|
Name |
Accession |
Description |
Interval |
E-value |
| thiol_BshA |
TIGR03999 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, ... |
3-373 |
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: 686.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 3 LKIGITCYPSVGGSGVVGTELGKQLAERGHEIHFITSGLPFRLNKVYPNIYFHEVTVNQYSVFQYPPYDLALASKMAEVA 82
Cdd:TIGR03999 1 MKIGITCYPTYGGSGVVATELGKALAERGHEVHFITSSQPFRLEKFHPNIFFHEVEVNQYPLFQYPPYDLALASKIAEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 83 QRESLDILHVHYAIPHAICAYLAKQMIGE---RIKIVTTLHGTDITVLGSDPSLNNLIRFGIEQSDVVTAVSHSLIDETH 159
Cdd:TIGR03999 81 KEEKLDLLHVHYAIPHAIAAYLARQMLGKegiDIPIVTTLHGTDITLVGADPSFKPAVRFSIEKSDGVTAVSESLKEETY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 160 ELVKPNKDIQTVYNFIDERVYFKRNMSQLKKEYGISESEKVLIHISNFRKVKRVQDVVQAFAKVAKEVDAKLLLVGDGPE 239
Cdd:TIGR03999 161 ELFDIDKPIEVIPNFVDTDRYRRKNDPALKRKLGAPEDEKVLIHISNFRPVKRVEDVIEVFARVQQEVPAKLLLVGDGPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 240 FCTILQIVKNLHIEDRVLFLGKQDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYLC 319
Cdd:TIGR03999 241 RSPAEQLVRELGLTDRVLFLGKQDDVAELLSISDLFLLPSEKESFGLAALEAMACGVPVIASNAGGIPEVVEHGVTGFLC 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446690964 320 EVGDTTGVANQAIQLLKNEEFHRNMGERARESVYEQFRSEKIVSQYEAIYYDIL 373
Cdd:TIGR03999 321 DVGDVETMAEYAISLLEDEELLQRFSAAARERAKERFDSEKIVPQYEALYRRLL 374
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
3-369 |
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: 582.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 3 LKIGITCYPSVGGSGVVGTELGKQLAERGHEIHFITSGLPFRLNKVYPNIYFHEVTVNQYSVFQYPPYDLALASKMAEVA 82
Cdd:cd04962 1 MKIGIVCYPSYGGSGVVATELGLELAERGHEVHFISSAIPFRLNLYSGNIFFHEVEVPNYPLFEYPPYTLALASKIVEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 83 QRESLDILHVHYAIPHAICAYLAKQMIGERIKIVTTLHGTDITVLGSDPSLNNLIRFGIEQSDVVTAVSHSLIDETHELV 162
Cdd:cd04962 81 KEHKLDVLHAHYAIPHASCAYLAREILGEKIPIVTTLHGTDITLVGYDPSLQPAVRFSINKSDRVTAVSSSLRQETYELF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 163 KPNKDIQTVYNFIDERVYFKRNMSQLKKEYGISESEKVLIHISNFRKVKRVQDVVQAFAKVAKEVDAKLLLVGDGPEFCT 242
Cdd:cd04962 161 DVDKDIEVIHNFIDEDVFKRKPAGALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIPAKLLLVGDGPERVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 243 ILQIVKNLHIEDRVLFLGKQDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYLCEVG 322
Cdd:cd04962 241 AEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446690964 323 DTTGVANQAIQLLKNEEFHRNMGERARESVYEQFRSEKIVSQYEAIY 369
Cdd:cd04962 321 DVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYY 367
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
11-369 |
1.66e-70 |
|
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: 225.11 E-value: 1.66e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 11 PSVGGSGVVGTELGKQLAERGHEIHFITSGLPFRLnkvyPNIYFHEVTVNQYSVFQYPPYDLALASKMAEVAQRESLDIL 90
Cdd:cd03801 11 PPVGGAERHVRELARALAARGHDVTVLTPADPGEP----PEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 91 HVHYAIPHAICAYLAKQMigeRIKIVTTLHGTDITVL-----GSDPSLNNLIRFgIEQSDVVTAVSHSLIDETHEL-VKP 164
Cdd:cd03801 87 HAHGLLAALLAALLALLL---GAPLVVTLHGAEPGRLllllaAERRLLARAEAL-LRRADAVIAVSEALRDELRALgGIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 165 NKDIQTVYNFIDERVYFKRnmsqLKKEYGISESEKVLIHISNFRKVKRVQDVVQAFAKVAKEV-DAKLLLVG-DGPEFCT 242
Cdd:cd03801 163 PEKIVVIPNGVDLERFSPP----LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGpDVRLVIVGgDGPLRAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 243 ILQIvkNLHIEDRVLFLGK--QDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYLCE 320
Cdd:cd03801 239 LEEL--ELGLGDRVRFLGFvpDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVP 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446690964 321 VGDTTGVANQAIQLLKNEEFHRNMGERARESVYEQFRSEKIVSQYEAIY 369
Cdd:cd03801 317 PDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
7-372 |
2.12e-68 |
|
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: 219.94 E-value: 2.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 7 ITCYP--SVGGSGVVGTELGKQLAERGHEIHFIT---------SGLPFRLNKVYPNIYFHEVTVNQYSVFQYPPYDLALA 75
Cdd:cd03798 5 TNIYPnaNSPGRGIFVRRQVRALSRRGVDVEVLApapwgpaaaRLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRAPSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 76 SKMAEVAQRESLDILHVHYAIPHAICAYLAKQMIGerIKIVTTLHGTDITVLGSDPSLNNLIRFGIEQSDVVTAVSHSLI 155
Cdd:cd03798 85 AKLLKRRRRGPPDLIHAHFAYPAGFAAALLARLYG--VPYVVTEHGSDINVFPPRSLLRKLLRWALRRAARVIAVSKALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 156 DETHELVKPNKDIQTVYNFIDERVYfkrnmSQLKKEYGISESEKVLIHISNFRKVKRVQDVVQAFAKVAKE-VDAKLLLV 234
Cdd:cd03798 163 EELVALGVPRDRVDVIPNGVDPARF-----QPEDRGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKArPDVVLLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 235 GDGPEFCTILQIVKNLHIEDRVLFLGKQDN--VAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQH 312
Cdd:cd03798 238 GDGPLREALRALAEDLGLGDRVTFTGRLPHeqVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGD 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 313 GETGYLCEVGDTTGVANQAIQLLkNEEFHRNMGERARESVYEQFRSEKIVSQYEAIYYDI 372
Cdd:cd03798 318 PETGLLVPPGDADALAAALRRAL-AEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
84-370 |
2.46e-52 |
|
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: 177.89 E-value: 2.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 84 RESLDILHVHyaIPHA-ICAYLAKQMIGERiKIVTTLHGTDItvlgSDPS-----LNNLIRFGIeqSDVVTAVSHSLIDE 157
Cdd:cd03807 77 KRNPDVVHTW--MYHAdLIGGLAAKLAGGV-KVIWSVRSSNI----PQRLtrlvrKLCLLLSKF--SPATVANSSAVAEF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 158 THELVKPNKDIQTVYNFID-ERV---YFKRnmSQLKKEYGISESEKVLIHISNFRKVKRVQDVVQAFAKVAKEV-DAKLL 232
Cdd:cd03807 148 HQEQGYAKNKIVVIYNGIDlFKLspdDASR--ARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHpDLRLL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 233 LVGDGPEFCTILQIVKNLHIEDRVLFLGKQDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQH 312
Cdd:cd03807 226 LVGRGPERPNLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDD 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446690964 313 GeTGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESVYEQFRSEKIVSQYEAIYY 370
Cdd:cd03807 306 G-TGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
4-366 |
7.15e-49 |
|
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: 169.00 E-value: 7.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 4 KIGI---TCYPSVGGsGVVGTE-LGKQLAERGHEIHFITsglPFRLNKVYPNIYfheVTVNQYSVFQYPPYDLALASKMA 79
Cdd:cd03817 1 KIAIftdTYLPQVNG-VATSVRnLARALEKRGHEVYVIT---PSDPGAEDEEEV---VRYRSFSIPIRKYHRQHIPFPFK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 80 EVAQRE----SLDILHVHyaIPHA---ICAYLAKQMigeRIKIVTTLHgT---DIT--VLGSDPSLNNLIRFGI----EQ 143
Cdd:cd03817 74 KAVIDRikelGPDIIHTH--TPFSlgkLGLRIARKL---KIPIVHTYH-TmyeDYLhyIPKGKLLVKAVVRKLVrrfyNH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 144 SDVVTAVSHSLIDETHEL-VKpnKDIQTVYNFIDERVYFKRNMSQLKKEYGISESEKVLIHISNFRKVKRVQDVVQAFAK 222
Cdd:cd03817 148 TDAVIAPSEKIKDTLREYgVK--GPIEVIPNGIDLDKFEKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 223 VAKEVDAKLLLVGDGPEFCTILQIVKNLHIEDRVLFLGKQDN--VAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIG 300
Cdd:cd03817 226 LKKEPNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPReeLPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVA 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446690964 301 TRVGGIPEVIQHGETGYLCEVGDTTgVANQAIQLLKNEEFHRNMGERARESVYEQFRSEKIVSQYE 366
Cdd:cd03817 306 AKDPAASELVEDGENGFLFEPNDET-LAEKLLHLRENLELLRKLSKNAEISAREFAFAKSVEKLYE 370
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
12-335 |
1.42e-48 |
|
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: 167.92 E-value: 1.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 12 SVGGSGVVGTELGKQLAERGHEIHFITSGLPFRLNKVYPNIYFHEVTVNQYsVFQYPPYDLALASKMAEVAQRESLDILH 91
Cdd:cd03811 10 SGGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRV-LKLIKLGLLKAILKLKRILKRAKPDVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 92 VHyaipHAICAYLAKQMIGERIKIVTTLHGtDITVLGSDPSLNNLIRFGIEQSDVVTAVSHSLIDETHELVKPNKD-IQT 170
Cdd:cd03811 89 SF----LGFATYIVAKLAAARSKVIAWIHS-SLSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSPPEkIEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 171 VYNFIDerVYFKRNMSQlKKEYGISESEKVLIHISNFRKVKRVQDVVQAFAKVAKEV-DAKLLLVGDGPEFCTILQIVKN 249
Cdd:cd03811 164 IYNPID--IDRIRALAK-EPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYpDVKLVILGDGPLREELEKLAKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 250 LHIEDRVLFLGKQDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYLCEVGDTTGVAN 329
Cdd:cd03811 241 LGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAG 320
|
....*.
