|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
11-406 |
0e+00 |
|
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: 728.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 11 RILMVSDFFYPNFGGVESHIYYLSQCLLKLGHKVVVLTHAYEKRSGVRYMTGGLKVYYLPWKPFLMQNTLPTFYGTLPII 90
Cdd:cd03796 1 RICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVITHAYGNRVGVRYLTNGLKVYYLPFKVFYNQSTLPTLFSTFPLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 91 RTILIREKISLVHGHQAFSTLCHEALMHARTMGYKVVFTDHSLYGFADAGSIHMNKVLQFTLADVSQAICVSHTSKENTV 170
Cdd:cd03796 81 RNILIRERIQIVHGHQAFSSLAHEALFHARTLGLKTVFTDHSLFGFADASSILTNKLLRFSLADIDHVICVSHTSKENTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 171 LRSGLPPEKVFVIPNAVDTAMFKPAPERLSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFVVGGDGPKRVRLE 250
Cdd:cd03796 161 LRASLDPRIVSVIPNAVDSSDFTPDPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 251 EMREKHSLQDRVEMLGAVPHAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPEVLPDDMVVLAKPDP 330
Cdd:cd03796 241 EMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPDP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1585744225 331 IDMVQAIQKAIAMLP--KIDPQDMHLRMKKLYSWHDVAKRTEIVYDRALRCSNQSLLERLSRYLTCGAWAGKLFCLVM 406
Cdd:cd03796 321 EDIVRKLEEAISILRtgKHDPWSFHNRVKKMYSWEDVARRTEKVYDRILSTPNRPFLERLKRYYNCGPIAGKIFCLLA 398
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
11-373 |
1.35e-64 |
|
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: 212.01 E-value: 1.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 11 RILMVSDFFYPNFGGVESHIYYLSQCLLKLGHKVVVLTHAYEKRSGVRYMTGGLKVYYLPWKPFLMQNTLptfygtLPII 90
Cdd:cd03801 1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRL------LREL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 91 RTILIREKISLVHGHQAFSTLCHEALMHARtmGYKVVFTDHSL-YGFADAGSIHMNKVLQFTLADVSQA---ICVSHTSK 166
Cdd:cd03801 75 RPLLRLRKFDVVHAHGLLAALLAALLALLL--GAPLVVTLHGAePGRLLLLLAAERRLLARAEALLRRAdavIAVSEALR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 167 ENTVLRSGLPPEKVFVIPNAVDTAMFKPAPER---LSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFV-VGGD 242
Cdd:cd03801 153 DELRALGGIPPEKIVVIPNGVDLERFSPPLRRklgIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLViVGGD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 243 GPKRVRLEEMreKHSLQDRVEMLGAVPHAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPEVLPDDM 322
Cdd:cd03801 233 GPLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGE 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 323 VVLAKP--DPIDMVQAIQKAIAmlpkiDPQDM-------HLRMKKLYSWHDVAKRTEIVY 373
Cdd:cd03801 311 GGLVVPpdDVEALADALLRLLA-----DPELRarlgraaRERVAERFSWERVAERLLDLY 365
|
|
| PIGA |
pfam08288 |
PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol ... |
49-138 |
7.41e-51 |
|
PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol n-acetylglucosaminyltransferase proteins. These proteins are involved in GPI anchor biosynthesis and are associated with disease the paroxysmal nocturnal haemoglobinuria.
Pssm-ID: 400541 Cd Length: 90 Bit Score: 166.66 E-value: 7.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 49 HAYEKRSGVRYMTGGLKVYYLPWKPFLMQNTLPTFYGTLPIIRTILIREKISLVHGHQAFSTLCHEALMHARTMGYKVVF 128
Cdd:pfam08288 1 HAYGDRTGVRYLTNGLKVYYVPFLVIYRQSTFPTVFGTFPLFRNILLRERIDIVHGHGSFSTLAHEAILHARTMGLKTVF 80
|
90
....*....|
gi 1585744225 129 TDHSLYGFAD 138
Cdd:pfam08288 81 TDHSLFGFAD 90
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
12-319 |
1.06e-45 |
|
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: 161.75 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 12 ILMVSDFFYPnfGGVESHIYYLSQCLLKLGHKVVVLTHAYEKRSGVRYMTGGLKVYYLPWkpflmqntLPTFYGTLPIIR 91
Cdd:cd03819 1 ILMLTPALEI--GGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGIGLPGLKVPL--------LRALLGNVRLAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 92 TILiREKISLVHGH-QAFSTLCHEAlmhARTMGYKVVFTDHSLYgfadAGSIHMNKVLQFTLADVSQAICVSHTSKENTV 170
Cdd:cd03819 71 LIR-RERIDLIHAHsRAPAWLGWLA---SRLTGVPLVTTVHGSY----LATYHPKDFALAVRARGDRVIAVSELVRDHLI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 171 LRSGLPPEKVFVIPNAVDTAMFKPAPE-------RLSTDEIVIVVISRLVYRKGADLLVEVIPEVcRKYPNVRFVVGGDG 243
Cdd:cd03819 143 EALGVDPERIRVIPNGVDTDRFPPEAEaeeraqlGLPEGKPVVGYVGRLSPEKGWLLLVDAAAEL-KDEPDFRLLVAGDG 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1585744225 244 PKRVRLEEMREKHSLQDRVEMLGavPHAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPEVLP 319
Cdd:cd03819 222 PERDEIRRLVERLGLRDRVTFTG--FREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVV 295
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
18-376 |
7.45e-41 |
|
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: 149.45 E-value: 7.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 18 FFYPN--FGGVESHIYYLSQCLLKLGHKVVVLTHAYEKrSGVRYMTGGLKVYYLPWKPFLMQntLPTFYGTLPIIRTI-- 93
Cdd:cd03798 6 NIYPNanSPGRGIFVRRQVRALSRRGVDVEVLAPAPWG-PAAARLLRKLLGEAVPPRDGRRL--LPLKPRLRLLAPLRap 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 94 --------LIREKISLVHGHQAFSTLChEALMHARTMGYKVVFTDHS--LYGFADAGSIHmnKVLQFTLADVSQAICVSH 163
Cdd:cd03798 83 slakllkrRRRGPPDLIHAHFAYPAGF-AAALLARLYGVPYVVTEHGsdINVFPPRSLLR--KLLRWALRRAARVIAVSK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 164 TSKEnTVLRSGLPPEKVFVIPNAVDTAMFKPAPERL--STDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFVVGG 241
Cdd:cd03798 160 ALAE-ELVALGVPRDRVDVIPNGVDPARFQPEDRGLglPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 242 DGPKRVRLEEMREKHSLQDRVEMLGAVPHAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPEVLPDD 321
Cdd:cd03798 239 DGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDP 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 322 MV-VLAKPDPID-MVQAIQKAIAmlPKIDPQDMHLRMKKL---YSWHDVAKRTEIVYDRA 376
Cdd:cd03798 319 ETgLLVPPGDADaLAAALRRALA--EPYLRELGEAARARVaerFSWVKAADRIAAAYRDV 376
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
22-346 |
6.21e-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: 138.60 E-value: 6.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 22 NFGGVESHIYYLSQCLLKLGHKVVV--LTHAYEKrsGVRYMTGGLKVYYLPWKPFLMqntlptfYGTLPIIRTILIREKI 99
Cdd:cd03807 10 NVGGAETMLLRLLEHMDKSRFEHVVisLTGDGVL--GEELLAAGVPVVCLGLSSGKD-------PGVLLRLAKLIRKRNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 100 SLVHGHQA----FSTLCheALMHArtmGYKVVFTDHSLYGFADAgSIHMNKVLQFtLADVSQA-ICVSHTSKEnTVLRSG 174
Cdd:cd03807 81 DVVHTWMYhadlIGGLA--AKLAG---GVKVIWSVRSSNIPQRL-TRLVRKLCLL-LSKFSPAtVANSSAVAE-FHQEQG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 175 LPPEKVFVIPNAVDTAMFKPAPER---------LSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFVVGGDGPK 245
Cdd:cd03807 153 YAKNKIVVIYNGIDLFKLSPDDASrararrrlgLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 246 RVRLEEMREKHSLQDRVEMLGAVPHakVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPEVLPD--DMV 323
Cdd:cd03807 233 RPNLERLLLELGLEDRVHLLGERSD--VPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDgtGFL 310
|
330 340
....*....|....*....|...
