NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|544212080|ref|XP_005536439|]
View 

similar to glycosyl transferase [Cyanidioschyzon merolae strain 10D]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 41-529 1.41e-102

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 cd03806:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 419  Bit Score: 314.93  E-value: 1.41e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080  41 FGFLHPSCAGGGGGERVLWCAVRALcsetrrlasdrpQNgSTPHSTIVaprvwLYTARYRSSVAEIrafLDvRLAEQFGA 120
Cdd:cd03806    3 VGFFHPYCNAGGGGERVLWCAVKAT------------QK-AYPNNICV-----IYTGDTDSSPEEI---LE-KVESRFNI 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 121 EAFTNAVQQVRLVPLYtavLLEPRWYPYFTMLFQLLAGMPVAVEIMLrhasflvthllsKCVswfrkryrtpledyrlPS 200
Cdd:cd03806   61 DLDSPRIVFFLLKYRK---LVEAKTYPRFTLLGQALGSMILGFEALL------------KLV----------------PD 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 201 IFLDTVGVPLALLCLKWWtcGRIRTGAYVHYPFVSNEM--------MSHEPRSTGSGSrKLRSVCRRGYYRAVVLpLYAA 272
Cdd:cd03806  110 VFIDTMGYPFTYPLVRLL--GGCPVVAYVHYPTISTDMlnkvrsreASYNNDSTIARS-SVLSIAKLLYYRLFAF-LYGL 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 273 CGAATDLVMANSSWTLQRMEQLWcgsgasssrasctgHHRRNIFLVYPPCGArrTHSSFPALERDAVRQRVVSIAQFRPE 352
Cdd:cd03806  186 AGSFADVVMVNSTWTYNHIRQLW--------------KRNIKPSIVYPPCDT--EELTKLPIDEKTRENQILSIAQFRPE 249

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 353 KRHETQLDCFVELLQRYPRET-SQARLLMIGGARNHADRMRAERLLQRAVALtgsaSSGGRIEVHVNASRIEIEEVLAG- 430
Cdd:cd03806  250 KNHPLQLRAFAELLKRLPESIrSNPKLVLIGSCRNEEDKERVEALKLLAKEL----ILEDSVEFVVDAPYEELKELLSTa 325

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 431 EFGcfLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAALDILRPVSpDSPLGLVYRTRHELTECLADAlFRLPVATLQSMQ 510
Cdd:cd03806  326 SIG--LHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWD-GGPTGFLASTPEEYAEAIEKI-LTLSEEERLQRR 401

                        490
                 ....*....|....*....
gi 544212080 511 RRAYARAQReFSDEAFSER 529
Cdd:cd03806  402 EAARSSAER-FSDEEFERD 419
 
Name Accession Description Interval E-value
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
 41-529 1.41e-102

alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.


Pssm-ID: 340835 [Multi-domain]  Cd Length: 419  Bit Score: 314.93  E-value: 1.41e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080  41 FGFLHPSCAGGGGGERVLWCAVRALcsetrrlasdrpQNgSTPHSTIVaprvwLYTARYRSSVAEIrafLDvRLAEQFGA 120
Cdd:cd03806    3 VGFFHPYCNAGGGGERVLWCAVKAT------------QK-AYPNNICV-----IYTGDTDSSPEEI---LE-KVESRFNI 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 121 EAFTNAVQQVRLVPLYtavLLEPRWYPYFTMLFQLLAGMPVAVEIMLrhasflvthllsKCVswfrkryrtpledyrlPS 200
Cdd:cd03806   61 DLDSPRIVFFLLKYRK---LVEAKTYPRFTLLGQALGSMILGFEALL------------KLV----------------PD 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 201 IFLDTVGVPLALLCLKWWtcGRIRTGAYVHYPFVSNEM--------MSHEPRSTGSGSrKLRSVCRRGYYRAVVLpLYAA 272
Cdd:cd03806  110 VFIDTMGYPFTYPLVRLL--GGCPVVAYVHYPTISTDMlnkvrsreASYNNDSTIARS-SVLSIAKLLYYRLFAF-LYGL 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 273 CGAATDLVMANSSWTLQRMEQLWcgsgasssrasctgHHRRNIFLVYPPCGArrTHSSFPALERDAVRQRVVSIAQFRPE 352
Cdd:cd03806  186 AGSFADVVMVNSTWTYNHIRQLW--------------KRNIKPSIVYPPCDT--EELTKLPIDEKTRENQILSIAQFRPE 249