gi 446690964 330 QAIQLL 335
Cdd:cd03811 321 ILAALL 326
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
22-366 |
1.27e-47 |
|
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: 165.46 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 22 ELGKQLAERGHEIHFITSGLPFRLNKVYP-NIYFHEVTVNQYSVFqyPPYDLALASKMAEVAQRESLDILHVHYAIPhAI 100
Cdd:cd03808 18 PLIKALVKKGYEVHVIAPDGDKLSDELKElGVKVIDIPILRRGIN--PLKDLKALFKLYKLLKKEKPDIVHCHTPKP-GI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 101 CAYLAKQMIGeRIKIVTTLHGtditvLG---SDPSLNNLIRFGIEQ-----SDVVTAVSHSLIDETHEL--VKPNKDIQT 170
Cdd:cd03808 95 LGRLAARLAG-VPKVIYTVHG-----LGfvfTEGKLLRLLYLLLEKlallfTDKVIFVNEDDRDLAIKKgiIKKKKTVLI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 171 VYNFIDERVYFKrnmsqlkKEYGISESEKVLIHISNFRKVKRVQDVVQAFAKVA-KEVDAKLLLVGDGPEFCTILQIVKN 249
Cdd:cd03808 169 PGSGVDLDRFQY-------SPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKkKGPNVRFLLVGDGELENPSEILIEK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 250 LHIEDRVLFLGKQDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYLCEVGDTTGVAN 329
Cdd:cd03808 242 LGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALAD 321
|
330 340 350
....*....|....*....|....*....|....*..
gi 446690964 330 QAIQLLKNEEFHRNMGERARESVYEQFRSEKIVSQYE 366
Cdd:cd03808 322 AIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
7-350 |
6.35e-46 |
|
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: 160.60 E-value: 6.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 7 ITCYPSVGGSGVVGTELGKQLAERGHEIHFITSGLPFRlnkvypniYFHEVTVNQYSVFQYPPY-DLALASKMAEVAQRE 85
Cdd:cd03819 4 LTPALEIGGAETYILDLARALAERGHRVLVVTAGGPLL--------PRLRQIGIGLPGLKVPLLrALLGNVRLARLIRRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 86 SLDILHVHYAIPHAICAYLAKQMigeRIKIVTTLHGTDITVLGSDPSLNNLIRFGieqsDVVTAVSHSLIDETHELVKPN 165
Cdd:cd03819 76 RIDLIHAHSRAPAWLGWLASRLT---GVPLVTTVHGSYLATYHPKDFALAVRARG----DRVIAVSELVRDHLIEALGVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 166 KD-IQTVYNFIDERVYFKRNMSQLKKEYGISESEKVLIHISNFRKVKRVQDVVQAFAKVAKEVDAKLLLVGDGPEFCTIL 244
Cdd:cd03819 149 PErIRVIPNGVDTDRFPPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFRLLVAGDGPERDEIR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 245 QIVKNLHIEDRVLFLGKQDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYLCEVGDT 324
Cdd:cd03819 229 RLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDA 308
|
330 340
....*....|....*....|....*.
gi 446690964 325 TGVANQAIQLLKNEEFHRNMGERARE 350
Cdd:cd03819 309 EALADAIRAAKLLPEAREKLQAAAAL 334
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
198-350 |
9.83e-44 |
|
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: 148.96 E-value: 9.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 198 EKVLIHISNFRKVKRVQDVVQAFAKVAKEV-DAKLLLVGDGPEFCTILQIVKNLHIEDRVLFLGKQDN--VAELLAMSDL 274
Cdd:pfam00534 2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNpNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDedLPELLKIADV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446690964 275 MLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARE 350
Cdd:pfam00534 82 FVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARK 157
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
4-367 |
8.59e-42 |
|
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: 149.70 E-value: 8.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 4 KIGItCYPSVGGSGvvGTE-----LGKQLAERGHEIHFITSGLPFRLN--KVYPNIYFHEVTVNQYSVFQYPPYDLALAS 76
Cdd:cd03820 1 KIAI-VIPSISNAG--GAErvainLANHLAKKGYDVTIISLDSAEKPPfyELDDNIKIKNLGDRKYSHFKLLLKYFKKVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 77 KMAEVAQRESLDILhvhYAIPHAICAYLAKqmIGERIKIVTTLHGTDITVLGSDPSLNnLIRFGIEQSDVVTAVSHSliD 156
Cdd:cd03820 78 RLRKYLKNNKPDVV---ISFRTSLLTFLAL--IGLKSKLIVWEHNNYEAYNKGLRRLL-LRRLLYKRADKIVVLTEA--D 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 157 ETHELVKPNKDIQTVYNFIDErvyfkrnmsqLKKEYGISESEKVLIHISNFRKVKRVQDVVQAFAKVAKEVDA-KLLLVG 235
Cdd:cd03820 150 KLKKYKQPNSNVVVIPNPLSF----------PSEEPSTNLKSKRILAVGRLTYQKGFDLLIEAWALIAKKHPDwKLRIYG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 236 DGPEFCTILQIVKNLHIEDRVLFLGKQDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGT-RVGGIPEVIQHGE 314
Cdd:cd03820 220 DGPEREELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFdCPTGPSEIIEDGE 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446690964 315 TGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESVyEQFRSEKIVSQYEA 367
Cdd:cd03820 300 NGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNA-ERFSIEKIIKQWEE 351
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
198-337 |
1.79e-39 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 137.26 E-value: 1.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 198 EKVLIHISNF-RKVKRVQDVVQAFAKV-AKEVDAKLLLVGDGPEFcTILQIVKNLhiEDRVLFLGKQDNVAELLAMSDLM 275
Cdd:pfam13692 1 RPVILFVGRLhPNVKGVDYLLEAVPLLrKRDNDVRLVIVGDGPEE-ELEELAAGL--EDRVIFTGFVEDLAELLAAADVF 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446690964 276 LLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIqHGETGYLCEVGDTTGVANQAIQLLKN 337
Cdd:pfam13692 78 VLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLLED 138
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
268-374 |
9.05e-36 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 127.03 E-value: 9.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 268 LLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGER 347
Cdd:COG0438 17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96
|
90 100
....*....|....*....|....*..
