVKKLGLGGRVRFLGYvsDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIA 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 616541834 299 SNAGGIKEVIkhGETGFVVDVGDCDSASDyAI-RLLEDKVLYNKLQKNMLAdIAERF 354
Cdd:cd03809 299 SNISVLPEVA--GDAALYFDPLDPESIAD-AIlRLLEDPSLREELIRKGLE-RAKKF 351
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
3-358 |
3.95e-17 |
|
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: 81.55 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 3 IGITCYPSMGGSGIIATELGIKLAERGHEVHFIT-SNIPFRIRKPLPNMIFHQVEVNQYAVFQypPYDITLSTKIAEVIK 81
Cdd:cd03795 5 VFKFYYPDIGGIEQVIYDLAEGLKKKGIEVDVLCfSKEKETPEKEENGIRIHRVKSFLNVAST--PFSPSYIKRFKKLAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 82 EYDLdlLHMHYAVPHAIcgiLAREMSGKDIKIMTTLHgTDIT----VLGYDHSLQgaiKFGIEKSDIVTSVSKSLAQETH 157
Cdd:cd03795 83 EYDI--IHYHFPNPLAD---LLLFFSGAKKPVVVHWH-SDIVkqkkLLKLYKPLM---TRFLRRADRIIATSPNYVETSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 158 EI--IETNKEIIPI------YNFVRENEFPTKHNtalksqfgiAPDEKVLIHVSNFRQVKRIDTIIEtfAKVRDKIPskL 229
Cdd:cd03795 154 TLreFKNKVRVIPLgidknvYNIPRVDFENIKRE---------KKGKKIFLFIGRLVYYKGLDYLIE--AAQYLNYP--I 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 230 ILLGDGPELVPMRQLTkELNVEEDVLFLGKQDCVSE--FYQLSDLVLLLS--EKESFGLTLLEAMKTGVVPIGSN-AGGI 304
Cdd:cd03795 221 VIGGEGPLKPDLEAQI-ELNLLDNVKFLGRVDDEEKviYLHLCDVFVFPSvlRSEAFGIVLLEAMMCGKPVISTNiGTGV 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 616541834 305 KEVIKHGETGFVVDVGDCDSASDYAIRLLEDKVLYNKLQKNMLADIAERFGSEL 358
Cdd:cd03795 300 PYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEK 353
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
9-364 |
2.96e-16 |
|
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: 79.34 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 9 PSMGGSGIIATELGIKLAERGHEVHFITSNIPFRIRKPLPNMIFHQVEVNQYAVFQYPP----YDITLSTKIA--EVIKE 82
Cdd:cd03821 11 PKAGGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVEENGRYIPPQDGFASIPLLRQgagrTDFSPGLPNWlrRNLRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 83 YDLDLLHMHYAVPHAICGILARemsGKDIKIMTTLHGTditVLGYDHSLQGAIK-----------FGIEKSDIVTSvsKS 151
Cdd:cd03821 91 YDVVHIHGVWTYTSLAACKLAR---RRGIPYVVSPHGM---LDPWALQQKHWKKrialhlierrnLNNAALVHFTS--EQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 152 LAQETHEIIETNKE-IIPiyNFVRENEFPTKHntALKSQFGIAPDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPS-KL 229
Cdd:cd03821 163 EADELRRFGLEPPIaVIP--NGVDIPEFDPGL--RDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDwHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 230 ILLGDGPELVPM-RQLTKELNVEEDVLFLGK--QDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKE 306
Cdd:cd03821 239 VIAGPDDGAYPAfLQLQSSLGLGDRVTFTGPlyGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSE 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616541834 307 VIKHGeTGFVVDvgdcDSASDYA---IRLLEDKVLYNKLQKNMLA--DIAERFGSELITDQYE 364
Cdd:cd03821 319 LVEAG-CGVVVD----PNVSSLAealAEALRDPADRKRLGEMARRarQVEENFSWEAVAGQLG 376
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
25-362 |
8.97e-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: 77.49 E-value: 8.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 25 LAERGHEVHFITSNipfrirkPLPNMIFHQvevnqyAVFQYPPYDITLSTKIAEVIKEYDLDLLHMHYAVPHAIcGILAR 104
Cdd:cd03799 24 LIDRGHEVDIYAVN-------PGDLVKRHP------DVEKYNVPSLNLLYAIVGLNKKGAYDIIHCQFGPLGAL-GALLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 105 EMSGKDIKIMTTLHGTDITVLgydHSLQGAIKFG--IEKSDIVTSVSKSLAQETHEIIETNKEIIPIYNFVRENEFPTKH 182