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 353 KRHETQLDCFVELLQRYPRET-SQARLLMIGGARNHADRMRAERLLQRAVALtgsaSSGGRIEVHVNASRIEIEEVLAG- 430
Cdd:cd03806  250 KNHPLQLRAFAELLKRLPESIrSNPKLVLIGSCRNEEDKERVEALKLLAKEL----ILEDSVEFVVDAPYEELKELLSTa 325

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 431 EFGcfLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAALDILRPVSpDSPLGLVYRTRHELTECLADAlFRLPVATLQSMQ 510
Cdd:cd03806  326 SIG--LHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWD-GGPTGFLASTPEEYAEAIEKI-LTLSEEERLQRR 401

                        490
                 ....*....|....*....
gi 544212080 511 RRAYARAQReFSDEAFSER 529
Cdd:cd03806  402 EAARSSAER-FSDEEFERD 419
PLN02949 PLN02949
transferase, transferring glycosyl groups
 6-537 1.04e-74

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 244.26  E-value: 1.04e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080   6 VVALALVGLLWLALCRQLVesepRQVAASDSSRASFGFLHPSCAGGGGGERVLWCAVRALCSEtrrlasdrpqngsTPHS 85
Cdd:PLN02949   5 LILYHLLTSIVLLLVAIAL----SVLRARRSRKRAVGFFHPYTNDGGGGERVLWCAVRAIQEE-------------NPDL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080  86 TIVaprvwLYTARYRSSVAEIRAfldvRLAEQFGAEAFTnaVQQVrlVPLYTAVLLEPRWYPYFTMLFQLLAGMPVAVEI 165
Cdd:PLN02949  68 DCV-----IYTGDHDASPDSLAA----RARDRFGVELLS--PPKV--VHLRKRKWIEEETYPRFTMIGQSLGSVYLAWEA 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 166 MLRhasflvthllskcvswFRkryrtpledyrlPSIFLDTVG----VPLALLclkwWTCgriRTGAYVHYPFVSNEMMSH 241
Cdd:PLN02949 135 LCK----------------FT------------PLYFFDTSGyaftYPLARL----FGC---KVVCYTHYPTISSDMISR 179

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 242 -EPRST-----GSGSR-KLRSVCRRGYYRAVVLpLYAACGAATDLVMANSSWTLQRMEQLWcgsgasssrascTGHHRrn 314
Cdd:PLN02949 180 vRDRSSmynndASIARsFWLSTCKILYYRAFAW-MYGLVGRCAHLAMVNSSWTKSHIEALW------------RIPER-- 244

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 315 IFLVYPPCGArRTHSSFPaLERDAVRQRVVSIAQFRPEKRHETQLDCFVELLQRYPRETSQARLLMIGGARNHADRMRAE 394
Cdd:PLN02949 245 IKRVYPPCDT-SGLQALP-LERSEDPPYIISVAQFRPEKAHALQLEAFALALEKLDADVPRPKLQFVGSCRNKEDEERLQ 322

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 395 RLLQRAVALtgsaSSGGRIEVHVNASRIEIEEVLAGEFGCfLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAALDILRPv 474
Cdd:PLN02949 323 KLKDRAKEL----GLDGDVEFHKNVSYRDLVRLLGGAVAG-LHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIVLD- 396

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544212080 475 SPDSPLGLVYRTRHELTECLADALfRLPVATLQSMQRRAYARAQReFSDEAFSERFLTAVASL 537
Cdd:PLN02949 397 EDGQQTGFLATTVEEYADAILEVL-RMRETERLEIAAAARKRANR-FSEQRFNEDFKDAIRPI 457
ALG11_N pfam15924
ALG11 mannosyltransferase N-terminus;
38-295 2.33e-49

ALG11 mannosyltransferase N-terminus;