gi 446690964 348 ARESVYEQFRSEKIVSQYEAIYYDILR 374
Cdd:COG0438 97 ARERAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
10-370 |
1.14e-35 |
|
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: 133.57 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 10 YPSVGGsgVVGT--ELGKQLAERGHEIHFITSGLPFRLNKVYPNIyfheVTVNQYSVFQYPPYDLAL--ASKMAEVAQRE 85
Cdd:cd03814 10 HPQVNG--VVRTleRLVDHLRRRGHEVRVVAPGPFDEAESAEGRV----VSVPSFPLPFYPEYRLALplPRRVRRLIKEF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 86 SLDILHVHYAIPHAICAYLAKQMIGerIKIVTTLHgTDI-------TVLGSDPSLNNLIRFGIEQSDVVTAVSHSLIDET 158
Cdd:cd03814 84 QPDIIHIATPGPLGLAALRAARRLG--LPVVTSYH-TDFpeylsyyTLGPLSWLAWAYLRWFHNPFDTTLVPSPSIAREL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 159 HElvKPNKDIQTVYNFIDeRVYFK--RNMSQLKKEYGiSESEKVLIHISNFRKVKRVQDVVQAFAKVAKEVDAKLLLVGD 236
Cdd:cd03814 161 EG--HGFERVRLWPRGVD-TELFHpsRRDAALRRRLG-PPGRPLLLYVGRLAPEKNLEALLDADLPLAASPPVRLVVVGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 237 GP-----EFCtilqivkNLHiedrVLFLGKQD--NVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEV 309
Cdd:cd03814 237 GParaelEAR-------GPD----VIFTGFLTgeELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDI 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446690964 310 IQHGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESVyEQFRSEKIVSQYEAIYY 370
Cdd:cd03814 306 VRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEA-ERYSWEAFLDNLLDYYA 365
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
164-372 |
5.87e-35 |
|
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: 131.69 E-value: 5.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 164 PNKDIQTVYNFIDERVYFKRNMSQLKKEYGISESEKVLIHISN--FRKVKRVQDVVQAFAKVAKEVDAKLLLVGDGPEFc 241
Cdd:cd03825 159 KGLPVVVIPNGIDTEIFAPVDKAKARKRLGIPQDKKVILFGAEsvTKPRKGFDELIEALKLLATKDDLLLVVFGKNDPQ- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 242 tilqivkNLHIEDRVLFLGKQDNVAEL---LAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYL 318
Cdd:cd03825 238 -------IVILPFDIISLGYIDDDEQLvdiYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYL 310
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446690964 319 CEVGDTTGVANqAIQ-LLKNEEFHRNMGERARESVYEQFRSEKIVSQYEAIYYDI 372
Cdd:cd03825 311 VPPGDVQALAE-AIEwLLANPKERESLGERARALAENHFDQRVQAQRYLELYKDL 364
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
144-369 |
2.44e-34 |
|
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: 130.26 E-value: 2.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 144 SDVVTAVSHSLIDE--THELVKPNKDIqTVYNFIDeRVYFKRNMSQLKK---EYGISESEKVLIHISNFRKVKRVQDVVQ 218
Cdd:cd04951 131 CDITTNVSREALDEfiAKKAFSKNKSV-PVYNGID-LNKFKKDINVRLKirnKLNLKNDEFVILNVGRLTEAKDYPNLLL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 219 AFAKV-AKEVDAKLLLVGDGPEFCTILQIVKNLHIEDRVLFLGKQDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVP 297
Cdd:cd04951 209 AISELiLSKNDFKLLIAGDGPLRNELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERP 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446690964 298 CIGTRVGGIPEVIqhGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESVYEQFRSEKIVSQYEAIY 369
Cdd:cd04951 289 VVATDAGGVAEVV--GDHNYVVPVSDPQLLAEKIKEIFDMSDEERDILGNKNEYIAKNFSINTIVNEWERLY 358
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
11-367 |
7.10e-34 |
|
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: 129.67 E-value: 7.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 11 PSVGGSGVVGTELGKQLAERGHEIHFIT----SGLPFRLNkVYPNIYFHEVT---VNQYSVFQYPPYDLALASKMAEVAQ 83
Cdd:cd03800 18 ADTGGQNVYVLELARALAELGYQVDIFTrrisPADPEVVE-IAPGARVIRVPagpPEYLPKEELWPYLEEFADGLLRFIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 84 RESL--DILHVHYAIPHAICAYLAKQMigeRIKIVTTLHGTDIT---VLGSDPSLNNLIRFGIEQ-----SDVVTAVSHS 153
Cdd:cd03800 97 REGGryDLIHSHYWDSGLVGALLARRL---GVPLVHTFHSLGRVkyrHLGAQDTYHPSLRITAEEqileaADRVIASTPQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 154 LIDETHELVKPNKD-IQTVYNFIDERVYF--KRNMSQLKkEYGISESEKVLIHISNFRKVKRVQDVVQAFAKVAKE-VDA 229
Cdd:cd03800 174 EADELISLYGADPSrINVVPPGVDLERFFpvDRAEARRA-RLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELrELA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 230 KLLLVG-------DGPEFcTILQIVKNLHIEDRVLFLG--KQDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIG 300
Cdd:cd03800 253 NLVLVGgpsddplSMDRE-ELAELAEELGLIDRVRFPGrvSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVA 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446690964 301 TRVGGIPEVIQHGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESVYEQFRSEKIVSQYEA 367
Cdd:cd03800 332 TAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQLLT 398
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
79-368 |
1.04e-32 |
|
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: 125.64 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 79 AEVAQRESLDILHVHYAIPHAICAYLAKQMigeRIKIVTTLHGTDITV----LGSDPSLNN----LIRFGIEQSDVVTAV 150
Cdd:cd05844 74 LGGAAGLAPALVHAHFGRDGVYALPLARAL---GVPLVVTFHGFDITTsrawLAASPGWPSqfqrHRRALQRPAALFVAV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 151 SHSLIDETHELVKPNKDIQTVYNFIDERVYFKRNmsqlkkeygISESEKVLIHISNFRKVKRVQDVVQAFAKVA-KEVDA 229
Cdd:cd05844 151 SGFIRDRLLARGLPAERIHVHYIGIDPAKFAPRD---------PAERAPTILFVGRLVEKKGCDVLIEAFRRLAaRHPTA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 230 KLLLVGDGPEFCTILQIVKNLhieDRVLFLGKQ--DNVAELLAMSDLMLLLS------EKESFGLVLLEAMACGVPCIGT 301
Cdd:cd05844 222 RLVIAGDGPLRPALQALAAAL---GRVRFLGALphAEVQDWMRRAEIFCLPSvtaasgDSEGLGIVLLEAAACGVPVVSS 298
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446690964 302 RVGGIPEVIQHGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESVYEQFRSEKIVSQYEAI 368
Cdd:cd05844 299 RHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFDIRVQTAKLEAI 365
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
5-366 |
1.24e-32 |
|
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: 125.92 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 5 IGITCYPSVGGSGVVGTELGKQLAERGHEIHFITSGLPFRLNKVYPNIYFHEVTVNQYSVFQYPPYDLALASKMAE---- 80
Cdd:cd03794 5 ISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGATETKDGIRVIRVKLGPIKKNGLIRRLLNylsf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 81 --------VAQRESLDILHVhYAIPH--AICAYLAKQMIGerIKIVttLHGTDITV-------LGSDPSLNNLIRFG--- 140
Cdd:cd03794 85 alaallklLVREERPDVIIA-YSPPItlGLAALLLKKLRG--APFI--LDVRDLWPeslialgVLKKGSLLKLLKKLerk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 141 -IEQSDVVTAVSHSLIDETHELVKPNKDIQTVYNFIDERvYFKRNMSQLKKEYGISESEKVLIHISNFRKVKRVQDVVQA 219
Cdd:cd03794 160 lYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLE-EFKPPPKDELRKKLGLDDKFVVVYAGNIGKAQGLETLLEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 220 FAKVAKEVDAKLLLVGDGPEFCTILQIVKNLHIeDRVLFLGKQ--DNVAELLAMSDLMLL-LSEKESFGLV----LLEAM 292
Cdd:cd03794 239 AERLKRRPDIRFLFVGDGDEKERLKELAKARGL-DNVTFLGRVpkEEVPELLSAADVGLVpLKDNPANRGSspskLFEYM 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446690964 293 ACGVPCIGTRVGGIPEVIQHGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESVYEQFRSEKIVSQYE 366
Cdd:cd03794 318 AAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRLL 391
|
|
| stp2 |
TIGR03088 |
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ... |
59-373 |
1.86e-32 |
|
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.