Cdd:cd03799 90 RLKVLKGKLVTSFRGYDISMY---VILEGNKVYPqlFAQGDLFLPNCELFKHRLIALGCDEKKIIVHRSGIDCNKFRFKP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 183 NTalksqfgIAPDEKV-LIHVSNFRQVKRIDTIIETFAKVRDKIPS-KLILLGDGPELVPMRQLTKELNVEEDVLFLG-- 258
Cdd:cd03799 167 RY-------LPLDGKIrILTVGRLTEKKGLEYAIEAVAKLAQKYPNiEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGwk 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 259 KQDCVSEFYQLSDLVLLLS------EKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDVGDCDSASDYAIRL 332
Cdd:cd03799 240 PQEEIIEILDEADIFIAPSvtaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYL 319
|
330 340 350
....*....|....*....|....*....|
gi 616541834 333 LEDKVLYNKLQKNMLADIAERFGSELITDQ 362
Cdd:cd03799 320 IEHPAIWPEMGKAGRARVEEEYDINKLNDE 349
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
194-338 |
2.60e-15 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 77.06 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 194 PDEKVLIHVSNFRQVKRIDTIietfAKVRDKIP-SKLILLGDGPELVPMRQLTKELNVeedvLFLG--KQDCVSEFYQLS 270
Cdd:PLN02871 261 PEKPLIVYVGRLGAEKNLDFL----KRVMERLPgARLAFVGDGPYREELEKMFAGTPT----VFTGmlQGDELSQAYASG 332
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616541834 271 DLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVI---KHGETGFVVDVGDCDSASDYAIRLLEDKVL 338
Cdd:PLN02871 333 DVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPEL 403
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
25-369 |
2.20e-14 |
|
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: 73.48 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 25 LAERGHEVHFITS--------------NIPFRIRKPLPNMIFHQVEVnqyavfqyppyditlstkIAEVIKEYDLDLLHM 90
Cdd:cd03802 31 LVRRGHEVTLFAPgdshtsaplvavipRALRLDPIPQESKLAELLEA------------------LEVQLRASDFDVIHN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 91 HYAVPHaicGILAREMsgkDIKIMTTLHGTDItvlgydhsLQGAIKFGIEKSDIVTSVSKSLAQETHEIietnKEIIPIY 170
Cdd:cd03802 93 HSYDWL---PPFAPLI---GTPFVTTLHGPSI--------PPSLAIYAAEPPVNYVSISDAQRAATPPI----DYLTVVH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 171 NFVRENEFPtkhntalkSQFgiaPDEKVLIHVSNFRQVKRIDTIIEtFAKvRDKIPSKLIllgdGPELVPMR-QLTKELN 249
Cdd:cd03802 155 NGLDPADYR--------FQP---DPEDYLAFLGRIAPEKGLEDAIR-VAR-RAGLPLKIA----GKVRDEDYfYYLQEPL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 250 VEEDVLFLG------KQDcvsefyQLSDLVLLLSEK---ESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVD-- 318
Cdd:cd03802 218 PGPRIEFIGevghdeKQE------LLGGARALLFPInwdEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDsv 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 616541834 319 ------VGDCDSASDYAIRlledkvlynklqknmlADIAERFGSELITDQYEYYYQK 369
Cdd:cd03802 292 eemaeaIANIDRIDRAACR----------------RYAEDRFSAARMADRYEALYRK 332
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
192-362 |
1.51e-13 |
|
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: 71.47 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 192 IAPDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPS----KLILLGDGPELVP--------MRQLTKEL-NVEEDVLFL- 257
Cdd:cd03805 207 AKSNKKFFLSINRFERKKNIALAIEAFAKLKQKLPEfenvRLVIAGGYDPRVAenveyleeLQRLAEELlNVEDQVLFLr 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 258 ---GKQDCVseFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDvGDCDSASDYAIRLLE 334
Cdd:cd03805 287 sisDSQKEQ--LLSSALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCE-PTPEAFAEAMLKLAN 363
|
170 180
....*....|....*....|....*...