gi 1585744225 324 VLAKpDPIDMVQAIQKAIAMLPK 346
Cdd:cd03807 311 VPAG-DPQALADAIRALLEDPEK 332
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
11-376 |
3.60e-35 |
|
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: 133.94 E-value: 3.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 11 RILMVSDFFYPNFGGVESHIYYLSQCLLKLGHKVVVLT----HAYEKRSGVRYMTGGLKVYYLPWKPflmqntLPTFYGT 86
Cdd:cd03817 1 KIAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITpsdpGAEDEEEVVRYRSFSIPIRKYHRQH------IPFPFKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 87 LPIIRtiLIREKISLVHGHQAFST--LcheALMHARTMGYKVVFTDHSLY---------GFADAGSIHMNKVLQFtLADV 155
Cdd:cd03817 75 AVIDR--IKELGPDIIHTHTPFSLgkL---GLRIARKLKIPIVHTYHTMYedylhyipkGKLLVKAVVRKLVRRF-YNHT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 156 SQAICVSHTSKEntVLRSGLPPEKVFVIPNAVDTAMFKPAPE-------RLSTDEIVIVVISRLVYRKGADLLVEVIPEV 228
Cdd:cd03817 149 DAVIAPSEKIKD--TLREYGVKGPIEVIPNGIDLDKFEKPLNteerrklGLPPDEPILLYVGRLAKEKNIDFLLRAFAEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 229 cRKYPNVRFVVGGDGPKRVRLEEMREKHSLQDRVEMLGAVPHAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVS 308
Cdd:cd03817 227 -KKEPNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVA 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1585744225 309 TRVGGVPEVLPD-DMVVLAKPDPIDMVQAIQKAIAMLpkidpqDMHLRMKKLY----SWHDVAKRTEIVYDRA 376
Cdd:cd03817 306 AKDPAASELVEDgENGFLFEPNDETLAEKLLHLRENL------ELLRKLSKNAeisaREFAFAKSVEKLYEEV 372
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
11-351 |
5.42e-35 |
|
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: 133.25 E-value: 5.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 11 RILmvsdFFYP--NFGGVESHIYYLSQCLLKLGHKVVVLTHAYEkrsGVRYMTGGLKVYYLPWKPFLMQNTLPTFYGTLP 88
Cdd:cd03811 1 KIL----FVIPslSGGGAERVLLNLANALDKRGYDVTLVLLRDE---GDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 89 IIRTILIREKISLVHGHQAFSTLCheaLMHARTMGYKVVFTDHSLYGfaDAGSIHMNKVLQFTLADVSQAI-CVSHTSKE 167
Cdd:cd03811 74 KLKRILKRAKPDVVISFLGFATYI---VAKLAAARSKVIAWIHSSLS--KLYYLKKKLLLKLKLYKKADKIvCVSKGIKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 168 NTVLRSGLPPEKVFVIPNAVD----TAMFKPAPERLSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFVVGGDG 243
Cdd:cd03811 149 DLIRLGPSPPEKIEVIYNPIDidriRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 244 PKRVRLEEMREKHSLQDRVEMLGAVP-------HAKVqsvlisghiFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPE 316
Cdd:cd03811 229 PLREELEKLAKELGLAERVIFLGFQSnpypylkKADL---------FVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPRE 299
|
330 340 350
....*....|....*....|....*....|....*.
gi 1585744225 317 VLPD-DMVVLAKPDPIDmvQAIQKAIAMLPKIDPQD 351
Cdd:cd03811 300 ILDDgENGLLVPDGDAA--ALAGILAALLQKKLDAA 333
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
11-370 |
1.01e-34 |
|
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: 132.88 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 11 RILMVSDFFYPNFGGVESHIYYLSQCLLKLGHKVVVLTHA--YEKRSGVRYMTGGLKVYYLPWKPFLMQNTLPTFY-GTL 87
Cdd:cd03821 1 KILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGdgYESLVVEENGRYIPPQDGFASIPLLRQGAGRTDFsPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 88 PIIRTILIREkISLVHGHQAFSTLCHEALMHARTMGYKVVFTDHSLYGFADAGSIHMNKVLQFTLAD---VSQAICVSHT 164
Cdd:cd03821 81 PNWLRRNLRE-YDVVHIHGVWTYTSLAACKLARRRGIPYVVSPHGMLDPWALQQKHWKKRIALHLIErrnLNNAALVHFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 165 S-KENTVLRSGLPPEKVFVIPNAVDTAMFKPAPER-----LSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFV 238
Cdd:cd03821 160 SeQEADELRRFGLEPPIAVIPNGVDIPEFDPGLRDrrkhnGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 239 VGG--DGPKRVRLEEMrEKHSLQDRVEMLGAVPHAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGL-LTVSTRVGGVP 315
Cdd:cd03821 240 IAGpdDGAYPAFLQLQ-SSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLpVVITDKCGLSE 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1585744225 316 EVLPDDMVVlAKPDPIDMVQAIQKAIAMlpKIDPQDMHLR------MKKLYSWHDVAKRTE 370
Cdd:cd03821 319 LVEAGCGVV-VDPNVSSLAEALAEALRD--PADRKRLGEMarrarqVEENFSWEAVAGQLG 376
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
101-342 |
1.76e-31 |
|
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: 123.72 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 101 LVHGHQAFSTLchEALMHARTMGYKVVFTDH------SLYGFADAGSIHMNKVLQFTLADVSQA--ICVSHTSKEnTVLR 172
Cdd:cd05844 84 LVHAHFGRDGV--YALPLARALGVPLVVTFHgfdittSRAWLAASPGWPSQFQRHRRALQRPAAlfVAVSGFIRD-RLLA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 173 SGLPPEKVFVIPNAVDTAMFKPAPERLSTDEIVIVviSRLVYRKGADLLVEVIPEVCRKYPNVRFVVGGDGPKRVRLEEM 252
Cdd:cd05844 161 RGLPAERIHVHYIGIDPAKFAPRDPAERAPTILFV--GRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQAL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 253 REKhslQDRVEMLGAVPHAKVQSVLISGHIFLNSSLT------EAFCIAILEAASCGLLTVSTRVGGVPEVLPDDMVVLA 326
Cdd:cd05844 239 AAA---LGRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFL 315
|
250
....*....|....*...