Pssm-ID: 132132 [Multi-domain] Cd Length: 374 Bit Score: 125.22 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 59 VNQYSVFQYPPYDLALASKMAEVAQRESLDILHVH--YAIPHAICAYLAkqmiGERIKIVTTlHGTDITVL-GSDPSLNN 135
Cdd:TIGR03088 54 VAFYALHKQPGKDVAVYPQLYRLLRQLRPDIVHTRnlAALEAQLPAALA----GVPARIHGE-HGRDVFDLdGSNWKYRW 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 136 LIRFGIEQSDVVTAVSHSLIDETHELVK--PNKdIQTVYNFIDERVYFKRNM--SQLKKEYGISESEKVLIHISNFRKVK 211
Cdd:TIGR03088 129 LRRLYRPLIHHYVAVSRDLEDWLRGPVKvpPAK-IHQIYNGVDTERFHPSRGdrSPILPPDFFADESVVVGTVGRLQAVK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 212 RVQDVVQAFAKVAKEV-----DAKLLLVGDGPEFCTILQIVKNLHIEDRVLFLGKQDNVAELLAMSDLMLLLSEKESFGL 286
Cdd:TIGR03088 208 DQPTLVRAFALLVRQLpegaeRLRLVIVGDGPARGACEQMVRAAGLAHLVWLPGERDDVPALMQALDLFVLPSLAEGISN 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 287 VLLEAMACGVPCIGTRVGGIPEVIQHGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESVYEQFRSEKIVSQYE 366
Cdd:TIGR03088 288 TILEAMASGLPVIATAVGGNPELVQHGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARAEQQFSINAMVAAYA 367
|
....*..
gi 446690964 367 AIYYDIL 373
Cdd:TIGR03088 368 GLYDQLL 374
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
4-369 |
2.80e-32 |
|
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: 123.94 E-value: 2.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 4 KIGITCYP--SVGGSGVVGTE-----LGKQLAERGHEIHFITSGLPF---RLNKVYPNIYFHEVTVNqysvfqypPYDLA 73
Cdd:cd03802 1 RIAQVSPPrgPVPPGKYGGTElvvsaLTEGLVRRGHEVTLFAPGDSHtsaPLVAVIPRALRLDPIPQ--------ESKLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 74 LASKMAEVAQR-ESLDILHVHyaIPHAICAYLAkqmiGERIKIVTTLHGTDITVLGSDPSLNNLIRFgieqsdvvTAVSH 152
Cdd:cd03802 73 ELLEALEVQLRaSDFDVIHNH--SYDWLPPFAP----LIGTPFVTTLHGPSIPPSLAIYAAEPPVNY--------VSISD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 153 SLIDETHELvkpnKDIQTVYNFIDERVYFKRNmsqlkkeygisESEKVLIHISNFRKVKRVQDVVqafaKVAKEVDAKLL 232
Cdd:cd03802 139 AQRAATPPI----DYLTVVHNGLDPADYRFQP-----------DPEDYLAFLGRIAPEKGLEDAI----RVARRAGLPLK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 233 LVG---DGPEFCTILQivknLHIEDRVLFLG--KQDNVAELLAMSDLMLLLSE-KESFGLVLLEAMACGVPCIGTRVGGI 306
Cdd:cd03802 200 IAGkvrDEDYFYYLQE----PLPGPRIEFIGevGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGL 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446690964 307 PEVIQHGETGYLCevgDTTGVANQAIQLLknEEFHRnmgERARESVYEQFRSEKIVSQYEAIY 369
Cdd:cd03802 276 PEVIQHGETGFLV---DSVEEMAEAIANI--DRIDR---AACRRYAEDRFSAARMADRYEALY 330
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
78-369 |
2.95e-30 |
|
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: 120.90 E-value: 2.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 78 MAEVAQRE--SLDILHVH---YAiphAICAYLAKQMIGerIKIVTTLHGT-----DITVLGS---DPSLNNL-IRF---- 139
Cdd:cd03813 163 KLAIAADDlpEADLYHSVstgYA---GLLGALARHRRG--IPFLLTEHGIytrerKIEILQStwiMGYIKKLwIRFferl 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 140 ---GIEQSDVVTAVSH--SLIDEthELVKPNKDIQTVYNFIDERVYfkrnmsqlkKEYGISESEKVLIHISNFRKVKRVQ 214
Cdd:cd03813 238 gklAYQQADKIISLYEgnRRRQI--RLGADPDKTRVIPNGIDIQRF---------APAREERPEKEPPVVGLVGRVVPIK 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 215 DVV---QAFAKVAKEV-DAKLLLVG---DGPEF---CtiLQIVKNLHIEDRVLFLGKQdNVAELLAMSDLMLLLSEKESF 284
Cdd:cd03813 307 DVKtfiRAFKLVRRAMpDAEGWLIGpedEDPEYaqeC--KRLVASLGLENKVKFLGFQ-NIKEYYPKLGLLVLTSISEGQ 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 285 GLVLLEAMACGVPCIGTRVGGIPEVI-----QHGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESVYEQFRSE 359
Cdd:cd03813 384 PLVILEAMASGVPVVATDVGSCRELIygaddALGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLE 463
|
330
....*....|
gi 446690964 360 KIVSQYEAIY 369
Cdd:cd03813 464 GMIDSYRKLY 473
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
141-356 |
3.53e-30 |
|
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: 118.96 E-value: 3.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 141 IEQSDVvtAVSHslideTHELVKPNKDIQTVY--NFIDERVYFKRNMSQ------LKKEYGISESEKVLIHISNFRKVKR 212
Cdd:cd03792 139 IEGYDL--FVFH-----PPEFVPPQVPPPKFYipPSIDPLSGKNKDLSPadiryyLEKPFVIDPERPYILQVARFDPSKD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 213 VQDVVQAFAKV-AKEVDAKLLLVG----DGPEFCTILQIVKNLHIEDR---VLFLGKQD---NVaeLLAMSDLMLLLSEK 281
Cdd:cd03792 212 PLGVIDAYKLFkRRAEEPQLVICGhgavDDPEGSVVYEEVMEYAGDDHdihVLRLPPSDqeiNA--LQRAATVVLQLSTR 289
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446690964 282 ESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYLCEVGDttGVANQAIQLLKNEEFHRNMGERARESVYEQF 356
Cdd:cd03792 290 EGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVE--GAAVRILRLLTDPELRRKMGLAAREHVRDNF 362
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
3-362 |
1.16e-29 |
|
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: 117.38 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 3 LKIGITCYPSVGGSGVVGTELGKQLAERGHEIHFITSGLpfRLNKVYPNIYFHEVtvnqysvfQYPPYDLALASKMAEVA 82
Cdd:cd03795 3 LHVFKFYYPDIGGIEQVIYDLAEGLKKKGIEVDVLCFSK--EKETPEKEENGIRI--------HRVKSFLNVASTPFSPS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 83 -------QRESLDILHVHYAIPHAICAYLakqMIGERIKIVTTLHgTDITVLGS-----DPSLNNLIRfgieQSDVVTAV 150
Cdd:cd03795 73 yikrfkkLAKEYDIIHYHFPNPLADLLLF---FSGAKKPVVVHWH-SDIVKQKKllklyKPLMTRFLR----RADRIIAT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 151 SHSLIDETHELVKPNKDIQTVYNFIDERVYFKRNMSQL--KKEYGIsesEKVLIHISNFRKVKRVQDVVQAfakvAKEVD 228
Cdd:cd03795 145 SPNYVETSPTLREFKNKVRVIPLGIDKNVYNIPRVDFEniKREKKG---KKIFLFIGRLVYYKGLDYLIEA----AQYLN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 229 AKLLLVGDGPEFCTILQIVKnLHIEDRVLFLGKQDNV--AELLAMSDLMLLLS--EKESFGLVLLEAMACGVPCIGTRVG 304
Cdd:cd03795 218 YPIVIGGEGPLKPDLEAQIE-LNLLDNVKFLGRVDDEekVIYLHLCDVFVFPSvlRSEAFGIVLLEAMMCGKPVISTNIG 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446690964 305 -GIPEVIQHGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESVYEQFRSEKIV 362
Cdd:cd03795 297 tGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFEELFTAEKMK 355
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
133-365 |
3.59e-28 |
|
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: 112.39 E-value: 3.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 133 LNNLIRFGIEQSDVVTAVshslIDETHElvkPNKDIQTVYNfIDERVYFKRNMS--QLKKEYGISESEKV-LIHISNFRK 209
Cdd:cd04949 100 IKNFYKYVFENLNKYDAI----IVSTEQ---QKQDLSERFN-KYPPIFTIPVGYvdQLDTAESNHERKSNkIITISRLAP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 210 VKRVQDVVQAFAKVAKEV-DAKLLLVGDGPEFCTILQIVKNLHIEDRVLFLGKQDNVAELLAMSDLMLLLSEKESFGLVL 288
Cdd:cd04949 172 EKQLDHLIEAVAKAVKKVpEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTL 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446690964 289 LEAMACGVPCIGTRVG-GIPEVIQHGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESVyEQFRSEKIVSQY 365
Cdd:cd04949 252 MEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIA-EKYSTENVMEKW 328
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
85-340 |
5.32e-28 |
|
