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Conserved domains on  [gi|529367223|ref|NP_001268755|]
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GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase isoform 2 [Danio rerio]

Protein Classification

GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase( domain architecture ID 10133525)

GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase catalyzes the addition of the 4th and 5th mannose residues to the dolichol-linked oligosaccharide chain, and is involved in the last steps of the synthesis of Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum

CAZY:  GT4
EC:  2.4.1.131
Gene Ontology:  GO:0004377|GO:0006486
SCOP:  3001586

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
33-457 0e+00

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: 734.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223  33 AVAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEILDGARRRFNIRLPRPVKFVF-LKHRLLVEAK 111
Cdd:cd03806    2 TVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFFlLKYRKLVEAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 112 LYPHFTLLGQSVGSIFLGWEALTEFVPDLYIDSMGFAFTLPVFRYLGGCQVGSYVHYPTISTDMLSVVRERNPRFNNADY 191
Cdd:cd03806   82 TYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGGCPVVAYVHYPTISTDMLNKVRSREASYNNDST 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 192 ISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILALWRTPNRTSVVYPPCDVQAFLDVPIgedneeKEQK 271
Cdd:cd03806  162 IARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPI------DEKT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 272 KCHSLVSVGQFRPEKDHQLQIRAFKKLLDRKEVEPagREAVKLVLIGGCRNQEDEDRVLMLRGLCQELGIADRVEFKLNI 351
Cdd:cd03806  236 RENQILSIAQFRPEKNHPLQLRAFAELLKRLPESI--RSNPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEFVVDA 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 352 PFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKLDIVVPYDGGPTGFLADDEDNYADAMERILSMS 431
Cdd:cd03806  314 PYEELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILTLS 393
                        410       420
                 ....*....|....*....|....*.
gi 529367223 432 PATRLEMRRRARLSVSRFSDQEFEGS 457
Cdd:cd03806  394 EEERLQRREAARSSAERFSDEEFERD 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 ...
33-457 0e+00

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: 734.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223  33 AVAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEILDGARRRFNIRLPRPVKFVF-LKHRLLVEAK 111
Cdd:cd03806    2 TVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFFlLKYRKLVEAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 112 LYPHFTLLGQSVGSIFLGWEALTEFVPDLYIDSMGFAFTLPVFRYLGGCQVGSYVHYPTISTDMLSVVRERNPRFNNADY 191
Cdd:cd03806   82 TYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGGCPVVAYVHYPTISTDMLNKVRSREASYNNDST 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 192 ISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILALWRTPNRTSVVYPPCDVQAFLDVPIgedneeKEQK 271
Cdd:cd03806  162 IARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPI------DEKT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 272 KCHSLVSVGQFRPEKDHQLQIRAFKKLLDRKEVEPagREAVKLVLIGGCRNQEDEDRVLMLRGLCQELGIADRVEFKLNI 351
Cdd:cd03806  236 RENQILSIAQFRPEKNHPLQLRAFAELLKRLPESI--RSNPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEFVVDA 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 352 PFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKLDIVVPYDGGPTGFLADDEDNYADAMERILSMS 431
Cdd:cd03806  314 PYEELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILTLS 393
                        410       420
                 ....*....|....*....|....*.
gi 529367223 432 PATRLEMRRRARLSVSRFSDQEFEGS 457
Cdd:cd03806  394 EEERLQRREAARSSAERFSDEEFERD 419
PLN02949 PLN02949
transferase, transferring glycosyl groups
7-467 0e+00

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 557.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223   7 FSLCLCDLISWLQMKRKTRRvqdgrpAVAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEILDGAR 86
Cdd:PLN02949  15 VLLLVAIALSVLRARRSRKR------AVGFFHPYTNDGGGGERVLWCAVRAIQEENPDLDCVIYTGDHDASPDSLAARAR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223  87 RRFNIRLPRPVKFVFLKHRLLVEAKLYPHFTLLGQSVGSIFLGWEALTEFVPDLYIDSMGFAFTLPVFRyLGGCQVGSYV 166
Cdd:PLN02949  89 DRFGVELLSPPKVVHLRKRKWIEEETYPRFTMIGQSLGSVYLAWEALCKFTPLYFFDTSGYAFTYPLAR-LFGCKVVCYT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 167 HYPTISTDMLSVVRERNPRFNNADYISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILALWRTPNRTSV 246
Cdd:PLN02949 168 HYPTISSDMISRVRDRSSMYNNDASIARSFWLSTCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPERIKR 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 247 VYPPCDVQAFLDVPIgEDNEEKEQkkchsLVSVGQFRPEKDHQLQIRAFKKLLDRKEVEPagrEAVKLVLIGGCRNQEDE 326
Cdd:PLN02949 248 VYPPCDTSGLQALPL-ERSEDPPY-----IISVAQFRPEKAHALQLEAFALALEKLDADV---PRPKLQFVGSCRNKEDE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 327 DRVLMLRGLCQELGIADRVEFKLNIPFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKLDIVVPYD 406
Cdd:PLN02949 319 ERLQKLKDRAKELGLDGDVEFHKNVSYRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIVLDED 398
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529367223 407 GGPTGFLADDEDNYADAMERILSMSPATRLEMRRRARLSVSRFSDQEFEGSFLSAMEPLMS 467
Cdd:PLN02949 399 GQQTGFLATTVEEYADAILEVLRMRETERLEIAAAARKRANRFSEQRFNEDFKDAIRPILN 459
ALG11_N pfam15924
ALG11 mannosyltransferase N-terminus;
31-238 1.00e-143

