|
Name |
Accession |
Description |
Interval |
E-value |
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
171-272 |
8.92e-11 |
|
Glycosyl transferases group 1;
:
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 59.45 E-value: 8.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 171 GKTVGFIGSQNAvNVESLKQLVAELVALRQmLPNDFRLRLAGSMT----RGTDIHLPGFVENCGYVDDLAGFYASADLMV 246
Cdd:pfam13692 1 RPVILFVGRLHP-NVKGVDYLLEAVPLLRK-RDNDVRLVIVGDGPeeelEELAAGLEDRVIFTGFVEDLAELLAAADVFV 78
|
90 100
....*....|....*....|....*.
gi 2193138507 247 LPLeFGTGLKVKSVEAVSFGVPVLGT 272
Cdd:pfam13692 79 LPS-LYEGFGLKLLEAMAAGLPVVAT 103
|
|
| Glycosyltransferase_GTB-type super family |
cl10013 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
28-313 |
1.54e-10 |
|
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.
The actual alignment was detected with superfamily member cd03801:
Pssm-ID: 471961 [Multi-domain] Cd Length: 366 Bit Score: 62.56 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 28 HVHVVPHSGPNGGFEGTLDALWTKGLEDMVGWLRLN------------FEFEVVWAHYVLLSKVCELFKGEATV-TVVDT 94
Cdd:cd03801 33 DVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARrllrelrpllrlRKFDVVHAHGLLAALLAALLALLLGApLVVTL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 95 HDVLGDRDAIFKPFGRKSDfasltrEEEKRGLARADFAVACQPEDEEYFKREYGLQNtltigqiQHATVIP--------- 165
Cdd:cd03801 113 HGAEPGRLLLLLAAERRLL------ARAEALLRRADAVIAVSEALRDELRALGGIPP-------EKIVVIPngvdlerfs 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 166 -------ERKGPGKTVGFIGSQNAV-NVESLKQLVAELVALRqmlpNDFRLRLAGS------MTRGTDIHLPGFVENCGY 231
Cdd:cd03801 180 pplrrklGIPPDRPVLLFVGRLSPRkGVDLLLEALAKLLRRG----PDVRLVIVGGdgplraELEELELGLGDRVRFLGF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 232 V--DDLAGFYASADLMVLPLEF-GTGLKVksVEAVSFGVPVLGTEH-AFIGLVTDEP---LHQFQTVKALVRAIPAVLAD 304
Cdd:cd03801 256 VpdEELPALYAAADVFVLPSRYeGFGLVV--LEAMAAGLPVVATDVgGLPEVVEDGEgglVVPPDDVEALADALLRLLAD 333
|
....*....
gi 2193138507 305 VDERVRLAA 313
Cdd:cd03801 334 PELRARLGR 342
|
|
| LbetaH super family |
cl00160 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
364-451 |
5.18e-03 |
|
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.
The actual alignment was detected with superfamily member cd03360:
Pssm-ID: 469633 [Multi-domain] Cd Length: 197 Bit Score: 38.23 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 364 IYGAGIGGKIVFDALADEQRAMCLGFLD--LHKAGSSFCDLPVLAPEQVPAPARAETGVIIAIMTLEW-KSVAQSLMDAG 440
Cdd:cd03360 1 IIGAGGHARVVADILEADSGYEVVGFLDddPELKGTEGLGLPVGLDELLLLYPPPDDEFVVAIGDNKLrRKLAEKLLAAG 80
|
90
....*....|...
gi 2193138507 441 FR--SLVSAQRFI 451
Cdd:cd03360 81 YRfaTLIHPSAVV 93
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
171-272 |
8.92e-11 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 59.45 E-value: 8.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 171 GKTVGFIGSQNAvNVESLKQLVAELVALRQmLPNDFRLRLAGSMT----RGTDIHLPGFVENCGYVDDLAGFYASADLMV 246
Cdd:pfam13692 1 RPVILFVGRLHP-NVKGVDYLLEAVPLLRK-RDNDVRLVIVGDGPeeelEELAAGLEDRVIFTGFVEDLAELLAAADVFV 78
|
90 100
....*....|....*....|....*.