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: 112.77 E-value: 5.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 85 ESLDILHVHYAIPHAICAYLAKQMiGERIKIVTTlHGTDITVLGSDPSLNNLIRFGIEQ-SDVVTAVSH----SLIDEth 159
Cdd:cd03812 79 EKYDIVHVHGSSSNGIILLLAAKA-GVPVRIAHS-HNTKDSSIKLRKIRKNVLKKLIERlSTKYLACSEdageWLFGE-- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 160 elvKPNKDIQTVYNFIDERVY-FKRNMSQLKKEYGISESEKVLIHISNFRKVKRVQDVVQAFAKVAKEV-DAKLLLVGDG 237
Cdd:cd03812 155 ---VENGKFKVIPNGIDIEKYkFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNpNVKLVLVGEG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 238 PEFCTILQIVKNLHIEDRVLFLGKQDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGY 317
Cdd:cd03812 232 ELKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITNNVEFL 311
|
250 260
....*....|....*....|...
gi 446690964 318 LCEVGDTTGvANQAIQLLKNEEF 340
Cdd:cd03812 312 PLNETPSTW-AEKILKLIKRKRR 333
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
8-367 |
1.29e-27 |
|
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: 111.65 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 8 TCYP--SVGGSGVVGTELGKQLAERGHEIHFITSG----LPFRLNKVYPNIYFHEVTVNQ-------YSVFQYppYDLAL 74
Cdd:cd03823 7 SLYPpqRVGGAEISVHDLAEALVAEGHEVAVLTAGvgppGQATVARSVVRYRRAPDETLPlalkrrgYELFET--YNPGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 75 ASKMAEVAQRESLDILHVHYAIP-HAICAYLAKQMigeRIKIVTTLHGTDITVLGSDPSLNNlirfgieqSDVVTAVSHS 153
Cdd:cd03823 85 RRLLARLLEDFRPDVVHTHNLSGlGASLLDAARDL---GIPVVHTLHDYWLLCPRQFLFKKG--------GDAVLAPSRF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 154 LIDeTHElvkpnkdiqtvYNFIDE-RVYFKRNMSQL---KKEYGISESEK-VLIHISNFRKVKRVQDVVQAFAKVAKEvD 228
Cdd:cd03823 154 TAN-LHE-----------ANGLFSaRISVIPNAVEPdlaPPPRRRPGTERlRFGYIGRLTEEKGIDLLVEAFKRLPRE-D 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 229 AKLLLVGDGPEfctiLQIVKnLHIEDRVLFLGK--QDNVAELLAMSDLMLLLSE-KESFGLVLLEAMACGVPCIGTRVGG 305
Cdd:cd03823 221 IELVIAGHGPL----SDERQ-IEGGRRIAFLGRvpTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGG 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446690964 306 IPEVIQHGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESVYEQFRSEKIVSQYEA 367
Cdd:cd03823 296 IAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAEEYLKLYRD 357
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
136-319 |
2.44e-27 |
|
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: 108.26 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 136 LIRFGIEQSDVVTAVSHSLIDETHELVKPNKDIQTVYNFID-ERVYFKRNMSQLKKEYGISESEKVLIHISNFRKVKRVQ 214
Cdd:cd01635 47 LKKLLELKPDVVHAHSPHAAALAALLAARLLGIPIVVTVHGpDSLESTRSELLALARLLVSLPLADKVSVGRLVPEKGID 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 215 DVVQAFAKVAKEV-DAKLLLVGDGPEFCTILQIVKNLHIEDRVLFLGKQ---DNVAELLAMSDLMLLLSEKESFGLVLLE 290
Cdd:cd01635 127 LLLEALALLKARLpDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLvddEVLELLLAAADVFVLPSRSEGFGLVLLE 206
|
170 180
....*....|....*....|....*....
gi 446690964 291 AMACGVPCIGTRVGGIPEVIQHGETGYLC 319
Cdd:cd01635 207 AMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
11-366 |
3.93e-27 |
|
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: 110.54 E-value: 3.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 11 PSVGGSGVVGTELGKQLAERGHEIHFITSGLPFRLNKVYPNIYFHEVTVNQYSV--FQYPPYDLALASKMAEVAQRESL- 87
Cdd:cd03821 11 PKAGGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVEENGRYIPPQDGFASIplLRQGAGRTDFSPGLPNWLRRNLRe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 88 -DILHVHyAI--PHAicAYLAKQMIGERIKIVTTLHGT-DITVLGSDPSLNNLIRFGIE-----QSDVVTAVSHSLIDET 158
Cdd:cd03821 91 yDVVHIH-GVwtYTS--LAACKLARRRGIPYVVSPHGMlDPWALQQKHWKKRIALHLIErrnlnNAALVHFTSEQEADEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 159 HELVKPNKdIQTVYNFIDERVYFKRNMsqLKKEYGISESEKVLIHISNFRKVKRVQDVVQAFAKVAKE-VDAKLLLVG-D 236
Cdd:cd03821 168 RRFGLEPP-IAVIPNGVDIPEFDPGLR--DRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQgRDWHLVIAGpD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 237 GPEFCTILQIVKNLHIEDRVLFLGK--QDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGe 314
Cdd:cd03821 245 DGAYPAFLQLQSSLGLGDRVTFTGPlyGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG- 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446690964 315 TGYLCEVGDTTgVANQAIQLLKNEEFHRNMGERARESVY--EQFRSEKIVSQYE 366
Cdd:cd03821 324 CGVVVDPNVSS-LAEALAEALRDPADRKRLGEMARRARQveENFSWEAVAGQLG 376
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
4-367 |
8.60e-27 |
|
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: 109.37 E-value: 8.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 4 KIGITCYPSVGGSGVVGT---ELGKQLAERGHEIHFITSGLPFRLNKVYPNIYFHEVTVNQYSVFQYPPYDLALASKMae 80
Cdd:cd03809 1 KILIDGRSLAQRLTGIGRytrELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQIL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 81 VAQRESLDILHV-HYAIPHAICAYlakqmigeriKIVTTLHgtDITVL----GSDPSLNNLIRFG----IEQSDVVTAVS 151
Cdd:cd03809 79 LPKKDKPDLLHSpHNTAPLLLKGC----------PQVVTIH--DLIPLrypeFFPKRFRLYYRLLlpisLRRADAIITVS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 152 HSLIDE-THELVKPNKDIQTVYNFIDERVYFKRNMSQLKKEYGISEseKVLIHISNFRKVKRVQDVVQAFAKVAKEV-DA 229
Cdd:cd03809 147 EATRDDiIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLPE--PYFLYVGTLEPRKNHERLLKAFALLKKQGgDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 230 KLLLVG-DGPEFCTILQIVKNLHIEDRVLFLGK--QDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGI 306
Cdd:cd03809 225 KLVIVGgKGWEDEELLDLVKKLGLGGRVRFLGYvsDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVL 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446690964 307 PEVIqhGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESVyEQFRSEKIVSQYEA 367
Cdd:cd03809 305 PEVA--GDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERA-KKFSWEKTAEKTLE 362
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
27-364 |
7.37e-25 |
|
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: 103.68 E-value: 7.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 27 LAERGHEIHfITSGLPFRLNKVYPNiyfhevtvnqysVFQYPPYDLALASKMAEVAQRESLDILHVHYAIPHAICAyLAK 106
Cdd:cd03799 24 LIDRGHEVD-IYAVNPGDLVKRHPD------------VEKYNVPSLNLLYAIVGLNKKGAYDIIHCQFGPLGALGA-LLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 107 QMIGERIKIVTTLHGTDITVLGSDPSlNNLIRFGIEQSDVVTAVSHSLIDETHELVKPNKDIQTVYNFID-ERVYFKrnM 185
Cdd:cd03799 90 RLKVLKGKLVTSFRGYDISMYVILEG-NKVYPQLFAQGDLFLPNCELFKHRLIALGCDEKKIIVHRSGIDcNKFRFK--P 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 186 SQLKKEYGISesekvLIHISNFRKVKRVQDVVQAFAKVA-KEVDAKLLLVGDGPEFCTILQIVKNLHIEDRVLFLG--KQ 262
Cdd:cd03799 167 RYLPLDGKIR-----ILTVGRLTEKKGLEYAIEAVAKLAqKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGwkPQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 263 DNVAELLAMSDLMLLLS------EKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYLCEVGDTTGVANQAIQLLK 336
Cdd:cd03799 242 EEIIEILDEADIFIAPSvtaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIE 321
|
330 340
....*....|....*....|....*...