Pssm-ID: 464944  Cd Length: 209  Bit Score: 169.19  E-value: 2.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080   38 RASFGFLHPSCAGGGGGERVLWCAVRALCSEtrrlasdrpqngsTPHSTIVaprvwLYTARYRSSVAEIRAfldvRLAEQ 117
Cdd:pfam15924   1 KGIVGFFHPYCNAGGGGERVLWCAVRATQRR-------------YPNAICV-----VYTGDIDASKEEILA----KVKSR 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080  118 FGAEAFTNAVQqvrLVPLYTAVLLEPRWYPYFTMLFQLLAGMPVAVEimlrhAsflvthlLSKCVswfrkryrtpledyr 197
Cdd:pfam15924  59 FNIELDPSRIV---FVYLRKRKLVEASTYPRFTLLGQSLGSIILAWE-----A-------LSKLV--------------- 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080  198 lPSIFLDTVGVPLALLCLKWWtcGRIRTGAYVHYPFVSNEMMS--------HEPRSTGSGSrKLRSVCRRGYYRAVVLpL 269
Cdd:pfam15924 109 -PDVFIDTMGYAFTYPLVRLL--GGCPVGAYVHYPTISTDMLSrvssreagYNNDSAIASS-GLLSKAKLIYYRLFAL-L 183

                         250       260
                  ....*....|....*....|....*.
gi 544212080  270 YAACGAATDLVMANSSWTLQRMEQLW 295
Cdd:pfam15924 184 YGLVGSFADVVMVNSSWTQNHIRSLW 209
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 434-538 5.99e-10

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 56.92  E-value: 5.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 434 CFLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAAlDILRpvspDSPLGLVYRTRHEltECLADALFRL--PVATLQSMQR 511
Cdd:COG0438   23 VFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLP-EVIE----DGETGLLVPPGDP--EALAEAILRLleDPELRRRLGE 95

                         90       100
                 ....*....|....*....|....*..
gi 544212080 512 RAYARAQREFSDEAFSERFLTAVASLC 538
Cdd:COG0438   96 AARERAEERFSWEAIAERLLALYEELL 122
 
Name Accession Description Interval E-value
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
 41-529 1.41e-102

alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.


Pssm-ID: 340835 [Multi-domain]  Cd Length: 419  Bit Score: 314.93  E-value: 1.41e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080  41 FGFLHPSCAGGGGGERVLWCAVRALcsetrrlasdrpQNgSTPHSTIVaprvwLYTARYRSSVAEIrafLDvRLAEQFGA 120
Cdd:cd03806    3 VGFFHPYCNAGGGGERVLWCAVKAT------------QK-AYPNNICV-----IYTGDTDSSPEEI---LE-KVESRFNI 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 121 EAFTNAVQQVRLVPLYtavLLEPRWYPYFTMLFQLLAGMPVAVEIMLrhasflvthllsKCVswfrkryrtpledyrlPS 200
Cdd:cd03806   61 DLDSPRIVFFLLKYRK---LVEAKTYPRFTLLGQALGSMILGFEALL------------KLV----------------PD 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 201 IFLDTVGVPLALLCLKWWtcGRIRTGAYVHYPFVSNEM--------MSHEPRSTGSGSrKLRSVCRRGYYRAVVLpLYAA 272
Cdd:cd03806  110 VFIDTMGYPFTYPLVRLL--GGCPVVAYVHYPTISTDMlnkvrsreASYNNDSTIARS-SVLSIAKLLYYRLFAF-LYGL 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 273 CGAATDLVMANSSWTLQRMEQLWcgsgasssrasctgHHRRNIFLVYPPCGArrTHSSFPALERDAVRQRVVSIAQFRPE 352
Cdd:cd03806  186 AGSFADVVMVNSTWTYNHIRQLW--------------KRNIKPSIVYPPCDT--EELTKLPIDEKTRENQILSIAQFRPE 249

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 353 KRHETQLDCFVELLQRYPRET-SQARLLMIGGARNHADRMRAERLLQRAVALtgsaSSGGRIEVHVNASRIEIEEVLAG- 430
Cdd:cd03806  250 KNHPLQLRAFAELLKRLPESIrSNPKLVLIGSCRNEEDKERVEALKLLAKEL----ILEDSVEFVVDAPYEELKELLSTa 325

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 431 EFGcfLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAALDILRPVSpDSPLGLVYRTRHELTECLADAlFRLPVATLQSMQ 510
Cdd:cd03806  326 SIG--LHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWD-GGPTGFLASTPEEYAEAIEKI-LTLSEEERLQRR 401

                        490
                 ....*....|....*....
gi 544212080 511 RRAYARAQReFSDEAFSER 529
Cdd:cd03806  402 EAARSSAER-FSDEEFERD 419
PLN02949 PLN02949
transferase, transferring glycosyl groups
 6-537 1.04e-74

