|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
31-404 |
2.34e-93 |
|
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: 295.83 E-value: 2.34e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 31 ILYMSSYPPRECGIATYTRDLVKAIDRKfSPYLESKILAMNENGssIYNYCSKVKYQINQTEIEDYINVARKINKDDsIR 110
Cdd:cd03822 2 IAVLGTLPPRKCGIATYTDDLVEGLRKG-GPVVIVVIVSPQDEI--LKDDDFEVPNEIKSWNSNEYFRLLDHLNFKK-PD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 111 LINIQHEFGLFGGEWGDYLLAFLEVVKKPVVVTFHSLI--PNPTPKLKKVIQAIAKRCEKIIVMADMAIEYYECDYGLKK 188
Cdd:cd03822 78 VVHIQHEFGIFGGKYGLYALGLLLHLRIPVITTLHTVLdlSDPGKQALKVLFRIATLSERVVVMAPISRFLLVRIKLIPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 189 SQLVVIPHGTPVIEPYSSEASKKKLGFEGKMLLSTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGETHPVVRKYEGE 268
Cdd:cd03822 158 VNIEVIPHGVPEVPQDPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGELHPSLARYEGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 269 KYRNKLIKLsqkLNLTNYVKFYNKYLTLEEIINYLKSTDIYLCPPLAVNQITSGTLAYALSAGKAIVSTPFLHAKEVLQQ 348
Cdd:cd03822 238 RYRKAAIEE---LGLQDHVDFHNNFLPEEEVPRYISAADVVVLPYLNTEQSSSGTLSYAIACGKPVISTPLRHAEELLAD 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1277773221 349 GRGEIVGFRDPTGISRVVNALIEKPETRKSMEKQSYLYGQKTSWPIAAIAHLNVFK 404
Cdd:cd03822 315 GRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIADRYLRLFN 370
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
231-384 |
3.40e-17 |
|
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: 79.24 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 231 KGVEYVIKALPKIIEKHPEVLYLIIGEthpvvrkyegEKYRNKLIKLSQKLNLTNYVKFYnKYLTLEEIINYLKSTDIYL 310
Cdd:pfam00534 15 KGLDLLIKAFALLKEKNPNLKLVIAGD----------GEEEKRLKKLAEKLGLGDNVIFL-GFVSDEDLPELLKIADVFV 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277773221 311 CP----PLAVnqitsgTLAYALSAGKAIVSTPFLHAKEVLQQG-RGEIVGFRDPTGISRVVNALIEKPETRKSMEKQSY 384
Cdd:pfam00534 84 LPsryeGFGI------VLLEAMACGLPVIASDVGGPPEVVKDGeTGFLVKPNNAEALAEAIDKLLEDEELRERLGENAR 156
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
296-408 |
1.31e-08 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 53.84 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 296 LEEIIN-YLKSTDIYLCPPLAVNqiTSGTLAYALSAGKAIVSTPFLHAKEVLQQGR-GEIVGFRDPTGISRVVNALIEKP 373
Cdd:COG0438 10 LDLLLEaLLAAADVFVLPSRSEG--FGLVLLEAMAAGLPVIATDVGGLPEVIEDGEtGLLVPPGDPEALAEAILRLLEDP 87
|
90 100 110
....*....|....*....|....*....|....*.
gi 1277773221 374 ETRKSMEKQSYLYGQKT-SWPIAAIAHLNVFKKIIN 408
Cdd:COG0438 88 ELRRRLGEAARERAEERfSWEAIAERLLALYEELLA 123
|
|
| YyaL |
COG1331 |
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ... |
607-700 |
5.41e-07 |
|
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only];
Pssm-ID: 440942 [Multi-domain] Cd Length: 672 Bit Score: 52.93 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 607 ITYDNGRLPEALFLAYEVTKNKLYLKIAKESLDFL-SSLVILNDKLVligqRGWYNHKGK-RAFFDqqplDAASMVQVFL 684
Cdd:COG1331 411 LTSWNGLMIAALAEAGRVLGDPEYLEAAERAADFIlDNLWDPDGRLL----RSYRDGEAGiPGFLE----DYAFLIEALL 482
|
90
....*....|....*.
gi 1277773221 685 RAYQVTDEKKYQHKAL 700
Cdd:COG1331 483 ALYEATGDPRWLERAL 498
|
|
| LanC_like |
cd04434 |
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ... |
518-748 |
4.39e-05 |
|
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.
Pssm-ID: 271198 [Multi-domain] Cd Length: 351 Bit Score: 46.34 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 518 ALWAAGFVMNSNLPENIKKTAKFIFDKAIKNIAKLKSP-----RGQAFSLIGLYYYYEAYPNPEIRQKIILLAERLVKFY 592
Cdd:cd04434 57 LLWALLELYEDLGDEKLLDALLDLLDDIALEAKEVWWSgndliLGDAGIILYLLYAAEKTGDEKYKELAAKIGDFLLQAA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 593 QKEKTKDWCWFEQTITYDN---GRLPEALFLA--YEVTKNKLYLKIAKESLDFLSSLVILNDKLVLIGQ--------RGW 659
Cdd:cd04434 137 EELDNGGNWGLPKGSIYPGfahGTAGIAYALArlYEETGDEDFLDAAKEGAEYLEAIAVGDEDGFLIPLpdekdlfyLGW 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 660 --------------YNHKGKRAFFD-----------QQPLD------------AASMVQVFLRAYQVTDEKKYQHKA--- 699
Cdd:cd04434 217 chgpagtallfyelYKATGDLDLADellegiiktgaPEKLSpgfwnnlclchgTAGVLEHLLYVYRLTGDEREYAKRlad 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1277773221 700 -LLAFSWFlgiNSINQPVYDQTTSGCFDGLLPDcvnLNQGAESTISYLLS 748
Cdd:cd04434 297 kLLGRATR---NGEGLRWYQAWTGPGRVDASLG---LMVGAAGIASALLK 340
|
|
| LanC_SerThrkinase |
cd04791 |
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ... |
563-696 |
2.44e-04 |
|
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.