gi 1585744225 327 KP--DPIDMVQAIQKAIA 342
Cdd:cd05844 316 VPegDVDALADALQALLA 333
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
202-341 |
9.09e-31 |
|
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: 116.22 E-value: 9.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 202 DEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFVVGGDGPKRVRLEEMREKHSLQDRVEMLGAVPHAKVQSVLISGH 281
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIAD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1585744225 282 IFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPEVLPD--DMVVLAKPDPIDMVQAIQKAI 341
Cdd:pfam00534 81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDgeTGFLVKPNNAEALAEAIDKLL 142
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
11-378 |
1.83e-28 |
|
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: 115.47 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 11 RILMVSDFFYPNFGGVESHIYYLSQCLLKLGHKVVVLThayeKRSGVRYMTGGLKVYYLPWKPFLMQNTLPTFYGTLPII 90
Cdd:cd03814 1 RIALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVA----PGPFDEAESAEGRVVSVPSFPLPFYPEYRLALPLPRRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 91 RTILIREKISLVHghqaFST---LCHEALMHARTMGYKVVFTDHSL------YGFADAGSIHMNKVLQFTLADVSQAICV 161
Cdd:cd03814 77 RRLIKEFQPDIIH----IATpgpLGLAALRAARRLGLPVVTSYHTDfpeylsYYTLGPLSWLAWAYLRWFHNPFDTTLVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 162 SHTSKEntvLRSGLPPEKVFVIPNAVDTAMFKPA-------PERLSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPn 234
Cdd:cd03814 153 SPSIAR---ELEGHGFERVRLWPRGVDTELFHPSrrdaalrRRLGPPGRPLLLYVGRLAPEKNLEALLDADLPLAASPP- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 235 VRFVVGGDGPKRVRLEEMrekhslQDRVEMLGAVPHAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGV 314
Cdd:cd03814 229 VRLVVVGDGPARAELEAR------GPDVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGP 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1585744225 315 PEVLPDDMV-VLAKP-DPIDMVQAIQkaiAMLpkIDPQDmHLRMKKLYSWHDVAKRTEIVYDRALR 378
Cdd:cd03814 303 RDIVRPGGTgALVEPgDAAAFAAALR---ALL--EDPEL-RRRMAARARAEAERYSWEAFLDNLLD 362
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
11-361 |
1.95e-28 |
|
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: 115.12 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 11 RILMVSDFFYPN-FGGVESHIYYLSQCLLKLGHKVVVLThAYEKRSGVRYMTGGLKVYYLPWKPFLMQNTLPTFY----- 84
Cdd:cd03823 1 KILLVNSLYPPQrVGGAEISVHDLAEALVAEGHEVAVLT-AGVGPPGQATVARSVVRYRRAPDETLPLALKRRGYelfet 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 85 ---GTLPIIRTILIREKISLVHGHqAFSTLCHEALMHARTMGYKVVFTDHSLYGFADagSIHMNKVLQFTLADVSQAIcv 161
Cdd:cd03823 80 ynpGLRRLLARLLEDFRPDVVHTH-NLSGLGASLLDAARDLGIPVVHTLHDYWLLCP--RQFLFKKGGDAVLAPSRFT-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 162 shtskENTVLRSGLPPEKVFVIPNAVdTAMFKPAPERLSTDE-IVIVVISRLVYRKGADLLVEVIPEVcrKYPNVRFVVG 240
Cdd:cd03823 155 -----ANLHEANGLFSARISVIPNAV-EPDLAPPPRRRPGTErLRFGYIGRLTEEKGIDLLVEAFKRL--PREDIELVIA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 241 GDGPkrvrlEEMREKHSLQDRVEMLGAVPHAKVQSVLISGHIFLNSSL-TEAFCIAILEAASCGLLTVSTRVGGVPEVLP 319
Cdd:cd03823 227 GHGP-----LSDERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAELIQ 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1585744225 320 DDM--VVLAKPDPIDMVQAIQKAIAM-----------LPKIDPQDMHLRMKKLYS 361
Cdd:cd03823 302 PGVngLLFAPGDAEDLAAAMRRLLTDpallerlragaEPPRSTESQAEEYLKLYR 356
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
203-342 |
4.32e-28 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 107.98 E-value: 4.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 203 EIVIVVISRLV-YRKGADLLVEVIPEVCRKYPNVRFVVGGDGPKRvRLEEMREKhsLQDRVEMLGAVPHakVQSVLISGH 281
Cdd:pfam13692 1 RPVILFVGRLHpNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEE-ELEELAAG--LEDRVIFTGFVED--LAELLAAAD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1585744225 282 IFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPEVLPDDMVVLAKP-DPIDMVQAIQKAIA 342
Cdd:pfam13692 76 VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGENGLLVPPgDPEALAEAILRLLE 137
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
22-341 |
3.34e-27 |
|
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: 111.53 E-value: 3.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 22 NFGGVESHIYYLSQCLLKLGHKVVVLTHAYEKRSgvRYMTG-GLKVYYLPWK-----PFlmqntlpTFYGTLPIIRTILI 95
Cdd:cd03808 8 VDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLS--DELKElGVKVIDIPILrrginPL-------KDLKALFKLYKLLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 96 REKISLVHGHQA----FSTLcheALMHARtmGYKVVFTDHSLyGFADAGSIHMNKVLQ----FTLADVSQAICVSHTSKE 167
Cdd:cd03808 79 KEKPDIVHCHTPkpgiLGRL---AARLAG--VPKVIYTVHGL-GFVFTEGKLLRLLYLllekLALLFTDKVIFVNEDDRD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 168 NTVLRSGLPPEKVFVIP-NAVDTAMFKPAPERLSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFVVGGDGPKR 246
Cdd:cd03808 153 LAIKKGIIKKKKTVLIPgSGVDLDRFQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 247 VRLEEMREKHSLQDRVEMLGAVPHakVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPE-VLPDDMVVL 325
Cdd:cd03808 233 NPSEILIEKLGLEGRIEFLGFRSD--VPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRElVIDGVNGFL 310
|
330
....*....|....*..