ALG11 mannosyltransferase N-terminus;


Pssm-ID: 464944  Cd Length: 209  Bit Score: 409.56  E-value: 1.00e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223   31 RPAVAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEILDGARRRFNIRLPR-PVKFVFLKHRLLVE 109
Cdd:pfam15924   1 KGIVGFFHPYCNAGGGGERVLWCAVRATQRRYPNAICVVYTGDIDASKEEILAKVKSRFNIELDPsRIVFVYLRKRKLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223  110 AKLYPHFTLLGQSVGSIFLGWEALTEFVPDLYIDSMGFAFTLPVFRYLGGCQVGSYVHYPTISTDMLSVVRERNPRFNNA 189
Cdd:pfam15924  81 ASTYPRFTLLGQSLGSIILAWEALSKLVPDVFIDTMGYAFTYPLVRLLGGCPVGAYVHYPTISTDMLSRVSSREAGYNND 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 529367223  190 DYISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILALW 238
Cdd:pfam15924 161 SAIASSGLLSKAKLIYYRLFALLYGLVGSFADVVMVNSSWTQNHIRSLW 209
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
360-467 5.88e-11

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 59.62  E-value: 5.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 360 LTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVVPydgGPTGFLAD--DEDNYADAMERILSmSPATRLE 437
Cdd:COG0438   18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLP-EVIED---GETGLLVPpgDPEALAEAILRLLE-DPELRRR 92
                         90       100       110
                 ....*....|....*....|....*....|.
gi 529367223 438 MRRRAR-LSVSRFSDQEFEGSFLSAMEPLMS 467
Cdd:COG0438   93 LGEAAReRAEERFSWEAIAERLLALYEELLA 123
 
Name Accession Description Interval E-value
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
33-457 0e+00

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: 734.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223  33 AVAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEILDGARRRFNIRLPRPVKFVF-LKHRLLVEAK 111
Cdd:cd03806    2 TVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFFlLKYRKLVEAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 112 LYPHFTLLGQSVGSIFLGWEALTEFVPDLYIDSMGFAFTLPVFRYLGGCQVGSYVHYPTISTDMLSVVRERNPRFNNADY 191
Cdd:cd03806   82 TYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGGCPVVAYVHYPTISTDMLNKVRSREASYNNDST 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 192 ISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILALWRTPNRTSVVYPPCDVQAFLDVPIgedneeKEQK 271
Cdd:cd03806  162 IARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPI------DEKT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 272 KCHSLVSVGQFRPEKDHQLQIRAFKKLLDRKEVEPagREAVKLVLIGGCRNQEDEDRVLMLRGLCQELGIADRVEFKLNI 351
Cdd:cd03806  236 RENQILSIAQFRPEKNHPLQLRAFAELLKRLPESI--RSNPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEFVVDA 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 352 PFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKLDIVVPYDGGPTGFLADDEDNYADAMERILSMS 431
Cdd:cd03806  314 PYEELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILTLS 393
                        410       420
                 ....*....|....*....|....*.
gi 529367223 432 PATRLEMRRRARLSVSRFSDQEFEGS 457
Cdd:cd03806  394 EEERLQRREAARSSAERFSDEEFERD 419
PLN02949 PLN02949
transferase, transferring glycosyl groups
7-467 0e+00

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 557.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223   7 FSLCLCDLISWLQMKRKTRRvqdgrpAVAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEILDGAR 86
Cdd:PLN02949  15 VLLLVAIALSVLRARRSRKR------AVGFFHPYTNDGGGGERVLWCAVRAIQEENPDLDCVIYTGDHDASPDSLAARAR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223  87 RRFNIRLPRPVKFVFLKHRLLVEAKLYPHFTLLGQSVGSIFLGWEALTEFVPDLYIDSMGFAFTLPVFRyLGGCQVGSYV 166
Cdd:PLN02949  89 DRFGVELLSPPKVVHLRKRKWIEEETYPRFTMIGQSLGSVYLAWEALCKFTPLYFFDTSGYAFTYPLAR-LFGCKVVCYT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 167 HYPTISTDMLSVVRERNPRFNNADYISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILALWRTPNRTSV 246
Cdd:PLN02949 168 HYPTISSDMISRVRDRSSMYNNDASIARSFWLSTCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPERIKR 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 247 VYPPCDVQAFLDVPIgEDNEEKEQkkchsLVSVGQFRPEKDHQLQIRAFKKLLDRKEVEPagrEAVKLVLIGGCRNQEDE 326
Cdd:PLN02949 248 VYPPCDTSGLQALPL-ERSEDPPY-----IISVAQFRPEKAHALQLEAFALALEKLDADV---PRPKLQFVGSCRNKEDE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 327 DRVLMLRGLCQELGIADRVEFKLNIPFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKLDIVVPYD 406
Cdd:PLN02949 319 ERLQKLKDRAKELGLDGDVEFHKNVSYRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIVLDED 398
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529367223 407 GGPTGFLADDEDNYADAMERILSMSPATRLEMRRRARLSVSRFSDQEFEGSFLSAMEPLMS 467
Cdd:PLN02949 399 GQQTGFLATTVEEYADAILEVLRMRETERLEIAAAARKRANRFSEQRFNEDFKDAIRPILN 459
ALG11_N pfam15924
ALG11 mannosyltransferase N-terminus;
31-238 1.00e-143

ALG11 mannosyltransferase N-terminus;