gi 446690964 337 NEEFHRNMGERARESVYEQFRSEKIVSQ 364
Cdd:cd03799 322 HPAIWPEMGKAGRARVEEEYDINKLNDE 349
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
14-176 |
3.34e-23 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 94.91 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 14 GGSGVVGTELGKQLAERGHEIHFITSGLPFRLNKVYPNIyfHEVTVNQYSVFQYPPYDLALASKMAEVAQRESLDILHVH 93
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRV--VRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 94 YAIPHAICAYLAKqmIGERIKIVTTLHGTDITVLGSDPSL-------NNLIRFGIEQSDVVTAVSHSLIDETHELVK-PN 165
Cdd:pfam13439 79 SPFPLGLAALAAR--LRLGIPLVVTYHGLFPDYKRLGARLsplrrllRRLERRLLRRADRVIAVSEAVADELRRLYGvPP 156
|
170
....*....|.
gi 446690964 166 KDIQTVYNFID 176
Cdd:pfam13439 157 EKIRVIPNGVD 167
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
199-352 |
5.00e-23 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 100.17 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 199 KVLIHISNFRKVKRVQDVVQAFAKVAkevDAKLLLVGDGPEFCTILQIVKNLhiedRVLFLG--KQDNVAELLAMSDLML 276
Cdd:PLN02871 264 PLIVYVGRLGAEKNLDFLKRVMERLP---GARLAFVGDGPYREELEKMFAGT----PTVFTGmlQGDELSQAYASGDVFV 336
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446690964 277 LLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVI---QHGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESV 352
Cdd:PLN02871 337 MPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEV 415
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
254-367 |
2.88e-16 |
|
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: 79.71 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 254 DRVLFLGK--QDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYLCEVGDTTGVANQA 331
Cdd:cd03818 281 ERVHFVGKvpYDQYVRLLQLSDAHVYLTYPFVLSWSLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAV 360
|
90 100 110
....*....|....*....|....*....|....*.
gi 446690964 332 IQLLKNEEFHRNMGERARESVYEQFRSEKIVSQYEA 367
Cdd:cd03818 361 LELLEDPDRAAALRRAARRTVERSDSLDVCLARYLA 396
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
164-371 |
4.83e-16 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 78.68 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 164 PNKDIQTVYNFIDERVYFKRNMSQLKKEYGISESEKVLIHISNFRKVKRVQDVVQAFAKVAKEVD-AKLLLVGD------ 236
Cdd:PRK15484 159 PNADISIVPNGFCLETYQSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSnLKLVVVGDptassk 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 237 ---GPEFCTILQIVKnlHIEDRVLFLGKQ--DNVAELLAMSDLMLLLSE-KESFGLVLLEAMACGVPCIGTRVGGIPEVI 310
Cdd:PRK15484 239 gekAAYQKKVLEAAK--RIGDRCIMLGGQppEKMHNYYPLADLVVVPSQvEEAFCMVAVEAMAAGKPVLASTKGGITEFV 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446690964 311 QHGETGY-LCEVGDTTGVANQAIQLLKNEEFHrNMGERARESVYEQFRSEKIVSQYEAIYYD 371
Cdd:PRK15484 317 LEGITGYhLAEPMTSDSIISDINRTLADPELT-QIAEQAKDFVFSKYSWEGVTQRFEEQIHN 377
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
211-359 |
2.16e-15 |
|
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.
Pssm-ID: 340833 [Multi-domain] Cd Length: 356 Bit Score: 76.55 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 211 KRVQDVVQAFAKVAKevdaKLLLVGDGPEFCTILQIVKNlhiedRVLFLGKQDN--VAELLAMSDLMLLLSEkESFGLVL 288
Cdd:cd03804 212 KRIDLAVEAFNELPK----RLVVIGDGPDLDRLRAMASP-----NVEFLGYQPDevLKELLSKARAFVFAAE-EDFGIVP 281
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446690964 289 LEAMACGVPCIGTRVGGIPEVIQHGETGYLcevgdttgVANQAIQLLK--NEEFHRNMG----ERARESVyEQFRSE 359
Cdd:cd03804 282 VEAQACGTPVIAFGKGGALETVRPGPTGIL--------FGEQTVESLKaaVEEFEQNFDrfkpQAIRANA-ERFSRA 349
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
21-151 |
3.69e-15 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 71.58 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 21 TELGKQLAERGHEIHFITSGLPFRLNKVYPNIYFHEVTVNQYSVFQYppydlALASKMAEVAQRESLDILHVHYAIPHAI 100
Cdd:pfam13477 14 LRWADALADRGYDVHVISSKGPAKDELIAEGIHVHRLKVPRKGPLGY-----LKAFRLKKLIKKIKPDVVHVHYAKPYGL 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446690964 101 CAYLAKQmIGERIKIVTTLHGTDITVLGSDPSLN-NLIRFGIEQSDVVTAVS 151
Cdd:pfam13477 89 LAGLAAR-LSGFPPVVLSAWGLDVYKFPNKSRLKkLLLKLNLKKATLIISTS 139
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
10-373 |
1.29e-14 |
|
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: 74.58 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 10 YPSVGGSGVVGTELGKQLAERGHE-------------IHFITSGLpfrlnKVY--PNIYFHEVTV--NQYSVFqypPYdl 72
Cdd:cd03796 10 YPNLGGVETHIYQLSQCLIKRGHKvivithaygnrvgVRYLTNGL-----KVYylPFKVFYNQSTlpTLFSTF---PL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 73 alaskMAEVAQRESLDILHVHYAIphaicAYLAkqmiGERIKIVTTLhgtDITVLGSDPSL-----------NNLIRFGI 141
Cdd:cd03796 80 -----LRNILIRERIQIVHGHQAF-----SSLA----HEALFHARTL---GLKTVFTDHSLfgfadassiltNKLLRFSL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 142 EQSDVVTAVSHSLIDETH--ELVKPNKdIQTVYNFIDERVyFKRNMSQLKKEygisesEKVLIHISN--FRK-VKRVQDV 216
Cdd:cd03796 143 ADIDHVICVSHTSKENTVlrASLDPRI-VSVIPNAVDSSD-FTPDPSKPDPN------KITIVVISRlvYRKgIDLLVGI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 217 VQAFAKvaKEVDAKLLLVGDGPEFCTILQIVKNLHIEDRVLFLG--KQDNVAELLAMSDLMLLLSEKESFGLVLLEAMAC 294
Cdd:cd03796 215 IPRICK--KHPNVRFIIGGDGPKRIELEEMREKYQLQDRVELLGavPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASC 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 295 GVPCIGTRVGGIPEVIQHGETgYLCE--VGDTTGVANQAIQLLKN-----EEFHrnmgerarESVYEQFRSEKIVSQYEA 367
Cdd:cd03796 293 GLLVVSTRVGGIPEVLPPDMI-LLAEpdPEDIVRKLEEAISILRTgkhdpWSFH--------NRVKKMYSWEDVARRTEK 363
|
....*.