gi 616541834 335 DKVLYNKLQKNMLADIAERFGSELITDQ 362
Cdd:cd03805 364 DPDLADRMGAAGRKRVKEKFSREAFAER 391
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
209-315 |
1.68e-13 |
|
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: 70.78 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 209 KRIDTIIETFAKvrdkIPSKLILLGDGPELVPMRQLTKElNVEedvlFLGKQDcvseFYQLSDLV-----LLLSEKESFG 283
Cdd:cd03804 212 KRIDLAVEAFNE----LPKRLVVIGDGPDLDRLRAMASP-NVE----FLGYQP----DEVLKELLskaraFVFAAEEDFG 278
|
90 100 110
....*....|....*....|....*....|..
gi 616541834 284 LTLLEAMKTGVVPIGSNAGGIKEVIKHGETGF 315
Cdd:cd03804 279 IVPVEAQACGTPVIAFGKGGALETVRPGPTGI 310
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
25-149 |
2.76e-12 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 63.50 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 25 LAERGHEVHFITSNIPFRIRKPLPNMIFHQVEVNQYAVFQYppydiTLSTKIAEVIKEYDLDLLHMHYAVPHAICGILAR 104
Cdd:pfam13477 20 LADRGYDVHVISSKGPAKDELIAEGIHVHRLKVPRKGPLGY-----LKAFRLKKLIKKIKPDVVHVHYAKPYGLLAGLAA 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 616541834 105 EMSGKdIKIMTTLHGTDITVLGYDHSLQGAI-KFGIEKSDIVTSVS 149
Cdd:pfam13477 95 RLSGF-PPVVLSAWGLDVYKFPNKSRLKKLLlKLNLKKATLIISTS 139
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
7-348 |
1.31e-10 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 62.58 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 7 CYP--SMGGSGIIATELGIKLAERGHEVHFIT---SNIPFRIRKPLPN-------------MIFHQVEVN---------- 58
Cdd:cd03791 9 VAPfaKTGGLGDVAGALPKALAKLGHDVRVILpryGQIPDELDGYLRVlglevkvggrgeeVGVFELPVDgvdyyfldnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 59 -------QYAVFQYPPYD-----ITLSTKIAEVIKEYDL--DLLHMH----YAVPhaicgILAREMSG----KDIKIMTT 116
Cdd:cd03791 89 effdrpgLPGPPGYDYPDnaerfAFFSRAALELLRRLGFqpDIIHANdwhtALVP-----AYLKTRYRgpgfKKIKTVFT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 117 LH-------------------GTDITVLGYDHslQGAIKF---GIEKSDIVTSVSKSLAQE--THE-------------- 158
Cdd:cd03791 164 IHnlayqglfpldtlaelglpPELFHIDGLEF--YGQINFlkaGIVYADRVTTVSPTYAKEilTPEygegldgvlrarag 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 159 ----II----------ETNKEIIPIYNF-VRENEFPTKhnTALKSQFGIAPDEK--VLIHVSNFRQVKRIDTIIETFAKV 221
Cdd:cd03791 242 klsgILngidydewnpATDKLIPANYSAnDLEGKAENK--AALQKELGLPVDPDapLFGFVGRLTEQKGVDLILDALPEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 222 RDKiPSKLILLGDGPELV--PMRQLTKElnveedvlFLGKQDCVSEF--------YQLSDLVLLLSEKESFGLTLLEAMK 291
Cdd:cd03791 320 LEE-GGQLVVLGSGDPEYeqAFRELAER--------YPGKVAVVIGFdealahriYAGADFFLMPSRFEPCGLVQMYAMR 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616541834 292 TGVVPIGSNAGGIKEVIKHGE------TGFVV---DVGDCDSASDYAIRLLEDKVLYNKLQKNMLA 348