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 244.26  E-value: 1.04e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080   6 VVALALVGLLWLALCRQLVesepRQVAASDSSRASFGFLHPSCAGGGGGERVLWCAVRALCSEtrrlasdrpqngsTPHS 85
Cdd:PLN02949   5 LILYHLLTSIVLLLVAIAL----SVLRARRSRKRAVGFFHPYTNDGGGGERVLWCAVRAIQEE-------------NPDL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080  86 TIVaprvwLYTARYRSSVAEIRAfldvRLAEQFGAEAFTnaVQQVrlVPLYTAVLLEPRWYPYFTMLFQLLAGMPVAVEI 165
Cdd:PLN02949  68 DCV-----IYTGDHDASPDSLAA----RARDRFGVELLS--PPKV--VHLRKRKWIEEETYPRFTMIGQSLGSVYLAWEA 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 166 MLRhasflvthllskcvswFRkryrtpledyrlPSIFLDTVG----VPLALLclkwWTCgriRTGAYVHYPFVSNEMMSH 241
Cdd:PLN02949 135 LCK----------------FT------------PLYFFDTSGyaftYPLARL----FGC---KVVCYTHYPTISSDMISR 179

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 242 -EPRST-----GSGSR-KLRSVCRRGYYRAVVLpLYAACGAATDLVMANSSWTLQRMEQLWcgsgasssrascTGHHRrn 314
Cdd:PLN02949 180 vRDRSSmynndASIARsFWLSTCKILYYRAFAW-MYGLVGRCAHLAMVNSSWTKSHIEALW------------RIPER-- 244

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 315 IFLVYPPCGArRTHSSFPaLERDAVRQRVVSIAQFRPEKRHETQLDCFVELLQRYPRETSQARLLMIGGARNHADRMRAE 394
Cdd:PLN02949 245 IKRVYPPCDT-SGLQALP-LERSEDPPYIISVAQFRPEKAHALQLEAFALALEKLDADVPRPKLQFVGSCRNKEDEERLQ 322

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 395 RLLQRAVALtgsaSSGGRIEVHVNASRIEIEEVLAGEFGCfLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAALDILRPv 474
Cdd:PLN02949 323 KLKDRAKEL----GLDGDVEFHKNVSYRDLVRLLGGAVAG-LHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIVLD- 396

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544212080 475 SPDSPLGLVYRTRHELTECLADALfRLPVATLQSMQRRAYARAQReFSDEAFSERFLTAVASL 537
Cdd:PLN02949 397 EDGQQTGFLATTVEEYADAILEVL-RMRETERLEIAAAARKRANR-FSEQRFNEDFKDAIRPI 457
ALG11_N pfam15924
ALG11 mannosyltransferase N-terminus;
38-295 2.33e-49

ALG11 mannosyltransferase N-terminus;


Pssm-ID: 464944  Cd Length: 209  Bit Score: 169.19  E-value: 2.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080   38 RASFGFLHPSCAGGGGGERVLWCAVRALCSEtrrlasdrpqngsTPHSTIVaprvwLYTARYRSSVAEIRAfldvRLAEQ 117
Cdd:pfam15924   1 KGIVGFFHPYCNAGGGGERVLWCAVRATQRR-------------YPNAICV-----VYTGDIDASKEEILA----KVKSR 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080  118 FGAEAFTNAVQqvrLVPLYTAVLLEPRWYPYFTMLFQLLAGMPVAVEimlrhAsflvthlLSKCVswfrkryrtpledyr 197
Cdd:pfam15924  59 FNIELDPSRIV---FVYLRKRKLVEASTYPRFTLLGQSLGSIILAWE-----A-------LSKLV--------------- 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080  198 lPSIFLDTVGVPLALLCLKWWtcGRIRTGAYVHYPFVSNEMMS--------HEPRSTGSGSrKLRSVCRRGYYRAVVLpL 269
Cdd:pfam15924 109 -PDVFIDTMGYAFTYPLVRLL--GGCPVGAYVHYPTISTDMLSrvssreagYNNDSAIASS-GLLSKAKLIYYRLFAL-L 183

                         250       260
                  ....*....|....*....|....*.
gi 544212080  270 YAACGAATDLVMANSSWTLQRMEQLW 295
Cdd:pfam15924 184 YGLVGSFADVVMVNSSWTQNHIRSLW 209
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 277-531 1.04e-13