Pssm-ID: 271199 [Multi-domain] Cd Length: 327 Bit Score: 43.80 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 563 IGLY--YYYEAYPNPEIRQKIILLAERLVKFYQK-EKTKDWCWF-EQTITYDNGRLPEALFL--AYEVTKNKLYLKIAKE 636
Cdd:cd04791 91 IGLAllHLARATGDPEFLERAARIAERLAARLREdDPGVYWNDAgAVRAGLLHGWSGIALFLlrLYEATGDPAYLDLAER 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277773221 637 SLDF-LSSLVILNDKLVligqrgWYNHKGKRAFfdqqP-LD--AASMVQVFLRAYQVTDEKKYQ 696
Cdd:cd04791 171 ALRKdLARCVEDDDGAL------LQVDEGNRLL----PyLCsgSAGIGLVLLRYLRHRGDDRYR 224
|
|
| YihS |
COG2942 |
Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate ... |
557-641 |
3.32e-03 |
|
Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate transport and metabolism];
Pssm-ID: 442185 Cd Length: 380 Bit Score: 40.63 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 557 GQAFSLIGLYYYYEAYPNPEIRQKIILLAERLVKF--------YQKEKTKDWCWFEQTITYD-NGRLPEALFLAYEVTKN 627
Cdd:COG2942 110 GHAFALLALAEAYRATGDPEALELAKETFELLERRfwdpehggYAEAFDRDWSPLRPYRGQNaHMHLLEALLALYEATGD 189
|
90
....*....|....
gi 1277773221 628 KLYLKIAKESLDFL 641
Cdd:COG2942 190 ERWLERAEEIADLI 203
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
31-404 |
2.34e-93 |
|
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: 295.83 E-value: 2.34e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 31 ILYMSSYPPRECGIATYTRDLVKAIDRKfSPYLESKILAMNENGssIYNYCSKVKYQINQTEIEDYINVARKINKDDsIR 110
Cdd:cd03822 2 IAVLGTLPPRKCGIATYTDDLVEGLRKG-GPVVIVVIVSPQDEI--LKDDDFEVPNEIKSWNSNEYFRLLDHLNFKK-PD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 111 LINIQHEFGLFGGEWGDYLLAFLEVVKKPVVVTFHSLI--PNPTPKLKKVIQAIAKRCEKIIVMADMAIEYYECDYGLKK 188
Cdd:cd03822 78 VVHIQHEFGIFGGKYGLYALGLLLHLRIPVITTLHTVLdlSDPGKQALKVLFRIATLSERVVVMAPISRFLLVRIKLIPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 189 SQLVVIPHGTPVIEPYSSEASKKKLGFEGKMLLSTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGETHPVVRKYEGE 268
Cdd:cd03822 158 VNIEVIPHGVPEVPQDPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGELHPSLARYEGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 269 KYRNKLIKLsqkLNLTNYVKFYNKYLTLEEIINYLKSTDIYLCPPLAVNQITSGTLAYALSAGKAIVSTPFLHAKEVLQQ 348
Cdd:cd03822 238 RYRKAAIEE---LGLQDHVDFHNNFLPEEEVPRYISAADVVVLPYLNTEQSSSGTLSYAIACGKPVISTPLRHAEELLAD 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1277773221 349 GRGEIVGFRDPTGISRVVNALIEKPETRKSMEKQSYLYGQKTSWPIAAIAHLNVFK 404
Cdd:cd03822 315 GRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIADRYLRLFN 370
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
32-404 |
3.26e-33 |
|
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: 131.51 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 32 LYMSSYPPRECGIATYTRDLVKAIDRK------FSPYLESKILAMNENGSSIYNYCSKVKYQinqteieDYINVARKINK 105
Cdd:cd03801 4 LLSPELPPPVGGAERHVRELARALAARghdvtvLTPADPGEPPEELEDGVIVPLLPSLAALL-------RARRLLRELRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 106 DDSIRLINIQHEFGLFGGEWGDYLLAFLevvKKPVVVTFHSLIPNPTPKL----KKVIQAIAKRCE---KIIVMADMAIE 178
Cdd:cd03801 77 LLRLRKFDVVHAHGLLAALLAALLALLL---GAPLVVTLHGAEPGRLLLLlaaeRRLLARAEALLRradAVIAVSEALRD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 179 YYECDYGLKKSQLVVIPHGTPvIEPYSSEASKKKLGFEGKMLLSTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGET 258
Cdd:cd03801 154 ELRALGGIPPEKIVVIPNGVD-LERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 259 HPvvrkyegekYRNKLIKLsqKLNLTNYVKFYNkYLTLEEIINYLKSTDIYLCP------PLAVNQitsgtlayALSAGK 332
Cdd:cd03801 233 GP---------LRAELEEL--ELGLGDRVRFLG-FVPDEELPALYAAADVFVLPsryegfGLVVLE--------AMAAGL 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277773221 333 AIVSTPFLHAKEVLQQGR-GEIVGFRDPTGISRVVNALIEKPETRKSMEKQSYLYGQKT-SWPIAAIAHLNVFK 404
Cdd:cd03801 293 PVVATDVGGLPEVVEDGEgGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERfSWERVAERLLDLYR 366
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
231-384 |
3.40e-17 |
|
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: 79.24 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 231 KGVEYVIKALPKIIEKHPEVLYLIIGEthpvvrkyegEKYRNKLIKLSQKLNLTNYVKFYnKYLTLEEIINYLKSTDIYL 310
Cdd:pfam00534 15 KGLDLLIKAFALLKEKNPNLKLVIAGD----------GEEEKRLKKLAEKLGLGDNVIFL-GFVSDEDLPELLKIADVFV 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277773221 311 CP----PLAVnqitsgTLAYALSAGKAIVSTPFLHAKEVLQQG-RGEIVGFRDPTGISRVVNALIEKPETRKSMEKQSY 384
Cdd:pfam00534 84 LPsryeGFGI------VLLEAMACGLPVIASDVGGPPEVVKDGeTGFLVKPNNAEALAEAIDKLLEDEELRERLGENAR 156
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
43-381 |
1.24e-14 |
|
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.