Cdd:cd03791 391 YGTLPIVRRTGGLADTVFDYDpetgegTGFVFedyDAEALLAALRRALALYRNPELWRKLQKNAMK 456
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
243-354 |
2.57e-10 |
|
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: 61.61 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 243 QLTKELNVE-EDVLFLGK--QDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDV 319
Cdd:cd03818 271 KMLAELGVDlERVHFVGKvpYDQYVRLLQLSDAHVYLTYPFVLSWSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDF 350
|
90 100 110
....*....|....*....|....*....|....*
gi 616541834 320 GDCDSASDYAIRLLEDKVLYNKLQKNMLADIAERF 354
Cdd:cd03818 351 FDPDALAAAVLELLEDPDRAAALRRAARRTVERSD 385
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
195-329 |
3.55e-10 |
|
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: 61.09 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 195 DEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPS------KLILLG----DGPE--LVPMRQLTKELNVEEDVLFlgKQDC 262
Cdd:cd03806 236 RENQILSIAQFRPEKNHPLQLRAFAELLKRLPEsirsnpKLVLIGscrnEEDKerVEALKLLAKELILEDSVEF--VVDA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 263 VSEfyqlsDLVLLLS---------EKESFGLTLLEAMKTGVVPIGSNAGGIKEVI----KHGETGFVvdvgdCDSASDYA 329
Cdd:cd03806 314 PYE-----ELKELLStasiglhtmWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIvvpwDGGPTGFL-----ASTPEEYA 383
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
194-334 |
6.10e-10 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 60.52 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 194 PDEKVLIHVSNFRQVKRIDTIIETFAKVRDKIPS-----KLILLG------DGPELVPMRQLTKELNVEEDVLFlgkqdC 262
Cdd:PLN02949 266 EDPPYIISVAQFRPEKAHALQLEAFALALEKLDAdvprpKLQFVGscrnkeDEERLQKLKDRAKELGLDGDVEF-----H 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 263 VSEFYqlSDLVLLLSE---------KESFGLTLLEAMKTGVVPIGSNAGGIKEVI---KHGE-TGFVvdvgdCDSASDYA 329
Cdd:PLN02949 341 KNVSY--RDLVRLLGGavaglhsmiDEHFGISVVEYMAAGAVPIAHNSAGPKMDIvldEDGQqTGFL-----ATTVEEYA 413
|
....*
gi 616541834 330 IRLLE 334
Cdd:PLN02949 414 DAILE 418
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
199-357 |
1.24e-09 |
|
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: 59.40 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 199 LIHVSNFRQVKRIDTIIETFAKVRDKIPSKLIL---LGDGPELVPMRQLTKELNVEEDVLFLG--KQDCVSEFYQLS--D 271
Cdd:cd04946 227 LVSCSSIVPVKRIDLIIETLNSLCVAHPSICISwthIGGGPLKERLEKLAENKLENVKVNFTGevSNKEVKQLYKENdvD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 272 LVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDvGDCdSASDYAIRLLE---DKVLYNKLQKNMLA 348
Cdd:cd04946 307 VFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLLLD-KDP-TPNEIVSSIMKfylDGGDYKTMKISARE 384
|
....*....