gi 1585744225 326 AKP-DPIDMVQAIQKAI 341
Cdd:cd03808 311 VPPgDVEALADAIEKLI 327
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
11-370 |
1.25e-26 |
|
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: 110.15 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 11 RILMVSDFFYPNFGGVESHIYYLSQCLLKLGHKVVVLTHAYEKRSGVRYMTGGLKVYYLPWKPFLMqntlPTFYGTLPII 90
Cdd:cd03809 1 KILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLW----RELALLRWLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 91 RTILIREKISLVHGhqafstLCHEALMHARtmGYKVVFTDHSL------YGFADAGSIHMNKVLQFTLADVSQAICVSHT 164
Cdd:cd03809 77 ILLPKKDKPDLLHS------PHNTAPLLLK--GCPQVVTIHDLiplrypEFFPKRFRLYYRLLLPISLRRADAIITVSEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 165 SKENTVLRSGLPPEKVFVIPNAVDTAMFKPAPERLSTDEIV-----IVVISRLVYRKGADLLVEVIPEVCRKYPNVRFV- 238
Cdd:cd03809 149 TRDDIIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLlpepyFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVi 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 239 VGGDGPKRVRLEEMREKHSLQDRVEMLGAVPHAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPEVL 318
Cdd:cd03809 229 VGGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVA 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1585744225 319 PDDMVVLAKPDPIDMVQAIQKAIAMLPKID-PQDMHLRMKKLYSWHDVAKRTE 370
Cdd:cd03809 309 GDAALYFDPLDPESIADAILRLLEDPSLREeLIRKGLERAKKFSWEKTAEKTL 361
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
24-370 |
1.42e-24 |
|
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: 104.63 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 24 GGVESHIYYLSQCLLKLGHKVVVLTHAYEKRSGVR-YMTGGLKVYYLPWKP--FLMQNTLPTFYGTLP--IIRTILiREK 98
Cdd:cd03800 21 GGQNVYVLELARALAELGYQVDIFTRRISPADPEVvEIAPGARVIRVPAGPpeYLPKEELWPYLEEFAdgLLRFIA-REG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 99 I--SLVHGHQAFSTLCheALMHARTMGYKVVFTDHSL----YGFADA-GSIHMNKVLQFTLADVSQAICV-SHTSKENTV 170
Cdd:cd03800 100 GryDLIHSHYWDSGLV--GALLARRLGVPLVHTFHSLgrvkYRHLGAqDTYHPSLRITAEEQILEAADRViASTPQEADE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 171 LRS--GLPPEKVFVIPNAVDTAMFKPAPER--------LSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFVVG 240
Cdd:cd03800 178 LISlyGADPSRINVVPPGVDLERFFPVDRAearrarllLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 241 G---DGPK---RVRLEEMREKHSLQDRVEMLGAVPHAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGV 314
Cdd:cd03800 258 GgpsDDPLsmdREELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGL 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1585744225 315 PEVLPDDMV-VLAKP-DPIDMVQAIQKAIAmlpkiDPQDMH-------LRMKKLYSWHDVAKRTE 370
Cdd:cd03800 338 QDIVRDGRTgLLVDPhDPEALAAALRRLLD-----DPALWQrlsraglERARAHYTWESVADQLL 397
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
96-317 |
2.71e-24 |
|
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: 103.59 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 96 REKISLVHGHQAfstLCHE-ALMHARTM---GYKVVFTDH----SLYG----FADAGSIHMNKvlqftlADVSQAicVSH 163
Cdd:cd04962 82 EHKLDVLHAHYA---IPHAsCAYLAREIlgeKIPIVTTLHgtdiTLVGydpsLQPAVRFSINK------SDRVTA--VSS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 164 TSKENTvlRSGLPPEK-VFVIPNAVDTAMFKPAP------ERLST-DEIVIVVISRLVYRKGADLLVEVIPEVCRKYPnV 235
Cdd:cd04962 151 SLRQET--YELFDVDKdIEVIHNFIDEDVFKRKPagalkrRLLAPpDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIP-A 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 236 RFVVGGDGPKRVRLEEMREKHSLQDRVEMLGAVPHakVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVP 315
Cdd:cd04962 228 KLLLVGDGPERVPAEELARELGVEDRVLFLGKQDD--VEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIP 305
|
..
gi 1585744225 316 EV 317
Cdd:cd04962 306 EV 307
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
12-321 |
4.39e-24 |
|
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: 100.17 E-value: 4.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 12 ILMVSDFFYPNFGGVESHIYYLSQCLLKLGHKVVVLTHAYEKrsgvrymtgglkvyylpwkpflmqntlptfygtLPIIR 91
Cdd:cd01635 1 ILLVTGEYPPLRGGLELHVRALARALAALGHEVTVLALLLLA---------------------------------LRRIL 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 92 TILIREKISLVHGHQAFSTLcHEALMHARTMGYKVVFTDHSLYGFADAGSIhmnkvlqftladvsqaicvshtskentvl 171
Cdd:cd01635 48 KKLLELKPDVVHAHSPHAAA-LAALLAARLLGIPIVVTVHGPDSLESTRSE----------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 172 rsglppekvfvipnavdtaMFKPAPERLSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFVVGGDGPKRVRLEE 251
Cdd:cd01635 98 -------------------LLALARLLVSLPLADKVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEA 158
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1585744225 252 MREKHSLQDRVEMLGAVPH-AKVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPEVLPDD 321
Cdd:cd01635 159 LAAALGLLERVVIIGGLVDdEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDG 229
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
24-190 |
7.12e-24 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 97.60 E-value: 7.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 24 GGVESHIYYLSQCLLKLGHKVVVLTHAYEKRSGVRYMTgglkVYYLPWKPFLMQNTLPTFYGTLPIIRTILIREKISLVH 103
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVR----VVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 104 GHQAFStLCHEALMHARTMGYKVVFTDHSLY-------GFADAGSIHMNKVLQFTLADVSQAICVSHTSKENTVLRSGLP 176
Cdd:pfam13439 77 AHSPFP-LGLAALAARLRLGIPLVVTYHGLFpdykrlgARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVP 155
|
170
....*....|....
gi 1585744225 177 PEKVFVIPNAVDTA 190
Cdd:pfam13439 156 PEKIRVIPNGVDLE 169
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
11-342 |
2.91e-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: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 11 RILMVSDFFYPNFGGVESHIYYLSQCLLKLGHKVVVLTHAY-----EKRSGVRYMTGGLKVYYLP----WKPFLMQNTLP 81
Cdd:cd03794 1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPnyplgRIFAGATETKDGIRVIRVKlgpiKKNGLIRRLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 82 TFYGTLPIIRTILIR-EKISLVHGHQAFSTLCHEALMHARTMGYKVVFTDHSLY--GFADAGSIH-------MNKVLQFT 151
Cdd:cd03794 81 YLSFALAALLKLLVReERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLWpeSLIALGVLKkgsllklLKKLERKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 152 LADVSQAICVSHTSKENtVLRSGLPPEKVFVIPNAVDTAMFKPAP------ERLSTDEIVIVVISRLVYRKGADLLVEVI 225
Cdd:cd03794 161 YRLADAIIVLSPGLKEY-LLRKGVPKEKIIVIPNWADLEEFKPPPkdelrkKLGLDDKFVVVYAGNIGKAQGLETLLEAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 226 PEVcRKYPNVRFVVGGDGPKRVRLEEMREKHSLQDrVEMLGAVPHAKVQSVLISGHIFL-----NSSLTEAFCIAILEAA 300
Cdd:cd03794 240 ERL-KRRPDIRFLFVGDGDEKERLKELAKARGLDN-VTFLGRVPKEEVPELLSAADVGLvplkdNPANRGSSPSKLFEYM 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1585744225 301 SCGLLTVSTRVGGVPEVLPDDM--VVLAKPDPIDMVQAIQKAIA 342
Cdd:cd03794 318 AAGKPILASDDGGSDLAVEINGcgLVVEPGDPEALADAILELLD 361
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
24-357 |
5.98e-23 |
|
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: 99.23 E-value: 5.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 24 GGVESHIYYLSQCLLKLGHKVVVLTHAYEKRSGVRYMTGGLKVYYLPWKPFLMQNTLPTFYGTLPIIRTILIREKISLVh 103
Cdd:cd03820 13 GGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYELDDNIKIKNLGDRKYSHFKLLLKYFKKVRRLRKYLKNNKPDVV- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 104 ghqaFSTLCHE-ALMHARTMGYKVVFTDHSLYGFA-DAGSIHMNKVLQFTLADvsqAICVshTSKENTVLRSGLPPEKVF 181
