|
Name |
Accession |
Description |
Interval |
E-value |
| DUF4422 |
pfam14393 |
Domain of unknown function (DUF4422); This family of proteins is found in bacteria and archaea. ... |
6-244 |
1.72e-89 |
|
Domain of unknown function (DUF4422); This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 255 and 371 amino acids in length.
Pssm-ID: 433931 Cd Length: 219 Bit Score: 276.72 E-value: 1.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 6 KIYTSHHKPSAFLNAAIIKPLHVGKANSCNEIGCPGDDTGDNISFKNPFYCELTAHYWVWKNEELADYVGFMHYRRHLNF 85
Cdd:pfam14393 1 KIYVATHKKYDMPTDPLYLPIQVGAALKELDLGYLGDNTGDNISEKNPYYCELTALYWAWKNLTDADYIGLVHYRRYFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 86 SEKQTFSEDtwgvvnhpcideeyekiFGLNEETIQRCVEGIDILLPKKWSVTAagsKNNYDHYErgEYLHIRDYQAAIAI 165
Cdd:pfam14393 81 KKKIEDKLK-----------------NILTEEEIEELLKKYDIILPKKRNYYI---ETLYEHYA--HAHHIEDLDLTREI 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805564396 166 VEKLYPEYSAAIKTFNDASDGYYTNMFVMRKDIFVDYSEWLFSILDNLEDAISMNNYNAQEKRVIGHIAERLFNIYIIK 244
Cdd:pfam14393 139 IKEKYPEYLPAFDKVMKGKSAHFFNMFIMKKELFDEYCEWLFDILFELEKRIDISNYDDYQKRVFGFLSERLLNVWLEK 217
|
|
| RfaJ |
COG1442 |
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ... |
275-574 |
7.30e-73 |
|
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441051 [Multi-domain] Cd Length: 301 Bit Score: 236.41 E-value: 7.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 275 DSAVPVVISFDDNYAVSGGALINSIVRHAdKNKNYDIVVLENKVSYLNKTRLVNLTSAHpNISLRFFDVNAfTEINGVHT 354
Cdd:COG1442 3 KNTINIVFAIDDNYLPGLGVSIASLLENN-PDRPYDFHILTDGLSDENKERLEALAAKY-NVSIEFIDVDD-ELLKDLPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 355 RAHFSASTYARLFIPQLF-RRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVKDIVMEGFVKfsamsasddgvmpage 433
Cdd:COG1442 80 SKHISKATYYRLLIPELLpDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTGSQK---------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 434 YLQKTLNMNNPDEYFQAGIIVFNVKQMVEENTFAELMRVLKAK--KYWFLDQDIMNKVFYSRVTFLPLEWNVYHGNGNTD 511
Cdd:COG1442 144 KRAKRLGLPDDDGYFNSGVLLINLKKWREENITEKALEFLKENpdKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYEL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805564396 512 DFFPNLKfatymKFLAARKKPKMIHYAGENKPWNTE-KVDFYDDFIENIANTPWEMEIYKRQMS 574
Cdd:COG1442 224 KDKSNKK-----ELLEARKNPVIIHYTGPTKPWHKWcTHPYADLYWEYLKKTPWKDIPLKKALR 282
|
|
| GT8_A4GalT_like |
cd04194 |
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ... |
278-546 |
1.37e-64 |
|
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface; The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.
Pssm-ID: 133037 [Multi-domain] Cd Length: 248 Bit Score: 212.85 E-value: 1.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 278 VPVVISFDDNYAVSGGALINSIVRHADKnKNYDIVVLENKVSYLNKTRLvNLTSAHPNISLRFFDVNAFTEINGVHTRAH 357
Cdd:cd04194 1 MNIVFAIDDNYAPYLAVTIKSILANNSK-RDYDFYILNDDISEENKKKL-KELLKKYNSSIEFIKIDNDDFKFFPATTDH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 358 FSASTYARLFIPQLFRRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVKDIVMEGFvkfsamsasddgvmpagEYLQK 437
Cdd:cd04194 79 ISYATYYRLLIPDLLPDYDKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQE-----------------KKRKR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 438 TLNMNNPDEYFQAGIIVFNVKQMVEENTFAELMRVLKA--KKYWFLDQDIMNKVFYSRVTFLPLEWNVYHGngntDDFFP 515
Cdd:cd04194 142 RLGGYDDGSYFNSGVLLINLKKWREENITEKLLELIKEygGRLIYPDQDILNAVLKDKILYLPPRYNFQTG----FYYLL 217
|
250 260 270
....*....|....*....|....*....|.