gi 616541834 349 DIAERFGSE 357
Cdd:cd04946 385 CWEERFNAE 393
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
186-315 |
1.53e-09 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 59.03 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 186 LKSQFGIAPDEKVLIHVSNFRQVKRIDTIIETFAKV---RDKIpsKLILLGD---------GPELVPMRQLTKELNveED 253
Cdd:PRK15484 183 LRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLataHSNL--KLVVVGDptasskgekAAYQKKVLEAAKRIG--DR 258
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616541834 254 VLFLGKQ--DCVSEFYQLSDLVLLLSE-KESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGF 315
Cdd:PRK15484 259 CIMLGGQppEKMHNYYPLADLVVVPSQvEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGY 323
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
102-341 |
7.92e-09 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 56.64 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 102 LAREMSGKDIKIMTTLHGT-------DITVLGY-DHSLqgAIKFGIEKSDIVTSVSkslAQETHEI---IETNKEIIPIy 170
Cdd:PRK09922 101 KARKKSGKQFKIFSWPHFSldhkkhaECKKITCaDYHL--AISSGIKEQMMARGIS---AQRISVIynpVEIKTIIIPP- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 171 nfvrenefPTKHNTAlksqfgiapdekVLIHVSN--FRQVKRIDTIIETFAKVrdKIPSKLILLGDGPELVPMRQLTKEL 248
Cdd:PRK09922 175 --------PERDKPA------------VFLYVGRlkFEGQKNVKELFDGLSQT--TGEWQLHIIGDGSDFEKCKAYSREL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 249 NVEEDVLFLGKQDCVSEFYQLS----DLVLLLSEKESFGLTLLEAMKTGVVPIGSNA-GGIKEVIKHGETGFVVDVGDCD 323
Cdd:PRK09922 233 GIEQRIIWHGWQSQPWEVVQQKiknvSALLLTSKFEGFPMTLLEAMSYGIPCISSDCmSGPRDIIKPGLNGELYTPGNID 312
|
250
....*....|....*...
gi 616541834 324 SASDYAIRLLEDKVLYNK 341
Cdd:PRK09922 313 EFVGKLNKVISGEVKYQH 330
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
218-321 |
1.64e-08 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 56.20 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 218 FAKVRDKIpsKLILLGDGPELVPMRQLTKELNVEEDVLFLGKQDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPI 297
Cdd:PRK15179 542 FAASHPKV--RFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVV 619
|
90 100
....*....|....*....|....
gi 616541834 298 GSNAGGIKEVIKHGETGFVVDVGD 321
Cdd:PRK15179 620 TTLAGGAGEAVQEGVTGLTLPADT 643
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
78-363 |
7.74e-08 |
|
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: 53.54 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 78 EVIKEYDLDLLHMHYAVPHAIC-----GILAREMSG--------KDIKIMTTLHgtdiTVLGYDHSLQGAIKFGIEKSDI 144
Cdd:cd03822 59 WNSNEYFRLLDHLNFKKPDVVHiqhefGIFGGKYGLyalglllhLRIPVITTLH----TVLDLSDPGKQALKVLFRIATL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 145 VTSV------SKSLAQETHEIIETNKEIIPIYNFvrenEFPTKHNTALKSQFGIApDEKVLIHVSNFRQVKRIDTIIETF 218
Cdd:cd03822 135 SERVvvmapiSRFLLVRIKLIPAVNIEVIPHGVP----EVPQDPTTALKRLLLPE-GKKVILTFGFIGPGKGLEILLEAL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 219 AKVRDKIPS--KLILLGDGPELV-------PMRQLtKELNVEEDVLFLGK---QDCVSEFYQLSDLVLL--LSEKESFGL 284
Cdd:cd03822 210 PELKAEFPDvrLVIAGELHPSLAryegeryRKAAI-EELGLQDHVDFHNNflpEEEVPRYISAADVVVLpyLNTEQSSSG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 285 TLLEAMKTGVvPIGSNAGGIKEVIKHGETGFVVDVGDCDSASDYAIRLLEDkvlyNKLQKNMlADIAERFGS----ELIT 360
Cdd:cd03822 289 TLSYAIACGK-PVISTPLRHAEELLADGRGVLVPFDDPSAIAEAILRLLED----DERRQAI-AERAYAYARamtwESIA 362
|
...
gi 616541834 361 DQY 363
Cdd:cd03822 363 DRY 365
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
227-333 |
3.48e-07 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 52.01 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 227 SKLILLGDGPELVPMRQLTKELNVEEDVLFLGKQDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKE 306
Cdd:PRK15490 430 TRFVLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGSAE 509
|
90 100 110
....*....|....*....|....*....|
gi 616541834 307 VIKHGETGFVVDVG---DCDSASDYAIRLL 333
Cdd:PRK15490 510 CFIEGVSGFILDDAqtvNLDQACRYAEKLV 539
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
280-372 |
6.12e-07 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 51.52 E-value: 6.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 280 ESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDVGDCDSAS----DYAIRLLEDKVLYNKLQKNMLADIAERFg 355
Cdd:PLN00142 677 EAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDEAAnkiaDFFEKCKEDPSYWNKISDAGLQRIYECY- 755
|
90
....*....|....*..