gi 2193138507 247 LPLeFGTGLKVKSVEAVSFGVPVLGT 272
Cdd:pfam13692 79 LPS-LYEGFGLKLLEAMAAGLPVVAT 103
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
28-313 |
1.54e-10 |
|
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: 62.56 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 28 HVHVVPHSGPNGGFEGTLDALWTKGLEDMVGWLRLN------------FEFEVVWAHYVLLSKVCELFKGEATV-TVVDT 94
Cdd:cd03801 33 DVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARrllrelrpllrlRKFDVVHAHGLLAALLAALLALLLGApLVVTL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 95 HDVLGDRDAIFKPFGRKSDfasltrEEEKRGLARADFAVACQPEDEEYFKREYGLQNtltigqiQHATVIP--------- 165
Cdd:cd03801 113 HGAEPGRLLLLLAAERRLL------ARAEALLRRADAVIAVSEALRDELRALGGIPP-------EKIVVIPngvdlerfs 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 166 -------ERKGPGKTVGFIGSQNAV-NVESLKQLVAELVALRqmlpNDFRLRLAGS------MTRGTDIHLPGFVENCGY 231
Cdd:cd03801 180 pplrrklGIPPDRPVLLFVGRLSPRkGVDLLLEALAKLLRRG----PDVRLVIVGGdgplraELEELELGLGDRVRFLGF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 232 V--DDLAGFYASADLMVLPLEF-GTGLKVksVEAVSFGVPVLGTEH-AFIGLVTDEP---LHQFQTVKALVRAIPAVLAD 304
Cdd:cd03801 256 VpdEELPALYAAADVFVLPSRYeGFGLVV--LEAMAAGLPVVATDVgGLPEVVEDGEgglVVPPDDVEALADALLRLLAD 333
|
....*....
gi 2193138507 305 VDERVRLAA 313
Cdd:cd03801 334 PELRARLGR 342
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
168-329 |
1.25e-06 |
|
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: 50.41 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 168 KGPGKTVGFIgsqnAVNVESLKQLVAELV-ALRQMLPND-FRLRLAGSmTRGTDIHLPGFVENCGYVDD---LAGFYASA 242
Cdd:cd03825 190 PQDKKVILFG----AESVTKPRKGFDELIeALKLLATKDdLLLVVFGK-NDPQIVILPFDIISLGYIDDdeqLVDIYSAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 243 DLMVLP-LE--FGTGLkvksVEAVSFGVPVLGTEHAFIGLVTDEPLHQF----QTVKALVRAIPAVLADVDERVRLAAIS 315
Cdd:cd03825 265 DLFVHPsLAdnLPNTL----LEAMACGTPVVAFDTGGSPEIVQHGVTGYlvppGDVQALAEAIEWLLANPKERESLGERA 340
|
170
....*....|....*
gi 2193138507 316 SA-VFKEYQTRTEEQ 329
Cdd:cd03825 341 RAlAENHFDQRVQAQ 355
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
235-342 |
4.81e-06 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 45.75 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 235 LAGFYASADLMVLPLEF-GTGLKVksVEAVSFGVPVLGTEHAFIG-LVTDEP---LHQFQTVKALVRAIPAVLADVDERV 309
Cdd:COG0438 14 LEALLAAADVFVLPSRSeGFGLVL--LEAMAAGLPVIATDVGGLPeVIEDGEtglLVPPGDPEALAEAILRLLEDPELRR 91
|
90 100 110
....*....|....*....|....*....|...
gi 2193138507 310 RLAAISSAVFKEYQTRtEEQFRAFERLKEERLA 342
Cdd:COG0438 92 RLGEAARERAEERFSW-EAIAERLLALYEELLA 123
|
|
| LbH_AT_putative |
cd03360 |
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ... |
364-451 |
5.18e-03 |
|
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.