Pssm-ID: 464944  Cd Length: 209  Bit Score: 409.56  E-value: 1.00e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223   31 RPAVAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEILDGARRRFNIRLPR-PVKFVFLKHRLLVE 109
Cdd:pfam15924   1 KGIVGFFHPYCNAGGGGERVLWCAVRATQRRYPNAICVVYTGDIDASKEEILAKVKSRFNIELDPsRIVFVYLRKRKLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223  110 AKLYPHFTLLGQSVGSIFLGWEALTEFVPDLYIDSMGFAFTLPVFRYLGGCQVGSYVHYPTISTDMLSVVRERNPRFNNA 189
Cdd:pfam15924  81 ASTYPRFTLLGQSLGSIILAWEALSKLVPDVFIDTMGYAFTYPLVRLLGGCPVGAYVHYPTISTDMLSRVSSREAGYNND 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 529367223  190 DYISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILALW 238
Cdd:pfam15924 161 SAIASSGLLSKAKLIYYRLFALLYGLVGSFADVVMVNSSWTQNHIRSLW 209
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
34-458 1.25e-36

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: 138.88  E-value: 1.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223  34 VAFFHPYCnaG-GGGERVLWCALRALQNRYQDVSFvvYTG--DQGVTAEEILDGarrRFNIR-----LPRpvkfvflkhr 105
Cdd:cd03805    3 VAFLHPDL--GiGGAERLVVDAALALQSRGHEVTI--YTShhDPSHCFEETKDG---TLPVRvrgdwLPR---------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 106 llveaKLYPHFTLLGQSVGSIFLGWEALTEFV--PDLYI-DSMgfAFTLPVFRYLGGCQVGSYVHYPtistDMLSVVREr 182
Cdd:cd03805   66 -----SIFGRFHALCAYLRMLYLALYLLLFSGekYDVFIvDQV--SACVPLLKLFRPSKILFYCHFP----DQLLAQRK- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 183 nprfnnadyissnpvlSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHIL----ALWRTPNRtsVVYPPCDVQAFLD 258
Cdd:cd03805  134 ----------------SLLKRLYRKPFDWLEEFTTGMADQIVVNSNFTAGVFKktfpSLAKNPPE--VLYPCVDTDSFDS 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 259 VPIGEDNEEKEQKKC-HSLVSVGQFRPEKDHQLQIRAFKKLLDRKEvepaGREAVKLVLIGGC--RNQEDEDRVLMLRGL 335
Cdd:cd03805  196 TSEDPDPGDLIAKSNkKFFLSINRFERKKNIALAIEAFAKLKQKLP----EFENVRLVIAGGYdpRVAENVEYLEELQRL 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 336 CQEL-GIADRVEFKLNIPfQELKKDLTDATIG-LHTMWNEHFGIGIVECMAAGTIILAHKSGGPKLDIVVpydgGPTGFL 413
Cdd:cd03805  272 AEELlNVEDQVLFLRSIS-DSQKEQLLSSALAlLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVE----GVTGFL 346
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 529367223 414 AD-DEDNYADAMERILSMsPATRLEMRRRARLSVS-RFSDQEFEGSF 458
Cdd:cd03805  347 CEpTPEAFAEAMLKLAND-PDLADRMGAAGRKRVKeKFSREAFAERL 392
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
276-443 2.13e-27

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: 107.36  E-value: 2.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223  276 LVSVGQFRPEKDHQLQIRAFKKLLDRKEVepagreaVKLVLIGgcrNQEDEDRvlmLRGLCQELGIADRVEFKLNIPFQE 355
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFALLKEKNPN-------LKLVIAG---DGEEEKR---LKKLAEKLGLGDNVIFLGFVSDED 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223  356 LKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVVPYDggpTGFLAD--DEDNYADAMERILSmSPA 433
Cdd:pfam00534  72 LPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPP-EVVKDGE---TGFLVKpnNAEALAEAIDKLLE-DEE 146
                         170
                  ....*....|
gi 529367223  434 TRLEMRRRAR 443
Cdd:pfam00534 147 LRERLGENAR 156
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
34-450 9.34e-24

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: 102.23  E-value: 9.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223  34 VAFFHPYCNAG-GGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEIldgarRRFNIRLPRPVKFVFLKHRLLVEAKL 112
Cdd:cd03801    2 ILLLSPELPPPvGGAERHVRELARALAARGHDVTVLTPADPGEPPEELE-----DGVIVPLLPSLAALLRARRLLRELRP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 113 YPHFtllgqsvgsiflgwealteFVPDL-YIDSMGFAFTLPVFRYLGGCQVGSYVHYPTistdmlsvvrernPRFNNADY 191
Cdd:cd03801   77 LLRL-------------------RKFDVvHAHGLLAALLAALLALLLGAPLVVTLHGAE-------------PGRLLLLL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 192 ISSNPVLSAIKVIYYCVfallyglagscsDVIMVNSTWTLGHILAL-WRTPNRTSVVYPPCDVQAFlDVPIGEDNEEKEQ 270
Cdd:cd03801  125 AAERRLLARAEALLRRA------------DAVIAVSEALRDELRALgGIPPEKIVVIPNGVDLERF-SPPLRRKLGIPPD 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 271 KKchSLVSVGQFRPEKDHQLQIRAFKKLLDRkevepagREAVKLVLIGgcRNQEDEDRVLMLrglcqELGIADRVEFKLN 350
Cdd:cd03801  192 RP--VLLFVGRLSPRKGVDLLLEALAKLLRR-------GPDVRLVIVG--GDGPLRAELEEL-----ELGLGDRVRFLGF 255
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 351 IPFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVVPydgGPTGFLA--DDEDNYADAMERIL 428
Cdd:cd03801  256 VPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLP-EVVED---GEGGLVVppDDVEALADALLRLL 331
                        410       420
                 ....*....|....*....|...
gi 529367223 429 SmSPATRLEMRRRARLSVS-RFS 450
Cdd:cd03801  332 A-DPELRARLGRAARERVAeRFS 353
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
34-455 1.60e-22