gi 616541834 356 selitdQYEYYYQKMLN 372
Cdd:PLN00142 756 ------TWKIYAERLLT 766
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
185-353 |
3.77e-06 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 48.56 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 185 ALKSQFGIAPDEKVLIH--VSNFRQVKRIDTIIETFaKVRDKIPSKLILLGDG-PELVPMRQLTKELNVEEDVLFLGKQD 261
Cdd:PRK14099 282 ALQARFGLDPDPDALLLgvISRLSWQKGLDLLLEAL-PTLLGEGAQLALLGSGdAELEARFRAAAQAYPGQIGVVIGYDE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 262 CVSEFYQL-SDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKE-VIKHGETGFVVDVGD-----------CDSASDY 328
Cdd:PRK14099 361 ALAHLIQAgADALLVPSRFEPCGLTQLCALRYGAVPVVARVGGLADtVVDANEMAIATGVATgvqfspvtadaLAAALRK 440
|
170 180
....*....|....*....|....*.
gi 616541834 329 AIRLLEDKVLYNKLQKN-MLADIAER 353
Cdd:PRK14099 441 TAALFADPVAWRRLQRNgMTTDVSWR 466
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
12-171 |
5.45e-06 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 45.85 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 12 GGSGIIATELGIKLAERGHEVHFITSnipfriRKPLPNMIFHQVEVNQYAV----FQYPPYDITLSTKIAEVIKEYDLDL 87
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTP------GGPPGRPELVGDGVRVHRLpvppRPSPLADLAALRRLRRLLRAERPDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 88 LHMHYAvPHAICGILARemSGKDIKIMTTLHGTDITvlGYDHSLQGAI----KFGIEKSDIVTSVSKSLAQETHEIIETN 163
Cdd:pfam13579 75 VHAHSP-TAGLAARLAR--RRRGVPLVVTVHGLALD--YGSGWKRRLAraleRRLLRRADAVVVVSEAEAELLRALGVPA 149
|
....*...
gi 616541834 164 KEIIPIYN 171
Cdd:pfam13579 150 ARVVVVPN 157
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
131-349 |
6.58e-06 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 47.78 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 131 LQGAIKFgiekSDIVTSVSKSLAQE--THE------------------II----------ETNKEIIpiYNFVRENEFPT 180
Cdd:COG0297 203 LKAGIVY----ADRVTTVSPTYAREiqTPEfgegldgllrarsgklsgILngidydvwnpATDPYLP--ANYSADDLEGK 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 181 KHN-TALKSQFGIAPDEKVLI--HVSNF-RQvKRIDTIIETFAKVRDKiPSKLILLGDG-PELVPM-RQLTKELNveEDV 254
Cdd:COG0297 277 AANkAALQEELGLPVDPDAPLigMVSRLtEQ-KGLDLLLEALDELLEE-DVQLVVLGSGdPEYEEAfRELAARYP--GRV 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 255 LFLGKQDcvSEFYQL----SDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVIKH------GETGFV---VDVGD 321
Cdd:COG0297 353 AVYIGYD--EALAHRiyagADFFLMPSRFEPCGLNQMYALRYGTVPIVRRTGGLADTVIDyneatgEGTGFVfdeYTAEA 430
|
250 260
....*....|....*....|....*....
gi 616541834 322 CDSASDYAIRLLEDKVLYNKLQKN-MLAD 349
Cdd:COG0297 431 LLAAIRRALALYRDPEAWRKLQRNaMKQD 459
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
270-372 |
1.29e-05 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 47.04 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 270 SDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKE-VIKHGE-----TGFV---VDVGDCDSASDYAIRLLEDKVLYN 340
Cdd:PRK00654 357 ADMFLMPSRFEPCGLTQLYALRYGTLPIVRRTGGLADtVIDYNPedgeaTGFVfddFNAEDLLRALRRALELYRQPPLWR 436
|
90 100 110
....*....|....*....|....*....|...