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: 72.57  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 277 TDLVMANSSWTLQRMEQLWcgsgasssrasctGHHRRNIFLVYPPCGARRTHSSF-PALERDAVRQRVVSIAQFRPEKRH 355
Cdd:cd03801  141 ADAVIAVSEALRDELRALG-------------GIPPEKIVVIPNGVDLERFSPPLrRKLGIPPDRPVLLFVGRLSPRKGV 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 356 ETqldcFVELLQRYPRETSQARLLMIGGARNHADRMRAERLlqravaltgsaSSGGRIEVHVNASRIEIEEVLAgEFGCF 435
Cdd:cd03801  208 DL----LLEALAKLLRRGPDVRLVIVGGDGPLRAELEELEL-----------GLGDRVRFLGFVPDEELPALYA-AADVF 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 436 LHTMEEEHFGISIVEAMSHGLLVIAHGSGGaaldiLRPVSPDSPLGLVYRTrhELTECLADALFRL--PVATLQSMQRRA 513
Cdd:cd03801  272 VLPSRYEGFGLVVLEAMAAGLPVVATDVGG-----LPEVVEDGEGGLVVPP--DDVEALADALLRLlaDPELRARLGRAA 344

                        250
                 ....*....|....*...
gi 544212080 514 YARAQREFSDEAFSERFL 531
Cdd:cd03801  345 RERVAERFSWERVAERLL 362
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 317-532 3.96e-11

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: 64.65  E-value: 3.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 317 LVYPPCGARRTHSSFPaLERDAVRqrVVSIAQFRPEKRHETQLDCFVELLQRYPretsQARLLMIG--GARNHADRMRAE 394
Cdd:cd03807  170 LSPDDASRARARRRLG-LAEDRRV--IGIVGRLHPVKDHSDLLRAAALLVETHP----DLRLLLVGrgPERPNLERLLLE 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 395 RLLQRAVALTGsassggrievhvnasriEIEEV--LAGEFGCFLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAAlDILR 472
Cdd:cd03807  243 LGLEDRVHLLG-----------------ERSDVpaLLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAA-ELVD 304

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544212080 473 P-----VSPDSPLGLVyrtrheltECLaDALFRLPvATLQSMQRRAYARAQREFSDEAFSERFLT 532
Cdd:cd03807  305 DgtgflVPAGDPQALA--------DAI-RALLEDP-EKRARLGRAARERIANEFSIDAMVRRYET 359
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 343-473 2.85e-10

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: 58.82  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080  343 VVSIAQFRPEKRHETQLDCFVELLQRYPretsQARLLMIGG--ARNHADRMRAERLLQRAVALTGSASSGGRIEVHVNAS 420
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFALLKEKNP----NLKLVIAGDgeEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIAD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 544212080  421 rieieevlagefgCFLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAAlDILRP 473
Cdd:pfam00534  81 -------------VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPP-EVVKD 119
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 434-538 5.99e-10

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 56.92  E-value: 5.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 434 CFLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAAlDILRpvspDSPLGLVYRTRHEltECLADALFRL--PVATLQSMQR 511
Cdd:COG0438   23 VFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLP-EVIE----DGETGLLVPPGDP--EALAEAILRLleDPELRRRLGE 95

                         90       100
                 ....*....|....*....|....*..
gi 544212080 512 RAYARAQREFSDEAFSERFLTAVASLC 538
Cdd:COG0438   96 AARERAEERFSWEAIAERLLALYEELL 122
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 314-532 8.72e-10

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: 60.72  E-value: 8.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 314 NIFLVYPPCGARRThssfpALERDAVRQRVVSIAQFRPEKRHETQLDCFVELlqryPRETSQARLLMIGGARNHADRMRA 393
Cdd:cd03800  199 ERFFPVDRAEARRA-----RLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQL----PELRELANLVLVGGPSDDPLSMDR 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 394 ERLLQRAVALTGSassgGRIEVHVNASRIEIEEV--LAGEFGCFLHTmeeEHFGISIVEAMSHGLLVIAHGSGGAAlDIL 471
Cdd:cd03800  270 EELAELAEELGLI----DRVRFPGRVSRDDLPELyrAADVFVVPSLY---EPFGLTAIEAMACGTPVVATAVGGLQ-DIV 341

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544212080 472 RP------VSPDSPlglvyrtrHELTECLADaLFRLPvATLQSMQRRAYARAQREFSDEAFSERFLT 532
Cdd:cd03800  342 RDgrtgllVDPHDP--------EALAAALRR-LLDDP-ALWQRLSRAGLERARAHYTWESVADQLLT 398
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 318-530 7.53e-09