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: 98.58  E-value: 1.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223  34 VAFFHPyCNAGGGGERVLWCALRALQNRYQDVSFVVYTGdqgvtaEEILDGARRRFNIRLPRPVKFVFLKHRLLVEAKLY 113
Cdd:cd03811    2 ILFVIP-SLSGGGAERVLLNLANALDKRGYDVTLVLLRD------EGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 114 phftllgqsVGSIFLgwealtEFVPDLYIDSMGFAFTLPVFRYLGGCQVgsyvhyptistdmlsVVRERNPRFNNadYIS 193
Cdd:cd03811   75 ---------LKRILK------RAKPDVVISFLGFATYIVAKLAAARSKV---------------IAWIHSSLSKL--YYL 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 194 SNPVLSAIKVIYYCvfallyglagscsDVIMVNSTWTLGHILAL-WRTPNRTSVVYPPCDVQAFLDVPIGEDNEEKEQKK 272
Cdd:cd03811  123 KKKLLLKLKLYKKA-------------DKIVCVSKGIKEDLIRLgPSPPEKIEVIYNPIDIDRIRALAKEPILNEPEDGP 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 273 chSLVSVGQFRPEKDHQLQIRAFKKLLDRkevepagREAVKLVLIGgcrNQEDEDRvlmLRGLCQELGIADRVEF---KL 349
Cdd:cd03811  190 --VILAVGRLDPQKGHDLLIEAFAKLRKK-------YPDVKLVILG---DGPLREE---LEKLAKELGLAERVIFlgfQS 254
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 350 NiPFQELKKdltdATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVvpyDGGPTGFLADDEDNYADAMERILS 429
Cdd:cd03811  255 N-PYPYLKK----ADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPR-EIL---DDGENGLLVPDGDAAALAGILAAL 325
                        410       420
                 ....*....|....*....|....*.
gi 529367223 430 MSPATRLEMRRRARLSVSRFSDQEFE 455
Cdd:cd03811  326 LQKKLDAALRERLAKAQEAVFREYTI 351
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
215-449 2.20e-19

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: 89.61  E-value: 2.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 215 LAGSCSDVIMVNSTWTLGHILALWRT-PNRTSVVYPPCDVQAFldVPIGEDNEE-----KEQKKcHSLVSVGQFRPEKDH 288
Cdd:cd03800  159 QILEAADRVIASTPQEADELISLYGAdPSRINVVPPGVDLERF--FPVDRAEARrarllLPPDK-PVVLALGRLDPRKGI 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 289 QLQIRAFKKLLDRkevepagREAVKLVLIGGCRNQEDEDRVLMLRGLCQELGIADRVEFKLNIPFQELKKDLTDATIGLH 368
Cdd:cd03800  236 DTLVRAFAQLPEL-------RELANLVLVGGPSDDPLSMDREELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVV 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 369 TMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVVPydgGPTGFLAD--DEDNYADAMERILsMSPATRLEMRRRARLSV 446
Cdd:cd03800  309 PSLYEPFGLTAIEAMACGTPVVATAVGGLQ-DIVRD---GRTGLLVDphDPEALAAALRRLL-DDPALWQRLSRAGLERA 383

                 ...
gi 529367223 447 SRF 449
Cdd:cd03800  384 RAH 386
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
277-454 4.72e-18

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: 85.51  E-value: 4.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 277 VSVGQFRPEKDHQLQIRAFKKLLDRkevepagREAVKLVLIGgcrNQEDEDRvlmLRGLCQELGIADRVEFKLNIPFQEL 356
Cdd:cd03798  204 LFVGRLIPRKGIDLLLEAFARLAKA-------RPDVVLLIVG---DGPLREA---LRALAEDLGLGDRVTFTGRLPHEQV 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 357 KKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVvpyDGGPTGFLAD--DEDNYADAMERILsMSPAT 434
Cdd:cd03798  271 PAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIP-EVV---GDPETGLLVPpgDADALAAALRRAL-AEPYL 345
                        170       180
                 ....*....|....*....|
gi 529367223 435 RLEMRRRARLSVSRFSDQEF 454
Cdd:cd03798  346 RELGEAARARVAERFSWVKA 365
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
219-450 1.94e-16

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: 80.49  E-value: 1.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 219 CSDVIMVNSTWTLGHILALWRTP-NRTSVVYPPCDVQAFLDVPIGEDNEEKEQKkCHSLVSVGQFRPEKDHQLQIRAFKK 297
Cdd:cd03809  138 RADAIITVSEATRDDIIKFYGVPpEKIVVIPLGVDPSFFPPESAAVLIAKYLLP-EPYFLYVGTLEPRKNHERLLKAFAL 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 298 LLDRKEVepagreaVKLVLIGGcrnqeDEDRVLMLRGLCQELGIADRVEFKLNIPFQELKKDLTDATI----GLHtmwnE 373
Cdd:cd03809  217 LKKQGGD-------LKLVIVGG-----KGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAfvfpSLY----E 280
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529367223 374 HFGIGIVECMAAGTIILAhkSGGPKLDIVVpydgGPTGFLAD--DEDNYADAMERILSmSPATRLEMRRRARLSVSRFS 450
Cdd:cd03809  281 GFGLPVLEAMACGTPVIA--SNISVLPEVA----GDAALYFDplDPESIADAILRLLE-DPSLREELIRKGLERAKKFS 352
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
246-450 1.84e-14