Pssm-ID: 340839 [Multi-domain] Cd Length: 351 Bit Score: 75.86 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 43 GIATYTRDLVKAIDRKFspyLESKILAMNENGssiyNYCSKVKYQINQTEIEDYINVARKINKDDSIRLIN---IQHEFG 119
Cdd:cd03811 13 GAERVLLNLANALDKRG---YDVTLVLLRDEG----DLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKrilKRAKPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 120 LF--GGEWGDYLLAFLEVVKKPVVVTFHSLIPNPTPKLKKVIQAIA--KRCEKIIV----MADMAIEYYecdyGLKKSQL 191
Cdd:cd03811 86 VVisFLGFATYIVAKLAAARSKVIAWIHSSLSKLYYLKKKLLLKLKlyKKADKIVCvskgIKEDLIRLG----PSPPEKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 192 VVIPHGTPV--IEPySSEASKKKLGFEGKMLLsTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGethpvvrkyEGEK 269
Cdd:cd03811 162 EVIYNPIDIdrIRA-LAKEPILNEPEDGPVIL-AVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILG---------DGPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 270 yRNKLIKLSQKLNLTNYVKFY----NKYltleeiiNYLKSTDIYLCP------PLavnqitsgTLAYALSAGKAIVSTPF 339
Cdd:cd03811 231 -REELEKLAKELGLAERVIFLgfqsNPY-------PYLKKADLFVLSsryegfPN--------VLLEAMALGTPVVSTDC 294
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1277773221 340 LHAKEVLQQGR-GEIVGFRDPTGISRVVNALIEKPETRKSMEK 381
Cdd:cd03811 295 PGPREILDDGEnGLLVPDGDAAALAGILAALLQKKLDAALRER 337
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
139-385 |
1.82e-14 |
|
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: 75.47 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 139 PVVVTFHSLIPnPTPKLKKVIQAIAKRCEKIIVMADMAIEYYECDYGLKKSQLVVIPHG--TPVIEPYSSEASKKKLGF- 215
Cdd:cd03819 101 PLVTTVHGSYL-ATYHPKDFALAVRARGDRVIAVSELVRDHLIEALGVDPERIRVIPNGvdTDRFPPEAEAEERAQLGLp 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 216 EGKMLLSTFGLLNQGKGVEYVIKALPKIiEKHPEVLYLIIGETHPvvrkyegekyRNKLIKLSQKLNLTNYVKF--YNky 293
Cdd:cd03819 180 EGKPVVGYVGRLSPEKGWLLLVDAAAEL-KDEPDFRLLVAGDGPE----------RDEIRRLVERLGLRDRVTFtgFR-- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 294 ltlEEIINYLKSTDIYLCPPLavNQITSGTLAYALSAGKAIVSTPFLHAKEVLQQGR-GEIVGFRDPTGISRVVNALIEK 372
Cdd:cd03819 247 ---EDVPAALAASDVVVLPSL--HEEFGRVALEAMACGTPVVATDVGGAREIVVHGRtGLLVPPGDAEALADAIRAAKLL 321
|
250
....*....|...