Pssm-ID: 100050 [Multi-domain] Cd Length: 197 Bit Score: 38.23 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 364 IYGAGIGGKIVFDALADEQRAMCLGFLD--LHKAGSSFCDLPVLAPEQVPAPARAETGVIIAIMTLEW-KSVAQSLMDAG 440
Cdd:cd03360 1 IIGAGGHARVVADILEADSGYEVVGFLDddPELKGTEGLGLPVGLDELLLLYPPPDDEFVVAIGDNKLrRKLAEKLLAAG 80
|
90
....*....|...
gi 2193138507 441 FR--SLVSAQRFI 451
Cdd:cd03360 81 YRfaTLIHPSAVV 93
|
|
| COG4641 |
COG4641 |
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]; |
164-313 |
9.34e-03 |
|
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443679 [Multi-domain] Cd Length: 303 Bit Score: 37.99 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 164 IPERKGPGKTVGFIGSQNAVNVESLKQLVAELValrqmlpnDFRLRLAGS----MTRGTDIHLPGFVENcgyvDDLAGFY 239
Cdd:COG4641 130 VPPEARFRYDVAFVGNYYPDRRARLEELLLAPA--------GLRLKIYGPgwpkLALPANVRRGGHLPG----EEHPAAY 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 240 ASAdLMVLPL----EFGTGLKVKSVEAVSFGVPVL-----GTEHAFiglVTDEPLHQFQTVKALVRAIPAVLADVDERVR 310
Cdd:COG4641 198 ASS-KITLNVnrmaASPDSPTRRTFEAAACGAFLLsdpweGLEELF---EPGEEVLVFRDGEELAEKLRYLLADPEERRA 273
|
...
gi 2193138507 311 LAA 313
Cdd:COG4641 274 IAE 276
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
171-272 |
8.92e-11 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 59.45 E-value: 8.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 171 GKTVGFIGSQNAvNVESLKQLVAELVALRQmLPNDFRLRLAGSMT----RGTDIHLPGFVENCGYVDDLAGFYASADLMV 246
Cdd:pfam13692 1 RPVILFVGRLHP-NVKGVDYLLEAVPLLRK-RDNDVRLVIVGDGPeeelEELAAGLEDRVIFTGFVEDLAELLAAADVFV 78
|
90 100
....*....|....*....|....*.
gi 2193138507 247 LPLeFGTGLKVKSVEAVSFGVPVLGT 272
Cdd:pfam13692 79 LPS-LYEGFGLKLLEAMAAGLPVVAT 103
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
28-313 |
1.54e-10 |
|
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: 62.56 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 28 HVHVVPHSGPNGGFEGTLDALWTKGLEDMVGWLRLN------------FEFEVVWAHYVLLSKVCELFKGEATV-TVVDT 94
Cdd:cd03801 33 DVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARrllrelrpllrlRKFDVVHAHGLLAALLAALLALLLGApLVVTL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 95 HDVLGDRDAIFKPFGRKSDfasltrEEEKRGLARADFAVACQPEDEEYFKREYGLQNtltigqiQHATVIP--------- 165
Cdd:cd03801 113 HGAEPGRLLLLLAAERRLL------ARAEALLRRADAVIAVSEALRDELRALGGIPP-------EKIVVIPngvdlerfs 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 166 -------ERKGPGKTVGFIGSQNAV-NVESLKQLVAELVALRqmlpNDFRLRLAGS------MTRGTDIHLPGFVENCGY 231
Cdd:cd03801 180 pplrrklGIPPDRPVLLFVGRLSPRkGVDLLLEALAKLLRRG----PDVRLVIVGGdgplraELEELELGLGDRVRFLGF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 232 V--DDLAGFYASADLMVLPLEF-GTGLKVksVEAVSFGVPVLGTEH-AFIGLVTDEP---LHQFQTVKALVRAIPAVLAD 304
Cdd:cd03801 256 VpdEELPALYAAADVFVLPSRYeGFGLVV--LEAMAAGLPVVATDVgGLPEVVEDGEgglVVPPDDVEALADALLRLLAD 333
|
....*....
gi 2193138507 305 VDERVRLAA 313
Cdd:cd03801 334 PELRARLGR 342
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
168-329 |
1.25e-06 |
|
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: 50.41 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 168 KGPGKTVGFIgsqnAVNVESLKQLVAELV-ALRQMLPND-FRLRLAGSmTRGTDIHLPGFVENCGYVDD---LAGFYASA 242
Cdd:cd03825 190 PQDKKVILFG----AESVTKPRKGFDELIeALKLLATKDdLLLVVFGK-NDPQIVILPFDIISLGYIDDdeqLVDIYSAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 243 DLMVLP-LE--FGTGLkvksVEAVSFGVPVLGTEHAFIGLVTDEPLHQF----QTVKALVRAIPAVLADVDERVRLAAIS 315
Cdd:cd03825 265 DLFVHPsLAdnLPNTL----LEAMACGTPVVAFDTGGSPEIVQHGVTGYlvppGDVQALAEAIEWLLANPKERESLGERA 340
|
170
....*....|....*
gi 2193138507 316 SA-VFKEYQTRTEEQ 329
Cdd:cd03825 341 RAlAENHFDQRVQAQ 355
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
235-342 |
4.81e-06 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 45.75 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 235 LAGFYASADLMVLPLEF-GTGLKVksVEAVSFGVPVLGTEHAFIG-LVTDEP---LHQFQTVKALVRAIPAVLADVDERV 309
Cdd:COG0438 14 LEALLAAADVFVLPSRSeGFGLVL--LEAMAAGLPVIATDVGGLPeVIEDGEtglLVPPGDPEALAEAILRLLEDPELRR 91
|
90 100 110
....*....|....*....|....*....|...
gi 2193138507 310 RLAAISSAVFKEYQTRtEEQFRAFERLKEERLA 342
Cdd:COG0438 92 RLGEAARERAEERFSW-EAIAERLLALYEELLA 123
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
184-312 |
5.74e-06 |
|
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: 46.11 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 184 NVESLKQLVAELVALRQmlpnDFRLRLAGSMTR-------------GTDIHLPGFVENcgyvDDLAGFYASADLMVLPLE 250
Cdd:pfam00534 16 GLDLLIKAFALLKEKNP----NLKLVIAGDGEEekrlkklaeklglGDNVIFLGFVSD----EDLPELLKIADVFVLPSR 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2193138507 251 F-GTGLKVksVEAVSFGVPVLGT---------EHAFIGLVTDEPlhqfqTVKALVRAIPAVLADVDERVRLA 312
Cdd:pfam00534 88 YeGFGIVL--LEAMACGLPVIASdvggppevvKDGETGFLVKPN-----NAEALAEAIDKLLEDEELRERLG 152
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
2-329 |
5.08e-05 |
|
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: 45.45 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 2 HFVWLASEWRGVISHDalNAMRDAWDHVHVVPHSGPNGGFEG-TLDALWtkgledmvgWLRLNFEFEVVWAHYVLLSK-V 79
Cdd:cd03798 42 WGPAAARLLRKLLGEA--VPPRDGRRLLPLKPRLRLLAPLRApSLAKLL---------KRRRRGPPDLIHAHFAYPAGfA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 80 CELFKGEATVTVVDThdVLGDRDAIFkpfgrksDFASLTREEEKRGLARADFAVACQPEDEEYFKREYGLQNTLTI---- 155
Cdd:cd03798 111 AALLARLYGVPYVVT--EHGSDINVF-------PPRSLLRKLLRWALRRAARVIAVSKALAEELVALGVPRDRVDVipng 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 156 ---GQIQHATVIPERKGPGKTVGFIGSQNAVN-----VESLKQLVAELVALRQMLPNDFRLR-----LAGSMTRGTDIHL 222
Cdd:cd03798 182 vdpARFQPEDRGLGLPLDAFVILFVGRLIPRKgidllLEAFARLAKARPDVVLLIVGDGPLRealraLAEDLGLGDRVTF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 223 PGFVENcgyvDDLAGFYASADLMVLP-LEFGTGLKVksVEAVSFGVPVLGTEHAFIG-LVTDEPLHQF---QTVKALVRA 297
Cdd:cd03798 262 TGRLPH----EQVPAYYRACDVFVLPsRHEGFGLVL--LEAMACGLPVVATDVGGIPeVVGDPETGLLvppGDADALAAA 335
|
330 340 350
....*....|....*....|....*....|..
gi 2193138507 298 IPAVLADVDERVRLAAISSAVFKEYQTRTEEQ 329
Cdd:cd03798 336 LRRALAEPYLRELGEAARARVAERFSWVKAAD 367
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
161-273 |
1.88e-04 |
|
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: 43.47 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 161 ATVIPERKGPGKTVGFIGSQNavNVESLKQLVAelvALRQMLPNDFRLRLAGSmtrGTD-----IHLPGFVENCGYV--D 233
Cdd:cd03823 181 PPPRRRPGTERLRFGYIGRLT--EEKGIDLLVE---AFKRLPREDIELVIAGH---GPLsderqIEGGRRIAFLGRVptD 252
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2193138507 234 DLAGFYASADLMVLP---LEfGTGLKVksVEAVSFGVPVLGTE 273
Cdd:cd03823 253 DIKDFYEKIDVLVVPsiwPE-PFGLVV--REAIAAGLPVIASD 292
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
126-316 |
2.72e-04 |
|
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: 43.11 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 126 LARADFAVACQPEDEEYFKREYG--------LQNTLTIGQIQHATVIPERKGPGK-----TVGFIG--SQNAvNVESLKQ 190
Cdd:cd03819 124 RARGDRVIAVSELVRDHLIEALGvdperirvIPNGVDTDRFPPEAEAEERAQLGLpegkpVVGYVGrlSPEK-GWLLLVD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 191 LVAELVALRqmlpnDFRLRLAGSMTRGTDIH-------LPGFVENCGYVDDLAGFYASADLMVLP-LEFGTGLKVksVEA 262
Cdd:cd03819 203 AAAELKDEP-----DFRLLVAGDGPERDEIRrlverlgLRDRVTFTGFREDVPAALAASDVVVLPsLHEEFGRVA--LEA 275
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2193138507 263 VSFGVPVLGT-EHAFIGLVT---DEPLHQFQTVKALVRAIPAVLADVDERVRLAAISS 316
Cdd:cd03819 276 MACGTPVVATdVGGAREIVVhgrTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAAA 333
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
221-312 |
8.54e-04 |
|
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: 41.53 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 221 HLPGFVENCGYVDDLAGFYASADLMVLPLEFgTGLKVKSVEAVSFGVPVLGTEHAFIGLVTDEP---LHQFQTVKALVRA 297
Cdd:cd03807 244 GLEDRVHLLGERSDVPALLPAMDIFVLSSRT-EGFPNALLEAMACGLPVVATDVGGAAELVDDGtgfLVPAGDPQALADA 322
|
90
....*....|....*
gi 2193138507 298 IPAVLADVDERVRLA 312
Cdd:cd03807 323 IRALLEDPEKRARLG 337
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
197-322 |
1.71e-03 |
|
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: 40.42 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 197 ALRQMLPN--DFRLRLAGS-------MTRGTDIHLPGFVENCGYVDDLAGFYASADLMVLP--LE-FGTGLkvksVEAVS 264
Cdd:cd03811 209 AFAKLRKKypDVKLVILGDgplreelEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSsrYEgFPNVL----LEAMA 284
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2193138507 265 FGVPVLGT---------EHAFIGLVTDEPLHQFQtvKALVRAIPAVLADVDERVRLAAISSAVFKEY 322
Cdd:cd03811 285 LGTPVVSTdcpgpreilDDGENGLLVPDGDAAAL--AGILAALLQKKLDAALRERLAKAQEAVFREY 349
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
117-270 |
1.96e-03 |
|
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: 40.42 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 117 LTREEEKRGLARADFAVACQPEDEEYFkreyglqntLTIGQIQ----HATVI------PERKGPGKTVgFIGSQNAvNVE 186
Cdd:cd03809 169 LGVDPSFFPPESAAVLIAKYLLPEPYF---------LYVGTLEprknHERLLkafallKKQGGDLKLV-IVGGKGW-EDE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 187 SLKQLVAELVAlrqmlpndfrlrlagsmtrGTDIHLPGFVENcgyvDDLAGFYASADLMVLPLEF-GTGLKVksVEAVSF 265
Cdd:cd03809 238 ELLDLVKKLGL-------------------GGRVRFLGYVSD----EDLPALYRGARAFVFPSLYeGFGLPV--LEAMAC 292
|
....*
gi 2193138507 266 GVPVL 270
Cdd:cd03809 293 GTPVI 297
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
108-272 |
1.96e-03 |
|
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: 40.27 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 108 FGRKSDFASLTREEEKRGLARADfAVACQ-PEDEEYFKREYGLQ--NTLTIG-------QIQHATVIPERKGPgkTVGFI 177
Cdd:cd03808 119 FTEGKLLRLLYLLLEKLALLFTD-KVIFVnEDDRDLAIKKGIIKkkKTVLIPgsgvdldRFQYSPESLPSEKV--VFLFV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 178 GsqnavnvESLKQ-LVAELVA----LRQMLPNdFRLRLAG-------SMTRGTDIHLPGFVENCGYVDDLAGFYASADLM 245
Cdd:cd03808 196 A-------RLLKDkGIDELIEaakiLKKKGPN-VRFLLVGdgelenpSEILIEKLGLEGRIEFLGFRSDVPELLAESDVF 267
|
170 180
....*....|....*....|....*....