gi 446690964 368 IYYDIL 373
Cdd:cd03796 364 VYDRIL 369
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
248-356 |
1.30e-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: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 248 KNLHIEDRVLFL----GKQDNVaeLLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYLCEvGD 323
Cdd:cd03805 274 ELLNVEDQVLFLrsisDSQKEQ--LLSSALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCE-PT 350
|
90 100 110
....*....|....*....|....*....|...
gi 446690964 324 TTGVANQAIQLLKNEEFHRNMGERARESVYEQF 356
Cdd:cd03805 351 PEAFAEAMLKLANDPDLADRMGAAGRKRVKEKF 383
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
211-348 |
1.88e-12 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 68.52 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 211 KRVQDVVQAFAKVAKE-VDAKLLLVGDGPEFCTILQIVKNLHIEDRVLFLGKQDNVAELLAMSDLMLLLSEKESFGLVLL 289
Cdd:PRK15179 530 KRPFLWVEAAQRFAAShPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQFNAFLLLSRFEGLPNVLI 609
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446690964 290 EAMACGVPCIGTRVGGIPEVIQHGETGYLCEVGDTT------GVANQAIQLLKNEEFHRNMGERA 348
Cdd:PRK15179 610 EAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTapdvaeALARIHDMCAADPGIARKAADWA 674
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
14-173 |
8.19e-12 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 62.80 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 14 GGSGVVGTELGKQLAERGHEIHFITSGLPfrlnkvYPNIYFHEVTVNQYSV----FQYPPYDLALASKMAEVAQRESLDI 89
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGP------PGRPELVGDGVRVHRLpvppRPSPLADLAALRRLRRLLRAERPDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 90 LHVHYAiPHAICAYLAKQMIGerIKIVTTLHGTDITVLGS--DPSLNNLIRFGIEQSDVVTAVSHSLIDETHELVKPNKD 167
Cdd:pfam13579 75 VHAHSP-TAGLAARLARRRRG--VPLVVTVHGLALDYGSGwkRRLARALERRLLRRADAVVVVSEAEAELLRALGVPAAR 151
|
....*.
gi 446690964 168 IQTVYN 173
Cdd:pfam13579 152 VVVVPN 157
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
149-343 |
3.44e-11 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 63.96 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 149 AVSHSLIDETHELVKPNKDIQTVYNFIDERVYFkrnMSQLKKEygiseSEKVLIHISN--FRKVKRVQDVVQAFAKVAKE 226
Cdd:PRK09922 139 AISSGIKEQMMARGISAQRISVIYNPVEIKTII---IPPPERD-----KPAVFLYVGRlkFEGQKNVKELFDGLSQTTGE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 227 VdaKLLLVGDGPEFCTILQIVKNLHIEDRVLFLGKQDNVAELLAMS----DLMLLLSEKESFGLVLLEAMACGVPCIGTR 302
Cdd:PRK09922 211 W--QLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQPWEVVQQKiknvSALLLTSKFEGFPMTLLEAMSYGIPCISSD 288
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446690964 303 -VGGIPEVIQHGETGYLCEVGDTTGVAnQAIQLLKNEEFHRN 343
Cdd:PRK09922 289 cMSGPRDIIKPGLNGELYTPGNIDEFV-GKLNKVISGEVKYQ 329
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
246-339 |
1.35e-10 |
|
GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.
Pssm-ID: 411604 [Multi-domain] Cd Length: 489 Bit Score: 62.64 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 246 IVKNLHIEDRVLFLGKQdNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQH--------GETGY 317
Cdd:NF038011 359 LVASLGLQDKVKFLGFQ-KIDDLLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQLIEGldeedralGAAGE 437
|
90 100
....*....|....*....|..
gi 446690964 318 LCEVGDTTGVANQAIQLLKNEE 339
Cdd:NF038011 438 VVAIADPQALARAALDLLRDPQ 459
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
9-371 |
5.76e-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: 60.65 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 9 CYP--SVGGSGVVGTELGKQLAERGHEIHFIT-----------SGLPFRLNKVYPN-----IYFHEVTVN---------- 60
Cdd:cd03791 9 VAPfaKTGGLGDVAGALPKALAKLGHDVRVILprygqipdeldGYLRVLGLEVKVGgrgeeVGVFELPVDgvdyyfldnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 61 ----QYSVFQYPPYD-------LALASKMA-EVAQRESL--DILHVH-YaipHA--ICAYLA---KQMIGERIKIVTTLH 120
Cdd:cd03791 89 effdRPGLPGPPGYDypdnaerFAFFSRAAlELLRRLGFqpDIIHANdW---HTalVPAYLKtryRGPGFKKIKTVFTIH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 121 -----GT----DITVLGSDPSLN-----------NLIRFGIEQSDVVTAVSHSLIDE--THE--------LVKPNKDIQT 170
Cdd:cd03791 166 nlayqGLfpldTLAELGLPPELFhidglefygqiNFLKAGIVYADRVTTVSPTYAKEilTPEygegldgvLRARAGKLSG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 171 VYNFIDERV-------YFKRNMS------------QLKKEYGISESEK--VLIHISNFRKVKRVQDVVQAFAKVAKEvDA 229
Cdd:cd03791 246 ILNGIDYDEwnpatdkLIPANYSandlegkaenkaALQKELGLPVDPDapLFGFVGRLTEQKGVDLILDALPELLEE-GG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 230 KLLLVGDGPEfctilqivknlHIEDRVLFLGKQ--DNVA-----------ELLAMSDLMLLLSEKESFGLVLLEAMACGV 296
Cdd:cd03791 325 QLVVLGSGDP-----------EYEQAFRELAERypGKVAvvigfdealahRIYAGADFFLMPSRFEPCGLVQMYAMRYGT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 297 PCIGTRVGG-----IPEVIQHGE-TGYLCEVGDTTGVANQ---AIQLLKNEEFHRNMGERARESvyeQFRSEKIVSQYEA 367
Cdd:cd03791 394 LPIVRRTGGladtvFDYDPETGEgTGFVFEDYDAEALLAAlrrALALYRNPELWRKLQKNAMKQ---DFSWDKSAKEYLE 470
|
....
gi 446690964 368 IYYD 371
Cdd:cd03791 471 LYRS 474
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
84-369 |
1.53e-09 |
|
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: 58.94 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 84 RESLDILHVHY--------AIPHAICAYLAKQMigeriKIVTTLHgtdiTVLGSDPSLNNLIRFGIEQSDVVTAV-SHSL 154
Cdd:cd03822 73 FKKPDVVHIQHefgifggkYGLYALGLLLHLRI-----PVITTLH----TVLDLSDPGKQALKVLFRIATLSERVvVMAP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 155 IDEthelvkpnKDIQTVYNFIDERV---------YFKRNMSQLKKEYGiSESEKVLIHISNFRKVKRVQDVVQAFAKVAK 225
Cdd:cd03822 144 ISR--------FLLVRIKLIPAVNIeviphgvpeVPQDPTTALKRLLL-PEGKKVILTFGFIGPGKGLEILLEALPELKA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 226 EV-DAKLLLVG-DGPE------FCTILQIVKNLHIEDRVLFLGK---QDNVAELLAMSDLMLL--LSEKESFGLVLLEAM 292
Cdd:cd03822 215 EFpDVRLVIAGeLHPSlaryegERYRKAAIEELGLQDHVDFHNNflpEEEVPRYISAADVVVLpyLNTEQSSSGTLSYAI 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446690964 293 ACGVPCIGTRVGGIpEVIQHGETGYLCEVGDTTGVANQAIQLLKNEEFHRNMGERAREsvYEQFRS-EKIVSQYEAIY 369
Cdd:cd03822 295 ACGKPVISTPLRHA-EELLADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYA--YARAMTwESIADRYLRLF 369
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
201-318 |
6.57e-08 |
|
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.