gi 1277773221 373 PETRKSMEKQSYL 385
Cdd:cd03819 322 PEAREKLQAAAAL 334
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
217-381 |
1.42e-13 |
|
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: 72.87 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 217 GKMLLSTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGethpvvrkyEGEkYRNKLIKLSQKLNLTNYVKFYNkYLTL 296
Cdd:cd03799 173 GKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIG---------DGD-LKEQLQQLIQELNIGDCVKLLG-WKPQ 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 297 EEIINYLKSTDIYLCPPLAVNQ----ITSGTLAYALSAGKAIVSTPFLHAKEVLQQG-RGEIVGFRDPTGISRVVNALIE 371
Cdd:cd03799 242 EEIIEILDEADIFIAPSVTAADgdqdGPPNTLKEAMAMGLPVISTEHGGIPELVEDGvSGFLVPERDAEAIAEKLTYLIE 321
|
170
....*....|
gi 1277773221 372 KPETRKSMEK 381
Cdd:cd03799 322 HPAIWPEMGK 331
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
231-371 |
3.47e-11 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 61.37 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 231 KGVEYVIKALPKIIEKHPEVLYLIIGEthpvvrkYEGEKYRNKLIKLSQKLNLTNYVkfynkyltlEEIINYLKSTDIYL 310
Cdd:pfam13692 15 KGVDYLLEAVPLLRKRDNDVRLVIVGD-------GPEEELEELAAGLEDRVIFTGFV---------EDLAELLAAADVFV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277773221 311 CP------PLAVNQitsgtlayALSAGKAIVSTPFLHAKEVLQQGRGEIVGFRDPTGISRVVNALIE 371
Cdd:pfam13692 79 LPslyegfGLKLLE--------AMAAGLPVVATDVGGIPELVDGENGLLVPPGDPEALAEAILRLLE 137
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
36-383 |
3.52e-11 |
|
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: 65.76 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 36 SYPPRECGIATYTRDLVKAIDRKfspYLESKILAMNENGSSIYNYCSKVKYQINQTEIEDYINVARKINKDDSIR----- 110
Cdd:cd03817 8 TYLPQVNGVATSVRNLARALEKR---GHEVYVITPSDPGAEDEEEVVRYRSFSIPIRKYHRQHIPFPFKKAVIDRikelg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 111 --LINIQHEFGLFggewgdylLAFLEVVKK---PVVVTFHSL-------IPNPTPKLKKVIQAIAKR----CEKIIVMAD 174
Cdd:cd03817 85 pdIIHTHTPFSLG--------KLGLRIARKlkiPIVHTYHTMyedylhyIPKGKLLVKAVVRKLVRRfynhTDAVIAPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 175 MAIEYYEcDYGLKKsQLVVIPHGTP--VIEPYSSEASKKKLGF--EGKMLLSTfGLLNQGKGVEYVIKALPKIIEKhPEV 250
Cdd:cd03817 157 KIKDTLR-EYGVKG-PIEVIPNGIDldKFEKPLNTEERRKLGLppDEPILLYV-GRLAKEKNIDFLLRAFAELKKE-PNI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 251 LYLIIGEthpvvrkyeGeKYRNKLIKLSQKLNLTNYVKFYNkYLTLEEIINYLKSTDIYLCPPLAVNQitsgTLAY--AL 328
Cdd:cd03817 233 KLVIVGD---------G-PEREELKELARELGLADKVIFTG-FVPREELPEYYKAADLFVFASTTETQ----GLVYleAM 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1277773221 329 SAGKAIVSTPFLHAKEVLQQGRGeivGFRDPTGISRVVNALIEKPETRKSMEKQS 383
Cdd:cd03817 298 AAGLPVVAAKDPAASELVEDGEN---GFLFEPNDETLAEKLLHLRENLELLRKLS 349
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
119-386 |
2.36e-10 |
|
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: 63.00 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 119 GLFGGewgdylLAFLEVVKKPVVVTFHSL--IPNPTPKLKKVIQAI----AKRCEKIIVMADMAIEYYECDYGLKKSQLV 192
Cdd:cd03808 93 GILGR------LAARLAGVPKVIYTVHGLgfVFTEGKLLRLLYLLLeklaLLFTDKVIFVNEDDRDLAIKKGIIKKKKTV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 193 VIPH-GTPVIE----PYSSEASKKKLGFEGKMLLStfgllnqgKGVEYVIKALPKIIEKHPEVLYLIIGETHPvvrkyeg 267
Cdd:cd03808 167 LIPGsGVDLDRfqysPESLPSEKVVFLFVARLLKD--------KGIDELIEAAKILKKKGPNVRFLLVGDGEL------- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 268 ekyRNKLIKLSQKLNLTNYVKFYNKyltLEEIINYLKSTDIYLCP------PLAVNQitsgtlayALSAGKAIVSTPFLH 341
Cdd:cd03808 232 ---ENPSEILIEKLGLEGRIEFLGF---RSDVPELLAESDVFVLPsyreglPRSLLE--------AMAAGRPVITTDVPG 297
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1277773221 342 AKEVLQQGR-GEIVGFRDPTGISRVVNALIEKPETRKSMEKQSYLY 386
Cdd:cd03808 298 CRELVIDGVnGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKR 343
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
123-401 |
9.27e-10 |
|
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: 61.23 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 123 GEWGDYLLAFLEVVKK---PVVVTFHSLIPNPTPKLKKVIQAIAK-RCEK--------IIVMADMaiEYYECDYGLKKSQ 190