Cdd:cd03820 92 ----ISFRTSLlTFLALIGLKSKLIVWEHNNYEAYnKGLRRLLLRRLLYKRAD---KIVV--LTEADKLKKYKQPNSNVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 182 VIPNAVDTAMFKPAPERLSTdeiVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFVVGGDGPKRVRLEEMREKHSLQDR 261
Cdd:cd03820 163 VIPNPLSFPSEEPSTNLKSK---RILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 262 VEMLGAVphAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVST-RVGGVPEVLpDDMV--VLAKP-DPIDMVQAI 337
Cdd:cd03820 240 VKLLGPT--KNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFdCPTGPSEII-EDGEngLLVPNgDVDALAEAL 316
|
330 340
....*....|....*....|
gi 1585744225 338 QKAIamlpkidpQDMHLRMK 357
Cdd:cd03820 317 LRLM--------EDEELRKK 328
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
11-339 |
3.84e-22 |
|
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: 96.96 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 11 RILMVSDFFYPNFGGVESHIYYLSQCLLKLGHKVVVLTHAYEKrSGVRYMTGGLKVYYLpwKPFLMQNTLPTFYgtLPII 90
Cdd:cd03795 1 KVLHVFKFYYPDIGGIEQVIYDLAEGLKKKGIEVDVLCFSKEK-ETPEKEENGIRIHRV--KSFLNVASTPFSP--SYIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 91 RTILIREKISLVHGHQAFSTLCHEALMHARTMgyKVVFTDHS----------LYgfadagsihmnKVLQF-TLADVSQAI 159
Cdd:cd03795 76 RFKKLAKEYDIIHYHFPNPLADLLLFFSGAKK--PVVVHWHSdivkqkkllkLY-----------KPLMTrFLRRADRII 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 160 CVSHTSKENT-VLRSglPPEKVFVIPNAVDTAmfKPAPERLSTDEI--------VIVVISRLVYRKGADLLVEVIpevcr 230
Cdd:cd03795 143 ATSPNYVETSpTLRE--FKNKVRVIPLGIDKN--VYNIPRVDFENIkrekkgkkIFLFIGRLVYYKGLDYLIEAA----- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 231 KYPNVRFVVGGDGPKRVRLEEMREKHsLQDRVEMLGAVPHAKVQSVLISGHIFLNSSL--TEAFCIAILEAASCGLLTVS 308
Cdd:cd03795 214 QYLNYPIVIGGEGPLKPDLEAQIELN-LLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKPVIS 292
|
330 340 350
....*....|....*....|....*....|....
gi 1585744225 309 TRVG-GVPEVLPDDMVVLAKP--DPIDMVQAIQK 339
Cdd:cd03795 293 TNIGtGVPYVNNNGETGLVVPpkDPDALAEAIDK 326
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
24-371 |
6.32e-22 |
|
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: 96.75 E-value: 6.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 24 GGVESHIYYLSQCLLKLGHKVVVLthayekrsgvrYMTG---------GLKVYYLPwkpflMQNTLPTFYGTLPIIRTIL 94
Cdd:cd04951 12 GGAEKQTVLLADQMFIRGHDVNIV-----------YLTGevevkplnnNIIIYNLG-----MDKNPRSLLKALLKLKKII 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 95 IREKISLVHGHqafstlcheaLMHARTMG---------YKVVFTDHSLygfADAGSIHMnKVLQFT--LADVSQAicVSH 163
Cdd:cd04951 76 SAFKPDVVHSH----------MFHANIFArflrmlypiPLLICTAHNK---NEGGRIRM-FIYRLTdfLCDITTN--VSR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 164 TSKENTVLRSGLPPEKVFVIPNAVDTAMFKPAPER---------LSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPN 234
Cdd:cd04951 140 EALDEFIAKKAFSKNKSVPVYNGIDLNKFKKDINVrlkirnklnLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKND 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 235 VRFVVGGDGPKRVRLEEMREKHSLQDRVEMLGAvpHAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGV 314
Cdd:cd04951 220 FKLLIAGDGPLRNELERLICNLNLVDRVILLGQ--ISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGV 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1585744225 315 PEVLPDDMVVLAKPDPIDMVQAIQKAIAMLPKIdpQDMHLRMKKlyswhDVAKRTEI 371
Cdd:cd04951 298 AEVVGDHNYVVPVSDPQLLAEKIKEIFDMSDEE--RDILGNKNE-----YIAKNFSI 347
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
11-375 |
2.19e-20 |
|
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: 91.58 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 11 RILMVSDFFYP----NFGGVESHIYYLSQCLLKLGHKVVVLThAYEKRSGVRymtgGLKVYYLPWKPFLMQNTlPTFYGT 86
Cdd:cd03802 1 RIAQVSPPRGPvppgKYGGTELVVSALTEGLVRRGHEVTLFA-PGDSHTSAP----LVAVIPRALRLDPIPQE-SKLAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 87 LPIIRTILIREKISLVHGHqafstLCHEALMHARTMGYKVVFTDHslyGFADAgsihmnKVLQFTLADVSQA-ICVSHTS 165
Cdd:cd03802 75 LEALEVQLRASDFDVIHNH-----SYDWLPPFAPLIGTPFVTTLH---GPSIP------PSLAIYAAEPPVNyVSISDAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 166 KENTvlrsgLPPEKVFVIPNAVDTAMFKPAPERlstdEIVIVVISRLVYRKGADLLVEVipevCRKyPNVRFVVGGDGPK 245
Cdd:cd03802 141 RAAT-----PPIDYLTVVHNGLDPADYRFQPDP----EDYLAFLGRIAPEKGLEDAIRV----ARR-AGLPLKIAGKVRD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 246 RVRLEEMREKHsLQDRVEMLGAVPHAKVQSVLISGHIFLNSSL-TEAFCIAILEAASCGLLTVSTRVGGVPEVLPDDMVV 324
Cdd:cd03802 207 EDYFYYLQEPL-PGPRIEFIGEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETG 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1585744225 325 LAKPDPIDMVQAIQKaiamLPKIDPQDMHLRMKKLYSWHDVAKRTEIVYDR 375
Cdd:cd03802 286 FLVDSVEEMAEAIAN----IDRIDRAACRRYAEDRFSAARMADRYEALYRK 332
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
174-320 |
9.71e-20 |
|
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: 90.20 E-value: 9.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 174 GLPPEKVFVIPNAVDTAMFKPAPERLSTDE-IVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFVVGGDGPKRVRLEEM 252
Cdd:cd03799 144 GCDEKKIIVHRSGIDCNKFRFKPRYLPLDGkIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQL 223
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1585744225 253 REKHSLQDRVEMLGAVPHAKVQSVLISGHIFLNSSLT------EAFCIAILEAASCGLLTVSTRVGGVPEVLPD 320
Cdd:cd03799 224 IQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTaadgdqDGPPNTLKEAMAMGLPVISTEHGGIPELVED 297
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
22-304 |
2.12e-19 |
|
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: 89.27 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 22 NFGGVESHIYYLSQCLLKLGHKVVVLTH-----AYEKRsgVRYMtgGLKVYYLPWKpflMQNTLPTFYGTLPIIRtiliR 96
Cdd:cd03812 10 NVGGIETFLMNLYRKLDKSKIEFDFLATsddkgEYDEE--LEEL--GGKIFYIPPK---KKNIIKYFIKLLKLIK----K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 97 EKISLVHGHQAFSTLCHEALmhARTMGYKV-VFTDHSlygfADAGSIHMNKVLQFTLADV-----SQAICVSHtsKENTV 170
Cdd:cd03812 79 EKYDIVHVHGSSSNGIILLL--AAKAGVPVrIAHSHN----TKDSSIKLRKIRKNVLKKLierlsTKYLACSE--DAGEW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 171 LRSGLPPEKVFVIPNAVDTAMFKPAPER--------LSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFVVGGD 242
Cdd:cd03812 151 LFGEVENGKFKVIPNGIDIEKYKFNKEKrrkrrkllILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGE 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1585744225 243 GPKRVRLEEMREKHSLQDRVEMLGAVphAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGL 304
Cdd:cd03812 231 GELKEKIKEKVKELGLEDKVIFLGFR--NDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGL 290
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
171-339 |
1.90e-17 |
|
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: 84.31 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 171 LRSGLPPEKVFVIPNAVDTAMFKPAPERLSTDE-IVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRF-VVGGDGPKRVR 248
Cdd:cd03813 260 IRLGADPDKTRVIPNGIDIQRFAPAREERPEKEpPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGwLIGPEDEDPEY 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 249 LEEMRE--KH-SLQDRVEMLGavpHAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPEVLPDDM--- 322
Cdd:cd03813 340 AQECKRlvASlGLENKVKFLG---FQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELIYGADdal 416
|
170 180
....*....|....*....|.