gi 616541834 341 KLQKN-MLADiaerFGSELITDQYEYYYQKMLN 372
Cdd:PRK00654 437 ALQRQaMAQD----FSWDKSAEEYLELYRRLLG 465
|
|
| sucrsPsyn_pln |
TIGR02468 |
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
280-350 |
1.82e-05 |
|
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: 46.70 E-value: 1.82e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616541834 280 ESFGLTLLEAMKTGVVPIGSNAGGIKEVIKHGETGFVVDVGDCDSASDYAIRLLEDKVLYNKLQKNMLADI 350
Cdd:TIGR02468 582 EPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALLKLVADKQLWAECRQNGLKNI 652
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
8-353 |
5.14e-05 |
|
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: 44.92 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 8 YPSMGGSGIIATELGIKLAERGHEVHFITSNIPFR--IR------KP--LPNMIFHQvEVNQYAVFQYPPY--DITLSTK 75
Cdd:cd03796 10 YPNLGGVETHIYQLSQCLIKRGHKVIVITHAYGNRvgVRyltnglKVyyLPFKVFYN-QSTLPTLFSTFPLlrNILIRER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 76 IaevikeydlDLLHMHYAV-PHAICGIL-AREMsgkDIKIMTTlhgtditvlgyDHSLQG-----------AIKFGIEKS 142
Cdd:cd03796 89 I---------QIVHGHQAFsSLAHEALFhARTL---GLKTVFT-----------DHSLFGfadassiltnkLLRFSLADI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 143 DIVTSVSKSLAQETHEIIETNKEIIP-IYNFVRENEF---PTKHntalksqfgiAPDEKVLIHVSNFRQVKRIDTIIETF 218
Cdd:cd03796 146 DHVICVSHTSKENTVLRASLDPRIVSvIPNAVDSSDFtpdPSKP----------DPNKITIVVISRLVYRKGIDLLVGII 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 219 AKVRDKIPS-KLILLGDGPELVPMRQLTKELNVEEDVLFLG--KQDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVV 295
Cdd:cd03796 216 PRICKKHPNvRFIIGGDGPKRIELEEMREKYQLQDRVELLGavPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLL 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616541834 296 PIGSNAGGIKEVIKHGETGF----VVDVgdCDSASDYAIRLLEDKVL---YNKLQKNMLA--DIAER 353
Cdd:cd03796 296 VVSTRVGGIPEVLPPDMILLaepdPEDI--VRKLEEAISILRTGKHDpwsFHNRVKKMYSweDVARR 360
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
15-335 |
9.67e-05 |
|
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274943 [Multi-domain] Cd Length: 373 Bit Score: 43.92 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 15 GIIAT-ELGIKLAERGHEVHFITSNIP--FRIRKPlpnmifhQVEVnQYAVFQYPPYDIT--LSTKIAEVIkEYDLDLLH 89
Cdd:TIGR04047 14 GVVHTlELAEALTALGHDVTVWALAADgfGFFRDP-------PCAV-RLVPVAPAPGDTDamVEQRIARSI-DHLRAHFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 90 MHYAVPHAICGILA------REMSGKDIKIMTTLHGTDITvlgyDHSLQGAIKFGIEKSDIVTSVSKSLAQETHEIIETN 163
Cdd:TIGR04047 85 RGFDVVHAQDCISGnalatlRAEGLIPGFVRTVHHLDDFD----DPRLAACQERAIVEADAVLCVSAAWAAELRAEWGID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 164 KEIIPiyNFVRENEF---PTKHNTALKSQFGI--APdekVLIHVSNFRQVKRIDTIIETFAKVRDKIPSKLILLGDGPEL 238
Cdd:TIGR04047 161 ATVVP--NGVDAARFspaADAADAALRRRLGLrgGP---YVLAVGGIEPRKNTIDLLEAFALLRARRPQAQLVIAGGATL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 239 V-------PMRQLTKELNVE-EDVLFLG--KQDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVI 308
Cdd:TIGR04047 236 FdydayrrEFRARAAELGVDpGPVVITGpvPDADLPALYRCADAFAFPSLKEGFGLVVLEALASGIPVVASDIAPFTEYL 315
|
330 340
....*....|....*....|....*..
