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Conserved domains on  [gi|238624126|ref|NP_001154823|]
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GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase isoform 1 [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 ...
62-486 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: 733.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126  62 AVAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEILDGARRRFNIRLPRPVKFVF-LKHRLLVEAK 140
Cdd:cd03806    2 TVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFFlLKYRKLVEAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 141 LYPHFTLLGQSVGSIFLGWEALTEFVPDLYIDSMGFAFTLPVFRYLGGCQVGSYVHYPTISTDMLSVVRERNPRFNNADY 220
Cdd:cd03806   82 TYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGGCPVVAYVHYPTISTDMLNKVRSREASYNNDST 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 221 ISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILALWRTPNRTSVVYPPCDVQAFLDVPIgedneeKEQK 300
Cdd:cd03806  162 IARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPI------DEKT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 301 KCHSLVSVGQFRPEKDHQLQIRAFKKLLDRKEVEPagREAVKLVLIGGCRNQEDEDRVLMLRGLCQELGIADRVEFKLNI 380
Cdd:cd03806  236 RENQILSIAQFRPEKNHPLQLRAFAELLKRLPESI--RSNPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEFVVDA 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 381 PFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKLDIVVPYDGGPTGFLADDEDNYADAMERILSMS 460
Cdd:cd03806  314 PYEELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILTLS 393
                        410       420
                 ....*....|....*....|....*.
gi 238624126 461 PATRLEMRRRARLSVSRFSDQEFEGS 486
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 ...
62-486 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: 733.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126  62 AVAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEILDGARRRFNIRLPRPVKFVF-LKHRLLVEAK 140
Cdd:cd03806    2 TVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFFlLKYRKLVEAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 141 LYPHFTLLGQSVGSIFLGWEALTEFVPDLYIDSMGFAFTLPVFRYLGGCQVGSYVHYPTISTDMLSVVRERNPRFNNADY 220
Cdd:cd03806   82 TYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGGCPVVAYVHYPTISTDMLNKVRSREASYNNDST 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 221 ISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILALWRTPNRTSVVYPPCDVQAFLDVPIgedneeKEQK 300
Cdd:cd03806  162 IARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPI------DEKT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 301 KCHSLVSVGQFRPEKDHQLQIRAFKKLLDRKEVEPagREAVKLVLIGGCRNQEDEDRVLMLRGLCQELGIADRVEFKLNI 380
Cdd:cd03806  236 RENQILSIAQFRPEKNHPLQLRAFAELLKRLPESI--RSNPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEFVVDA 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 381 PFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKLDIVVPYDGGPTGFLADDEDNYADAMERILSMS 460
Cdd:cd03806  314 PYEELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILTLS 393
                        410       420
                 ....*....|....*....|....*.
gi 238624126 461 PATRLEMRRRARLSVSRFSDQEFEGS 486
Cdd:cd03806  394 EEERLQRREAARSSAERFSDEEFERD 419
PLN02949 PLN02949
transferase, transferring glycosyl groups
26-496 0e+00

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 561.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126  26 FYLSFLLTTILFLFIMGVRSWLQMKRKTRRvqdgrpAVAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGV 105
Cdd:PLN02949   5 LILYHLLTSIVLLLVAIALSVLRARRSRKR------AVGFFHPYTNDGGGGERVLWCAVRAIQEENPDLDCVIYTGDHDA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 106 TAEEILDGARRRFNIRLPRPVKFVFLKHRLLVEAKLYPHFTLLGQSVGSIFLGWEALTEFVPDLYIDSMGFAFTLPVFRy 185
Cdd:PLN02949  79 SPDSLAARARDRFGVELLSPPKVVHLRKRKWIEEETYPRFTMIGQSLGSVYLAWEALCKFTPLYFFDTSGYAFTYPLAR- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 186 LGGCQVGSYVHYPTISTDMLSVVRERNPRFNNADYISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILA 265
Cdd:PLN02949 158 LFGCKVVCYTHYPTISSDMISRVRDRSSMYNNDASIARSFWLSTCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 266 LWRTPNRTSVVYPPCDVQAFLDVPIgEDNEEKEQkkchsLVSVGQFRPEKDHQLQIRAFKKLLDRKEVEPagrEAVKLVL 345
Cdd:PLN02949 238 LWRIPERIKRVYPPCDTSGLQALPL-ERSEDPPY-----IISVAQFRPEKAHALQLEAFALALEKLDADV---PRPKLQF 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 346 IGGCRNQEDEDRVLMLRGLCQELGIADRVEFKLNIPFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGG 425
Cdd:PLN02949 309 VGSCRNKEDEERLQKLKDRAKELGLDGDVEFHKNVSYRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAG 388
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238624126 426 PKLDIVVPYDGGPTGFLADDEDNYADAMERILSMSPATRLEMRRRARLSVSRFSDQEFEGSFLSAMEPLMS 496
Cdd:PLN02949 389 PKMDIVLDEDGQQTGFLATTVEEYADAILEVLRMRETERLEIAAAARKRANRFSEQRFNEDFKDAIRPILN 459
ALG11_N pfam15924
ALG11 mannosyltransferase N-terminus;
60-267 3.01e-142