gi 1585744225 323 ----VVLAKPDPIDMVQAIQK 339
Cdd:cd03813 417 gqagLVVPPADPEALAEALIK 437
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
281-378 |
1.95e-14 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 69.63 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 281 HIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPEVLPDDMV-VLAKP-DPIDMVQAIQKAIAmlpkiDPQDM------ 352
Cdd:COG0438 22 DVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETgLLVPPgDPEALAEAILRLLE-----DPELRrrlgea 96
|
90 100
....*....|....*....|....*..
gi 1585744225 353 -HLRMKKLYSWHDVAKRTEIVYDRALR 378
Cdd:COG0438 97 aRERAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
170-338 |
2.40e-14 |
|
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: 73.91 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 170 VLRSGL-PPEKVFVIPNAVDTAMFKP-----APERL--STDEIVIVVISRLV--YRKGADLLVEVipevCRKYPNVR--- 236
Cdd:cd03825 152 VRRSPLlKGLPVVVIPNGIDTEIFAPvdkakARKRLgiPQDKKVILFGAESVtkPRKGFDELIEA----LKLLATKDdll 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 237 -FVVGGDGPKRVRLE-EMREKHSLQDRVEMLgavphakvqSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGV 314
Cdd:cd03825 228 lVVFGKNDPQIVILPfDIISLGYIDDDEQLV---------DIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGS 298
|
170 180
....*....|....*....|....*..
gi 1585744225 315 PEVLpDDMVV--LAKP-DPIDMVQAIQ 338
Cdd:cd03825 299 PEIV-QHGVTgyLVPPgDVQALAEAIE 324
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
24-186 |
6.09e-12 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 63.57 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 24 GGVESHIYYLSQCLLKLGHKVVVLTHAYEkRSGVRYMTGGLKVYYLPWKPFLMQNTLPTFYGTLpiiRTILIREKISLVH 103
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGP-PGRPELVGDGVRVHRLPVPPRPSPLADLAALRRL---RRLLRAERPDVVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 104 GHQAFSTLcheALMHART-MGYKVVFTDHSL---YGFADAGSIhMNKVLQFTLADVSQAICVSHTSKEnTVLRSGLPPEK 179
Cdd:pfam13579 77 AHSPTAGL---AARLARRrRGVPLVVTVHGLaldYGSGWKRRL-ARALERRLLRRADAVVVVSEAEAE-LLRALGVPAAR 151
|
....*..
gi 1585744225 180 VFVIPNA 186
Cdd:pfam13579 152 VVVVPNG 158
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
178-362 |
9.40e-12 |
|
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: 66.33 E-value: 9.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 178 EKVFVIPNAVDTAMFKPAPErlSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFV---VGGdGPKRVRLEEMRE 254
Cdd:cd04946 201 EKIFVSRLGVSDKEQYSKVK--KEGDLRLVSCSSIVPVKRIDLIIETLNSLCVAHPSICISwthIGG-GPLKERLEKLAE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 255 KHSLQDRVEMLGAVPHAKVQSVLI--SGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPEVLPDDMVVL---AKPD 329
Cdd:cd04946 278 NKLENVKVNFTGEVSNKEVKQLYKenDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLlldKDPT 357
|
170 180 190
....*....|....*....|....*....|....
gi 1585744225 330 PIDMVQAIQKAIamlpkIDPQDMH-LRMKKLYSW 362
Cdd:cd04946 358 PNEIVSSIMKFY-----LDGGDYKtMKISARECW 386
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
37-321 |
2.28e-10 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 62.42 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 37 LLKLGHKVVVLT---HAYEKRSGVRYMtgGLKVYYLPWkpflmQNTLPTFYGTLPIIRTILIREKISLVH----GHQAFS 109
Cdd:PLN02871 87 LREMGDEVLVVTtdeGVPQEFHGAKVI--GSWSFPCPF-----YQKVPLSLALSPRIISEVARFKPDLIHasspGIMVFG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 110 tlcheALMHARTMGYKVVFTDHS-------LYGFAdAGSIHMNKVLQFTLADVSQAICVSHTSKENTVLRSGLPPEKVFV 182
Cdd:PLN02871 160 -----ALFYAKLLCVPLVMSYHThvpvyipRYTFS-WLVKPMWDIIRFLHRAADLTLVTSPALGKELEAAGVTAANRIRV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 183 IPNAVDTAMFKPA------PERLS---TDEIVIVVISRLVYRKGADLLVEVIpevcRKYPNVRFVVGGDGPKRVRLEEMR 253
Cdd:PLN02871 234 WNKGVDSESFHPRfrseemRARLSggePEKPLIVYVGRLGAEKNLDFLKRVM----ERLPGARLAFVGDGPYREELEKMF 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1585744225 254 EKHslqdRVEMLGAVPHAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPEVLPDD 321
Cdd:PLN02871 310 AGT----PTVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPD 373
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
92-373 |
2.40e-10 |
|
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: 62.02 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 92 TILIREKISLVHGHQAFSTLCHEALMHA----RTMGYKVVFTDHSLYGFADAGSIHMNKVlqFTLADVSQAICVSHTSKE 167
Cdd:cd03822 69 DHLNFKKPDVVHIQHEFGIFGGKYGLYAlgllLHLRIPVITTLHTVLDLSDPGKQALKVL--FRIATLSERVVVMAPISR 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 168 NTVLRSGLPP-EKVFVIPNAVDTAMFKPAP----ERLSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFVVGG- 241
Cdd:cd03822 147 FLLVRIKLIPaVNIEVIPHGVPEVPQDPTTalkrLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGe 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 242 --DGPKRVRLEEMR----EKHSLQDRVEM-LGAVPHAKVQSVLISGHIFL------NSSLTEAFCIAIleaaSCGLLTVS 308
Cdd:cd03822 227 lhPSLARYEGERYRkaaiEELGLQDHVDFhNNFLPEEEVPRYISAADVVVlpylntEQSSSGTLSYAI----ACGKPVIS 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1585744225 309 TRVGGVPEVLPDDMVVLAKPDPIDMVQAIQKAIAMLPKIDpQDMHLRMKKLY---SWHDVAKRTEIVY 373
Cdd:cd03822 303 TPLRHAEELLADGRGVLVPFDDPSAIAEAILRLLEDDERR-QAIAERAYAYAramTWESIADRYLRLF 369
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
172-320 |
6.57e-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: 60.45 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 172 RSGLPPE---KVFVIPNAVDTAMFKPAPE---------RLSTDEIVIVVISRLV--YRkGADLLVEVIPEVCRKYPNVRF 237
Cdd:cd03818 170 RSLFPAAyrdRISVIHDGVDTDRLAPDPAarlrllngtELKAGDPVITYVARNLepYR-GFHVFMRALPRIQARRPDARV 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 238 V-VGGD----GPKRVRLEEMREKHSLQ-----DRVEMLGAVPHAKVQSVL--ISGHIFLnsslTEAFCI--AILEAASCG 303
Cdd:cd03818 249 VvVGGDgvsyGSPPPDGGSWKQKMLAElgvdlERVHFVGKVPYDQYVRLLqlSDAHVYL----TYPFVLswSLLEAMACG 324
|
170
....*....|....*..