Pssm-ID: 340854 [Multi-domain] Cd Length: 401 Bit Score: 54.00 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 201 LIHISNFRKVKRVQ---DVVQAFAKVAKEVDAKLLLVGDGPEFCTILQIVKNLHIEDRVLFLGKQDN--VAELLAMS--D 273
Cdd:cd04946 227 LVSCSSIVPVKRIDliiETLNSLCVAHPSICISWTHIGGGPLKERLEKLAENKLENVKVNFTGEVSNkeVKQLYKENdvD 306
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446690964 274 LMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYL 318
Cdd:cd04946 307 VFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLL 351
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
230-365 |
4.76e-07 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 51.62 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 230 KLLLVGDGPEFCTILQIVKNLHIEDRVLFLGKQDNVAELLAMSDLMLLLSEKESFGLVLLEAMACGVPCIGTRVGGIPEV 309
Cdd:PRK15490 431 RFVLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGSAEC 510
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446690964 310 IQHGETGYLCEVGDTTGV------ANQAIQLLKNEEfhrNMGERARESVYEQFRSEKIVSQY 365
Cdd:PRK15490 511 FIEGVSGFILDDAQTVNLdqacryAEKLVNLWRSRT---GICQQTQSFLQERFTVEHMVGTF 569
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
282-367 |
1.83e-06 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 45.67 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 282 ESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGYLCEvgDTTGVANQAIQLLKNEEFHRNMGERARESVYEQFRSEKI 361
Cdd:pfam13524 10 DSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERVLAEHTYAHR 87
|
....*.
gi 446690964 362 VSQYEA 367
Cdd:pfam13524 88 AEQLLD 93
|
|
| MSMEG_0565_glyc |
TIGR04047 |
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ... |
17-297 |
5.45e-06 |
|
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: 47.78 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 17 GVVGT-ELGKQLAERGHEIHFITSGLP--FRlnkvypniyFHEVTVN-QYSVFQYPPYDLAlaskmAEVAQR--ESLDIL 90
Cdd:TIGR04047 14 GVVHTlELAEALTALGHDVTVWALAADgfGF---------FRDPPCAvRLVPVAPAPGDTD-----AMVEQRiaRSIDHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 91 HVH----YAIPHA---IC--AYLAKQMIGERIKIVTTLHGTDITvlgSDPSLNNLIRFGIEQSDVVTAVSHSLIDE---T 158
Cdd:TIGR04047 80 RAHfargFDVVHAqdcISgnALATLRAEGLIPGFVRTVHHLDDF---DDPRLAACQERAIVEADAVLCVSAAWAAElraE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 159 HELvkpnkDIQTVYNFIDERVY---FKRNMSQLKKEYGISESEKVLIhISNFRKVKRVQDVVQAFAKVAKEV-DAKLLLV 234
Cdd:TIGR04047 157 WGI-----DATVVPNGVDAARFspaADAADAALRRRLGLRGGPYVLA-VGGIEPRKNTIDLLEAFALLRARRpQAQLVIA 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446690964 235 G-------DG--PEFctiLQIVKNLHIE-DRVLFLGKQDNVA--ELLAMSDLMLLLSEKESFGLVLLEAMACGVP 297
Cdd:TIGR04047 231 GgatlfdyDAyrREF---RARAAELGVDpGPVVITGPVPDADlpALYRCADAFAFPSLKEGFGLVVLEALASGIP 302
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
211-352 |
2.18e-05 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 46.52 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 211 KRVQDVVQAFAKVAKEV-DAKLLLVGDGPEFC--TILQIVKNLHIE-DRVLFLGKQDNvAELLAM---SDLMLllsekES 283
Cdd:COG3914 481 KITPEVFALWARILKAVpNSVLLLKGGGLPEAreRLRAAAAARGVDpDRLIFLPRLPR-AEHLARyalADLFL-----DT 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 284 F----GLVLLEAMACGVPCIgTRVG---------------GIPEVIQHGETGYLcevgdttgvaNQAIQLLKNEEFHRNM 344
Cdd:COG3914 555 FpyngGTTTLEALWMGVPVV-TLAGetfasrvgaslltalGLPELIATSEEEYV----------ALAVALATDPELLAAL 623
|
....*...
gi 446690964 345 GERARESV 352
Cdd:COG3914 624 RAKLRERR 631
|
|
| PLN00142 |
PLN00142 |
sucrose synthase |
282-317 |
2.56e-05 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 46.13 E-value: 2.56e-05
10 20 30
....*....|....*....|....*....|....*.
gi 446690964 282 ESFGLVLLEAMACGVPCIGTRVGGIPEVIQHGETGY 317
Cdd:PLN00142 677 EAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGF 712
|
|
| GT33_ALG1-like |
cd03816 |
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ... |
215-342 |
7.20e-05 |
|
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.
Pssm-ID: 340843 [Multi-domain] Cd Length: 411 Bit Score: 44.57 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 215 DVVQAFAKVAKEVDA---KLLLV--GDGPEFCTILQIVKNLHIED---RVLFLGKQDnVAELLAMSDLMLLLSEKESfGL 286
Cdd:cd03816 248 DALKAYESSAATEPAllpSLLCIitGKGPLKEMYLELIKELKLKKvtiRTPWLSAED-YPRLLASADLGVCLHTSSS-GL 325
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 287 VL----LEAMACGVPCIGTRVGGIPEVIQHGETGYLceVGDTTGVANQAIQLLKNEEFHR 342
Cdd:cd03816 326 DLpmkvVDMFGCGLPVCAMDFKCIGELVKHGVNGLV--FGDSEELAEQLIDLLSDFDRGK 383
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
196-360 |
3.67e-04 |
|
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: 42.21 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 196 ESEKVLIHISNFRKVKRVQDVVQAFAKVAKE------VDAKLLLVG----DGPE--FCTILQIVKNLHIEDRVLFlgKQD 263
Cdd:cd03806 235 TRENQILSIAQFRPEKNHPLQLRAFAELLKRlpesirSNPKLVLIGscrnEEDKerVEALKLLAKELILEDSVEF--VVD 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446690964 264 nvaelLAMSDLMLLLS---------EKESFGLVLLEAMACGVPCIGTRVGG----IPEVIQHGETGYLCEVGDTTGVANQ 330
Cdd:cd03806 313 -----APYEELKELLStasiglhtmWNEHFGIGVVEYMAAGLIPLAHASAGplldIVVPWDGGPTGFLASTPEEYAEAIE 387
|
170 180 190
....*....|....*....|....*....|
gi 446690964 331 AIQLLKNEEfhRNMGERARESVYEQFRSEK 360
Cdd:cd03806 388 KILTLSEEE--RLQRREAARSSAERFSDEE 415
|
|
| KdtA |
COG1519 |
3-deoxy-D-manno-octulosonic-acid transferase [Cell wall/membrane/envelope biogenesis]; ... |
288-355 |
8.44e-04 |
|
3-deoxy-D-manno-octulosonic-acid transferase [Cell wall/membrane/envelope biogenesis]; 3-deoxy-D-manno-octulosonic-acid transferase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 441128 [Multi-domain] Cd Length: 424 Bit Score: 41.28 E-value: 8.44e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446690964 288 LLEAMACGVPCI-GTRVGGIPEV----IQHGEtgyLCEVGDTTGVANQAIQLLKNEEFHRNMGERARESVYEQ 355
Cdd:COG1519 337 PLEPAALGKPVLfGPHTFNFAEAaellIAAGA---AIQVADAEELAAAVLALLADPELRAAMGAAARAVVEAN 406
|
|
| YfcH |
COG1090 |
NAD dependent epimerase/dehydratase family enzyme [General function prediction only]; |
4-38 |
1.37e-03 |
|
NAD dependent epimerase/dehydratase family enzyme [General function prediction only];
Pssm-ID: 440707 [Multi-domain] Cd Length: 298 Bit Score: 40.05 E-value: 1.37e-03
10 20 30
....*....|....*....|....*....|....*
gi 446690964 4 KIGITcypsvGGSGVVGTELGKQLAERGHEIHFIT 38
Cdd:COG1090 1 KILIT-----GGTGFIGSALVAALLARGHEVVVLT 30
|
|
| |