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: 74.62  E-value: 1.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 246 VVYPPCDVQAFLDVPIGEDNEE---KEQKKchSLVSVGQFRPEKDHQLQIRAFKKLLDRKEvepagreaVKLVLIG-GCR 321
Cdd:cd03817  173 VIPNGIDLDKFEKPLNTEERRKlglPPDEP--ILLYVGRLAKEKNIDFLLRAFAELKKEPN--------IKLVIVGdGPE 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 322 NQEdedrvlmLRGLCQELGIADRVEFKLNIPFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDI 401
Cdd:cd03817  243 REE-------LKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAAS-EL 314
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 529367223 402 VvpyDGGPTGFL-ADDEDNYADAMERILSMsPATRLEMRRRARLSVSRFS 450
Cdd:cd03817  315 V---EDGENGFLfEPNDETLAEKLLHLREN-LELLRKLSKNAEISAREFA 360
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
276-450 1.26e-13

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: 71.96  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 276 LVSVGQFRPEKDHQLQIRAFKKLLDRkevepagREAVKLVLIG-GCRNQEDEdrvLMLRglcqELGIADRVEFKLNIpfQ 354
Cdd:cd03807  193 IGIVGRLHPVKDHSDLLRAAALLVET-------HPDLRLLLVGrGPERPNLE---RLLL----ELGLEDRVHLLGER--S 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 355 ELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGpKLDIVVPydggPTGFL--ADDEDNYADAMERILSMsP 432
Cdd:cd03807  257 DVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGG-AAELVDD----GTGFLvpAGDPQALADAIRALLED-P 330
                        170
                 ....*....|....*....
gi 529367223 433 ATRLEMRRRARLSV-SRFS 450
Cdd:cd03807  331 EKRARLGRAARERIaNEFS 349
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
221-408 6.57e-13

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: 68.20  E-value: 6.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 221 DVIMVNSTW--TLGHILALWRTPNRTSVVYPPCDVQAFLDVPIGEDNEEKEQKKCHSLVSVGQFRPEKDHQLQIRAFKKL 298
Cdd:cd01635   56 DVVHAHSPHaaALAALLAARLLGIPIVVTVHGPDSLESTRSELLALARLLVSLPLADKVSVGRLVPEKGIDLLLEALALL 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 299 ldrkevePAGREAVKLVLIGGCRNQEDEDRVLmlrglcQELGIADRVEFKLNIPFQELKKDLT-DATIGLHTMWNEHFGI 377
Cdd:cd01635  136 -------KARLPDLVLVLVGGGGEREEEEALA------AALGLLERVVIIGGLVDDEVLELLLaAADVFVLPSRSEGFGL 202
                        170       180       190
                 ....*....|....*....|....*....|.
gi 529367223 378 GIVECMAAGTIILAHKSGGPKLDIVVPYDGG 408
Cdd:cd01635  203 VLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
236-452 2.95e-12

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 67.70  E-value: 2.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 236 ALWRTPNRTSVVYPPCDVQAFLDVPIGEDNeekeqkkchsLVSVGQFRPEKDHQLQIRAFKKlldrkevepAGReavKLV 315
Cdd:cd03802  142 AATPPIDYLTVVHNGLDPADYRFQPDPEDY----------LAFLGRIAPEKGLEDAIRVARR---------AGL---PLK 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 316 LIGGCRNQEDEDRVlmlrglcQELGIADRVEFKLNIPFQELKKDLTDATIGLHT-MWNEHFGIGIVECMAAGTIILAHKS 394
Cdd:cd03802  200 IAGKVRDEDYFYYL-------QEPLPGPRIEFIGEVGHDEKQELLGGARALLFPiNWDEPFGLVMIEAMACGTPVIAYRR 272
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 395 GGPkLDIVVPydgGPTGFLADDEDNYADAMERILSMSPATrleMRRRA--RLSVSRFSDQ 452
Cdd:cd03802  273 GGL-PEVIQH---GETGFLVDSVEEMAEAIANIDRIDRAA---CRRYAedRFSAARMADR 325
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
34-450 1.32e-11

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: 65.72  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223  34 VAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEildgarrrfnirLPRPVKFVFLKHRLLVEAKLY 113
Cdd:cd03820    2 IAIVIPSISNAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYE------------LDDNIKIKNLGDRKYSHFKLL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 114 PHFtllgQSVGSIFLgwEALTEFVPDLYIDSMGFAFTLPvfrylggcqvgsyvhyPTISTDMLSVVRERNPRFNNADYIS 193
Cdd:cd03820   70 LKY----FKKVRRLR--KYLKNNKPDVVISFRTSLLTFL----------------ALIGLKSKLIVWEHNNYEAYNKGLR 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 194 SnpvlsaikviyYCVFALLYGLAgscsDVIMVNSTWTLghILALWRTPNRTSVVYPPCDvqaFLDVPIGEDNEEKeqkkc 273
Cdd:cd03820  128 R-----------LLLRRLLYKRA----DKIVVLTEADK--LKKYKQPNSNVVVIPNPLS---FPSEEPSTNLKSK----- 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 274 hSLVSVGQFRPEKDHQLQIRAFKKLLDRkevepagREAVKLVLIGGCrnqEDEDRvlmLRGLCQELGIADRVEFKLNIpf 353
Cdd:cd03820  183 -RILAVGRLTYQKGFDLLIEAWALIAKK-------HPDWKLRIYGDG---PEREE---LEKLIDKLGLEDRVKLLGPT-- 246
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 354 QELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKS-GGPKlDIVvpyDGGPTGFLADDED--NYADAMERILSm 430
Cdd:cd03820  247 KNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCpTGPS-EII---EDGENGLLVPNGDvdALAEALLRLME- 321
                        410       420
                 ....*....|....*....|
gi 529367223 431 SPATRLEMRRRARLSVSRFS 450
Cdd:cd03820  322 DEELRKKMGKNARKNAERFS 341
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
221-458 1.33e-11