Cdd:cd03821 98 GVWTYTSLAACKLARRrgiPYVVSPHGMLDPWALQQKHWKKRIALhLIERrnlnnaalVHFTSEQ--EADELRRFGLEPP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 191 LVVIPHG--TPVIEPYSSEASKKKLGFEGKMLLsTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGethpvvrkyEGE 268
Cdd:cd03821 176 IAVIPNGvdIPEFDPGLRDRRKHNGLEDRRIIL-FLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAG---------PDD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 269 KYRNKLIKLSQKLNLTNYVKFYNKyLTLEEIINYLKSTDIYLCP------PLAVnqitsgtlAYALSAGKAIVSTPFLHA 342
Cdd:cd03821 246 GAYPAFLQLQSSLGLGDRVTFTGP-LYGEAKWALYASADLFVLPsysenfGNVV--------AEALACGLPVVITDKCGL 316
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277773221 343 KEVLQQGRGEIVGFRDpTGISRVVNALIEKPETRKSME---KQSYLYGQKTSWPIAAIAHLN 401
Cdd:cd03821 317 SELVEAGCGVVVDPNV-SSLAEALAEALRDPADRKRLGemaRRARQVEENFSWEAVAGQLGE 377
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
36-382 |
1.31e-09 |
|
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340826 [Multi-domain] Cd Length: 355 Bit Score: 60.75 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 36 SYPPRECGIATYTRDLVKAIDRKfspYLESKILAMNENGSSIYN-------YCSKVKYQINQTEIE-DYINVARKINKDD 107
Cdd:cd03795 8 FYYPDIGGIEQVIYDLAEGLKKK---GIEVDVLCFSKEKETPEKeengiriHRVKSFLNVASTPFSpSYIKRFKKLAKEY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 108 SIrlINIQHEFGLfggewGDyLLAFLEVVKKPVVVTFHSLIPNpTPKLKKVIQAIAKR-CEKIIVMADMAIEYYECDYGL 186
Cdd:cd03795 85 DI--IHYHFPNPL-----AD-LLLFFSGAKKPVVVHWHSDIVK-QKKLLKLYKPLMTRfLRRADRIIATSPNYVETSPTL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 187 K--KSQLVVIPHGTPVIEP--YSSEASKKKLGFEGKMLLSTFGLLNQGKGVEYVIKALpKIIEkhpevLYLIIGETHPVV 262
Cdd:cd03795 156 RefKNKVRVIPLGIDKNVYniPRVDFENIKREKKGKKIFLFIGRLVYYKGLDYLIEAA-QYLN-----YPIVIGGEGPLK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 263 RKYEgekyrnKLIklsqKLNLTNYVKFYnKYLTLEEIINYLKSTDIYLCPPLAVNQITSGTLAYALSAGKAIVST----- 337
Cdd:cd03795 230 PDLE------AQI----ELNLLDNVKFL-GRVDDEEKVIYLHLCDVFVFPSVLRSEAFGIVLLEAMMCGKPVISTnigtg 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1277773221 338 -PFLhakeVLQQGRGEIVGFRDPTGISRVVNALIEKPETRKSMEKQ 382
Cdd:cd03795 299 vPYV----NNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGEN 340
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
43-312 |
3.58e-09 |
|
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: 59.30 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 43 GIATYTRDLVKAIDRKFSPYLEskILAmneNGSSIYNYCSKVKYQINQTEIEDYINVARKINKDDSIRLINIQHEFGLFg 122
Cdd:cd03809 15 GIGRYTRELLKALAKNDPDESV--LAV---PPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDKPDLL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 123 geWGDYLLAFLEVVKKPVVVTFHSLI----PNPTPK-----LKKVIQAIAKRCEKIIV----MADMAIEYyecdYGLKKS 189
Cdd:cd03809 89 --HSPHNTAPLLLKGCPQVVTIHDLIplryPEFFPKrfrlyYRLLLPISLRRADAIITvseaTRDDIIKF----YGVPPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 190 QLVVIPHGtpVIEPYSSEASKKKLGFEGKMLLSTFGLLNQ---GKGVEYVIKALPKIIEKHPEVLYLIIGETHPvvrKYE 266
Cdd:cd03809 163 KIVVIPLG--VDPSFFPPESAAVLIAKYLLPEPYFLYVGTlepRKNHERLLKAFALLKKQGGDLKLVIVGGKGW---EDE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1277773221 267 gekyrnKLIKLSQKLNLTNYVKFYNkYLTLEEIINYLKSTDIYLCP 312
Cdd:cd03809 238 ------ELLDLVKKLGLGGRVRFLG-YVSDEDLPALYRGARAFVFP 276
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
137-379 |
9.39e-09 |
|
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: 58.10 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 137 KKPVVVTFHSLI--PNPTPKLKKVIQAIAKRCEKIIVMADMAIEYYEcDYGLKKSQLVVIPHGtpvIEPYSSEASKKKLG 214
Cdd:cd03807 103 GVKVIWSVRSSNipQRLTRLVRKLCLLLSKFSPATVANSSAVAEFHQ-EQGYAKNKIVVIYNG---IDLFKLSPDDASRA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 215 F--------EGKMLLSTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGEthpvvrkyeGEKYRNkLIKLSQKLNLTNY 286
Cdd:cd03807 179 RarrrlglaEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGR---------GPERPN-LERLLLELGLEDR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 287 VKFYNkylTLEEIINYLKSTDIYLCPplAVNQITSGTLAYALSAGKAIVSTPFLHAKEVLQQGRGEIVGFRDPTGISRVV 366
Cdd:cd03807 249 VHLLG---ERSDVPALLPAMDIFVLS--SRTEGFPNALLEAMACGLPVVATDVGGAAELVDDGTGFLVPAGDPQALADAI 323
|
250
....*....|...