gi 1805564396 516 NLKFATYMKFLAARKKPKMIHYAGENKPWNT 546
Cdd:cd04194 218 KKKSKEEQELEEARKNPVIIHYTGSDKPWNK 248
|
|
| Glyco_transf_8 |
pfam01501 |
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ... |
279-545 |
5.55e-38 |
|
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.
Pssm-ID: 279798 [Multi-domain] Cd Length: 252 Bit Score: 141.31 E-value: 5.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 279 PVVISFDDNYAVSGGALINSIVRHAdKNKNYDIVVLENKVSYLNKTRLVNLTSAH-PNISLRFFDVNAFTEINGVHTR-- 355
Cdd:pfam01501 1 CIALALDKNYLLGASVSIKSLLKNN-SDFALNFHIFTDDIPVENLDILNWLASSYkPVLPLLESDIKIFEYFSKLKLRsp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 356 AHFSASTYARLFIPQLFRRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVKDIVMEGFVKFSAMSASDDGVMPAGeyl 435
Cdd:pfam01501 80 KYWSLLNYLRLYLPDLFPKLDKILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDNYFQRYPNFSEPIILENFGPPAC--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 436 qktlnmnnpdeYFQAGIIVFNVKQMVEENTFA---ELMRVLKAKKYWFL-DQDIMNKVFYSRVTFLPLEWNVYHGNGNTD 511
Cdd:pfam01501 157 -----------YFNAGMLLFDLDAWRKENITEryiKWLNLNENRTLWKLgDQDPLNIVFYGKVKPLDPRWNVLGLGYYNK 225
|
250 260 270
....*....|....*....|....*....|....
gi 1805564396 512 DFFPNLkfatymkflaARKKPKMIHYAGENKPWN 545
Cdd:pfam01501 226 KKSLNE----------ITENAAVIHYNGPTKPWL 249
|
|
| PRK15171 |
PRK15171 |
lipopolysaccharide 3-alpha-galactosyltransferase; |
358-567 |
1.09e-09 |
|
lipopolysaccharide 3-alpha-galactosyltransferase;
Pssm-ID: 185093 [Multi-domain] Cd Length: 334 Bit Score: 60.54 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 358 FSASTYARLFIPQLF-RRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVkdiVMEGFVKFSAMSASDDGVmpagEYLQ 436
Cdd:PRK15171 103 WTYATYFRFIIADYFiDKTDKVLYLDADIACKGSIKELIDLDFAENEIAAV---VAEGDAEWWSKRAQSLQT----PGLA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 437 KTlnmnnpdeYFQAGIIVFNVKQMVEENTFAELMRVLK----AKKYWFLDQDIMNKVFYSRVTFLPLEWNV-YHGNGNTD 511
Cdd:PRK15171 176 SG--------YFNSGFLLINIPAWAQENISAKAIEMLAdpeiVSRITHLDQDVLNILLAGKVKFIDAKYNTqFSLNYELK 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1805564396 512 DFFPNlkfatymkflAARKKPKMIHYAGENKPWNT---EKVDFYddFIENIANTPWEME 567
Cdd:PRK15171 248 DSVIN----------PVNDETVFIHYIGPTKPWHSwadYPVSQY--FLKAKEASPWKNE 294
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DUF4422 |
pfam14393 |
Domain of unknown function (DUF4422); This family of proteins is found in bacteria and archaea. ... |
6-244 |
1.72e-89 |
|
Domain of unknown function (DUF4422); This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 255 and 371 amino acids in length.
Pssm-ID: 433931 Cd Length: 219 Bit Score: 276.72 E-value: 1.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 6 KIYTSHHKPSAFLNAAIIKPLHVGKANSCNEIGCPGDDTGDNISFKNPFYCELTAHYWVWKNEELADYVGFMHYRRHLNF 85
Cdd:pfam14393 1 KIYVATHKKYDMPTDPLYLPIQVGAALKELDLGYLGDNTGDNISEKNPYYCELTALYWAWKNLTDADYIGLVHYRRYFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 86 SEKQTFSEDtwgvvnhpcideeyekiFGLNEETIQRCVEGIDILLPKKWSVTAagsKNNYDHYErgEYLHIRDYQAAIAI 165
Cdd:pfam14393 81 KKKIEDKLK-----------------NILTEEEIEELLKKYDIILPKKRNYYI---ETLYEHYA--HAHHIEDLDLTREI 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805564396 166 VEKLYPEYSAAIKTFNDASDGYYTNMFVMRKDIFVDYSEWLFSILDNLEDAISMNNYNAQEKRVIGHIAERLFNIYIIK 244
Cdd:pfam14393 139 IKEKYPEYLPAFDKVMKGKSAHFFNMFIMKKELFDEYCEWLFDILFELEKRIDISNYDDYQKRVFGFLSERLLNVWLEK 217
|
|
| RfaJ |
COG1442 |
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ... |
275-574 |
7.30e-73 |
|
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441051 [Multi-domain] Cd Length: 301 Bit Score: 236.41 E-value: 7.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 275 DSAVPVVISFDDNYAVSGGALINSIVRHAdKNKNYDIVVLENKVSYLNKTRLVNLTSAHpNISLRFFDVNAfTEINGVHT 354
Cdd:COG1442 3 KNTINIVFAIDDNYLPGLGVSIASLLENN-PDRPYDFHILTDGLSDENKERLEALAAKY-NVSIEFIDVDD-ELLKDLPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 355 RAHFSASTYARLFIPQLF-RRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVKDIVMEGFVKfsamsasddgvmpage 433
Cdd:COG1442 80 SKHISKATYYRLLIPELLpDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTGSQK---------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 434 YLQKTLNMNNPDEYFQAGIIVFNVKQMVEENTFAELMRVLKAK--KYWFLDQDIMNKVFYSRVTFLPLEWNVYHGNGNTD 511
Cdd:COG1442 144 KRAKRLGLPDDDGYFNSGVLLINLKKWREENITEKALEFLKENpdKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYEL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805564396 512 DFFPNLKfatymKFLAARKKPKMIHYAGENKPWNTE-KVDFYDDFIENIANTPWEMEIYKRQMS 574
Cdd:COG1442 224 KDKSNKK-----ELLEARKNPVIIHYTGPTKPWHKWcTHPYADLYWEYLKKTPWKDIPLKKALR 282
|
|
| GT8_A4GalT_like |
cd04194 |
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ... |
278-546 |
1.37e-64 |
|
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface; The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.
Pssm-ID: 133037 [Multi-domain] Cd Length: 248 Bit Score: 212.85 E-value: 1.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 278 VPVVISFDDNYAVSGGALINSIVRHADKnKNYDIVVLENKVSYLNKTRLvNLTSAHPNISLRFFDVNAFTEINGVHTRAH 357
Cdd:cd04194 1 MNIVFAIDDNYAPYLAVTIKSILANNSK-RDYDFYILNDDISEENKKKL-KELLKKYNSSIEFIKIDNDDFKFFPATTDH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 358 FSASTYARLFIPQLFRRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVKDIVMEGFvkfsamsasddgvmpagEYLQK 437
Cdd:cd04194 79 ISYATYYRLLIPDLLPDYDKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQE-----------------KKRKR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 438 TLNMNNPDEYFQAGIIVFNVKQMVEENTFAELMRVLKA--KKYWFLDQDIMNKVFYSRVTFLPLEWNVYHGngntDDFFP 515
Cdd:cd04194 142 RLGGYDDGSYFNSGVLLINLKKWREENITEKLLELIKEygGRLIYPDQDILNAVLKDKILYLPPRYNFQTG----FYYLL 217
|
250 260 270
....*....|....*....|....*....|.
gi 1805564396 516 NLKFATYMKFLAARKKPKMIHYAGENKPWNT 546
Cdd:cd04194 218 KKKSKEEQELEEARKNPVIIHYTGSDKPWNK 248
|
|
| Glyco_transf_8 |
pfam01501 |
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ... |
279-545 |
5.55e-38 |
|
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.
Pssm-ID: 279798 [Multi-domain] Cd Length: 252 Bit Score: 141.31 E-value: 5.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 279 PVVISFDDNYAVSGGALINSIVRHAdKNKNYDIVVLENKVSYLNKTRLVNLTSAH-PNISLRFFDVNAFTEINGVHTR-- 355
Cdd:pfam01501 1 CIALALDKNYLLGASVSIKSLLKNN-SDFALNFHIFTDDIPVENLDILNWLASSYkPVLPLLESDIKIFEYFSKLKLRsp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 356 AHFSASTYARLFIPQLFRRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVKDIVMEGFVKFSAMSASDDGVMPAGeyl 435
Cdd:pfam01501 80 KYWSLLNYLRLYLPDLFPKLDKILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDNYFQRYPNFSEPIILENFGPPAC--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 436 qktlnmnnpdeYFQAGIIVFNVKQMVEENTFA---ELMRVLKAKKYWFL-DQDIMNKVFYSRVTFLPLEWNVYHGNGNTD 511
Cdd:pfam01501 157 -----------YFNAGMLLFDLDAWRKENITEryiKWLNLNENRTLWKLgDQDPLNIVFYGKVKPLDPRWNVLGLGYYNK 225
|
250 260 270
....*....|....*....|....*....|....
gi 1805564396 512 DFFPNLkfatymkflaARKKPKMIHYAGENKPWN 545
Cdd:pfam01501 226 KKSLNE----------ITENAAVIHYNGPTKPWL 249
|
|
| Glyco_transf_8 |
cd00505 |
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ... |
280-545 |
3.98e-25 |
|
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis; Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.
Pssm-ID: 132996 [Multi-domain] Cd Length: 246 Bit Score: 104.45 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 280 VVISFDDNYAVSGGALINSIVRHADKNKNYdiVVLENKVSYLNKTRLVNLtSAHPNISLRFFDVNAFTEINGVHTRAHFS 359
Cdd:cd00505 4 VIVATGDEYLRGAIVLMKSVLRHRTKPLRF--HVLTNPLSDTFKAALDNL-RKLYNFNYELIPVDILDSVDSEHLKRPIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 360 ASTYARLFIPQLFRRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAvkdivmegfvkfsamsASDDGVMPAGEYLQKTL 439
Cdd:cd00505 81 IVTLTKLHLPNLVPDYDKILYVDADILVLTDIDELWDTPLGGQELAA----------------APDPGDRREGKYYRQKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 440 NMNNPDEYFQAGIIVFNVKQMveenTFAELMRVLKAKKYWFL------DQDIMNKVFYS---RVTFLPLEWNVYHgngnT 510
Cdd:cd00505 145 SHLAGPDYFNSGVFVVNLSKE----RRNQLLKVALEKWLQSLsslsggDQDLLNTFFKQvpfIVKSLPCIWNVRL----T 216
|
250 260 270
....*....|....*....|....*....|....*.
gi 1805564396 511 DDFFpnlkfatYMKFLAARKKP-KMIHYAGENKPWN 545
Cdd:cd00505 217 GCYR-------SLNCFKAFVKNaKVIHFNGPTKPWN 245
|
|
| GT8_like_1 |
cd06429 |
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ... |
278-544 |
2.19e-11 |
|
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of glycosyltransferase family 8 with unknown function: Glycosyltransferase family 8 comprises enzymes with a number of known activities; lipopolysaccharide galactosyltransferase lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase and inositol 1-alpha-galactosyltransferase. It is classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed.
Pssm-ID: 133051 [Multi-domain] Cd Length: 257 Bit Score: 64.72 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 278 VPVVISFDDNYAVSggALINSIVRHADKNKN--YDIVVLENKV----SYLNKTRL----VNLTSAHPNISLRF------- 340
Cdd:cd06429 1 IHVVIFSDNRLAAA--VVINSSISNNKDPSNlvFHIVTDNQNYgamrSWFDLNPLkiatVKVLNFDDFKLLGKvkvdslm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 341 FDVNAFTEINGVHTRAH-FSASTYARLFIPQLFRRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVKDIVMEGfvkfs 419
Cdd:cd06429 79 QLESEADTSNLKQRKPEyISLLNFARFYLPELFPKLEKVIYLDDDVVVQKDLTELWNTDLGGGVAGAVETSWNPG----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 420 amsasddgvmpageylqktLNMNNPDEYFQAGiIVFNVKQMVEENTFAElmrvlkaKKYWFL-DQDIMNKVFYSRVTFLP 498
Cdd:cd06429 154 -------------------VNVVNLTEWRRQN-VTETYEKWMELNQEEE-------VTLWKLiTLPPGLIVFYGLTSPLD 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1805564396 499 LEWNV----YHGNGNTDDFfpnlkfatymkflaarKKPKMIHYAGENKPW 544
Cdd:cd06429 207 PSWHVrglgYNYGIRPQDI----------------KAAAVLHFNGNMKPW 240
|
|
| GT8_Glycogenin |
cd02537 |
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ... |
286-545 |
9.23e-11 |
|
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.
Pssm-ID: 133018 [Multi-domain] Cd Length: 240 Bit Score: 62.28 E-value: 9.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 286 DNYAVSGGALINSIVRHadkNKNYDIVVL-ENKVSYLNKTRLVNLtsahpNISLRFFDVNAFTEINGVHTRAHFSaSTYA 364
Cdd:cd02537 10 DDYLPGALVLGYSLRKV---GSSYDLVVLvTPGVSEESREALEEV-----GWIVREVEPIDPPDSANLLKRPRFK-DTYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 365 RLFIPQLFRrYDKVVFIDSDTVVKADLGELLDVPlgnnlvaavkdivmegfvkfSAMSASDDgvmpageylqktlnmNNP 444
Cdd:cd02537 81 KLRLWNLTE-YDKVVFLDADTLVLRNIDELFDLP--------------------GEFAAAPD---------------CGW 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 445 DEYFQAGIIVFNVKqmveENTFAELMRVLKAK-KYWFLDQDIMNKVFYSRVTFLPLEWnVYhgngNTDdfFPNlkFATYM 523
Cdd:cd02537 125 PDLFNSGVFVLKPS----EETFNDLLDALQDTpSFDGGDQGLLNSYFSDRGIWKRLPF-TY----NAL--KPL--RYLHP 191
|
250 260
....*....|....*....|..
gi 1805564396 524 KFLAARKKPKMIHYAGENKPWN 545
Cdd:cd02537 192 EALWFGDEIKVVHFIGGDKPWS 213
|
|
| PRK15171 |
PRK15171 |
lipopolysaccharide 3-alpha-galactosyltransferase; |
358-567 |
1.09e-09 |
|
lipopolysaccharide 3-alpha-galactosyltransferase;
Pssm-ID: 185093 [Multi-domain] Cd Length: 334 Bit Score: 60.54 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 358 FSASTYARLFIPQLF-RRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVkdiVMEGFVKFSAMSASDDGVmpagEYLQ 436
Cdd:PRK15171 103 WTYATYFRFIIADYFiDKTDKVLYLDADIACKGSIKELIDLDFAENEIAAV---VAEGDAEWWSKRAQSLQT----PGLA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 437 KTlnmnnpdeYFQAGIIVFNVKQMVEENTFAELMRVLK----AKKYWFLDQDIMNKVFYSRVTFLPLEWNV-YHGNGNTD 511
Cdd:PRK15171 176 SG--------YFNSGFLLINIPAWAQENISAKAIEMLAdpeiVSRITHLDQDVLNILLAGKVKFIDAKYNTqFSLNYELK 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1805564396 512 DFFPNlkfatymkflAARKKPKMIHYAGENKPWNT---EKVDFYddFIENIANTPWEME 567
Cdd:PRK15171 248 DSVIN----------PVNDETVFIHYIGPTKPWHSwadYPVSQY--FLKAKEASPWKNE 294
|
|
| PLN02870 |
PLN02870 |
Probable galacturonosyltransferase |
365-558 |
9.46e-08 |
|
Probable galacturonosyltransferase
Pssm-ID: 215468 [Multi-domain] Cd Length: 533 Bit Score: 54.94 E-value: 9.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 365 RLFIPQLFRRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVKdivmegfvkfsAMSASDDGVMpaGEYLQKTLNMN-- 442
Cdd:PLN02870 333 RIYLPELFPNLDKVVFLDDDVVIQRDLSPLWDIDLGGKVNGAVE-----------TCRGEDEWVM--SKRFRNYFNFShp 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 443 ------NPDEYFQA-GIIVFNVKQMVEENtfaelmrvLKAKKYWFLDQDIMNKVFYSRVTFLPLEWNVYHGNGNTDDFFP 515
Cdd:PLN02870 400 liaknlDPEECAWAyGMNIFDLRAWRKTN--------IRETYHSWLKENLKSNLTMWKLGTLPPALIAFKGHVHPIDPSW 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1805564396 516 NLKFATYMKF--LAARKKPKMIHYAGENKPWN-----------TEKVDFYDDFIEN 558
Cdd:PLN02870 472 HMLGLGYQSKtnIESVKKAAVIHYNGQSKPWLeigfehlrpfwTKYVNYSNDFIRN 527
|
|
| PLN02659 |
PLN02659 |
Probable galacturonosyltransferase |
359-557 |
7.39e-07 |
|
Probable galacturonosyltransferase
Pssm-ID: 215356 [Multi-domain] Cd Length: 534 Bit Score: 52.34 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 359 SASTYARLFIPQLFRRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVKdivmegfvkfsAMSASDDGVMpaGEYLQKT 438
Cdd:PLN02659 328 SVMNHIRIHLPELFPSLNKVVFLDDDIVVQTDLSPLWDIDMNGKVNGAVE-----------TCRGEDKFVM--SKKLKSY 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805564396 439 LNMN--------NPDEYFQA-GIIVFNVKQMVEENtfaelmrvLKAKKYWFLDQDIMNKVFYSRVTFLPLEWNVYHGNGN 509
Cdd:PLN02659 395 LNFShpliaknfDPNECAWAyGMNIFDLEAWRKTN--------ISSTYHHWLEENLKSDLSLWQLGTLPPGLIAFHGHVH 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805564396 510 TDDFFPNLKFATYMK--FLAARKKPKMIHYAGENKPWN-----------TEKVDFYDDFIE 557
Cdd:PLN02659 467 VIDPFWHMLGLGYQEntSLADAESAGVVHFNGRAKPWLdiafpqlrplwAKYIDSSDKFIK 527
|
|
| PLN02742 |
PLN02742 |
Probable galacturonosyltransferase |
365-418 |
1.44e-05 |
|
Probable galacturonosyltransferase
Pssm-ID: 215395 [Multi-domain] Cd Length: 534 Bit Score: 47.85 E-value: 1.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1805564396 365 RLFIPQLFRRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVkDIVMEGFVKF 418
Cdd:PLN02742 343 RFYIPEIYPALEKVVFLDDDVVVQKDLTPLFSIDLHGNVNGAV-ETCLETFHRY 395
|
|
| PLN02867 |
PLN02867 |
Probable galacturonosyltransferase |
365-409 |
5.16e-05 |
|
Probable galacturonosyltransferase
Pssm-ID: 178458 [Multi-domain] Cd Length: 535 Bit Score: 46.43 E-value: 5.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1805564396 365 RLFIPQLFRRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVKD 409
Cdd:PLN02867 335 RIYIPELFPDLNKIVFLDDDVVVQHDLSSLWELDLNGKVVGAVVD 379
|
|
| PLN02718 |
PLN02718 |
Probable galacturonosyltransferase |
359-422 |
9.18e-04 |
|
Probable galacturonosyltransferase
Pssm-ID: 178320 [Multi-domain] Cd Length: 603 Bit Score: 42.19 E-value: 9.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805564396 359 SASTYARLFIPQLFRRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVkDIVMEGFVKFSAMS 422
Cdd:PLN02718 402 SALNHARFYLPDIFPGLNKIVLFDHDVVVQRDLSRLWSLDMKGKVVGAV-ETCLEGEPSFRSMD 464
|
|
| PLN02829 |
PLN02829 |
Probable galacturonosyltransferase |
365-408 |
1.34e-03 |
|
Probable galacturonosyltransferase
Pssm-ID: 215443 [Multi-domain] Cd Length: 639 Bit Score: 41.76 E-value: 1.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1805564396 365 RLFIPQLFRRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVK 408
Cdd:PLN02829 447 RFYLPEIFPKLNKVLFLDDDIVVQKDLTGLWSIDLKGNVNGAVE 490
|
|
| GT8_HUGT1_C_like |
cd06432 |
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain ... |
363-402 |
1.52e-03 |
|
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain of glycoprotein glucosyltransferase (UGT). UGT is a large glycoprotein whose C-terminus contains the catalytic activity. This catalytic C-terminal domain is highly homologous to Glycosyltransferase Family 8 (GT 8) and contains the DXD motif that coordinates donor sugar binding, characteristic for Family 8 glycosyltransferases. GT 8 proteins are retaining enzymes based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. The non-catalytic N-terminal portion of the human UTG1 (HUGT1) has been shown to monitor the protein folding status and activate its glucosyltransferase activity.
Pssm-ID: 133054 Cd Length: 248 Bit Score: 40.84 E-value: 1.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1805564396 363 YARLFIPQLF-RRYDKVVFIDSDTVVKADLGELLDVPLGNN 402
Cdd:cd06432 83 YKILFLDVLFpLNVDKVIFVDADQIVRTDLKELMDMDLKGA 123
|
|
| PLN02769 |
PLN02769 |
Probable galacturonosyltransferase |
358-408 |
2.75e-03 |
|
Probable galacturonosyltransferase
Pssm-ID: 215412 [Multi-domain] Cd Length: 629 Bit Score: 40.83 E-value: 2.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1805564396 358 FSASTYarlFIPQLFRRYDKVVFIDSDTVVKADLGELLDVPLGNNLVAAVK 408
Cdd:PLN02769 438 FSHSHF---LLPEIFKKLKKVVVLDDDVVVQRDLSFLWNLDMGGKVNGAVQ 485
|
|
| Glyco_transf_24 |
pfam18404 |
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein ... |
363-402 |
3.89e-03 |
|
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT). This domain belongs to glucosyltransferase 24 family (GT24) A-type domain. The GT domain displays the expected glycosyltransferase type A (GT-A) fold.
Pssm-ID: 436473 Cd Length: 268 Bit Score: 39.52 E-value: 3.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1805564396 363 YARLFIPQLF-RRYDKVVFIDSDTVVKADLGELLDVPLGNN 402
Cdd:pfam18404 83 YKILFLDVLFpLDLDKVIFVDADQVVRTDLKELVDMDLEGA 123
|
|
| |