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: 65.77  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 221 DVIMVNSTWTLGHIlalWRTPNRTS-VVYPPCDVQAFLDVPIGEDneekeqkkchSLVSVGQFRPEKDHQLQIRAFKKLl 299
Cdd:cd03804  159 DLFIANSQFVARRI---KKFYGREStVIYPPVDTDAFAPAADKED----------YYLTASRLVPYKRIDLAVEAFNEL- 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 300 drkevepaGReavKLVLIGgcrNQEDEDRvlmLRGlcqelgIADR-VEFKLNIPFQELKKDLTDATiGLHTMWNEHFGIG 378
Cdd:cd03804  225 --------PK---RLVVIG---DGPDLDR---LRA------MASPnVEFLGYQPDEVLKELLSKAR-AFVFAAEEDFGIV 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 379 IVECMAAGTIILAHKSGGpKLDIVVPydgGPTGFLADDEDNYA--DAMERILSMSPATRLEmrrRARLSVSRFSDQEFEG 456
Cdd:cd03804  281 PVEAQACGTPVIAFGKGG-ALETVRP---GPTGILFGEQTVESlkAAVEEFEQNFDRFKPQ---AIRANAERFSRARFRQ 353

                 ..
gi 529367223 457 SF 458
Cdd:cd03804  354 EI 355
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
360-467 5.88e-11

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 59.62  E-value: 5.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 360 LTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVVPydgGPTGFLAD--DEDNYADAMERILSmSPATRLE 437
Cdd:COG0438   18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLP-EVIED---GETGLLVPpgDPEALAEAILRLLE-DPELRRR 92
                         90       100       110
                 ....*....|....*....|....*....|.
gi 529367223 438 MRRRAR-LSVSRFSDQEFEGSFLSAMEPLMS 467
Cdd:COG0438   93 LGEAAReRAEERFSWEAIAERLLALYEELLA 123
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
276-429 1.41e-10

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 59.06  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223  276 LVSVGQFRPE-KDHQLQIRAFKKLLDRkevepagREAVKLVLIGGCRNQEDEDRVLmlrglcqelGIADRVEFklnIPF- 353
Cdd:pfam13692   4 ILFVGRLHPNvKGVDYLLEAVPLLRKR-------DNDVRLVIVGDGPEEELEELAA---------GLEDRVIF---TGFv 64
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529367223  354 QELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVVpydgGPTGFLA--DDEDNYADAMERILS 429
Cdd:pfam13692  65 EDLAELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIP-ELVD----GENGLLVppGDPEALAEAILRLLE 137
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
208-453 3.18e-10

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 61.46  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 208 VFALLYGLAGSCSDVIMVNSTWTLGHILALWRTPNRTSVVYPPCDVQAFLDVPIGEDNEEKEqkkcHSLVSVGQFRPEKD 287
Cdd:cd03808  128 LYLLLEKLALLFTDKVIFVNEDDRDLAIKKGIIKKKKTVLIPGSGVDLDRFQYSPESLPSEK----VVFLFVARLLKDKG 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 288 HQLQIRAFKKLLDRKevepagrEAVKLVLIGGCRnqEDEDRVLMLrglcQELGIADRVEF---KLNIPfqelkKDLTDAT 364
Cdd:cd03808  204 IDELIEAAKILKKKG-------PNVRFLLVGDGE--LENPSEILI----EKLGLEGRIEFlgfRSDVP-----ELLAESD 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 365 IGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVVPydgGPTGFLAD--DEDNYADAMERILSmSPATRLEMRRRA 442
Cdd:cd03808  266 VFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCR-ELVID---GVNGFLVPpgDVEALADAIEKLIE-DPELRKEMGEAA 340
                        250
                 ....*....|..
gi 529367223 443 RLSV-SRFSDQE 453
Cdd:cd03808  341 RKRVeEKFDEEK 352
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
263-450 1.32e-09

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: 59.67  E-value: 1.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 263 EDNEEKEQKKCHS----LVSVGQFRPEKDHQLQIRAFKKLldRKEVePAgreavKLVLIGgcrnqEDEDRVLMLRgLCQE 338
Cdd:cd04962  182 PAGALKRRLLAPPdekvVIHVSNFRPVKRIDDVVRVFARV--RRKI-PA-----KLLLVG-----DGPERVPAEE-LARE 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 339 LGIADRVEFKLNIPfqELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGpkLDIVVpyDGGPTGFLAD--D 416
Cdd:cd04962  248 LGVEDRVLFLGKQD--DVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGG--IPEVV--KHGETGFLSDvgD 321
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 529367223 417 EDNYADAMERILSmSPATRLEMRRRARL-SVSRFS 450
Cdd:cd04962  322 VDAMAKSALSILE-DDELYNRMGRAARKrAAERFD 355
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
276-463 7.13e-09

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: 57.30  E-value: 7.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 276 LVSVGQFRPEKDhqlqIRAFKKLLDRkevePAGREAVKLVLIGGCRNQEdedrVLMLRGLCQE-LGIADRvefklnipfQ 354
Cdd:cd03814  201 LLYVGRLAPEKN----LEALLDADLP----LAASPPVRLVVVGDGPARA----ELEARGPDVIfTGFLTG---------E 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 355 ELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVvpyDGGPTGFLAD--DEDNYADAMERiLSMSP 432
Cdd:cd03814  260 ELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPR-DIV---RPGGTGALVEpgDAAAFAAALRA-LLEDP 334
                        170       180       190
                 ....*....|....*....|....*....|.
gi 529367223 433 ATRLEMRRRARLSVSRFSDQEFEGSFLSAME 463
Cdd:cd03814  335 ELRRRMAARARAEAERYSWEAFLDNLLDYYA 365
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
279-444 3.53e-08

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: 55.05  E-value: 3.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 279 VGQFRPEKDHQLQIRAFKKLLDRKEVepagreavkLVLIGGCRNQEDEDRVLMlrglcQELGIADRVEFKLNIPfqELKK 358
Cdd:cd03819  188 VGRLSPEKGWLLLVDAAAELKDEPDF---------RLLVAGDGPERDEIRRLV-----ERLGLRDRVTFTGFRE--DVPA 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 359 DLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPkLDIVVPydgGPTGFLADDEDN--YADAMERiLSMSPATRL 436
Cdd:cd03819  252 ALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGA-REIVVH---GRTGLLVPPGDAeaLADAIRA-AKLLPEARE 326

                 ....*...
gi 529367223 437 EMRRRARL 444
Cdd:cd03819  327 KLQAAAAL 334
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
241-450 1.28e-07

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 53.50  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 241 PNRTSVVYPPCDVQAFLDVPIGEDNEEKEQKKCHSLVSVGQFRPEKDHQLQIRAFKKLLDRKEVepagreavKLVLIGGC 320
Cdd:cd03794  185 KEKIIVIPNWADLEEFKPPPKDELRKKLGLDDKFVVVYAGNIGKAQGLETLLEAAERLKRRPDI--------RFLFVGDG 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 321 RNQEDEDRVLMLRGLcqelgiaDRVEFKLNIPFQELKKDLTDATIGLHTMWNEHFGIGIV-----ECMAAGTIILAHKSG 395
Cdd:cd03794  257 DEKERLKELAKARGL-------DNVTFLGRVPKEEVPELLSAADVGLVPLKDNPANRGSSpsklfEYMAAGKPILASDDG 329
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 529367223 396 GPKLDIVVpydgGPTGFLADDEDN--YADAMERiLSMSPATRLEMRRRAR-LSVSRFS 450
Cdd:cd03794  330 GSDLAVEI----NGCGLVVEPGDPeaLADAILE-LLDDPELRRAMGENGReLAEEKFS 382
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
190-453 3.83e-07

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


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 52.34  E-value: 3.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 190 DYISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILALWRTPNRTSVVYPPCDVQAFLDVPigednEEKE 269
Cdd:cd03813  215 EILQSTWIMGYIKKLWIRFFERLGKLAYQQADKIISLYEGNRRRQIRLGADPDKTRVIPNGIDIQRFAPAR-----EERP 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 270 QKKCHSLVSVGQFRPEKDHQLQIRAFKKLLDRkevepagREAVKLVLIGGcrNQEDEDRVLMLRGLCQELGIADRVEFkl 349
Cdd:cd03813  290 EKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRA-------MPDAEGWLIGP--EDEDPEYAQECKRLVASLGLENKVKF-- 358
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 350 nIPFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVvpYDG----GPTGFL---ADDEDnYAD 422
Cdd:cd03813  359 -LGFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCR-ELI--YGAddalGQAGLVvppADPEA-LAE 433
                        250       260       270
                 ....*....|....*....|....*....|.
gi 529367223 423 AMERILSmSPATRLEMRRRARLSVSRFSDQE 453
Cdd:cd03813  434 ALIKLLR-DPELRQAFGEAGRKRVEKYYTLE 463
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
248-448 1.77e-06

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 50.01  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 248 YPPCDVQAFLDVPIGEDNEEKeqkkchSLVSVGQFRPEKDHQLQIRAFKKLLDRKEVepagreaVKLVLIGGcRNQEDED 327
Cdd:cd03792  178 LSPADIRYYLEKPFVIDPERP------YILQVARFDPSKDPLGVIDAYKLFKRRAEE-------PQLVICGH-GAVDDPE 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 328 RVLMLRGLCQELGIADRVEF-KLNIPFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKLDIVvpyd 406
Cdd:cd03792  244 GSVVYEEVMEYAGDDHDIHVlRLPPSDQEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVI---- 319
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 529367223 407 GGPTGFLADDEDNYADAMERILSmSPATRLEMRRRARLSVSR 448
Cdd:cd03792  320 DGETGFLVNSVEGAAVRILRLLT-DPELRRKMGLAAREHVRD 360
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
268-451 5.52e-06

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: 48.07  E-value: 5.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 268 KEQKKcHSLVSVGQFRPEKDHQLQIRAFKKLldRKEVePagreAVKLVLIGgcRNQEDEDrvlmLRGLCQELGIADRVEF 347
Cdd:cd04949  156 HERKS-NKIITISRLAPEKQLDHLIEAVAKA--VKKV-P----EITLDIYG--YGEEREK----LKKLIEELHLEDNVFL 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 348 K--LNIPFQELKkdltDATIGLHTMWNEHFGIGIVECMAAGTIILAHKsggpkldivVPYdgGPTGFLADDE-------- 417
Cdd:cd04949  222 KgyHSNLDQEYQ----DAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYD---------VKY--GPSELIEDGEngyliekn 286
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 529367223 418 --DNYADAMERILSmSPATRLEMRRRARLSVSRFSD 451
Cdd:cd04949  287 niDALADKIIELLN-DPEKLQQFSEESYKIAEKYST 321
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
279-452 8.91e-06

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: 47.71  E-value: 8.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 279 VGQFRPEKDHQLQIRAFKKLlDRKEVEpagreavkLVLIGGCRNQEdedrvlmlrglCQELGIADRVEFKLNIPFQELKK 358
Cdd:cd03823  197 IGRLTEEKGIDLLVEAFKRL-PREDIE--------LVIAGHGPLSD-----------ERQIEGGRRIAFLGRVPTDDIKD 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 359 --DLTDATIgLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKLDIVvpydGGPTGFL--ADDEDNYADAMERI-----LS 429
Cdd:cd03823  257 fyEKIDVLV-VPSIWPEPFGLVVREAIAAGLPVIASDLGGIAELIQ----PGVNGLLfaPGDAEDLAAAMRRLltdpaLL 331
                        170       180
                 ....*....|....*....|...
gi 529367223 430 MSPATRLEMRRRARLSVSRFSDQ 452
Cdd:cd03823  332 ERLRAGAEPPRSTESQAEEYLKL 354
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
373-450 1.81e-05

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 47.01  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 373 EHFGIGIVECMAAGTIILAHKSGGPKlDIVVPYDGGPTGFLADDEDnYADAMERI--LSMSPATRLEMRRRARLSVSRFS 450
Cdd:PLN02871 342 ETLGFVVLEAMASGVPVVAARAGGIP-DIIPPDQEGKTGFLYTPGD-VDDCVEKLetLLADPELRERMGAAAREEVEKWD 419
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
256-450 4.67e-05

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: 45.51  E-value: 4.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 256 FLDVPIGEDNEEKEQKKCHSL---------VSVGQFRPEKDHQLQIRAFKKLLDRKEvepagreAVKLVLIGgcrnqEDE 326
Cdd:cd04951  162 GIDLNKFKKDINVRLKIRNKLnlkndefviLNVGRLTEAKDYPNLLLAISELILSKN-------DFKLLIAG-----DGP 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 327 DRVLMLRGLCQeLGIADRVEFklnIPFQELKKDLTDAT--IGLHTMWnEHFGIGIVECMAAGTIILAHKSGGPKlDIVVP 404
Cdd:cd04951  230 LRNELERLICN-LNLVDRVIL---LGQISNISEYYNAAdlFVLSSEW-EGFGLVVAEAMACERPVVATDAGGVA-EVVGD 303
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 529367223 405 YDggptgFLADDEDNY--ADAMERILSMSPATRLEMRRRARLSVSRFS 450
Cdd:cd04951  304 HN-----YVVPVSDPQllAEKIKEIFDMSDEERDILGNKNEYIAKNFS 346
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
276-450 6.43e-05

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 45.05  E-value: 6.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 276 LVSVGQFRPEKDHQLQIRAFKKLLDrkevepAGREaVKLVLIGgcrnqEDEDRVLMLRGLCQELGIADRVEFKLNIPFQE 355
Cdd:cd03821  207 ILFLGRIHPKKGLDLLIRAARKLAE------QGRD-WHLVIAG-----PDDGAYPAFLQLQSSLGLGDRVTFTGPLYGEA 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 356 LKKDLTDATIGLHTMWNEHFGIGIVECMAAGT-IILAHKSGGPKLdivvpYDGGpTGFLADDEDNY-ADAMERILS--MS 431
Cdd:cd03821  275 KWALYASADLFVLPSYSENFGNVVAEALACGLpVVITDKCGLSEL-----VEAG-CGVVVDPNVSSlAEALAEALRdpAD 348
                        170
                 ....*....|....*....
gi 529367223 432 PATRLEMRRRARLSVSRFS 450
Cdd:cd03821  349 RKRLGEMARRARQVEENFS 367
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
346-452 2.60e-04

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 43.09  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367223 346 EFKLNIPFQELKKDLTDATIGLHTMWN-----------EHFGIGIVECMAAGTIILAHKSGGPkLDIVvpyDGGPTGFLA 414
Cdd:cd03825  236 PQIVILPFDIISLGYIDDDEQLVDIYSaadlfvhpslaDNLPNTLLEAMACGTPVVAFDTGGS-PEIV---QHGVTGYLV 311
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 529367223 415 DDED--NYADAMERILsMSPATRLEMRRRAR-LSVSRFSDQ 452
Cdd:cd03825  312 PPGDvqALAEAIEWLL-ANPKERESLGERARaLAENHFDQR 351
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
373-442 6.69e-03

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 38.70  E-value: 6.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529367223 373 EHFGIGIVECMAAGTIILAHKSGGPKlDIVVPYD---GGPTGFLADDEDNYA--DAMERILSM--SPATRLEMRRRA 442
Cdd:cd03791  379 EPCGLVQMYAMRYGTLPIVRRTGGLA-DTVFDYDpetGEGTGFVFEDYDAEAllAALRRALALyrNPELWRKLQKNA 454
 
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.
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