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 57.60  E-value: 7.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 318 VYPPCGArrthSSFPALERDAVRQR---------VVSIAQFRPEKRHETQLDCFVELLQRYPrETSQARLLMIGG--ARN 386
Cdd:cd03805  184 LYPCVDT----DSFDSTSEDPDPGDliaksnkkfFLSINRFERKKNIALAIEAFAKLKQKLP-EFENVRLVIAGGydPRV 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 387 HADRMRAERLLQRAVALTGSASsggrievHV----NASRIEIEEVLAgEFGCFLHTMEEEHFGISIVEAMSHGLLVIAHG 462
Cdd:cd03805  259 AENVEYLEELQRLAEELLNVED-------QVlflrSISDSQKEQLLS-SALALLYTPSNEHFGIVPLEAMYAGKPVIACN 330

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544212080 463 SGGAALDI-------LRPVSPDSplglvyrtrheltecLADA---LFRLPVaTLQSMQRRAYARAQREFSDEAFSERF 530
Cdd:cd03805  331 SGGPLETVvegvtgfLCEPTPEA---------------FAEAmlkLANDPD-LADRMGAAGRKRVKEKFSREAFAERL 392
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 319-471 7.16e-08

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: 53.56  E-value: 7.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 319 YPPCGARRTHSSFPALERDAVRQRVVSIAQFRPEKRHETqldcFVELLQRYPRETSQARLLMIGGARNHADRMRAERLLQ 398
Cdd:cd01635   89 DSLESTRSELLALARLLVSLPLADKVSVGRLVPEKGIDL----LLEALALLKARLPDLVLVLVGGGGEREEEEALAAALG 164

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544212080 399 RavaltgsassGGRIEVHVNASRIEIEEVLAGEFGCFLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAALDIL 471
Cdd:cd01635  165 L----------LERVVIIGGLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVV 227
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 318-465 1.76e-07

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 53.51  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 318 VYPPCGARRTHSSFPALERDAVrqrVVSIAQFRPEKRHETQLDCFVELlqrypRETSQARLLMIGgarNHADRMRAERLL 397
Cdd:cd04962  177 VFKRKPAGALKRRLLAPPDEKV---VIHVSNFRPVKRIDDVVRVFARV-----RRKIPAKLLLVG---DGPERVPAEELA 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544212080 398 QRAvaltgsassGGRIEVHVNASRIEIEEVLaGEFGCFLHTMEEEHFGISIVEAMSHGLLVIAHGSGG 465
Cdd:cd04962  246 REL---------GVEDRVLFLGKQDDVEELL-SIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGG 303
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 343-533 6.59e-07

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: 51.61  E-value: 6.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 343 VVSIAQFRPEKRHETQLDCFVELLQRYPRetsqARLLMIGGARnhadrmraerLLQRAVALTGSASSGGRIEVHVNASRI 422
Cdd:cd03798  203 ILFVGRLIPRKGIDLLLEAFARLAKARPD----VVLLIVGDGP----------LREALRALAEDLGLGDRVTFTGRLPHE 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 423 EIEEVLAGeFGCFLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAAlDILRpvspDSPLGLVYRTR--HELTECLADALFR 500
Cdd:cd03798  269 QVPAYYRA-CDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIP-EVVG----DPETGLLVPPGdaDALAAALRRALAE 342

                        170       180       190
                 ....*....|....*....|....*....|...
gi 544212080 501 lpvATLQSMQRRAYARAQREFSDEAFSERFLTA 533
Cdd:cd03798  343 ---PYLRELGEAARARVAERFSWVKAADRIAAA 372
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 328-529 4.59e-05

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 45.76  E-value: 4.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 328 HSSFPALERDAVRQRVVSIAQFRPEKRHETQLDCFVELLQRYPretsQARLLMIG-GARNHADRMRAERL-LQRAVALTG 405
Cdd:cd04949  148 QLDTAESNHERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVP----EITLDIYGyGEEREKLKKLIEELhLEDNVFLKG 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 406 SASSggrievhvnasrieIEEVLAgEFGCFLHTMEEEHFGISIVEAMSHGLLVIAHgsggaaldilrpvspDSPLG---L 482
Cdd:cd04949  224 YHSN--------------LDQEYQ-DAYLSLLTSQMEGFGLTLMEAIGHGLPVVSY---------------DVKYGpseL 273