gi 1585744225 304 LLTVSTRVGGVPEVLPD 320
Cdd:cd03818 325 CPVIGSDTAPVREVIRD 341
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
135-311 |
1.12e-09 |
|
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: 59.62 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 135 GFADAGSIHMNKVLQFTLADVSQ--AICVS-HTSKENTVLRSGlPPEKVFVIPNAVDTAMFKPApERLSTDEIVIVVISR 211
Cdd:cd04949 91 NNDDPEHSLIKNFYKYVFENLNKydAIIVStEQQKQDLSERFN-KYPPIFTIPVGYVDQLDTAE-SNHERKSNKIITISR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 212 LVYRKGADLLVEVIPEVCRKYPNVRFVVGGDGPKRVRLEEMREKHSLQDRVEMLGAvpHAKVQSVLISGHIFLNSSLTEA 291
Cdd:cd04949 169 LAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGY--HSNLDQEYQDAYLSLLTSQMEG 246
|
170 180
....*....|....*....|
gi 1585744225 292 FCIAILEAASCGLLTVSTRV 311
Cdd:cd04949 247 FGLTLMEAIGHGLPVVSYDV 266
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
182-350 |
1.46e-08 |
|
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: 56.14 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 182 VIPNAVDTAMFKPAPERLStdeiVIVVISRLVYRKGADLLVEVipevCRKYPNvRFVVGGDGPKRVRLEEMrekhsLQDR 261
Cdd:cd03804 182 VIYPPVDTDAFAPAADKED----YYLTASRLVPYKRIDLAVEA----FNELPK-RLVVIGDGPDLDRLRAM-----ASPN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 262 VEMLGAVPHAKVQSVLISGHIFLNSSlTEAFCIAILEAASCGLLTVSTRVGGVPEVLPDDM--VVLAKPDPIDMVQAIQK 339
Cdd:cd03804 248 VEFLGYQPDEVLKELLSKARAFVFAA-EEDFGIVPVEAQACGTPVIAFGKGGALETVRPGPtgILFGEQTVESLKAAVEE 326
|
170
....*....|.
gi 1585744225 340 AIAMLPKIDPQ 350
Cdd:cd03804 327 FEQNFDRFKPQ 337
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
172-370 |
6.52e-08 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 54.41 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 172 RSGLPPEKVFVIPNAVDTAMFKPAPER-------LSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFVVGGD-- 242
Cdd:PRK15484 155 EERLPNADISIVPNGFCLETYQSNPQPnlrqqlnISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGDpt 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 243 ----GPKRVRLEEMRE-KHSLQDRVEMLGAVPHAKVQSVL-ISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPE 316
Cdd:PRK15484 235 asskGEKAAYQKKVLEaAKRIGDRCIMLGGQPPEKMHNYYpLADLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITE 314
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1585744225 317 VLPDDMV--VLAKP-DPIDMVQAIQKAIA--MLPKIDPQDMHLRMKKlYSWHDVAKRTE 370
Cdd:PRK15484 315 FVLEGITgyHLAEPmTSDSIISDINRTLAdpELTQIAEQAKDFVFSK-YSWEGVTQRFE 372
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
179-373 |
4.18e-07 |
|
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: 52.18 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 179 KVFVIPNAVDTAMFKPA-----PERLSTDEI-----------------------VIVVISRLVYRKGADLLVEVIPEVCR 230
Cdd:cd03791 242 KLSGILNGIDYDEWNPAtdkliPANYSANDLegkaenkaalqkelglpvdpdapLFGFVGRLTEQKGVDLILDALPELLE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 231 KypNVRFVVGGDGPKRV--RLEEMREKHslqdrvemlgavphakvqsvliSGHIFLNSSLTEAF--CIailEAAS----- 301
Cdd:cd03791 322 E--GGQLVVLGSGDPEYeqAFRELAERY----------------------PGKVAVVIGFDEALahRI---YAGAdfflm 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 302 ------CGL----------LTVSTRVGG----VPEVLPDDMV----VLAKPDPIDMVQAIQKAIAMlpKIDPQD-MHLR- 355
Cdd:cd03791 375 psrfepCGLvqmyamrygtLPIVRRTGGladtVFDYDPETGEgtgfVFEDYDAEALLAALRRALAL--YRNPELwRKLQk 452
|
250 260
....*....|....*....|
gi 1585744225 356 --MKKLYSWHDVAKRTEIVY 373
Cdd:cd03791 453 naMKQDFSWDKSAKEYLELY 472
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
205-376 |
8.61e-07 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 51.25 E-value: 8.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 205 VIVVISRLVYRKGADLLVEVIPEVCRKypNVRFVVGGDGPKRV--RLEEMREKHSlqDRVemlgAVphakvqsvlisgHI 282
Cdd:COG0297 297 LIGMVSRLTEQKGLDLLLEALDELLEE--DVQLVVLGSGDPEYeeAFRELAARYP--GRV----AV------------YI 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 283 FLNSSLteafciA-ILEAAS-----------CGL----------LTVSTRVGG----VPEVLPDDMV----VLAKPDPID 332
Cdd:COG0297 357 GYDEAL------AhRIYAGAdfflmpsrfepCGLnqmyalrygtVPIVRRTGGladtVIDYNEATGEgtgfVFDEYTAEA 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1585744225 333 MVQAIQKAIAMLPkiDPQDMH-LR---MKKLYSWHDVAKRTEIVYDRA 376
Cdd:COG0297 431 LLAAIRRALALYR--DPEAWRkLQrnaMKQDFSWEKSAKEYLELYREL 476
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
170-374 |
1.62e-06 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 50.42 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 170 VLRSGLPPEKVFVIPNavDTAMFKPAPERLSTDEIVIVVISRLVYRKGADLLVEVIPEVCRKYPNVRFVVGGDGPKRVRL 249
Cdd:PRK15179 486 VVYNGLAPLKSVQDDA--CTAMMAQFDARTSDARFTVGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESV 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 250 EEMREKHSLQDRVEMLGAVPHakVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGVPE---------VLPD 320
Cdd:PRK15179 564 REFAQRLGMGERILFTGLSRR--VGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEavqegvtglTLPA 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1585744225 321 DMVvlAKPDPIDMVQAIQKAIAMLPKIDPQDMHlRMKKLYSWHDVAKRTEIVYD 374
Cdd:PRK15179 642 DTV--TAPDVAEALARIHDMCAADPGIARKAAD-WASARFSLNQMIASTVRCYQ 692
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
172-256 |
1.04e-05 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 47.66 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 172 RSGLPPEKVFVIPNAVDTAMFKPAPERLST---------DEIVIVVISRLVYRK-GADLLVEVIPEVCRKyPNVRFVVGG 241
Cdd:PRK10307 188 EKGVAAEKVIFFPNWSEVARFQPVADADVDalraqlglpDGKKIVLYSGNIGEKqGLELVIDAARRLRDR-PDLIFVICG 266
|
90
....*....|....*.
gi 1585744225 242 DGPKRVRLEEM-REKH 256
Cdd:PRK10307 267 QGGGKARLEKMaQCRG 282
|
|
| COG4641 |
COG4641 |
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]; |
175-342 |
1.40e-05 |
|
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443679 [Multi-domain] Cd Length: 303 Bit Score: 46.85 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 175 LPPEKVFVIPNAVDTAMFKPAPERLSTDEIVIVVISRLVYRKgaDLLVEVIPEvcrkYPNVRFVVGGDGpkrvrleemRE 254
Cdd:COG4641 110 LGARRVFYLPFAADPELHRPVPPEARFRYDVAFVGNYYPDRR--ARLEELLLA----PAGLRLKIYGPG---------WP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 255 KHSLQDRVEMLGAVPHAKVQSVLISGHIFLN--SSLTEAFCIAI--LEAASCGLLTVSTRVGGVPEVL-PDDMVVLAKpD 329
Cdd:COG4641 175 KLALPANVRRGGHLPGEEHPAAYASSKITLNvnRMAASPDSPTRrtFEAAACGAFLLSDPWEGLEELFePGEEVLVFR-D 253
|
170
....*....|...
gi 1585744225 330 PIDMVQAIQKAIA 342
Cdd:COG4641 254 GEELAEKLRYLLA 266
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
174-312 |
1.44e-05 |
|
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: 47.23 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 174 GLPPEKVFVIPNAVDTAMFKPAPERlSTDEIVIVV--ISRLVYRKGADLLVEVIPEVCRKYPNVR-FVVGGDGPKRVRLE 250
Cdd:NF038011 276 GAPPERTRVIPNGIDLPRLAPLRAQ-RPAGIPPVVglIGRVVPIKDIKTFIRAMRTVVRAMPEAEgWIVGPEEEDPAYAA 354
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1585744225 251 EMR---EKHSLQDRVEMLGavpHAKVQSVLIS-GHIFLnSSLTEAFCIAILEAASCGLLTVSTRVG 312
Cdd:NF038011 355 ECRslvASLGLQDKVKFLG---FQKIDDLLPQvGLMVL-SSISEALPLVVLEAFAAGVPVVTTDVG 416
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
161-315 |
1.76e-05 |
|
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: 46.55 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 161 VSHTSKentVLRSGLPPEKvFVIPNAVD-----TAMFKPA--------PERLSTDEIVIVVISRLVYRKGADLLVEVIPE 227
Cdd:cd03792 146 VFHPPE---FVPPQVPPPK-FYIPPSIDplsgkNKDLSPAdiryylekPFVIDPERPYILQVARFDPSKDPLGVIDAYKL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 228 VCRKYPNVRFVVGG----DGPK-RVRLEEMREKHSLQDRVEMLGAVPHAKVQSVLISG-HIFLNSSLTEAFCIAILEAAS 301
Cdd:cd03792 222 FKRRAEEPQLVICGhgavDDPEgSVVYEEVMEYAGDDHDIHVLRLPPSDQEINALQRAaTVVLQLSTREGFGLTVSEALW 301
|
170
....*....|....
gi 1585744225 302 CGLLTVSTRVGGVP 315
Cdd:cd03792 302 KGKPVIATPAGGIP 315
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
187-343 |
1.35e-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: 44.14 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 187 VDTAMFKPAPERLSTDEIVIVVISRlvYR--KGADLLVEVIPEVCRKYP-----NVRFV-VGG----DGPKRVR-LEEMR 253
Cdd:cd03806 221 CDTEELTKLPIDEKTRENQILSIAQ--FRpeKNHPLQLRAFAELLKRLPesirsNPKLVlIGScrneEDKERVEaLKLLA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 254 EKHSLQDRVEMLGAVPHAKVQSVLISGHIFLNSSLTEAFCIAILEAASCGLLTVSTRVGGvPE---VLP-DDMVV--LAK 327
Cdd:cd03806 299 KELILEDSVEFVVDAPYEELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAG-PLldiVVPwDGGPTgfLAS 377
|
170
....*....|....*.
gi 1585744225 328 pDPIDMVQAIQKAIAM 343
Cdd:cd03806 378 -TPEEYAEAIEKILTL 392
|
|
| PHA01630 |
PHA01630 |
putative group 1 glycosyl transferase |
137-372 |
2.89e-04 |
|
putative group 1 glycosyl transferase
Pssm-ID: 164861 Cd Length: 331 Bit Score: 42.85 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 137 ADAGSIHMNKVLQFTLADVSQAICVSHTSKeNTVLRSGLP-PEKVFVIPNAVDTAMFKPAPERLSTdEIVIVVISRLVYR 215
Cdd:PHA01630 77 ADTDAISHTALYFFRNQPVDEIVVPSQWSK-NAFYTSGLKiPQPIYVIPHNLNPRMFEYKPKEKPH-PCVLAILPHSWDR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 216 KGADLLVEVIPEVCRKYPNVRFVVggdgpKRVRLEEMRekhsLQDRVEMLGAVPHAKVQSVLISGHIFLNSSLTEAFCIA 295
Cdd:PHA01630 155 KGGDIVVKIFHELQNEGYDFYFLI-----KSSNMLDPR----LFGLNGVKTPLPDDDIYSLFAGCDILFYPVRGGAFEIP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 296 ILEAASCGLLTVSTRVGGVPE-VLPDDMVVLAK--------PD-PI--------DMVQAIQKAIAMLPKIDPQDMHLRMK 357
Cdd:PHA01630 226 VIEALALGLDVVVTEKGAWSEwVLSNLDVYWIKsgrkpklwYTnPIhvgyfldpDIEDAYQKLLEALANWTPEKKKENLE 305
|
250 260
....*....|....*....|..
gi 1585744225 358 -------KLYSWHDVAKRTEIV 372
Cdd:PHA01630 306 grailyrENYSYNAIAKMWEKI 327
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
205-378 |
7.02e-03 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 38.56 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 205 VIVVISRLVYRKGADLLVEVIPEVCRKypNVRFVVGGDGPKrvRLEE-MRE-KHSLQDRVemlgavphakvqSVLIsGH- 281
Cdd:PRK00654 284 LFAMVSRLTEQKGLDLVLEALPELLEQ--GGQLVLLGTGDP--ELEEaFRAlAARYPGKV------------GVQI-GYd 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585744225 282 ------------IFLNSSLTEAfciaileaasCGL----------LTVSTRVGG----VPEVLPDDMV----VLAKPDPI 331
Cdd:PRK00654 347 ealahriyagadMFLMPSRFEP----------CGLtqlyalrygtLPIVRRTGGladtVIDYNPEDGEatgfVFDDFNAE 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1585744225 332 DMVQAIQKAIAMLpkIDPQDMH-LR---MKKLYSWHDVAKRTEIVYDRALR 378
Cdd:PRK00654 417 DLLRALRRALELY--RQPPLWRaLQrqaMAQDFSWDKSAEEYLELYRRLLG 465
|
|
| |