gi 2193138507 246 VLP--LEfgtGLKVKSVEAVSFGVPVLGT 272
Cdd:cd03808 268 VLPsyRE---GLPRSLLEAMAAGRPVITT 293
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
197-313 |
4.47e-03 |
|
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: 39.27 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 197 ALRQMLP--NDFRLRLAGSMTRGTD--------------IHLPGFVencgYVDDLAGFYASADLMVLPLE---FGtglkV 257
Cdd:cd03821 225 AARKLAEqgRDWHLVIAGPDDGAYPaflqlqsslglgdrVTFTGPL----YGEAKWALYASADLFVLPSYsenFG----N 296
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2193138507 258 KSVEAVSFGVPVL---------GTEHAfIGLVTDEplhqfqTVKALVRAIPAVLADVDERVRLAA 313
Cdd:cd03821 297 VVAEALACGLPVVitdkcglseLVEAG-CGVVVDP------NVSSLAEALAEALRDPADRKRLGE 354
|
|
| LbH_AT_putative |
cd03360 |
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ... |
364-451 |
5.18e-03 |
|
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.
Pssm-ID: 100050 [Multi-domain] Cd Length: 197 Bit Score: 38.23 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 364 IYGAGIGGKIVFDALADEQRAMCLGFLD--LHKAGSSFCDLPVLAPEQVPAPARAETGVIIAIMTLEW-KSVAQSLMDAG 440
Cdd:cd03360 1 IIGAGGHARVVADILEADSGYEVVGFLDddPELKGTEGLGLPVGLDELLLLYPPPDDEFVVAIGDNKLrRKLAEKLLAAG 80
|
90
....*....|...
gi 2193138507 441 FR--SLVSAQRFI 451
Cdd:cd03360 81 YRfaTLIHPSAVV 93
|
|
| COG4641 |
COG4641 |
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]; |
164-313 |
9.34e-03 |
|
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443679 [Multi-domain] Cd Length: 303 Bit Score: 37.99 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 164 IPERKGPGKTVGFIGSQNAVNVESLKQLVAELValrqmlpnDFRLRLAGS----MTRGTDIHLPGFVENcgyvDDLAGFY 239
Cdd:COG4641 130 VPPEARFRYDVAFVGNYYPDRRARLEELLLAPA--------GLRLKIYGPgwpkLALPANVRRGGHLPG----EEHPAAY 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193138507 240 ASAdLMVLPL----EFGTGLKVKSVEAVSFGVPVL-----GTEHAFiglVTDEPLHQFQTVKALVRAIPAVLADVDERVR 310
Cdd:COG4641 198 ASS-KITLNVnrmaASPDSPTRRTFEAAACGAFLLsdpweGLEELF---EPGEEVLVFRDGEELAEKLRYLLADPEERRA 273
|
...
gi 2193138507 311 LAA 313
Cdd:COG4641 274 IAE 276
|
|
| |