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 544212080 483 V------YRTRHELTECLADALFRLPV--ATLQSMQRRAYARAQReFSDEAFSER 529
Cdd:cd04949  274 IedgengYLIEKNNIDALADKIIELLNdpEKLQQFSEESYKIAEK-YSTENVMEK 327
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 342-531 7.12e-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: 45.28  E-value: 7.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 342 RVVSIAQFRPEKRHETQLDCFVELLQRYPretsQARLLMIG-GARNHADRMRAERLlqravaltgsaSSGGRIEVHvnAS 420
Cdd:cd03808  191 VFLFVARLLKDKGIDELIEAAKILKKKGP----NVRFLLVGdGELENPSEILIEKL-----------GLEGRIEFL--GF 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 421 RIEIEEVLAgEFGCFLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAAlDILRP------VSPDSPlglvyrtrheltECL 494
Cdd:cd03808  254 RSDVPELLA-ESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCR-ELVIDgvngflVPPGDV------------EAL 319

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 544212080 495 ADALFRL--PVATLQSMQRRAYARAQREFSDEAFSERFL 531
Cdd:cd03808  320 ADAIEKLieDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 343-466 1.15e-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: 44.27  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 343 VVSIAQFRPEKRHetqlDCFVELLQRYPRETsQARLLMIG-GARNHADRMRAERLLQRavaltgsassgGRIEVHVNASR 421
Cdd:cd03819  185 VGYVGRLSPEKGW----LLLVDAAAELKDEP-DFRLLVAGdGPERDEIRRLVERLGLR-----------DRVTFTGFRED 248

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 544212080 422 IEieeVLAGEFGCFLHTMEEEHFGISIVEAMSHGLLVIAHGSGGA 466
Cdd:cd03819  249 VP---AALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGA 290
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
340-501 2.25e-04

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 41.34  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080  340 RQRVVSIAQFRPE-KRHETQLDCFVELLQRypreTSQARLLMIGGARnhadrmrAERLLQRAVALTGSassggrieVHVN 418
Cdd:pfam13692   1 RPVILFVGRLHPNvKGVDYLLEAVPLLRKR----DNDVRLVIVGDGP-------EEELEELAAGLEDR--------VIFT 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080  419 ASRIEIEEVLAgEFGCFLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAAlDILRPVSpdsplGLVYRTRHEltECLADAL 498
Cdd:pfam13692  62 GFVEDLAELLA-AADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIP-ELVDGEN-----GLLVPPGDP--EALAEAI 132


                  ...
gi 544212080  499 FRL 501
Cdd:pfam13692 133 LRL 135
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 342-467 2.98e-04

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: 43.04  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 342 RVVSIAQFRPEKRHETQLDCFVELLQRYPretsqARLLMIG-GARNHADRMRAERL-LQRAVALTGSassggrievhvna 419
Cdd:cd03817  203 ILLYVGRLAKEKNIDFLLRAFAELKKEPN-----IKLVIVGdGPEREELKELARELgLADKVIFTGF------------- 264

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 544212080 420 srIEIEEVL----AGEfgCFLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAA 467
Cdd:cd03817  265 --VPREELPeyykAAD--LFVFASTTETQGLVYLEAMAAGLPVVAAKDPAAS 312
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 278-530 3.51e-04

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 43.04  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 278 DLVMANSSWTLQRMEQlwcgsgasssrasctgHHRRNIFLVYPPCgarrthssfpALERDAVRQR----VVSIAQFRPEK 353
Cdd:cd03804  159 DLFIANSQFVARRIKK----------------FYGRESTVIYPPV----------DTDAFAPAADkedyYLTASRLVPYK 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 354 RhetqLDCFVELLQRYPRetsqaRLLMIGGArnhADRMRAERLLQRAVALTGSASSGGRIEVHVNASRIeieeVLAGefg 433
Cdd:cd03804  213 R----IDLAVEAFNELPK-----RLVVIGDG---PDLDRLRAMASPNVEFLGYQPDEVLKELLSKARAF----VFAA--- 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 434 cflhtmeEEHFGISIVEAMSHGLLVIAHGSGGaALDILRPvspdSPLGLVYRTRHelTECLADALFRLpVATLQSMQRRA 513
Cdd:cd03804  274 -------EEDFGIVPVEAQACGTPVIAFGKGG-ALETVRP----GPTGILFGEQT--VESLKAAVEEF-EQNFDRFKPQA 338

                        250
                 ....*....|....*..
gi 544212080 514 YARAQREFSDEAFSERF 530
Cdd:cd03804  339 IRANAERFSRARFRQEI 355
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 343-467 5.22e-04