ALG11 mannosyltransferase N-terminus;


Pssm-ID: 464944  Cd Length: 209  Bit Score: 406.86  E-value: 3.01e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126   60 RPAVAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEILDGARRRFNIRLPR-PVKFVFLKHRLLVE 138
Cdd:pfam15924   1 KGIVGFFHPYCNAGGGGERVLWCAVRATQRRYPNAICVVYTGDIDASKEEILAKVKSRFNIELDPsRIVFVYLRKRKLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126  139 AKLYPHFTLLGQSVGSIFLGWEALTEFVPDLYIDSMGFAFTLPVFRYLGGCQVGSYVHYPTISTDMLSVVRERNPRFNNA 218
Cdd:pfam15924  81 ASTYPRFTLLGQSLGSIILAWEALSKLVPDVFIDTMGYAFTYPLVRLLGGCPVGAYVHYPTISTDMLSRVSSREAGYNND 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 238624126  219 DYISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILALW 267
Cdd:pfam15924 161 SAIASSGLLSKAKLIYYRLFALLYGLVGSFADVVMVNSSWTQNHIRSLW 209
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
389-496 7.15e-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: 7.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 389 LTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVVPydgGPTGFLAD--DEDNYADAMERILSmSPATRLE 466
Cdd:COG0438   18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLP-EVIED---GETGLLVPpgDPEALAEAILRLLE-DPELRRR 92
                         90       100       110
                 ....*....|....*....|....*....|.
gi 238624126 467 MRRRAR-LSVSRFSDQEFEGSFLSAMEPLMS 496
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 ...
62-486 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: 733.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126  62 AVAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEILDGARRRFNIRLPRPVKFVF-LKHRLLVEAK 140
Cdd:cd03806    2 TVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFFlLKYRKLVEAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 141 LYPHFTLLGQSVGSIFLGWEALTEFVPDLYIDSMGFAFTLPVFRYLGGCQVGSYVHYPTISTDMLSVVRERNPRFNNADY 220
Cdd:cd03806   82 TYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGGCPVVAYVHYPTISTDMLNKVRSREASYNNDST 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 221 ISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILALWRTPNRTSVVYPPCDVQAFLDVPIgedneeKEQK 300
Cdd:cd03806  162 IARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPI------DEKT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 301 KCHSLVSVGQFRPEKDHQLQIRAFKKLLDRKEVEPagREAVKLVLIGGCRNQEDEDRVLMLRGLCQELGIADRVEFKLNI 380
Cdd:cd03806  236 RENQILSIAQFRPEKNHPLQLRAFAELLKRLPESI--RSNPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEFVVDA 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 381 PFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKLDIVVPYDGGPTGFLADDEDNYADAMERILSMS 460
Cdd:cd03806  314 PYEELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILTLS 393
                        410       420
                 ....*....|....*....|....*.
gi 238624126 461 PATRLEMRRRARLSVSRFSDQEFEGS 486
Cdd:cd03806  394 EEERLQRREAARSSAERFSDEEFERD 419
PLN02949 PLN02949
transferase, transferring glycosyl groups
26-496 0e+00

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 561.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126  26 FYLSFLLTTILFLFIMGVRSWLQMKRKTRRvqdgrpAVAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGV 105
Cdd:PLN02949   5 LILYHLLTSIVLLLVAIALSVLRARRSRKR------AVGFFHPYTNDGGGGERVLWCAVRAIQEENPDLDCVIYTGDHDA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 106 TAEEILDGARRRFNIRLPRPVKFVFLKHRLLVEAKLYPHFTLLGQSVGSIFLGWEALTEFVPDLYIDSMGFAFTLPVFRy 185
Cdd:PLN02949  79 SPDSLAARARDRFGVELLSPPKVVHLRKRKWIEEETYPRFTMIGQSLGSVYLAWEALCKFTPLYFFDTSGYAFTYPLAR- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 186 LGGCQVGSYVHYPTISTDMLSVVRERNPRFNNADYISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILA 265
Cdd:PLN02949 158 LFGCKVVCYTHYPTISSDMISRVRDRSSMYNNDASIARSFWLSTCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 266 LWRTPNRTSVVYPPCDVQAFLDVPIgEDNEEKEQkkchsLVSVGQFRPEKDHQLQIRAFKKLLDRKEVEPagrEAVKLVL 345
Cdd:PLN02949 238 LWRIPERIKRVYPPCDTSGLQALPL-ERSEDPPY-----IISVAQFRPEKAHALQLEAFALALEKLDADV---PRPKLQF 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 346 IGGCRNQEDEDRVLMLRGLCQELGIADRVEFKLNIPFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGG 425
Cdd:PLN02949 309 VGSCRNKEDEERLQKLKDRAKELGLDGDVEFHKNVSYRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAG 388
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238624126 426 PKLDIVVPYDGGPTGFLADDEDNYADAMERILSMSPATRLEMRRRARLSVSRFSDQEFEGSFLSAMEPLMS 496
Cdd:PLN02949 389 PKMDIVLDEDGQQTGFLATTVEEYADAILEVLRMRETERLEIAAAARKRANRFSEQRFNEDFKDAIRPILN 459
ALG11_N pfam15924
ALG11 mannosyltransferase N-terminus;
60-267 3.01e-142