gi 1277773221 367 NALIEKPETRKSM 379
Cdd:cd03807 324 RALLEDPEKRARL 336
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
137-406 |
1.24e-08 |
|
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: 57.77 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 137 KKPVVVTFHS----LIPnPTPKLKKVIQAIAKRCEKII-VMADMAIEYyeCDYGLKKSQLVVIPHG------TPVIEPYS 205
Cdd:cd03798 119 GVPYVVTEHGsdinVFP-PRSLLRKLLRWALRRAARVIaVSKALAEEL--VALGVPRDRVDVIPNGvdparfQPEDRGLG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 206 SEASKKKLGFEGKmllstfglLNQGKGVEYVIKALPKIIEKHPEVLYLIIGethpvvrkyEGEKyRNKLIKLSQKLNLTN 285
Cdd:cd03798 196 LPLDAFVILFVGR--------LIPRKGIDLLLEAFARLAKARPDVVLLIVG---------DGPL-REALRALAEDLGLGD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 286 YVKFYNkYLTLEEIINYLKSTDIYLCP------PLAVNQitsgtlayALSAGKAIVSTPFLHAKEVLQQGR-GEIVGFRD 358
Cdd:cd03798 258 RVTFTG-RLPHEQVPAYYRACDVFVLPsrhegfGLVLLE--------AMACGLPVVATDVGGIPEVVGDPEtGLLVPPGD 328
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1277773221 359 PTGISRVVNALIEKPETRKSMEKQSYLYGQKTSWPIAAIAHLNVFKKI 406
Cdd:cd03798 329 ADALAAALRRALAEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
296-408 |
1.31e-08 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 53.84 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 296 LEEIIN-YLKSTDIYLCPPLAVNqiTSGTLAYALSAGKAIVSTPFLHAKEVLQQGR-GEIVGFRDPTGISRVVNALIEKP 373
Cdd:COG0438 10 LDLLLEaLLAAADVFVLPSRSEG--FGLVLLEAMAAGLPVIATDVGGLPEVIEDGEtGLLVPPGDPEALAEAILRLLEDP 87
|
90 100 110
....*....|....*....|....*....|....*.
gi 1277773221 374 ETRKSMEKQSYLYGQKT-SWPIAAIAHLNVFKKIIN 408
Cdd:COG0438 88 ELRRRLGEAARERAEERfSWEAIAERLLALYEELLA 123
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
191-354 |
1.26e-07 |
|
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: 53.18 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 191 LVVIPHGTPVIEPYSSEASKK---KLGFEGKMLLStFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGETHPvvrKYEG 267
Cdd:cd01635 81 IVVTVHGPDSLESTRSELLALarlLVSLPLADKVS-VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGE---REEE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 268 EKYRNKLIKLSQklnltnyVKFYNKYLTLEEIINYLKSTDIYLCPPLAVNQitSGTLAYALSAGKAIVSTPFLHAKEVLQ 347
Cdd:cd01635 157 EALAAALGLLER-------VVIIGGLVDDEVLELLLAAADVFVLPSRSEGF--GLVLLEAMAAGKPVIATDVGGIPEFVV 227
|
....*...
gi 1277773221 348 QGR-GEIV 354
Cdd:cd01635 228 DGEnGLLV 235
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
128-384 |
1.65e-07 |
|
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: 54.17 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 128 YLLAFLEVvKKPVVVTFHS--LIPNPTPKLKKVIQAIAKRCEKIIVMADMAIEYYecdYGLKKSQLVVIPHgtpviePYS 205
Cdd:cd03820 100 TFLALIGL-KSKLIVWEHNnyEAYNKGLRRLLLRRLLYKRADKIVVLTEADKLKK---YKQPNSNVVVIPN------PLS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 206 SEASKKKLGFEGKMLLSTfGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGethpvvrkyEGEKyRNKLIKLSQKLNLTN 285
Cdd:cd03820 170 FPSEEPSTNLKSKRILAV-GRLTYQKGFDLLIEAWALIAKKHPDWKLRIYG---------DGPE-REELEKLIDKLGLED 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 286 YVKFYNkylTLEEIINYLKSTDIYLCP------PLavnqitsgTLAYALSAGKAIVSTPFLHA-KEVLQQGR-GEIVGFR 357
Cdd:cd03820 239 RVKLLG---PTKNIAEEYANSSIFVLSsryegfPM--------VLLEAMAYGLPIISFDCPTGpSEIIEDGEnGLLVPNG 307
|
250 260
....*....|....*....|....*..
gi 1277773221 358 DPTGISRVVNALIEKPETRKSMEKQSY 384
Cdd:cd03820 308 DVDALAEALLRLMEDEELRKKMGKNAR 334
|
|
| YyaL |
COG1331 |
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ... |
607-700 |
5.41e-07 |
|
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only];
Pssm-ID: 440942 [Multi-domain] Cd Length: 672 Bit Score: 52.93 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 607 ITYDNGRLPEALFLAYEVTKNKLYLKIAKESLDFL-SSLVILNDKLVligqRGWYNHKGK-RAFFDqqplDAASMVQVFL 684
Cdd:COG1331 411 LTSWNGLMIAALAEAGRVLGDPEYLEAAERAADFIlDNLWDPDGRLL----RSYRDGEAGiPGFLE----DYAFLIEALL 482
|
90
....*....|....*.
gi 1277773221 685 RAYQVTDEKKYQHKAL 700
Cdd:COG1331 483 ALYEATGDPRWLERAL 498
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
43-197 |
1.01e-06 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 49.45 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 43 GIATYTRDLVKAIDRK------FSPYLESKILAMNENGSSI--YNYCSKVKYQINQTEIEDYINVARKINKDdsirLINI 114
Cdd:pfam13439 2 GVERYVLELARALARRghevtvVTPGGPGPLAEEVVRVVRVprVPLPLPPRLLRSLAFLRRLRRLLRRERPD----VVHA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 115 QHEFGLFGGewgdyLLAFLEVVKKPVVVTFHSLIPNPTPK----------LKKVIQAIAKRCEKIIVMADMAIEYYECDY 184
Cdd:pfam13439 78 HSPFPLGLA-----ALAARLRLGIPLVVTYHGLFPDYKRLgarlsplrrlLRRLERRLLRRADRVIAVSEAVADELRRLY 152
|
170
....*....|...
gi 1277773221 185 GLKKSQLVVIPHG 197
Cdd:pfam13439 153 GVPPEKIRVIPNG 165
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
180-381 |
2.79e-06 |
|
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: 50.41 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 180 YECDYGLKKSQLVVIPHGTPvIEPYS--SEASKKKLGFegkmLLSTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGE 257
Cdd:cd03813 258 RQIRLGADPDKTRVIPNGID-IQRFApaREERPEKEPP----VVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIGP 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 258 ThpvvrkYEGEKYRNKLIKLSQKLNLTNYVKFynkyLTLEEIINYLKSTDIylcppLAVNQITSG---TLAYALSAGKAI 334
Cdd:cd03813 333 E------DEDPEYAQECKRLVASLGLENKVKF----LGFQNIKEYYPKLGL-----LVLTSISEGqplVILEAMASGVPV 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1277773221 335 VSTPFLHAKEVLQQGR------GEIVGFRDPTGISRVVNALIEKPETRKSMEK 381
Cdd:cd03813 398 VATDVGSCRELIYGADdalgqaGLVVPPADPEALAEALIKLLRDPELRQAFGE 450
|
|
| YyaL |
COG1331 |
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ... |
609-641 |
4.13e-05 |
|
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only];
Pssm-ID: 440942 [Multi-domain] Cd Length: 672 Bit Score: 47.15 E-value: 4.13e-05
10 20 30
....*....|....*....|....*....|...
gi 1277773221 609 YDNGRLPEALFLAYEVTKNKLYLKIAKESLDFL 641
Cdd:COG1331 269 YDNALLLRLYAEAYQLTGDPLYRRVAEETLDFL 301
|
|
| LanC_like |
cd04434 |
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ... |
518-748 |
4.39e-05 |
|
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.
Pssm-ID: 271198 [Multi-domain] Cd Length: 351 Bit Score: 46.34 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 518 ALWAAGFVMNSNLPENIKKTAKFIFDKAIKNIAKLKSP-----RGQAFSLIGLYYYYEAYPNPEIRQKIILLAERLVKFY 592
Cdd:cd04434 57 LLWALLELYEDLGDEKLLDALLDLLDDIALEAKEVWWSgndliLGDAGIILYLLYAAEKTGDEKYKELAAKIGDFLLQAA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 593 QKEKTKDWCWFEQTITYDN---GRLPEALFLA--YEVTKNKLYLKIAKESLDFLSSLVILNDKLVLIGQ--------RGW 659
Cdd:cd04434 137 EELDNGGNWGLPKGSIYPGfahGTAGIAYALArlYEETGDEDFLDAAKEGAEYLEAIAVGDEDGFLIPLpdekdlfyLGW 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 660 --------------YNHKGKRAFFD-----------QQPLD------------AASMVQVFLRAYQVTDEKKYQHKA--- 699
Cdd:cd04434 217 chgpagtallfyelYKATGDLDLADellegiiktgaPEKLSpgfwnnlclchgTAGVLEHLLYVYRLTGDEREYAKRlad 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1277773221 700 -LLAFSWFlgiNSINQPVYDQTTSGCFDGLLPDcvnLNQGAESTISYLLS 748
Cdd:cd04434 297 kLLGRATR---NGEGLRWYQAWTGPGRVDASLG---LMVGAAGIASALLK 340
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
163-409 |
6.43e-05 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic 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: 340818 [Multi-domain] Cd Length: 350 Bit Score: 45.67 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 163 AKRCEKIivmadmAIEYYECDYGLKKSQLVVIphGTPVI-EPYSSEASKKKLGF-EGKMLLSTFG------LLNQGkgve 234
Cdd:cd03785 132 SRFADKV------AVSFPETKKYFPAAKVVVT--GNPVReEILNLRKELKRFGLpPDKPTLLVFGgsqgarAINRA---- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 235 yVIKALPKIIEKHPEVLYliigethpVVRKYEGEKYRNKLIKLSQKLNLTNYVkfynkyltlEEIINYLKSTDIYLCPPL 314
Cdd:cd03785 200 -VPKALPKLLERGIQVIH--------QTGKGDYDEVKKLYEDLGINVKVFPFI---------DDMAAAYAAADLVISRAG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 315 AvnqitsGTLAYALSAGKAIVSTPFLH---------AKEVLQQGRGEIVGFRDPTG--ISRVVNALIEKPETRKSMEKqs 383
Cdd:cd03785 262 A------STIAELTAAGKPAILIPYPYaaddhqeanARALEKAGAAIVIDQEELTPevLAEAILDLLNDPERLKKMAE-- 333
|
250 260
....*....|....*....|....*.
gi 1277773221 384 ylygqktswPIAAIAHLNVFKKIINL 409
Cdd:cd03785 334 ---------AAKKLAKPDAAERIADL 350
|
|
| LanM-like |
cd04792 |
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ... |
562-644 |
7.03e-05 |
|
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.
Pssm-ID: 271200 [Multi-domain] Cd Length: 836 Bit Score: 46.54 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 562 LIGLYYYYEAYPNPEIRQKIILLAERLVKFYQK-EKTKDWCWFEQT------------ITYdngrlpeALFLAYEVTKNK 628
Cdd:cd04792 598 ILVLLALYERTGDERALELAIACGDHLLKNAVEnDGGARWKTPASSrpltgfahgaagIAW-------ALLRLAAVTGDE 670
|
90
....*....|....*.
gi 1277773221 629 LYLKIAKESLDFLSSL 644
Cdd:cd04792 671 RYLEAAKEALAYERSL 686
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
139-396 |
9.26e-05 |
|
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: 45.31 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 139 PVVVTFHSL--------IPNPTPKLKKVIQA---IAKRCEKIIVMADMAIEYYECDYGLKKSQLVVIPHGTPV--IEPYS 205
Cdd:cd03800 126 PLVHTFHSLgrvkyrhlGAQDTYHPSLRITAeeqILEAADRVIASTPQEADELISLYGADPSRINVVPPGVDLerFFPVD 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 206 -SEASKKKLGF--EGKMLLStFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGEThpvvRKYEGEKYRNKLIKLSQKLN 282
Cdd:cd03800 206 rAEARRARLLLppDKPVVLA-LGRLDPRKGIDTLVRAFAQLPELRELANLVLVGGP----SDDPLSMDREELAELAEELG 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 283 LTNYVKFYnKYLTLEEIINYLKSTDIYLCPPL-------AVNQITSGTlayalsagkAIVSTPFLHAKEVLQQGR-GEIV 354
Cdd:cd03800 281 LIDRVRFP-GRVSRDDLPELYRAADVFVVPSLyepfgltAIEAMACGT---------PVVATAVGGLQDIVRDGRtGLLV 350
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1277773221 355 GFRDPTGISRVVNALIEKPETRKSMEKQSYLYGQKT-SWPIAA 396
Cdd:cd03800 351 DPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHyTWESVA 393
|
|
| YesR |
COG4225 |
Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism]; |
541-695 |
1.84e-04 |
|
Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism];
Pssm-ID: 443369 Cd Length: 336 Bit Score: 44.42 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 541 IFDKAIKNIAKLKSPRG------QAFSLIGLYYYYEAYPNPEIRQKIILLAERLVkfyqkEKTKDWCWFEQTItyDNGRL 614
Cdd:COG4225 1 VADSQLKRYWDIDPGKFpkwdytQGVTLYGLLKLAEATGDKKYLDYIKRWFDFFI-----DEGNTYKLPPYNL--DDIAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 615 PEALFLAYEVTKNKLYLKIAKESLDFlsslvilndklVLIGQR----GWYNHKgkraffDQQP----LDAASMVQVFL-R 685
Cdd:COG4225 74 GLALLELYEQTGDPKYLKAADTLADW-----------QLNTQPrtseGGFWHK------KIYPnqlwLDGLYMAVPFLaQ 136
|
170
....*....|
gi 1277773221 686 AYQVTDEKKY 695
Cdd:COG4225 137 YGKLTGDPKY 146
|
|
| LanC_SerThrkinase |
cd04791 |
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ... |
563-696 |
2.44e-04 |
|
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.
Pssm-ID: 271199 [Multi-domain] Cd Length: 327 Bit Score: 43.80 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 563 IGLY--YYYEAYPNPEIRQKIILLAERLVKFYQK-EKTKDWCWF-EQTITYDNGRLPEALFL--AYEVTKNKLYLKIAKE 636
Cdd:cd04791 91 IGLAllHLARATGDPEFLERAARIAERLAARLREdDPGVYWNDAgAVRAGLLHGWSGIALFLlrLYEATGDPAYLDLAER 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277773221 637 SLDF-LSSLVILNDKLVligqrgWYNHKGKRAFfdqqP-LD--AASMVQVFLRAYQVTDEKKYQ 696
Cdd:cd04791 171 ALRKdLARCVEDDDGAL------LQVDEGNRLL----PyLCsgSAGIGLVLLRYLRHRGDDRYR 224
|
|
| YihS |
COG2942 |
Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate ... |
557-641 |
3.32e-03 |
|
Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate transport and metabolism];
Pssm-ID: 442185 Cd Length: 380 Bit Score: 40.63 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 557 GQAFSLIGLYYYYEAYPNPEIRQKIILLAERLVKF--------YQKEKTKDWCWFEQTITYD-NGRLPEALFLAYEVTKN 627
Cdd:COG2942 110 GHAFALLALAEAYRATGDPEALELAKETFELLERRfwdpehggYAEAFDRDWSPLRPYRGQNaHMHLLEALLALYEATGD 189
|
90
....*....|....
gi 1277773221 628 KLYLKIAKESLDFL 641
Cdd:COG2942 190 ERWLERAEEIADLI 203
|
|
| LcnDR2 |
COG4403 |
Lantibiotic modifying enzyme [Defense mechanisms]; |
557-644 |
8.97e-03 |
|
Lantibiotic modifying enzyme [Defense mechanisms];
Pssm-ID: 443528 [Multi-domain] Cd Length: 405 Bit Score: 39.34 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 557 GQAFSLIGLYYYYEAYPNPEIRQKIILLAERLVKFYQKEKTKdWCWfeQTITYDNGRLP----------EALFLAYEVTK 626
Cdd:COG4403 162 GAAGAILALLALYRATGDPAALDLAIRCGDRLLAAAVRDDGG-RAW--PTPEPAGRPLTgfahgaagiaYALLRLAAATG 238
|
90
....*....|....*...
gi 1277773221 627 NKLYLKIAKESLDFLSSL 644
Cdd:COG4403 239 DERYLEAAREALAYERSL 256
|
|
|