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 42.43  E-value: 5.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 343 VVSIAQFRPEKRHETQLDCFVELLQRYPRetsqARLLMIG--GARNHADRMRAERLLQRAVALTGSASSggrIEVHVNAS 420
Cdd:cd04951  191 ILNVGRLTEAKDYPNLLLAISELILSKND----FKLLIAGdgPLRNELERLICNLNLVDRVILLGQISN---ISEYYNAA 263

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 544212080 421 rieieevlagefGCFLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAA 467
Cdd:cd04951  264 ------------DLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVA 298
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 434-531 6.73e-04

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 41.90  E-value: 6.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 434 CFLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAAlDILRPvspdSPLGLVYR-TRHELTECLADALFRLPVaTLQSMQRR 512
Cdd:cd03814  270 VFVFPSRTETFGLVVLEAMASGLPVVAADAGGPR-DIVRP----GGTGALVEpGDAAAFAAALRALLEDPE-LRRRMAAR 343

                         90
                 ....*....|....*....
gi 544212080 513 AYARAQReFSDEAFSERFL 531
Cdd:cd03814  344 ARAEAER-YSWEAFLDNLL 361
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 258-529 8.37e-04

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: 41.58  E-value: 8.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 258 RRGYYRAvvlpLYAACGAATDLVMANSSWTLQRMEQLwcgsgasssrasctGHHRRNIFLVYPPCgarrTHSSFPALERD 337
Cdd:cd03809  124 FRLYYRL----LLPISLRRADAIITVSEATRDDIIKF--------------YGVPPEKIVVIPLG----VDPSFFPPESA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 338 AVRQR--------VVSIAQFRPEKRHETqldcFVELLQRYPRETSQARLLMIGGARNHADR---MRAERLLQRAVALTGS 406
Cdd:cd03809  182 AVLIAkyllpepyFLYVGTLEPRKNHER----LLKAFALLKKQGGDLKLVIVGGKGWEDEElldLVKKLGLGGRVRFLGY 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 407 ASSGGRIEVHVNASrieieevlagefgCFLHTMEEEHFGISIVEAMSHGLLVIA-HGS------GGAALdilrPVSPDSP 479
Cdd:cd03809  258 VSDEDLPALYRGAR-------------AFVFPSLYEGFGLPVLEAMACGTPVIAsNISvlpevaGDAAL----YFDPLDP 320

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 544212080 480 LGLvyrtRHELTECLADALFRlpvatlQSMQRRAYARAQReFSDEAFSER 529
Cdd:cd03809  321 ESI----ADAILRLLEDPSLR------EELIRKGLERAKK-FSWEKTAEK 359
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 273-532 7.25e-03

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: 38.85  E-value: 7.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 273 CGAATDLVMANSSWTLQRMEQlwcgsgASSSRASCTGHHRRNIFLVYPPCGARRTHSsfpalerdavRQRVVSIAQFRPE 352
Cdd:cd03823  140 FKKGGDAVLAPSRFTANLHEA------NGLFSARISVIPNAVEPDLAPPPRRRPGTE----------RLRFGYIGRLTEE 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 353 KrhetQLDCFVELLQRYPREtsQARLLMIGGARNHADRmraerllqravaltgSASSGGRIEVHVNASRIEIEEVLAGEF 432
Cdd:cd03823  204 K----GIDLLVEAFKRLPRE--DIELVIAGHGPLSDER---------------QIEGGRRIAFLGRVPTDDIKDFYEKID 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544212080 433 GCFLHTMEEEHFGISIVEAMSHGLLVIAHGSGGAALDIlrpvsPDSPLGLVYRTrhELTECLADALFRL--PVATLQSMQ 510
Cdd:cd03823  263 VLVVPSIWPEPFGLVVREAIAAGLPVIASDLGGIAELI-----QPGVNGLLFAP--GDAEDLAAAMRRLltDPALLERLR 335

                        250       260
                 ....*....|....*....|..
gi 544212080 511 RRAYARAQREFSDEAFSERFLT 532
Cdd:cd03823  336 AGAEPPRSTESQAEEYLKLYRD 357
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 435-465 8.36e-03

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 38.76  E-value: 8.36e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 544212080 435 FLHTMEEEHFGISIVEAMSHGLLVIAHGSGG 465
Cdd:cd03796  273 FLNTSLTEAFCIAIVEAASCGLLVVSTRVGG 303
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH