|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-389 |
3.86e-73 |
|
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: 235.90 E-value: 3.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 2 KILLAYYRYSPHTNGPSTYIDTLRKSLEEKGHTVDLMSHDKSWlniqiadqqsadkHSMKRELIRRFQTSYTAKYPLWIY 81
Cdd:cd03801 1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPG-------------EPPEELEDGVIVPLLPSLAALLRA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 82 WREMERYSLEQAIKQFDmsgydVIHCHDFMTARAMA-RSKPPHIPLIVSLHNFKYHEAKVTGEFYNKTEREQQYMkmeec 160
Cdd:cd03801 68 RRLLRELRPLLRLRKFD-----VVHAHGLLAALLAAlLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLARAEAL----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 161 lgAMSGDIVAVPCQWLKKQLIQIGVTP-SKIQVIPYGIVKEPFIENENpAKKSRDEGKKTILCPARLVPVKGHRYLIEAL 239
Cdd:cd03801 138 --LRRADAVIAVSEALRDELRALGGIPpEKIVVIPNGVDLERFSPPLR-RKLGIPPDRPVLLFVGRLSPRKGVDLLLEAL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 240 SKLSRERKDFHCLLAG-EGPELEALQRtaEQLDIGAAISFLGKR--HDIPHLMNGSDIIVLPSLHDTFPLVILEGQFSAK 316
Cdd:cd03801 215 AKLLRRGPDVRLVIVGgDGPLRAELEE--LELGLGDRVRFLGFVpdEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGL 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2474149534 317 PILAAEAGGIKEIIKDGADGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMKYWDISVHMASMERLY 389
Cdd:cd03801 293 PVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
9-389 |
2.23e-52 |
|
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: 181.42 E-value: 2.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 9 RYSPHTNGPSTYIDTLRKSLE--EKGHTVDLMSHDKSWLNIQIADQQSADKHSMKRELIRRFQTSYTAKYPLWIYWReme 86
Cdd:cd03798 6 NIYPNANSPGRGIFVRRQVRAlsRRGVDVEVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRAP--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 87 rySLEQAIKQFDMSGYDVIHCH----DFMTARAMARSKppHIPLIVSLHnfkyheakvtGEFYNKTEREQQYMKMEECLG 162
Cdd:cd03798 83 --SLAKLLKRRRRGPPDLIHAHfaypAGFAAALLARLY--GVPYVVTEH----------GSDINVFPPRSLLRKLLRWAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 163 AMSGDIVAVpCQWLKKQLIQIGVTPSKIQVIPYGIvkEPFIENENPAKKSRDEGKKTILCPARLVPVKGHRYLIEALSKL 242
Cdd:cd03798 149 RRAARVIAV-SKALAEELVALGVPRDRVDVIPNGV--DPARFQPEDRGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 243 SRERKDFHCLLAGEGPELEALQRTAEQLDIGAAISFLGK--RHDIPHLMNGSDIIVLPSLHDTFPLVILEGQFSAKPILA 320
Cdd:cd03798 226 AKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRlpHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVA 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2474149534 321 AEAGGIKEIIKDGADGLLVPTGNSDALAEKLRHLLdDDAFRSQLGRRAREKAMKYWDISVHMASMERLY 389
Cdd:cd03798 306 TDVGGIPEVVGDPETGLLVPPGDADALAAALRRAL-AEPYLRELGEAARARVAERFSWVKAADRIAAAY 373
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
23-366 |
1.34e-49 |
|
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: 173.31 E-value: 1.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 23 TLRKSLEEKGHTVDLMSHDKSwlniqiadqQSADKHSMKRELIRRFQTSYTAKYPLWIYWREMErysLEQAIKQFDmsgY 102
Cdd:cd03811 20 NLANALDKRGYDVTLVLLRDE---------GDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILK---LKRILKRAK---P 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 103 DVIHCHDFMTARAMARSKPPHIPLIVSLHNFkyheAKVTGEFYNKTEREQQYMKMeeclgamSGDIVAVpCQWLKKQLIQ 182
Cdd:cd03811 85 DVVISFLGFATYIVAKLAAARSKVIAWIHSS----LSKLYYLKKKLLLKLKLYKK-------ADKIVCV-SKGIKEDLIR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 183 IG-VTPSKIQVIPYGIVKEPFIENENPAKKSRDEGKKTILCPARLVPVKGHRYLIEALSKLSRERKDFHCLLAGEGPELE 261
Cdd:cd03811 153 LGpSPPEKIEVIYNPIDIDRIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 262 ALQRTAEQLDIGAAISFLGKRHDIPHLMNGSDIIVLPSLHDTFPLVILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPT 341
Cdd:cd03811 233 ELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPD 312
|
330 340
....*....|....*....|....*...
gi 2474149534 342 GNSDALAEKLRHLLD---DDAFRSQLGR 366
Cdd:cd03811 313 GDAAALAGILAALLQkklDAALRERLAK 340
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
89-392 |
9.15e-49 |
|
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: 171.73 E-value: 9.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 89 SLEQAIKQFDMSGYDVIHCHDFMTARA------MARSKPphipLIVSLHNfkyheakvTGEFYNKTEReqqYMKMEECLG 162
Cdd:cd03807 67 VLLRLAKLIRKRNPDVVHTWMYHADLIgglaakLAGGVK----VIWSVRS--------SNIPQRLTRL---VRKLCLLLS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 163 AMSGDIVAVpCQWLKKQLIQIGVTPSKIQVIPYGI-----VKEPFIENENPAKKSRDEGKKTILCPARLVPVKGHRYLIE 237
Cdd:cd03807 132 KFSPATVAN-SSAVAEFHQEQGYAKNKIVVIYNGIdlfklSPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 238 ALSKLSRERKDFHCLLAGEGPELEALQRTAEQLDIGAAISFLGKRHDIPHLMNGSDIIVLPSLHDTFPLVILEGQFSAKP 317
Cdd:cd03807 211 AAALLVETHPDLRLLLVGRGPERPNLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLP 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2474149534 318 ILAAEAGGIKEIIKDGAdGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMKYWDisvhMASMERLYLKC 392
Cdd:cd03807 291 VVATDVGGAAELVDDGT-GFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFS----IDAMVRRYETL 360
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
13-373 |
3.58e-47 |
|
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: 166.76 E-value: 3.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 13 HTNGPSTYIDTLRKSLEEKGHTVDLMSHDKSWLNIqiaDQQSADKHSM-KRELIRRfqtsytakyplWIYWREMERYSLE 91
Cdd:cd03819 9 EIGGAETYILDLARALAERGHRVLVVTAGGPLLPR---LRQIGIGLPGlKVPLLRA-----------LLGNVRLARLIRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 92 QAIkqfdmsgyDVIHCHdfmtARAMAR-----SKPPHIPLIVSLHNFkYHEAKVTGEFYNktereqQYMKMeeclgamsG 166
Cdd:cd03819 75 ERI--------DLIHAH----SRAPAWlgwlaSRLTGVPLVTTVHGS-YLATYHPKDFAL------AVRAR--------G 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 167 DIVAVPCQWLKKQLIQ-IGVTPSKIQVIPYGIVKEPFIENENPAKKSR---DEGKKTILCPARLVPVKGHRYLIEALSKL 242
Cdd:cd03819 128 DRVIAVSELVRDHLIEaLGVDPERIRVIPNGVDTDRFPPEAEAEERAQlglPEGKPVVGYVGRLSPEKGWLLLVDAAAEL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 243 sRERKDFHCLLAGEGPELEALQRTAEQLDIGAAISFLGKRHDIPHLMNGSDIIVLPSLHDTFPLVILEGQFSAKPILAAE 322
Cdd:cd03819 208 -KDEPDFRLLVAGDGPERDEIRRLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATD 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2474149534 323 AGGIKEIIKDGADGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAM 373
Cdd:cd03819 287 VGGAREIVVHGRTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAAALTEA 337
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
10-392 |
8.15e-47 |
|
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: 166.69 E-value: 8.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 10 YSPHTNGPSTYIDTLRKSLEEKGHTVDLmshdkswlniqIAdqQSADKHSMKRE-LIRRFQTSYTAKYPlwiyWREMERY 88
Cdd:cd03817 9 YLPQVNGVATSVRNLARALEKRGHEVYV-----------IT--PSDPGAEDEEEvVRYRSFSIPIRKYH----RQHIPFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 89 SLEQAIKQFDMSGYDVIHCHD----FMTARAMARSKppHIPLIVSLHN---------------FKYHEAKVTGEFYNKTe 149
Cdd:cd03817 72 FKKAVIDRIKELGPDIIHTHTpfslGKLGLRIARKL--KIPIVHTYHTmyedylhyipkgkllVKAVVRKLVRRFYNHT- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 150 reqqymkmeeclgamsgDIVAVPCQWLKKQLIQIGVTpSKIQVIPYGIVKEPFIENENPAKKSR---DEGKKTILCPARL 226
Cdd:cd03817 149 -----------------DAVIAPSEKIKDTLREYGVK-GPIEVIPNGIDLDKFEKPLNTEERRKlglPPDEPILLYVGRL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 227 VPVKGHRYLIEALSKLSrERKDFHCLLAGEGPELEALQRTAEQLDIGAAISFLG--KRHDIPHLMNGSDIIVLPSLHDTF 304
Cdd:cd03817 211 AKEKNIDFLLRAFAELK-KEPNIKLVIVGDGPEREELKELARELGLADKVIFTGfvPREELPEYYKAADLFVFASTTETQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 305 PLVILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPTGNsDALAEKLRHLLDDDAFRSQLGRRAREKAMKYWDISvhmaS 384
Cdd:cd03817 290 GLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPND-ETLAEKLLHLRENLELLRKLSKNAEISAREFAFAK----S 364
|
....*...
gi 2474149534 385 MERLYLKC 392
Cdd:cd03817 365 VEKLYEEV 372
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
26-379 |
3.87e-45 |
|
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: 161.61 E-value: 3.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 26 KSLEEKGHTVDLMSHDKSWLNIQIADQQ-SADKHSMKRELIRRFQTSYTakypLWIYWREMERYSleqaikqfdmsgYDV 104
Cdd:cd03808 21 KALVKKGYEVHVIAPDGDKLSDELKELGvKVIDIPILRRGINPLKDLKA----LFKLYKLLKKEK------------PDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 105 IHCHdfmTAR--------AMARSKPPHIPLIVSLHnFKYHEAKVTGEFYNKTEReqqymkmeecLGAMSGDIVAVPCQWL 176
Cdd:cd03808 85 VHCH---TPKpgilgrlaARLAGVPKVIYTVHGLG-FVFTEGKLLRLLYLLLEK----------LALLFTDKVIFVNEDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 177 KKQLIQIGVTPSKIQVIPYGI-VKepfIENENPAKKSRDEGKKTILCPARLVPVKGHRYLIEALSKLSRERKDFHCLLAG 255
Cdd:cd03808 151 RDLAIKKGIIKKKKTVLIPGSgVD---LDRFQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 256 EGPELEALQRTAEQLDIGAAISFLGKRHDIPHLMNGSDIIVLPSLHDTFPLVILEGQFSAKPILAAEAGGIKEIIKDGAD 335
Cdd:cd03808 228 DGELENPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVN 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2474149534 336 GLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMKYWDIS 379
Cdd:cd03808 308 GFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEE 351
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
216-371 |
2.60e-41 |
|
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: 145.11 E-value: 2.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 216 GKKTILCPARLVPVKGHRYLIEALSKLSRERKDFHCLLAGEGPELEALQRTAEQLDIGAAISFLG--KRHDIPHLMNGSD 293
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGfvSDEDLPELLKIAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2474149534 294 IIVLPSLHDTFPLVILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREK 371
Cdd:pfam00534 81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
217-357 |
2.90e-39 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 139.18 E-value: 2.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 217 KKTILCPARLVP-VKGHRYLIEALSKLSRERKDFHCLLAGEGPElEALQRTAEQLDIGaaISFLGKRHDIPHLMNGSDII 295
Cdd:pfam13692 1 RPVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPE-EELEELAAGLEDR--VIFTGFVEDLAELLAAADVF 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2474149534 296 VLPSLHDTFPLVILEGQFSAKPILAAEAGGIKEIIkDGADGLLVPTGNSDALAEKLRHLLDD 357
Cdd:pfam13692 78 VLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLLED 138
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
103-386 |
2.48e-38 |
|
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: 143.36 E-value: 2.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 103 DVIHCH---DFMTARAMARSKPphIPLIVSLHNFKYheAKVTGEFYNKTEREQQYMKMEECLGAMSGDIVAVPcQWLKKQ 179
Cdd:cd05844 83 ALVHAHfgrDGVYALPLARALG--VPLVVTFHGFDI--TTSRAWLAASPGWPSQFQRHRRALQRPAALFVAVS-GFIRDR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 180 LIQIGVTPSKIQVIPYGIVKEPFIENENPAKKsrdegkKTILCPARLVPVKGHRYLIEALSKLSRERKDFHCLLAGEGPE 259
Cdd:cd05844 158 LLARGLPAERIHVHYIGIDPAKFAPRDPAERA------PTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 260 LEALQRTAEQLDigaAISFLGK--RHDIPHLMNGSDIIVLPSL------HDTFPLVILEGQFSAKPILAAEAGGIKEIIK 331
Cdd:cd05844 232 RPALQALAAALG---RVRFLGAlpHAEVQDWMRRAEIFCLPSVtaasgdSEGLGIVLLEAAACGVPVVSSRHGGIPEAIL 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2474149534 332 DGADGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMKYWDISVHMASME 386
Cdd:cd05844 309 DGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFVCEQFDIRVQTAKLE 363
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
14-382 |
7.78e-38 |
|
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: 142.76 E-value: 7.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 14 TNGPSTYIDTLRKSLEEKGHTVDLMSHdkswlniQIADQQSADKHSMKRELIRRFQT---SYTAKYPLWIYwreMERYS- 89
Cdd:cd03800 20 TGGQNVYVLELARALAELGYQVDIFTR-------RISPADPEVVEIAPGARVIRVPAgppEYLPKEELWPY---LEEFAd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 90 -LEQAIKQFDMSgYDVIHCHDFMTARAMAR-SKPPHIPLIVSLHNF-----KYHEAKVTGEFYNKTEREQQYMkmEEClg 162
Cdd:cd03800 90 gLLRFIAREGGR-YDLIHSHYWDSGLVGALlARRLGVPLVHTFHSLgrvkyRHLGAQDTYHPSLRITAEEQIL--EAA-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 163 amsgDIVAVPCQWLKKQLI-QIGVTPSKIQVIPYGIVKEPFIE----NENPAKKSRDEGKKTILCPARLVPVKGHRYLIE 237
Cdd:cd03800 165 ----DRVIASTPQEADELIsLYGADPSRINVVPPGVDLERFFPvdraEARRARLLLPPDKPVVLALGRLDPRKGIDTLVR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 238 ALSKLSRERKDFHCLLAG--EGPEL----EALQRTAEQLDIGAAISFLG--KRHDIPHLMNGSDIIVLPSLHDTFPLVIL 309
Cdd:cd03800 241 AFAQLPELRELANLVLVGgpSDDPLsmdrEELAELAEELGLIDRVRFPGrvSRDDLPELYRAADVFVVPSLYEPFGLTAI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2474149534 310 EGQFSAKPILAAEAGGIKEIIKDGADGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMKY--WDISVHM 382
Cdd:cd03800 321 EAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHytWESVADQ 395
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
188-375 |
1.06e-35 |
|
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: 135.83 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 188 SKIQVIPyGIVKEPFIENENPAKKsrdegkKTILCPARLVPVKGHRYLIEALSKLSRERKDFHCLLAGEGPELEALQRTA 267
Cdd:cd03820 159 SNVVVIP-NPLSFPSEEPSTNLKS------KRILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLI 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 268 EQLDIGAAISFLGKRHDIPHLMNGSDIIVLPSLHDTFPLVILEGQFSAKPILAAEA-GGIKEIIKDGADGLLVPTGNSDA 346
Cdd:cd03820 232 DKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCpTGPSEIIEDGENGLLVPNGDVDA 311
|
170 180
....*....|....*....|....*....
gi 2474149534 347 LAEKLRHLLDDDAFRSQLGRRAREKAMKY 375
Cdd:cd03820 312 LAEALLRLMEDEELRKKMGKNARKNAERF 340
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
2-357 |
3.21e-33 |
|
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: 129.37 E-value: 3.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 2 KILLA--YYrYSPHTNGPSTYIDTLRKSLEEKGHTVDLMShdksWLNI--QIADQQSADKHSMKRELIRRFQTSYTAKYP 77
Cdd:cd03823 1 KILLVnsLY-PPQRVGGAEISVHDLAEALVAEGHEVAVLT----AGVGppGQATVARSVVRYRRAPDETLPLALKRRGYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 78 LWIYWREMERYSLEQAIKQFdmsGYDVIHCHDF--MTARAMARSKPPHIPLIVSLHNFKYheakvtgefynktereqqym 155
Cdd:cd03823 76 LFETYNPGLRRLLARLLEDF---RPDVVHTHNLsgLGASLLDAARDLGIPVVHTLHDYWL-------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 156 kmeECLGAM----SGDIVAVPCQWLKKQLIQIGVTPSKIQVIPYGIVKEPfieneNPAKKSRDEGKKTILCPA-RLVPVK 230
Cdd:cd03823 133 ---LCPRQFlfkkGGDAVLAPSRFTANLHEANGLFSARISVIPNAVEPDL-----APPPRRRPGTERLRFGYIgRLTEEK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 231 GHRYLIEALSKLSRErkDFHCLLAGEGPELEAlqrtaEQLDIGAAISFLGKRH--DIPHLMNGSDIIVLPSL-HDTFPLV 307
Cdd:cd03823 205 GIDLLVEAFKRLPRE--DIELVIAGHGPLSDE-----RQIEGGRRIAFLGRVPtdDIKDFYEKIDVLVVPSIwPEPFGLV 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2474149534 308 ILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPTGNSDALAEKLRHLLDD 357
Cdd:cd03823 278 VREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTD 327
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
167-389 |
2.27e-32 |
|
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: 127.06 E-value: 2.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 167 DIVAvPCQWLKKQLIQIGV-TPSKIQVIPYGIVKEPFIENENPAKKSRDEG---KKTILCPARLV--PVKGHRYLIEALS 240
Cdd:cd03825 140 TIVA-PSRWLADMVRRSPLlKGLPVVVIPNGIDTEIFAPVDKAKARKRLGIpqdKKVILFGAESVtkPRKGFDELIEALK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 241 KLSRERkDFHCLLAGEGPElealqrtaEQLDIGAAISFLGKRHDIPHLM---NGSDIIVLPSLHDTFPLVILEGQFSAKP 317
Cdd:cd03825 219 LLATKD-DLLLVVFGKNDP--------QIVILPFDIISLGYIDDDEQLVdiySAADLFVHPSLADNLPNTLLEAMACGTP 289
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2474149534 318 ILAAEAGGIKEIIKDGADGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMKYWDISVHMASMERLY 389
Cdd:cd03825 290 VVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELY 361
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
88-378 |
8.65e-32 |
|
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: 125.26 E-value: 8.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 88 YSLEQAIKQFdmsGYDVIHCHdFMTARAmarskpphipLIVSLHNFKYHEAKVTGEF--YNKTEREQQY-MKMEECLGAm 164
Cdd:cd03799 60 YAIVGLNKKG---AYDIIHCQ-FGPLGA----------LGALLRRLKVLKGKLVTSFrgYDISMYVILEgNKVYPQLFA- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 165 SGDIVAVPCQWLKKQLIQIGVTPSKIQVIPYGIVKEPFienenPAKKSRD--EGKKTILCPARLVPVKGHRYLIEALSKL 242
Cdd:cd03799 125 QGDLFLPNCELFKHRLIALGCDEKKIIVHRSGIDCNKF-----RFKPRYLplDGKIRILTVGRLTEKKGLEYAIEAVAKL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 243 SRERKDFHCLLAGEGPELEALQRTAEQLDIGAAISFLG--KRHDIPHLMNGSDIIVLPSL------HDTFPLVILEGQFS 314
Cdd:cd03799 200 AQKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGwkPQEEIIEILDEADIFIAPSVtaadgdQDGPPNTLKEAMAM 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2474149534 315 AKPILAAEAGGIKEIIKDGADGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMKYWDI 378
Cdd:cd03799 280 GLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDI 343
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
62-377 |
1.10e-30 |
|
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: 122.09 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 62 RELIRRFQTSYTAKYPLWIyWREMERYSLEQAIKQFDMsGYDVIHCHDFMTARamarsKPPHIPLIVSLHN---FKYhea 138
Cdd:cd03809 47 LRLLREYPELSLGVIKIKL-WRELALLRWLQILLPKKD-KPDLLHSPHNTAPL-----LLKGCPQVVTIHDlipLRY--- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 139 kvtGEFYNKTEREQQYMKMEECLgaMSGDIVAVPCQWLKKQLIQ-IGVTPSKIQVIPYGIVKEPFIENENPAKKSRDEGK 217
Cdd:cd03809 117 ---PEFFPKRFRLYYRLLLPISL--RRADAIITVSEATRDDIIKfYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 218 -KTILCPARLVPVKGHRYLIEALSKLSRERKDFHCLLAGE-GPELEALQRTAEQLDIGAAISFLGK--RHDIPHLMNGSD 293
Cdd:cd03809 192 ePYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGkGWEDEELLDLVKKLGLGGRVRFLGYvsDEDLPALYRGAR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 294 IIVLPSLHDTFPLVILEGQFSAKPILAAEAGGIKEIIKDGAdgLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAM 373
Cdd:cd03809 272 AFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDAA--LYFDPLDPESIADAILRLLEDPSLREELIRKGLERAK 349
|
....*
gi 2474149534 374 KY-WD 377
Cdd:cd03809 350 KFsWE 354
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
2-377 |
1.17e-30 |
|
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: 122.02 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 2 KILLAYYRYSPHTNGPSTYIDTLRKSLEEKGHTVDLmshdkswlniqIADQQSADKHSMKRELIR--RFQTSYTAKYPLW 79
Cdd:cd03814 1 RIALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRV-----------VAPGPFDEAESAEGRVVSvpSFPLPFYPEYRLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 80 IYWREMERysleQAIKQFDmsgYDVIHCHD--FMTARAMARSKPPHIPLIVSLHN--FKYHEAKVTGEFynkTEREQQYM 155
Cdd:cd03814 70 LPLPRRVR----RLIKEFQ---PDIIHIATpgPLGLAALRAARRLGLPVVTSYHTdfPEYLSYYTLGPL---SWLAWAYL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 156 KmeeclgAMSG--DIVAVPCQWLKKQLIQIGVtpSKIQVIPYGIVKEPFieneNPAKKSRD-------EGKKTILCPARL 226
Cdd:cd03814 140 R------WFHNpfDTTLVPSPSIARELEGHGF--ERVRLWPRGVDTELF----HPSRRDAAlrrrlgpPGRPLLLYVGRL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 227 VPVKGHRYLIEALSKLSRERKdFHCLLAGEGPELEALQRTaeQLDIgaaiSFLG--KRHDIPHLMNGSDIIVLPSLHDTF 304
Cdd:cd03814 208 APEKNLEALLDADLPLAASPP-VRLVVVGDGPARAELEAR--GPDV----IFTGflTGEELARAYASADVFVFPSRTETF 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2474149534 305 PLVILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMKY-WD 377
Cdd:cd03814 281 GLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERYsWE 354
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
279-389 |
3.16e-29 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 111.24 E-value: 3.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 279 LGKRHDIPHL----MNGSDIIVLPSLHDTFPLVILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPTGNSDALAEKLRHL 354
Cdd:COG0438 4 LVPRKGLDLLlealLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRL 83
|
90 100 110
....*....|....*....|....*....|....*
gi 2474149534 355 LDDDAFRSQLGRRAREKAMKYWDISVHMASMERLY 389
Cdd:COG0438 84 LEDPELRRRLGEAARERAEERFSWEAIAERLLALY 118
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
82-390 |
8.92e-29 |
|
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: 118.59 E-value: 8.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 82 WREMERYSLEQAIKQFDMSGYDVIHCHD-----FMTARAMARSKpphIPLIVSLHNFKYHEAKVtgEFYNKTEREQQYMK 156
Cdd:cd03813 154 LRNMLLPLFKLAIAADDLPEADLYHSVStgyagLLGALARHRRG---IPFLLTEHGIYTRERKI--EILQSTWIMGYIKK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 157 M----EECLGAM----SGDIVAVpcqWLKKQLIQI--GVTPSKIQVIPYGIVKEPFieneNPAKKSRDEGKK-TILCPAR 225
Cdd:cd03813 229 LwirfFERLGKLayqqADKIISL---YEGNRRRQIrlGADPDKTRVIPNGIDIQRF----APAREERPEKEPpVVGLVGR 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 226 LVPVKGHRYLIEALSKLSRERKDFHCLLAG---EGPELEA-LQRTAEQLDIGAAISFLGkRHDIPHLMNGSDIIVLPSLH 301
Cdd:cd03813 302 VVPIKDVKTFIRAFKLVRRAMPDAEGWLIGpedEDPEYAQeCKRLVASLGLENKVKFLG-FQNIKEYYPKLGLLVLTSIS 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 302 DTFPLVILEGQFSAKPILAAEAGGIKEIIKDGAD-----GLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMKYW 376
Cdd:cd03813 381 EGQPLVILEAMASGVPVVATDVGSCRELIYGADDalgqaGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYY 460
|
330
....*....|....
gi 2474149534 377 DISVHMASMERLYL 390
Cdd:cd03813 461 TLEGMIDSYRKLYL 474
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
188-391 |
1.57e-27 |
|
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: 113.31 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 188 SKIQVIPYGIVKEPFIENENPAKKSRDE-----GKKTILCPARLVPVKGHRYLIEALSKLSRERKDFHCLLAGEGPELEA 262
Cdd:cd04951 154 NKSVPVYNGIDLNKFKKDINVRLKIRNKlnlknDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDGPLRNE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 263 LQRTAEQLDIGAAISFLGKRHDIPHLMNGSDIIVLPSLHDTFPLVILEGQFSAKPILAAEAGGIKEIIKDGADglLVPTG 342
Cdd:cd04951 234 LERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHNY--VVPVS 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2474149534 343 NSDALAEKLRHLLDDDA-FRSQLGRRaREKAMKYWDISVHMASMERLYLK 391
Cdd:cd04951 312 DPQLLAEKIKEIFDMSDeERDILGNK-NEYIAKNFSINTIVNEWERLYSG 360
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-377 |
5.40e-27 |
|
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: 112.44 E-value: 5.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 2 KILLAYYRYSPHTNGPSTYIDTLRKSLEEKGHTVDLMSHDKSWLNIQIADQQSADKHSMKrelIRRFQTSYTAKYPLWIY 81
Cdd:cd03794 1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGATETKDGIR---VIRVKLGPIKKNGLIRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 82 WREMERYSLEQAIKQFDMSG-YDVIHCH--DFMTARAMAR-SKPPHIPLIVSLHNFkYHEAKVTGEFYNKTEREQQYMKM 157
Cdd:cd03794 78 LLNYLSFALAALLKLLVREErPDVIIAYspPITLGLAALLlKKLRGAPFILDVRDL-WPESLIALGVLKKGSLLKLLKKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 158 EE-CLGAMSGDIVAVPCqwLKKQLIQIGVTPSKIQVIPYGIVKEPFIEN--ENPAKKSRDEGKKTILC-----PARLVPV 229
Cdd:cd03794 157 ERkLYRLADAIIVLSPG--LKEYLLRKGVPKEKIIVIPNWADLEEFKPPpkDELRKKLGLDDKFVVVYagnigKAQGLET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 230 kghryLIEALSKLsRERKDFHCLLAGEGPELEALQRTAEQLDIgAAISFLGK--RHDIPHLMNGSDIIVLPsLHD----- 302
Cdd:cd03794 235 -----LLEAAERL-KRRPDIRFLFVGDGDEKERLKELAKARGL-DNVTFLGRvpKEEVPELLSAADVGLVP-LKDnpanr 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2474149534 303 -TFPLVILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMKYWD 377
Cdd:cd03794 307 gSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFS 382
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
1-378 |
5.67e-27 |
|
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: 111.67 E-value: 5.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 1 MKILLAYYryspHTNGPSTYIDT-LRKSLEEKGHTVDLMSHDKSWLNIQIADQqsadkhsmkreliRRFQTSYTAKYPLW 79
Cdd:cd04962 1 MKIGIVCY----PSYGGSGVVATeLGLELAERGHEVHFISSAIPFRLNLYSGN-------------IFFHEVEVPNYPLF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 80 IYwremERYSLEQAIKQFDMS---GYDVIHCH-------DFMTARAMARSKpphIPLIVSLHNfkyheAKVTGEFYNKTE 149
Cdd:cd04962 64 EY----PPYTLALASKIVEVAkehKLDVLHAHyaiphasCAYLAREILGEK---IPIVTTLHG-----TDITLVGYDPSL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 150 REQQYMKMEEclgamsGDIVAVPCQWLKKQLIQIGVTPSKIQVIPYGIVKEPFIENENPAKKSR---DEGKKTILCPARL 226
Cdd:cd04962 132 QPAVRFSINK------SDRVTAVSSSLRQETYELFDVDKDIEVIHNFIDEDVFKRKPAGALKRRllaPPDEKVVIHVSNF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 227 VPVKGHRYLIEALSKLSRERKDfHCLLAGEGPELEALQRTAEQLDIGAAISFLGKRHDIPHLMNGSDIIVLPSLHDTFPL 306
Cdd:cd04962 206 RPVKRIDDVVRVFARVRRKIPA-KLLLVGDGPERVPAEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGL 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2474149534 307 VILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMKYWDI 378
Cdd:cd04962 285 AALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDP 356
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
2-372 |
1.77e-26 |
|
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: 110.06 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 2 KILLAYYRYSPHTNGPSTYIDTLRKSLEEKGHTVDL--MSHDKSWLNIQIADQQSadkHSMKRELirrfqtsYTAKYPL- 78
Cdd:cd03795 1 KVLHVFKFYYPDIGGIEQVIYDLAEGLKKKGIEVDVlcFSKEKETPEKEENGIRI---HRVKSFL-------NVASTPFs 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 79 WIYWREMERYSLEqaikqfdmsgYDVIHCH---DFMTArAMARSKPPHiPLIVSlhnfkYHEAKVTGEFYNKTEREQQYM 155
Cdd:cd03795 71 PSYIKRFKKLAKE----------YDIIHYHfpnPLADL-LLFFSGAKK-PVVVH-----WHSDIVKQKKLLKLYKPLMTR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 156 KMEEclgamSGDIVAVPCQWLK--KQLIQIGVtpsKIQVIPYGIVKE--PFIENENPAKKSRDEGKKTILCPARLVPVKG 231
Cdd:cd03795 134 FLRR-----ADRIIATSPNYVEtsPTLREFKN---KVRVIPLGIDKNvyNIPRVDFENIKREKKGKKIFLFIGRLVYYKG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 232 HRYLIEALSKLsrerkDFHCLLAGEGPELEALQRTAEqLDIGAAISFLGK--RHDIPHLMNGSDIIVLPSL--HDTFPLV 307
Cdd:cd03795 206 LDYLIEAAQYL-----NYPIVIGGEGPLKPDLEAQIE-LNLLDNVKFLGRvdDEEKVIYLHLCDVFVFPSVlrSEAFGIV 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2474149534 308 ILEGQFSAKPILAAE-AGGIKEIIKDGADGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKA 372
Cdd:cd03795 280 LLEAMMCGKPVISTNiGTGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRF 345
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
2-370 |
8.61e-26 |
|
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: 108.61 E-value: 8.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 2 KILLAYYRYSPHTNGPSTYIDTLRKSLEEKGHTVDLMSHD-------KSWLNIQIADQQSADKHSMKRELIRRFQTSYTA 74
Cdd:cd03821 1 KILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGdgyeslvVEENGRYIPPQDGFASIPLLRQGAGRTDFSPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 75 KYPLWIYWREmerysleqaikqfdmsgYDVIHCHD---FMTARAMARSKPPHIPLIVSLHNFKYHEAKVTGEFYNKTERE 151
Cdd:cd03821 81 PNWLRRNLRE-----------------YDVVHIHGvwtYTSLAACKLARRRGIPYVVSPHGMLDPWALQQKHWKKRIALH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 152 QQYMKMeecLGAMSGDIVAVPcQWLKKQLIQigVTPSKIQVIPYGIVKEPF-IENENPAKKSRDEGKKTILCPARLVPVK 230
Cdd:cd03821 144 LIERRN---LNNAALVHFTSE-QEADELRRF--GLEPPIAVIPNGVDIPEFdPGLRDRRKHNGLEDRRIILFLGRIHPKK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 231 GHRYLIEALSKLSRERKDFHCLLAGEGP-ELEALQRTAEQLDIGAAISFLGKRH--DIPHLMNGSDIIVLPSLHDTFPLV 307
Cdd:cd03821 218 GLDLLIRAARKLAEQGRDWHLVIAGPDDgAYPAFLQLQSSLGLGDRVTFTGPLYgeAKWALYASADLFVLPSYSENFGNV 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2474149534 308 ILEGQFSAKPILAAEAGGIKEIIKDGaDGLLVPTgNSDALAEKLRHLLDDDAFRSQLGRRARE 370
Cdd:cd03821 298 VAEALACGLPVVITDKCGLSELVEAG-CGVVVDP-NVSSLAEALAEALRDPADRKRLGEMARR 358
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
56-379 |
9.07e-23 |
|
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: 99.29 E-value: 9.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 56 DKHSMKRELIRR----FQTSYTAKYPLwIYWREMerYSLEQAIKqfdmsgYDVIHCH-DFMTARAMARSKPPHIP-LIVS 129
Cdd:cd03812 40 DKGEYDEELEELggkiFYIPPKKKNII-KYFIKL--LKLIKKEK------YDIVHVHgSSSNGIILLLAAKAGVPvRIAH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 130 LHNFKYHEAKVTGEFYNKTER--EQQYMKMEEClgamsGDIVAVpcqWLKKQliqigVTPSKIQVIPYGIVKEPFIENEN 207
Cdd:cd03812 111 SHNTKDSSIKLRKIRKNVLKKliERLSTKYLAC-----SEDAGE---WLFGE-----VENGKFKVIPNGIDIEKYKFNKE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 208 PAKKSRDEG---KKTILCP-ARLVPVKGHRYLIEALSKLSRERKDFHCLLAGEGPELEALQRTAEQLDIGAAISFLGKRH 283
Cdd:cd03812 178 KRRKRRKLLileDKLVLGHvGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKIKEKVKELGLEDKVIFLGFRN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 284 DIPHLMNGSDIIVLPSLHDTFPLVILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPTGNSDAlAEKLRHLLDDDAFRSQ 363
Cdd:cd03812 258 DVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITNNVEFLPLNETPSTW-AEKILKLIKRKRRINK 336
|
330
....*....|....*.
gi 2474149534 364 LgRRAREKAMKYWDIS 379
Cdd:cd03812 337 E-INKEKKELGYDDES 351
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
221-339 |
3.18e-22 |
|
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 95.16 E-value: 3.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 221 LCPARLVPVKGHRYLIEALSKLSRERKDFHCLLAGEGPELEALQRTAEQLDIGAAISFLGKRHD---IPHLMNGSDIIVL 297
Cdd:cd01635 114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDdevLELLLAAADVFVL 193
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2474149534 298 PSLHDTFPLVILEGQFSAKPILAAEAGGIKEIIKDGADGLLV 339
Cdd:cd01635 194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
103-376 |
2.98e-21 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 96.32 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 103 DVIHCHD--FMTARAMARSKPPHIPLIVSLHNF------KYHEAKVTGEFYnktereqQYMKmeeCLGAmSGDIVAVPCQ 174
Cdd:PLN02871 146 DLIHASSpgIMVFGALFYAKLLCVPLVMSYHTHvpvyipRYTFSWLVKPMW-------DIIR---FLHR-AADLTLVTSP 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 175 WLKKQLIQIGVTPS-KIQVIPYGIVKEPFieneNPAKKSRD---------EGKKTILCPARLVPVKGHRYLIEALSKLSR 244
Cdd:PLN02871 215 ALGKELEAAGVTAAnRIRVWNKGVDSESF----HPRFRSEEmrarlsggePEKPLIVYVGRLGAEKNLDFLKRVMERLPG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 245 ERKDFhcllAGEGPELEALQRTAEqldiGAAISFLGKRH--DIPHLMNGSDIIVLPSLHDTFPLVILEGQFSAKPILAAE 322
Cdd:PLN02871 291 ARLAF----VGDGPYREELEKMFA----GTPTVFTGMLQgdELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAAR 362
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2474149534 323 AGGIKEII---KDGADGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMKY-W 376
Cdd:PLN02871 363 AGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVEKWdW 420
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
64-375 |
2.66e-17 |
|
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: 82.73 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 64 LIRRFQTSYTAKYPLWIYWR---EMERYSLEQAIKQfdmsGYDVIHC-HDFMTARAMARSKPPhIPLIVSLHNFKYHEAK 139
Cdd:cd04949 19 QINRLKLFKEHTRPYKIIFLneqELFAFFIEQLNLQ----KGDIFISdRPTLTGQVILNTKGP-AKKGAVLHNEHVKNND 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 140 VTGEFYNKTEREQQYMKMEEclgaMSGDIVAVPCQwlkKQLI--QIGVTPsKIQVIPYGivkepFIENENPAKKSRDEGK 217
Cdd:cd04949 94 DPEHSLIKNFYKYVFENLNK----YDAIIVSTEQQ---KQDLseRFNKYP-PIFTIPVG-----YVDQLDTAESNHERKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 218 KTILCPARLVPVKGHRYLIEALSKLSRERKD--FHclLAGEGPELEALQRTAEQLDIGAAISFLGKRHDIPHLMNGSDII 295
Cdd:cd04949 161 NKIITISRLAPEKQLDHLIEAVAKAVKKVPEitLD--IYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 296 VLPSLHDTFPLVILEGQFSAKPILAAEAG-GIKEIIKDGADGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMK 374
Cdd:cd04949 239 LLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIAEK 318
|
.
gi 2474149534 375 Y 375
Cdd:cd04949 319 Y 319
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
10-391 |
8.44e-17 |
|
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: 82.05 E-value: 8.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 10 YSPHTNGPSTYIDTLRKSLEEKGHTVDLmshdkswlnIQIADQqsadkhsmkrELIrrfQTSYTAKYPLWIY-WREMERY 88
Cdd:cd03822 8 LPPRKCGIATYTDDLVEGLRKGGPVVIV---------VIVSPQ----------DEI---LKDDDFEVPNEIKsWNSNEYF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 89 SLEQAIkqfDMSGYDVIHC-HDF------MTARAMARSKPPHIPLIVSLHNFkYHEAKVTgefynkterEQQYMKMEECL 161
Cdd:cd03822 66 RLLDHL---NFKKPDVVHIqHEFgifggkYGLYALGLLLHLRIPVITTLHTV-LDLSDPG---------KQALKVLFRIA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 162 GAMsgDIVAVPCQWLKKQLIQIGVTP-SKIQVIPYGiVKEPFIENENPAKKSRD-EGKKTILCPARLVPVKGHRYLIEAL 239
Cdd:cd03822 133 TLS--ERVVVMAPISRFLLVRIKLIPaVNIEVIPHG-VPEVPQDPTTALKRLLLpEGKKVILTFGFIGPGKGLEILLEAL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 240 SKLSRERKDFHCLLAGE-GPEL------EALQRTAEQLDIGAAISFLGK---RHDIPHLMNGSDIIVLP------SLHDT 303
Cdd:cd03822 210 PELKAEFPDVRLVIAGElHPSLaryegeRYRKAAIEELGLQDHVDFHNNflpEEEVPRYISAADVVVLPylnteqSSSGT 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 304 FPLVILEGqfsaKPILAAEAGGIKEIIKDGaDGLLVPTGNSDALAEKLRHLLDDDAFRsqlgRRAREKAMKYWDiSVHMA 383
Cdd:cd03822 290 LSYAIACG----KPVISTPLRHAEELLADG-RGVLVPFDDPSAIAEAILRLLEDDERR----QAIAERAYAYAR-AMTWE 359
|
....*...
gi 2474149534 384 SMERLYLK 391
Cdd:cd03822 360 SIADRYLR 367
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
95-369 |
2.12e-14 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 74.83 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 95 KQFDMSGYDVIHCHDFMTARAMARSKPPHIPLIVSLHNfkyheakvtgefynKTEREQ--QYMKMeeclgamsgdivAVP 172
Cdd:PRK15484 93 HKFTITKDSVIVIHNSMKLYRQIRERAPQAKLVMHMHN--------------AFEPELldKNAKI------------IVP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 173 CQWLKKqLIQIGVTPSKIQVIPYGIVKEPFIENENPAKKSR---DEGKKTILCPARLVPVKGHRYLIEALSKLSRERKDF 249
Cdd:PRK15484 147 SQFLKK-FYEERLPNADISIVPNGFCLETYQSNPQPNLRQQlniSPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 250 HCLLAGE-----GPELEALQR----TAEQldIGAAISFLG-----KRHDIPHLmngSDIIVLPS-LHDTFPLVILEGQFS 314
Cdd:PRK15484 226 KLVVVGDptassKGEKAAYQKkvleAAKR--IGDRCIMLGgqppeKMHNYYPL---ADLVVVPSqVEEAFCMVAVEAMAA 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2474149534 315 AKPILAAEAGGIKEIIKDGADGL-LVPTGNSDALAEKLRHLLDDDAfRSQLGRRAR 369
Cdd:PRK15484 301 GKPVLASTKGGITEFVLEGITGYhLAEPMTSDSIISDINRTLADPE-LTQIAEQAK 355
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
210-389 |
1.23e-13 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 73.53 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 210 KKSRDEGKKTILCPARLVPVKGHRYLIEALSKLSRERKDFHCLLAGEGPELEALQRTAEQLDIGAAISFLGKRHDIPHLM 289
Cdd:PRK15179 510 DARTSDARFTVGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWL 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 290 NGSDIIVLPSLHDTFPLVILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPTGNSDA--LAEKLRHLLDDDAFRSQLGRR 367
Cdd:PRK15179 590 TQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTApdVAEALARIHDMCAADPGIARK 669
|
170 180
....*....|....*....|..
gi 2474149534 368 AREKAMKYWDISVHMASMERLY 389
Cdd:PRK15179 670 AADWASARFSLNQMIASTVRCY 691
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
15-197 |
3.75e-13 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 67.56 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 15 NGPSTYIDTLRKSLEEKGHTVDLMSHDkswlniqiADQQSADKHSMKRELIRRFQTSYTAKYPLWIYWREMERysleqAI 94
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPG--------GPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRR-----LL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 95 KQFDmsgYDVIHCHDFMTARAMARS--KPPHIPLIVSLHNFkYHEAKVtgeFYNKTEREQQYMKMEECLGAMSGDIVAVP 172
Cdd:pfam13439 68 RRER---PDVVHAHSPFPLGLAALAarLRLGIPLVVTYHGL-FPDYKR---LGARLSPLRRLLRRLERRLLRRADRVIAV 140
|
170 180
....*....|....*....|....*.
gi 2474149534 173 CQWLKKQLIQ-IGVTPSKIQVIPYGI 197
Cdd:pfam13439 141 SEAVADELRRlYGVPPEKIRVIPNGV 166
|
|
| GT4_ExpC-like |
cd03818 |
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ... |
100-383 |
1.21e-12 |
|
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: 69.31 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 100 SGY--DVIHCHDFMTARAMARSKPPHIPLIvSLHNFKYHEAKVTGEFYNktEREQQYMK--------MEECLGAMSGDIV 169
Cdd:cd03818 86 EGFrpDVVVGHPGWGEALFVKDVFPDVPLI-GYCEYYYRAEGADVGFDP--EFPLDLMIrcrlrnrnIALLLSLEQADLG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 170 AVPCQWLKKQliQIGVTPSKIQVIPYGIVKEPFIENENPakkSRDEGKKTILCPARLV---------PVKGHRYLIEALS 240
Cdd:cd03818 163 VTPTRWQRSL--FPAAYRDRISVIHDGVDTDRLAPDPAA---RLRLLNGTELKAGDPVityvarnlePYRGFHVFMRALP 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 241 KLSRERKDFHCLLAGE-----GPELEAL----QRTAEQLDIG-AAISFLGKRhdiPH-----LMNGSDIIVLPslhdTFP 305
Cdd:cd03818 238 RIQARRPDARVVVVGGdgvsyGSPPPDGgswkQKMLAELGVDlERVHFVGKV---PYdqyvrLLQLSDAHVYL----TYP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 306 LV----ILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMKYWDISVH 381
Cdd:cd03818 311 FVlswsLLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVC 390
|
..
gi 2474149534 382 MA 383
Cdd:cd03818 391 LA 392
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
15-196 |
1.48e-12 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 65.50 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 15 NGPSTYIDTLRKSLEEKGHTVDLmshdkswlniqIADQQSADKHSMKRELIRRfqtsytakYPLWIYWREMERYS----- 89
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRV-----------VTPGGPPGRPELVGDGVRV--------HRLPVPPRPSPLADlaalr 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 90 -LEQAIKQFdmsGYDVIHCHDFMTARAMARSKPPH-IPLIVSLHNFKYHEAK-VTGEFYNKTEReqqymkmeecLGAMSG 166
Cdd:pfam13579 62 rLRRLLRAE---RPDVVHAHSPTAGLAARLARRRRgVPLVVTVHGLALDYGSgWKRRLARALER----------RLLRRA 128
|
170 180 190
....*....|....*....|....*....|
gi 2474149534 167 DIVAVPCQWLKKQLIQIGVTPSKIQVIPYG 196
Cdd:pfam13579 129 DAVVVVSEAEAELLRALGVPAARVVVVPNG 158
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
214-384 |
5.73e-12 |
|
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: 67.35 E-value: 5.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 214 DEGKKTILCPARLVPVKGHRYLIEALSKLSRERKDFHCLLAGEG----PELEALQRT---AEQLDIGAAISFLGKRH-DI 285
Cdd:cd03792 194 DPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGavddPEGSVVYEEvmeYAGDDHDIHVLRLPPSDqEI 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 286 PHLMNGSDIIVLPSLHDTFPLVILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPTGNSDALaeKLRHLLDDDAFRSQLG 365
Cdd:cd03792 274 NALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAV--RILRLLTDPELRRKMG 351
|
170
....*....|....*....
gi 2474149534 366 RRAREKAMKYWDISVHMAS 384
Cdd:cd03792 352 LAAREHVRDNFLITGNLRA 370
|
|
| PelF |
NF038011 |
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ... |
181-359 |
2.65e-11 |
|
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: 65.72 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 181 IQIGVTPSKIQVIPYGIVKEPFieneNPAKKSRDEGKKTILC-PARLVPVKGHRYLIEALSKLSRERKDFHCLLAG---E 256
Cdd:NF038011 273 IADGAPPERTRVIPNGIDLPRL----APLRAQRPAGIPPVVGlIGRVVPIKDIKTFIRAMRTVVRAMPEAEGWIVGpeeE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 257 GPELEALQRT-AEQLDIGAAISFLGKRHdIPHLMNGSDIIVLPSLHDTFPLVILEGQFSAKPILAAEAGGIKEII----- 330
Cdd:NF038011 349 DPAYAAECRSlVASLGLQDKVKFLGFQK-IDDLLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTTDVGSCRQLIeglde 427
|
170 180 190
....*....|....*....|....*....|..
gi 2474149534 331 KD---GADGLLVPTGNSDALAEKLRHLLDDDA 359
Cdd:NF038011 428 EDralGAAGEVVAIADPQALARAALDLLRDPQ 459
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
235-387 |
7.73e-10 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 60.76 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 235 LIEALSKLsRERKDFHCLLAGEGPELEALQRTAEQLDIGAAISF-LGKRHDIPHLMNGSDIIVLPSLHDTFPLVI---LE 310
Cdd:PRK10307 247 VIDAARRL-RDRPDLIFVICGQGGGKARLEKMAQCRGLPNVHFLpLQPYDRLPALLKMADCHLLPQKAGAADLVLpskLT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 311 GQF-SAKPILA-AEAG-GIKEIIkDGAdGLLVPTGNSDALAEKLRHLLDDDAFRSQLGRRAREKAMKYWDISVHMASMER 387
Cdd:PRK10307 326 NMLaSGRNVVAtAEPGtELGQLV-EGI-GVCVEPESVEALVAAIAALARQALLRPKLGTVAREYAERTLDKENVLRQFIA 403
|
|
| GT4_AmsK-like |
cd04946 |
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ... |
188-371 |
5.06e-09 |
|
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.
Pssm-ID: 340854 [Multi-domain] Cd Length: 401 Bit Score: 58.24 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 188 SKIQVIPYGIVKEPFIenenpAKKSRDEGKKTILCpARLVPVKGHRYLIEALSKLSRERKDF-----HCllaGEGPELEA 262
Cdd:cd04946 201 EKIFVSRLGVSDKEQY-----SKVKKEGDLRLVSC-SSIVPVKRIDLIIETLNSLCVAHPSIciswtHI---GGGPLKER 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 263 LQRTAEQLDIGAAISFLG--KRHDIP--HLMNGSDIIVLPSLHDTFPLVILEGQFSAKPILAAEAGGIKEIIKDGADGLL 338
Cdd:cd04946 272 LEKLAENKLENVKVNFTGevSNKEVKqlYKENDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLL 351
|
170 180 190
....*....|....*....|....*....|....*..
gi 2474149534 339 VptgNSDA----LAEKLRHLLDDDAFRSQLGRRAREK 371
Cdd:cd04946 352 L---DKDPtpneIVSSIMKFYLDGGDYKTMKISAREC 385
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
176-362 |
1.30e-08 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 56.64 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 176 LKKQLIQIGVTPSKIQVIpYGIVKE-----PFIENENPAkksrdegkkTILCPARLVpVKGHRYLIEALSKLSRERKDFH 250
Cdd:PRK09922 144 IKEQMMARGISAQRISVI-YNPVEIktiiiPPPERDKPA---------VFLYVGRLK-FEGQKNVKELFDGLSQTTGEWQ 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 251 CLLAGEGPELEALQRTAEQLDIGAAISFLGKRHDIPHLMNGS----DIIVLPSLHDTFPLVILEGQFSAKPILAAEA-GG 325
Cdd:PRK09922 213 LHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQPWEVVQQKiknvSALLLTSKFEGFPMTLLEAMSYGIPCISSDCmSG 292
|
170 180 190
....*....|....*....|....*....|....*..
gi 2474149534 326 IKEIIKDGADGLLVPTGNSDALAEKLRHLLDDDAFRS 362
Cdd:PRK09922 293 PRDIIKPGLNGELYTPGNIDEFVGKLNKVISGEVKYQ 329
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
225-375 |
1.88e-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: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 225 RLVPVKGHRYLIEALSKLSRErkdfhCLLAGEGPELEALQRTAeqldiGAAISFLGKRHD--IPHLMNGSDIIVLPSLHD 302
Cdd:cd03804 207 RLVPYKRIDLAVEAFNELPKR-----LVVIGDGPDLDRLRAMA-----SPNVEFLGYQPDevLKELLSKARAFVFAAEED 276
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2474149534 303 tFPLVILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPTGNSDALAEKLRHLLD-DDAFRSQlgrRAREKAMKY 375
Cdd:cd03804 277 -FGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEFEQnFDRFKPQ---AIRANAERF 346
|
|
| Glyco_trans_1_2 |
pfam13524 |
Glycosyl transferases group 1; |
294-377 |
3.33e-08 |
|
Glycosyl transferases group 1;
Pssm-ID: 433281 [Multi-domain] Cd Length: 93 Bit Score: 51.07 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 294 IIVLPSLH-DTFPLVILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPtgNSDALAEKLRHLLDDDAFRSQLGRRAREKA 372
Cdd:pfam13524 1 IVLNPSRRpDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERV 78
|
....*
gi 2474149534 373 MKYWD 377
Cdd:pfam13524 79 LAEHT 83
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
204-375 |
4.27e-08 |
|
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: 55.29 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 204 ENENPAKKSRDEGKKTILCPARLVPVKGHRYLIEALSKL---SRERKDFHCLLAG-------EGPE-LEALQRTAEQL-D 271
Cdd:cd03805 198 EDPDPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLkqkLPEFENVRLVIAGgydprvaENVEyLEELQRLAEELlN 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 272 IGAAISFLgkrHDIPH-----LMNGSDIIVL-PSlHDTFPLVILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPtGNSD 345
Cdd:cd03805 278 VEDQVLFL---RSISDsqkeqLLSSALALLYtPS-NEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCE-PTPE 352
|
170 180 190
....*....|....*....|....*....|
gi 2474149534 346 ALAEKLRHLLDDDAFRSQLGRRAREKAMKY 375
Cdd:cd03805 353 AFAEAMLKLANDPDLADRMGAAGRKRVKEK 382
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
102-379 |
2.40e-07 |
|
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273969 [Multi-domain] Cd Length: 473 Bit Score: 53.04 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 102 YDVIHCHDFMTARAMA----RSKPPHIPLIVSLHNFKYheakvTGEFYNKTEREQQ---------YMKMEECLGAMSGDI 168
Cdd:TIGR02095 129 PDVVHAHDWHTALVPAllkaVYRPNPIKTVFTIHNLAY-----QGVFPADDFSELGlppeyfhmeGLEFYGRVNFLKGGI 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 169 V---AVP----------------CqWLKKQLIQIgvtPSKIQVIPYGI-------VKEPFI----ENENPAKKSR----- 213
Cdd:TIGR02095 204 VyadRVTtvsptyareiltpefgY-GLDGVLKAR---SGKLRGILNGIdtevwnpATDPYLkanySADDLAGKAEnkeal 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 214 --------DEGKKTILCPARLVPVKGHRYLIEALSKLSreRKDFHCLLAGEG-PELE-ALQRTAEQL--DIGAAISFlgk 281
Cdd:TIGR02095 280 qeelglpvDDDVPLFGVISRLTQQKGVDLLLAALPELL--ELGGQLVVLGTGdPELEeALRELAERYpgNVRVIIGY--- 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 282 rhDIP--HLMN-GSDIIVLPSLHDTFPLVILEGQ-FSAKPIlAAEAGGIKEIIKDGADGLLVPTG------NSDALAEKL 351
Cdd:TIGR02095 355 --DEAlaHLIYaGADFILMPSRFEPCGLTQLYAMrYGTVPI-VRRTGGLADTVVDGDPEAESGTGflfeeyDPGALLAAL 431
|
330 340 350
....*....|....*....|....*....|.
gi 2474149534 352 RHLLDDDAFRSQLGRRAREKAMKY---WDIS 379
Cdd:TIGR02095 432 SRALRLYRQDPSLWEALQKNAMSQdfsWDKS 462
|
|
| PRK15490 |
PRK15490 |
Vi polysaccharide biosynthesis glycosyltransferase TviE; |
252-353 |
8.08e-07 |
|
Vi polysaccharide biosynthesis glycosyltransferase TviE;
Pssm-ID: 185387 [Multi-domain] Cd Length: 578 Bit Score: 51.62 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 252 LLAGEGPELEALQRTAEQLDIGAAISFLGKRHDIPHLMNGSDIIVLPSLHDTFPLVILEGQFSAKPILAAEAGGIKEIIK 331
Cdd:PRK15490 433 VLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGSAECFI 512
|
90 100
....*....|....*....|..
gi 2474149534 332 DGADGLLVPTGNSDALAEKLRH 353
Cdd:PRK15490 513 EGVSGFILDDAQTVNLDQACRY 534
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
184-329 |
1.24e-06 |
|
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: 50.70 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 184 GVTPSKIQVIPYGIVKEPFIENENPakksRDEGKKTILCPARLVPVKGHRYLIEALSKLSRERKDFHCLLAGEGPELEAL 263
Cdd:cd03796 164 SLDPRIVSVIPNAVDSSDFTPDPSK----PDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIEL 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2474149534 264 QRTAEQLDIGAAISFLG--KRHDIPHLMNGSDIIVLPSLHDTFPLVILEGQFSAKPILAAEAGGIKEI 329
Cdd:cd03796 240 EEMREKYQLQDRVELLGavPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEV 307
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
225-389 |
4.21e-05 |
|
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: 46.02 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 225 RLVPVKGHRYLIEALSKLSRERKDFHCLLAGEgPELE-ALQRTAEQL--DIGAAISFLGKrhdIPHLM-NGSDIIVLPSL 300
Cdd:cd03791 302 RLTEQKGVDLILDALPELLEEGGQLVVLGSGD-PEYEqAFRELAERYpgKVAVVIGFDEA---LAHRIyAGADFFLMPSR 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 301 HDTFPLVILEGQ-FSAKPIlAAEAGGIKEIIKDGADGLLVPTG------NSDALAEKLRHLLddDAFRSQ-LGRRAREKA 372
Cdd:cd03791 378 FEPCGLVQMYAMrYGTLPI-VRRTGGLADTVFDYDPETGEGTGfvfedyDAEALLAALRRAL--ALYRNPeLWRKLQKNA 454
|
170 180
....*....|....*....|
gi 2474149534 373 MKY---WDISVhmASMERLY 389
Cdd:cd03791 455 MKQdfsWDKSA--KEYLELY 472
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
66-392 |
3.05e-04 |
|
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: 43.05 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 66 RRFQTSYTAKYPLWIYWREMERYSLEQAIKQFDM-SGYDVIHCHDFMTARAMARskPPHIPLIVSLHNfkyheakvtgef 144
Cdd:cd03802 50 APLVAVIPRALRLDPIPQESKLAELLEALEVQLRaSDFDVIHNHSYDWLPPFAP--LIGTPFVTTLHG------------ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 145 yNKTEREQQYMKMEECLGamsgdIVAVpcqwLKKQLiQIGVTPSKIQVIPYGIVKEPFIENenpakksrDEGKKTILCPA 224
Cdd:cd03802 116 -PSIPPSLAIYAAEPPVN-----YVSI----SDAQR-AATPPIDYLTVVHNGLDPADYRFQ--------PDPEDYLAFLG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 225 RLVPVKGHRYLIEALSKLSRerkdfHCLLAGEGPELEALQRTAEQLdIGAAISFLGKRHDI---PHLMNGSDIIVLPSLH 301
Cdd:cd03802 177 RIAPEKGLEDAIRVARRAGL-----PLKIAGKVRDEDYFYYLQEPL-PGPRIEFIGEVGHDekqELLGGARALLFPINWD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 302 DTFPLVILEGQFSAKPILAAEAGGIKEIIKDGADGLLVPtgNSDALAEKLRHLldddafrSQLGRRA-REKAMKYWDISV 380
Cdd:cd03802 251 EPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVD--SVEEMAEAIANI-------DRIDRAAcRRYAEDRFSAAR 321
|
330
....*....|..
gi 2474149534 381 HMASMERLYLKC 392
Cdd:cd03802 322 MADRYEALYRKV 333
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
171-296 |
1.37e-03 |
|
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). 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: 340861 [Multi-domain] Cd Length: 364 Bit Score: 40.76 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2474149534 171 VPCQWLKKQLIQIGVTPSKIQVipYGIVKEPFIENENPAKKSRDE-----GKKTILCPARLVpvkGHRYLIEALSKLSRE 245
Cdd:cd17507 148 VASEEVKRELVERGVTPSQIKV--TGIPVRPSFAEVRDKDEARNElnlspDKPTVLLMGGGG---GMGPVKETVEALLDS 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2474149534 246 RKDFHCL-LAGEGPEL-EALQRTAEQLDigaAISFLGKRHDIPHLMNGSDIIV 296
Cdd:cd17507 223 LRAGQVLvVCGKNKKLyEKLSGLEEDYI---NVRVLGYVDDMNELMAASDLVI 272
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
81-135 |
2.62e-03 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 39.62 E-value: 2.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2474149534 81 YWREMERYSL-----EQAIKQFDMsGYDVIHCHDFMTA------RAMARSKPP-HIPLIVSLHNFKY 135
Cdd:pfam08323 105 YEDNAERFAFfsraaLELAKKLGW-IPDIIHCHDWHTAlvpaylKEAYADDPFkNIKTVFTIHNLAY 170
|
|
| COG4641 |
COG4641 |
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]; |
317-375 |
2.96e-03 |
|
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443679 [Multi-domain] Cd Length: 303 Bit Score: 39.53 E-value: 2.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2474149534 317 PILAAEAGGIKEIIKDGADGLLVPTGnsDALAEKLRHLLDDDAFRSQLGRRAREKAMKY 375
Cdd:COG4641 229 FLLSDPWEGLEELFEPGEEVLVFRDG--EELAEKLRYLLADPEERRAIAEAGRRRVLAE 285
|
|
| Por_Secre_tail |
TIGR04183 |
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ... |
447-481 |
6.64e-03 |
|
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.
Pssm-ID: 275036 [Multi-domain] Cd Length: 72 Bit Score: 35.46 E-value: 6.64e-03
10 20 30
....*....|....*....|....*....|....*
gi 2474149534 447 IHVYDLSGVLLQTKAVEPEGVYEFHHLPAGSYVLK 481
Cdd:TIGR04183 23 VEIYDLSGKLVKKTTLNNSNSIDLSNLSSGVYIVK 57
|
|
| |