gi 616541834 309 KHGEtGFVVDVGDCDSASDYAIRLLED 335
Cdd:TIGR04047 316 GRFD-AAWADPSDPDSIADALALALDP 341
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
132-369 |
1.75e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 132 QGAIKFgiekSDIVTSVSKSLAQET--------HEIIET-NKEIIPIYNFVRENEFPTKHNTALKSQF------GIAPDE 196
Cdd:PLN02939 688 KGAIVY----SNIVTTVSPTYAQEVrseggrglQDTLKFhSKKFVGILNGIDTDTWNPSTDRFLKVQYnandlqGKAANK 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 197 KVL-----IHVSNFRQ-----------VKRIDTIIETFAKVRDkIPSKLILLGDGPelVP---------MRQLTKELNVE 251
Cdd:PLN02939 764 AALrkqlgLSSADASQplvgcitrlvpQKGVHLIRHAIYKTAE-LGGQFVLLGSSP--VPhiqrefegiADQFQSNNNIR 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 252 edvLFLGKQDCVSE-FYQLSDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVI------------KHGETGFVVD 318
Cdd:PLN02939 841 ---LILKYDEALSHsIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSVfdfddetipvelRNGFTFLTPD 917
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 616541834 319 VGDCDSASDYAIRLLE-DKVLYNKL-QKNMLADiaerFGSELITDQYEYYYQK 369
Cdd:PLN02939 918 EQGLNSALERAFNYYKrKPEVWKQLvQKDMNID----FSWDSSASQYEELYQR 966
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
185-371 |
2.39e-03 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 39.72 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 185 ALKSQFGIAPDEK--VLIHVSNFRQVKRIDTIIETFAKVRDkIPSKLILLGDGPELVPMRQLTKELNVEEDVLFlgKQDC 262
Cdd:PRK14098 294 ALLEEVGLPFDEEtpLVGVIINFDDFQGAELLAESLEKLVE-LDIQLVICGSGDKEYEKRFQDFAEEHPEQVSV--QTEF 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 263 VSEFYQL----SDLVLLLSEKESFGLTLLEAMKTGVVPIGSNAGGIKEVI-KHGE---TGFVVDVGDCDSAS---DYAIR 331
Cdd:PRK14098 371 TDAFFHLaiagLDMLLMPGKIESCGMLQMFAMSYGTIPVAYAGGGIVETIeEVSEdkgSGFIFHDYTPEALVaklGEALA 450
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 616541834 332 LLEDKVLYNKLqknMLADIAERFGSELITDQYEYYYQKML 371
Cdd:PRK14098 451 LYHDEERWEEL---VLEAMERDFSWKNSAEEYAQLYRELL 487
|
|
| PHA01633 |
PHA01633 |
putative glycosyl transferase group 1 |
158-293 |
2.94e-03 |
|
putative glycosyl transferase group 1
Pssm-ID: 107050 [Multi-domain] Cd Length: 335 Bit Score: 39.19 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616541834 158 EIIETNKEIIPIYNFVRENEFPtkhNTAlksQFGIapdekvlihVSNFRQVKRIDTIIETFAKVRDKIP--SKLILLGdg 235
Cdd:PHA01633 125 KIVENAEKLVPQLKQKLDKDFP---DTI---KFGI---------VSGLTKRKNMDLMLQVFNELNTKYPdiAKKIHFF-- 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616541834 236 peLVPMRQLTKeLNVEEDVLFLGK-----QDCVSEFYQLSDLVLLLSEKESFGLTLLEAMKTG 293
Cdd:PHA01633 188 --VISHKQFTQ-LEVPANVHFVAEfghnsREYIFAFYGAMDFTIVPSGTEGFGMPVLESMAMG 247
|
|
| |
