|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02501 |
PLN02501 |
digalactosyldiacylglycerol synthase |
32-808 |
0e+00 |
|
digalactosyldiacylglycerol synthase
Pssm-ID: 215277 Cd Length: 794 Bit Score: 1615.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 32 NALSFLSKGWREVWDSADADLQLMRDRANSVKNLASTFDREIENFLNNSARSAFPVGSPSASSFSNEIGIMKKLQPKISE 111
Cdd:PLN02501 11 NAFSFLSKGWREVRDSADADLQLMRARANSFKNLASSFDREIENFFNSASRSSFPVGSPSASSFPTEIDFVKKLQPKISE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 112 FRRVYSAPEISRKVMERWGPaRAKLGMDLSAIKKAIVSEMELDERQGVLEMSRLRRRRNSDRVrFTEFFAEAERDGEAYF 191
Cdd:PLN02501 91 FRRVYSAPEISRKVLEKWGP-RAKLGIDLSAIKNAIVAEMELDDRGGIVEFDRVRRRRNSRVR-FTEFWGEAKEEGEGQF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 192 GDWEPIRSLKSRFKEFEKRS-SLEILSGFKNSEFVEKLKTSFKSIYKETDEAKDVPPLDVPELLACLVRQSEPFLDQIGV 270
Cdd:PLN02501 169 GEWEPIRALKTRFRELEKRSeSLEIFGGFKNSEFVEKLKSSLKAIYKEPQESKDVPPLDVPELLAYLVRQSEPFLDQLGV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 271 RKDTCDRIVESLC-KCKSQQLWRLPSAQASDLIENDNHGVDLDMRIASVLQSTGHHYDGGFWTDFVKPETPENKRHVAIV 349
Cdd:PLN02501 249 RKDICDKIVESLCsKRKNQLLLRSLSAGESSLLESDNHNDELDLRIASVLQSTGHCYDGGFWTDSSKHELSDGKRHVAIV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 350 TTASLPWMTGTAVNPLFRAAYLAKAAKQSVTLVVPWLCESDQELVYPNNLTFSSPEEQESYIRKWLEERIGFKADFKISF 429
Cdd:PLN02501 329 TTASLPWMTGTAVNPLFRAAYLAKSAKQNVTLLVPWLCKSDQELVYPNNLTFSSPEEQESYIRNWLEERIGFKADFKISF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 430 YPGKFSKERRSIFPAGDTSQFISSKDADIAILEEPEHLNWYYHGKRWTDKFNHVVGIVHTNYLEYIKREKNGALQAFFVN 509
Cdd:PLN02501 409 YPGKFSKERRSIIPAGDTSQFIPSKDADIAILEEPEHLNWYHHGKRWTDKFNHVVGVVHTNYLEYIKREKNGALQAFFVK 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 510 HVNNWVTRAYCDKVLRLSAATQDLPKSVVCNVHGVNPKFLMIGEKIAEERSRGEQAFSKGAYFLGKMVWAKGYRELIDLM 589
Cdd:PLN02501 489 HINNWVTRAYCHKVLRLSAATQDLPKSVICNVHGVNPKFLKIGEKVAEERELGQQAFSKGAYFLGKMVWAKGYRELIDLL 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 590 AKHKSELGSFNLDVYGNGEDAVEVQRAAKKHDLNLNFLKGRDHADDALHKYKVFINPSISDVLCTATAEALAMGKFVVCA 669
Cdd:PLN02501 569 AKHKNELDGFNLDVFGNGEDAHEVQRAAKRLDLNLNFLKGRDHADDSLHGYKVFINPSISDVLCTATAEALAMGKFVVCA 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 670 DHPSNEFFRSFPNCLTYKTSEDFVSKVQEAMTKEPLPLTPEQMYNLSWEAATQRFMEYSDLDKILNNGE-------GGRK 742
Cdd:PLN02501 649 DHPSNEFFRSFPNCLTYKTSEDFVAKVKEALANEPQPLTPEQRYNLSWEAATQRFMEYSDLDKVLNNGDdaklsksGGKS 728
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117910937 743 MRKSRSVPSFNEVVDGGLAFSHYVLTGNDFLRLCTGATPRTKDYDNQHCKDLNLVPPHVHKPIFGW 808
Cdd:PLN02501 729 ITKSVSMPNLSEMVDGGLAFAHYCLTGNEFLRLCTGAIPGTRDYDKQHCKDLHLLPPHVENPIYGW 794
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
475-677 |
3.60e-19 |
|
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: 87.46 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 475 RWTDKFNHVVGIVHTNYLEYIKREKNGALQAFFVNHVNNWVTRAYcdkVLRLSAATQDLPKSVVCnvHGVNPKFLMIGEK 554
Cdd:cd01635 24 RALAALGHEVTVLALLLLALRRILKKLLELKPDVVHAHSPHAAAL---AALLAARLLGIPIVVTV--HGPDSLESTRSEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 555 IAEERSRgEQAFSKGAYFLGKMVWAKGYRELIDLMAKHKSELGSFNLDVYGNGEDAVEVQRAAKKHDLNLN-----FLKG 629
Cdd:cd01635 99 LALARLL-VSLPLADKVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERvviigGLVD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 117910937 630 RDHADDALHKYKVFINPSISDVLCTATAEALAMGKFVVCADHPSNEFF 677
Cdd:cd01635 178 DEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEF 225
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
572-706 |
5.14e-11 |
|
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: 61.52 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 572 FLGKMVWAKGYRELIDLMAKHKSELGSFNLDVYGNGEDAVEVQRAAKKHDL--NLNFLKGRDHAD-DALHKY-KVFINPS 647
Cdd:pfam00534 7 FVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLgdNVIFLGFVSDEDlPELLKIaDVFVLPS 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117910937 648 ISDVLCTATAEALAMGKFVVCADHPSN-EFFRSFPN--CLTYKTSEDFVSKVQEAMTKEPLP 706
Cdd:pfam00534 87 RYEGFGIVLLEAMACGLPVIASDVGGPpEVVKDGETgfLVKPNNAEALAEAIDKLLEDEELR 148
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
623-726 |
1.91e-04 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 41.90 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 623 NLNFLKGRDHADDA-LHKYKVFINPSISDVLCTATAEALAMGKFVVCADHPSN-EFFRSFPNCLTYK--TSEDFVSKVQE 698
Cdd:COG0438 3 RLVPRKGLDLLLEAlLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLpEVIEDGETGLLVPpgDPEALAEAILR 82
|
90 100 110
....*....|....*....|....*....|....
gi 117910937 699 AMTKEPLPLTPEQ------MYNLSWEAATQRFME 726
Cdd:COG0438 83 LLEDPELRRRLGEaareraEERFSWEAIAERLLA 116
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02501 |
PLN02501 |
digalactosyldiacylglycerol synthase |
32-808 |
0e+00 |
|
digalactosyldiacylglycerol synthase
Pssm-ID: 215277 Cd Length: 794 Bit Score: 1615.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 32 NALSFLSKGWREVWDSADADLQLMRDRANSVKNLASTFDREIENFLNNSARSAFPVGSPSASSFSNEIGIMKKLQPKISE 111
Cdd:PLN02501 11 NAFSFLSKGWREVRDSADADLQLMRARANSFKNLASSFDREIENFFNSASRSSFPVGSPSASSFPTEIDFVKKLQPKISE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 112 FRRVYSAPEISRKVMERWGPaRAKLGMDLSAIKKAIVSEMELDERQGVLEMSRLRRRRNSDRVrFTEFFAEAERDGEAYF 191
Cdd:PLN02501 91 FRRVYSAPEISRKVLEKWGP-RAKLGIDLSAIKNAIVAEMELDDRGGIVEFDRVRRRRNSRVR-FTEFWGEAKEEGEGQF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 192 GDWEPIRSLKSRFKEFEKRS-SLEILSGFKNSEFVEKLKTSFKSIYKETDEAKDVPPLDVPELLACLVRQSEPFLDQIGV 270
Cdd:PLN02501 169 GEWEPIRALKTRFRELEKRSeSLEIFGGFKNSEFVEKLKSSLKAIYKEPQESKDVPPLDVPELLAYLVRQSEPFLDQLGV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 271 RKDTCDRIVESLC-KCKSQQLWRLPSAQASDLIENDNHGVDLDMRIASVLQSTGHHYDGGFWTDFVKPETPENKRHVAIV 349
Cdd:PLN02501 249 RKDICDKIVESLCsKRKNQLLLRSLSAGESSLLESDNHNDELDLRIASVLQSTGHCYDGGFWTDSSKHELSDGKRHVAIV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 350 TTASLPWMTGTAVNPLFRAAYLAKAAKQSVTLVVPWLCESDQELVYPNNLTFSSPEEQESYIRKWLEERIGFKADFKISF 429
Cdd:PLN02501 329 TTASLPWMTGTAVNPLFRAAYLAKSAKQNVTLLVPWLCKSDQELVYPNNLTFSSPEEQESYIRNWLEERIGFKADFKISF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 430 YPGKFSKERRSIFPAGDTSQFISSKDADIAILEEPEHLNWYYHGKRWTDKFNHVVGIVHTNYLEYIKREKNGALQAFFVN 509
Cdd:PLN02501 409 YPGKFSKERRSIIPAGDTSQFIPSKDADIAILEEPEHLNWYHHGKRWTDKFNHVVGVVHTNYLEYIKREKNGALQAFFVK 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 510 HVNNWVTRAYCDKVLRLSAATQDLPKSVVCNVHGVNPKFLMIGEKIAEERSRGEQAFSKGAYFLGKMVWAKGYRELIDLM 589
Cdd:PLN02501 489 HINNWVTRAYCHKVLRLSAATQDLPKSVICNVHGVNPKFLKIGEKVAEERELGQQAFSKGAYFLGKMVWAKGYRELIDLL 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 590 AKHKSELGSFNLDVYGNGEDAVEVQRAAKKHDLNLNFLKGRDHADDALHKYKVFINPSISDVLCTATAEALAMGKFVVCA 669
Cdd:PLN02501 569 AKHKNELDGFNLDVFGNGEDAHEVQRAAKRLDLNLNFLKGRDHADDSLHGYKVFINPSISDVLCTATAEALAMGKFVVCA 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 670 DHPSNEFFRSFPNCLTYKTSEDFVSKVQEAMTKEPLPLTPEQMYNLSWEAATQRFMEYSDLDKILNNGE-------GGRK 742
Cdd:PLN02501 649 DHPSNEFFRSFPNCLTYKTSEDFVAKVKEALANEPQPLTPEQRYNLSWEAATQRFMEYSDLDKVLNNGDdaklsksGGKS 728
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117910937 743 MRKSRSVPSFNEVVDGGLAFSHYVLTGNDFLRLCTGATPRTKDYDNQHCKDLNLVPPHVHKPIFGW 808
Cdd:PLN02501 729 ITKSVSMPNLSEMVDGGLAFAHYCLTGNEFLRLCTGAIPGTRDYDKQHCKDLHLLPPHVENPIYGW 794
|
|
| PLN02846 |
PLN02846 |
digalactosyldiacylglycerol synthase |
343-799 |
0e+00 |
|
digalactosyldiacylglycerol synthase
Pssm-ID: 166487 [Multi-domain] Cd Length: 462 Bit Score: 691.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 343 KRHVAIVTTASLPWMTGTAVNPLFRAAYLAKAAKQSVTLVVPWLCESDQELVYPNNLTFSSPEEQESYIRKWLEERIGFK 422
Cdd:PLN02846 4 KQHIAIFTTASLPWMTGTAVNPLFRAAYLAKDGDREVTLVIPWLSLKDQKLVYPNKITFSSPSEQEAYVRQWLEERISFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 423 ADFKISFYPGKFSKERRSIFPAGDTSQFISSKDADIAILEEPEHLNWYYHGKRWTDKFNHVVGIVHTNYLEYIKREKNGA 502
Cdd:PLN02846 84 PKFSIKFYPGKFSTDKRSILPVGDISETIPDEEADIAVLEEPEHLTWYHHGKRWKTKFRLVIGIVHTNYLEYVKREKNGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 503 LQAFFVNHVNNWVTRAYCDKVLRLSAATQDLPKSVVCNVHGVNPKFLMIGEKIAEERSRGEQAFSKGAYFLGKMVWAKGY 582
Cdd:PLN02846 164 VKAFLLKYINSWVVDIYCHKVIRLSAATQDYPRSIICNVHGVNPKFLEIGKLKLEQQKNGEQAFTKGAYYIGKMVWSKGY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 583 RELIDLMAKHKSELGSFNLDVYGNGEDAVEVQRAAKKHDLNLNFLKGRDHADDALHKYKVFINPSISDVLCTATAEALAM 662
Cdd:PLN02846 244 KELLKLLHKHQKELSGLEVDLYGSGEDSDEVKAAAEKLELDVRVYPGRDHADPLFHDYKVFLNPSTTDVVCTTTAEALAM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 663 GKFVVCADHPSNEFFRSFPNCLTYKTSEDFVSKVQEAMTKEPLPLTPEQMYNLSWEAATQRFMEYSDLDKILNNGEGGRK 742
Cdd:PLN02846 324 GKIVVCANHPSNEFFKQFPNCRTYDDGKGFVRATLKALAEEPAPLTDAQRHELSWEAATERFLRVADLDLPSSAKPNKSS 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 117910937 743 MRK-SRSVPSFNEVVDGGLAFSHYVLTGNDFLRLCTGATPRTKDYDNQHCKDLNLVPP 799
Cdd:PLN02846 404 LKNfMSTSPNLKKNMEDASAYLHNVASGFETSRRAFGAIPGSLQPDEQQCKELGLALQ 461
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
475-677 |
3.60e-19 |
|
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: 87.46 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 475 RWTDKFNHVVGIVHTNYLEYIKREKNGALQAFFVNHVNNWVTRAYcdkVLRLSAATQDLPKSVVCnvHGVNPKFLMIGEK 554
Cdd:cd01635 24 RALAALGHEVTVLALLLLALRRILKKLLELKPDVVHAHSPHAAAL---AALLAARLLGIPIVVTV--HGPDSLESTRSEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 555 IAEERSRgEQAFSKGAYFLGKMVWAKGYRELIDLMAKHKSELGSFNLDVYGNGEDAVEVQRAAKKHDLNLN-----FLKG 629
Cdd:cd01635 99 LALARLL-VSLPLADKVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERvviigGLVD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 117910937 630 RDHADDALHKYKVFINPSISDVLCTATAEALAMGKFVVCADHPSNEFF 677
Cdd:cd01635 178 DEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEF 225
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
572-706 |
5.14e-11 |
|
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: 61.52 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 572 FLGKMVWAKGYRELIDLMAKHKSELGSFNLDVYGNGEDAVEVQRAAKKHDL--NLNFLKGRDHAD-DALHKY-KVFINPS 647
Cdd:pfam00534 7 FVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLgdNVIFLGFVSDEDlPELLKIaDVFVLPS 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117910937 648 ISDVLCTATAEALAMGKFVVCADHPSN-EFFRSFPN--CLTYKTSEDFVSKVQEAMTKEPLP 706
Cdd:pfam00534 87 RYEGFGIVLLEAMACGLPVIASDVGGPpEVVKDGETgfLVKPNNAEALAEAIDKLLEDEELR 148
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
572-672 |
5.71e-10 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 57.91 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 572 FLGKMV-WAKGYRELIDLMAKHKSELGSFNLDVYGNGEDAvEVQRAAKKHDLNLNFLKGRDHADDALHKYKVFINPSISD 650
Cdd:pfam13692 6 FVGRLHpNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEE-ELEELAAGLEDRVIFTGFVEDLAELLAAADVFVLPSLYE 84
|
90 100
....*....|....*....|..
gi 117910937 651 VLCTATAEALAMGKFVVCADHP 672
Cdd:pfam13692 85 GFGLKLLEAMAAGLPVVATDVG 106
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
345-733 |
8.85e-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: 61.40 E-value: 8.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 345 HVAIVTTASLPWMTGTAVnplfRAAYLAKA---AKQSVTLVVPwlcesdqelvypnnltfssPEEQESYIRKWLEERIGF 421
Cdd:cd03801 1 KILLLSPELPPPVGGAER----HVRELARAlaaRGHDVTVLTP-------------------ADPGEPPEELEDGVIVPL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 422 KADFKISFYPGKFSKERRSifpagdtsqFISSKDADIAILEEPEHLNWYYHGKRwtdkFNHVVGIVHTNYLEYIKREKNG 501
Cdd:cd03801 58 LPSLAALLRARRLLRELRP---------LLRLRKFDVVHAHGLLAALLAALLAL----LLGAPLVVTLHGAEPGRLLLLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 502 ALQAFFVNHVNNWVTRAycDKVL--------RLSAATQDLPKSVVCNVHGVNPKFLMIGEKIAEERSRGEQAFSkgayFL 573
Cdd:cd03801 125 AAERRLLARAEALLRRA--DAVIavsealrdELRALGGIPPEKIVVIPNGVDLERFSPPLRRKLGIPPDRPVLL----FV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 574 GKMVWAKGYRELIDLMAKHKSELGSFNLDVYGN-GEDAVEVQRAAKKHDLNLNFLKGRDHAD--DALHKYKVFINPSISD 650
Cdd:cd03801 199 GRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGdGPLRAELEELELGLGDRVRFLGFVPDEElpALYAAADVFVLPSRYE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 651 VLCTATAEALAMGKFVVCADHPSN-EFFRSFPNCLTY--KTSEDFVSKVQEAMTKeplpltPEQMYNLSwEAATQRFMEY 727
Cdd:cd03801 279 GFGLVVLEAMAAGLPVVATDVGGLpEVVEDGEGGLVVppDDVEALADALLRLLAD------PELRARLG-RAARERVAER 351
|
....*.
gi 117910937 728 SDLDKI 733
Cdd:cd03801 352 FSWERV 357
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
345-695 |
3.95e-08 |
|
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: 56.13 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 345 HVAIVTTASLPWMTGTA--VNPLFRAayLAKAAKQsVTLVVPwlcesdqelVYPNnltfSSPEEQESYIRkwleerigfk 422
Cdd:cd03817 1 KIAIFTDTYLPQVNGVAtsVRNLARA--LEKRGHE-VYVITP---------SDPG----AEDEEEVVRYR---------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 423 adfkISFYPGKFSKERRSIFPAGDTSQ-FISSKDADIaileepehlnWYYH--------GKRWTDKFNhvVGIVHT---- 489
Cdd:cd03817 55 ----SFSIPIRKYHRQHIPFPFKKAVIdRIKELGPDI----------IHTHtpfslgklGLRIARKLK--IPIVHTyhtm 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 490 --NYLEYIkrekngALQAFFVNHVNNWVTRAYC---DKVLRLSAATQDL--------PKSVVCNvhGVNPKFLmigEKIA 556
Cdd:cd03817 119 yeDYLHYI------PKGKLLVKAVVRKLVRRFYnhtDAVIAPSEKIKDTlreygvkgPIEVIPN--GIDLDKF---EKPL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 557 EERSRGEQAFSKGAY---FLGKMVWAKGYRELIDLMAKHKSELGSFnLDVYGNGEDAVEVQRAAKKHDL--NLNFLKGRD 631
Cdd:cd03817 188 NTEERRKLGLPPDEPillYVGRLAKEKNIDFLLRAFAELKKEPNIK-LVIVGDGPEREELKELARELGLadKVIFTGFVP 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117910937 632 HaDDALHKYK---VFINPSISDVLCTATAEALAMGKFVVCADHPS-NEFFRSFPNCLTYKTSEDFVSK 695
Cdd:cd03817 267 R-EELPEYYKaadLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAaSELVEDGENGFLFEPNDETLAE 333
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
399-663 |
4.65e-06 |
|
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: 49.54 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 399 LTFSSPEEQESYIrkwLEERIGFKADFKISFYPGKFSKERRSIFPAgdTSQFISSKDADIAILEEPEHLNW---YYHGKR 475
Cdd:cd03820 36 ISLDSAEKPPFYE---LDDNIKIKNLGDRKYSHFKLLLKYFKKVRR--LRKYLKNNKPDVVISFRTSLLTFlalIGLKSK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 476 wtdkfnhVVGIVHTNYLEYIKREKNGALQAFFVNhvnnwvtraYCDKVLRLSAAT------QDLPKSVV----CNVHGVN 545
Cdd:cd03820 111 -------LIVWEHNNYEAYNKGLRRLLLRRLLYK---------RADKIVVLTEADklkkykQPNSNVVVipnpLSFPSEE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 546 PKFLMIGEKIAeersrgeqafskgayFLGKMVWAKGYRELIDLMAKHKSELGSFNLDVYGNGEDAVEVQRAAKKHDLN-L 624
Cdd:cd03820 175 PSTNLKSKRIL---------------AVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEdR 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 117910937 625 NFLKGR-DHADDALHKYKVFINPSISD----VLCtataEALAMG 663
Cdd:cd03820 240 VKLLGPtKNIAEEYANSSIFVLSSRYEgfpmVLL----EAMAYG 279
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
424-684 |
6.87e-06 |
|
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: 48.89 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 424 DFKISFYPGKFSKERRSIFPAGDTSQFISSKDADIAILeepehLNWYYHGKRWTDKFNH----VVGIVHtNYLEYIKREK 499
Cdd:cd03811 50 DVKLIRLLIRVLKLIKLGLLKAILKLKRILKRAKPDVV-----ISFLGFATYIVAKLAAarskVIAWIH-SSLSKLYYLK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 500 NGALQAFFVNHVNNW---VTRAYCDKVLRLSAatqdLPKSVVCNVH-GVNPKFLmigEKIAEERSRGEQAfsKGAYFL-- 573
Cdd:cd03811 124 KKLLLKLKLYKKADKivcVSKGIKEDLIRLGP----SPPEKIEVIYnPIDIDRI---RALAKEPILNEPE--DGPVILav 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 574 GKMVWAKGYRELIDLMAKHKSELGSFNLDVYGNGEDAVEVQRAAKkhDLNLN---FLKG-RDHADDALHKYKVFINPSIS 649
Cdd:cd03811 195 GRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAK--ELGLAervIFLGfQSNPYPYLKKADLFVLSSRY 272
|
250 260 270
....*....|....*....|....*....|....*.
gi 117910937 650 DVLCTATAEALAMGKFVVCADHP-SNEFFRSFPNCL 684
Cdd:cd03811 273 EGFPNVLLEAMALGTPVVSTDCPgPREILDDGENGL 308
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
572-672 |
1.17e-05 |
|
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: 48.36 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 572 FLGKMVWAKGYRELIDLMAKHKSELGSFNLDVYGNGEDAVEVQRAAKKHDL--NLNFLKGRDHADDALHKYKVFINPSIS 649
Cdd:cd03808 194 FVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLegRIEFLGFRSDVPELLAESDVFVLPSYR 273
|
90 100
....*....|....*....|...
gi 117910937 650 DVLCTATAEALAMGKFVVCADHP 672
Cdd:cd03808 274 EGLPRSLLEAMAAGRPVITTDVP 296
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
623-726 |
1.91e-04 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 41.90 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 623 NLNFLKGRDHADDA-LHKYKVFINPSISDVLCTATAEALAMGKFVVCADHPSN-EFFRSFPNCLTYK--TSEDFVSKVQE 698
Cdd:COG0438 3 RLVPRKGLDLLLEAlLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLpEVIEDGETGLLVPpgDPEALAEAILR 82
|
90 100 110
....*....|....*....|....*....|....
gi 117910937 699 AMTKEPLPLTPEQ------MYNLSWEAATQRFME 726
Cdd:COG0438 83 LLEDPELRRRLGEaareraEERFSWEAIAERLLA 116
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
543-667 |
1.90e-03 |
|
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: 41.49 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 543 GVNPKFLMIGEKiAEERSRGEQAFSKGAYFLGKMVWAKGYRELIDLMAKHKselgsFNLDVYGNGEDAVEVQRAAKKHDL 622
Cdd:cd03795 168 GIDKNVYNIPRV-DFENIKREKKGKKIFLFIGRLVYYKGLDYLIEAAQYLN-----YPIVIGGEGPLKPDLEAQIELNLL 241
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 117910937 623 NLNFLKGRDHADDALHKY---KVFINPSI--SDVLCTATAEALAMGKFVV 667
Cdd:cd03795 242 DNVKFLGRVDDEEKVIYLhlcDVFVFPSVlrSEAFGIVLLEAMMCGKPVI 291
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
572-671 |
2.33e-03 |
|
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: 41.19 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117910937 572 FLGKMVWAKGYRELIDLMAKHKSELGsFNLDVYGNGEDAVEVQRAAKKHdlnlnFLKGR----DHADDALHKYK---VFI 644
Cdd:cd03819 187 YVGRLSPEKGWLLLVDAAAELKDEPD-FRLLVAGDGPERDEIRRLVERL-----GLRDRvtftGFREDVPAALAasdVVV 260
|
90 100
....*....|....*....|....*..
gi 117910937 645 NPSISDVLCTATAEALAMGKFVVCADH 671
Cdd:cd03819 261 LPSLHEEFGRVALEAMACGTPVVATDV 287
|
|
| |