ALG11 mannosyltransferase N-terminus;


Pssm-ID: 464944  Cd Length: 209  Bit Score: 406.86  E-value: 3.01e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126   60 RPAVAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEILDGARRRFNIRLPR-PVKFVFLKHRLLVE 138
Cdd:pfam15924   1 KGIVGFFHPYCNAGGGGERVLWCAVRATQRRYPNAICVVYTGDIDASKEEILAKVKSRFNIELDPsRIVFVYLRKRKLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126  139 AKLYPHFTLLGQSVGSIFLGWEALTEFVPDLYIDSMGFAFTLPVFRYLGGCQVGSYVHYPTISTDMLSVVRERNPRFNNA 218
Cdd:pfam15924  81 ASTYPRFTLLGQSLGSIILAWEALSKLVPDVFIDTMGYAFTYPLVRLLGGCPVGAYVHYPTISTDMLSRVSSREAGYNND 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 238624126  219 DYISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILALW 267
Cdd:pfam15924 161 SAIASSGLLSKAKLIYYRLFALLYGLVGSFADVVMVNSSWTQNHIRSLW 209
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
63-487 4.53e-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: 138.11  E-value: 4.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126  63 VAFFHPYCnaG-GGGERVLWCALRALQNRYQDVSFvvYTG--DQGVTAEEILDGarrRFNIR-----LPRpvkfvflkhr 134
Cdd:cd03805    3 VAFLHPDL--GiGGAERLVVDAALALQSRGHEVTI--YTShhDPSHCFEETKDG---TLPVRvrgdwLPR---------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 135 llveaKLYPHFTLLGQSVGSIFLGWEALTEFV--PDLYI-DSMgfAFTLPVFRYLGGCQVGSYVHYPtistDMLSVVREr 211
Cdd:cd03805   66 -----SIFGRFHALCAYLRMLYLALYLLLFSGekYDVFIvDQV--SACVPLLKLFRPSKILFYCHFP----DQLLAQRK- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 212 nprfnnadyissnpvlSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHIL----ALWRTPNRtsVVYPPCDVQAFLD 287
Cdd:cd03805  134 ----------------SLLKRLYRKPFDWLEEFTTGMADQIVVNSNFTAGVFKktfpSLAKNPPE--VLYPCVDTDSFDS 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 288 VPIGEDNEEKEQKKC-HSLVSVGQFRPEKDHQLQIRAFKKLLDRKEvepaGREAVKLVLIGGC--RNQEDEDRVLMLRGL 364
Cdd:cd03805  196 TSEDPDPGDLIAKSNkKFFLSINRFERKKNIALAIEAFAKLKQKLP----EFENVRLVIAGGYdpRVAENVEYLEELQRL 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 365 CQEL-GIADRVEFKLNIPfQELKKDLTDATIG-LHTMWNEHFGIGIVECMAAGTIILAHKSGGPKLDIVVpydgGPTGFL 442
Cdd:cd03805  272 AEELlNVEDQVLFLRSIS-DSQKEQLLSSALAlLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVE----GVTGFL 346
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 238624126 443 AD-DEDNYADAMERILSMsPATRLEMRRRARLSVS-RFSDQEFEGSF 487
Cdd:cd03805  347 CEpTPEAFAEAMLKLAND-PDLADRMGAAGRKRVKeKFSREAFAERL 392
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
305-472 2.72e-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: 2.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126  305 LVSVGQFRPEKDHQLQIRAFKKLLDRKEVepagreaVKLVLIGgcrNQEDEDRvlmLRGLCQELGIADRVEFKLNIPFQE 384
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFALLKEKNPN-------LKLVIAG---DGEEEKR---LKKLAEKLGLGDNVIFLGFVSDED 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126  385 LKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVVPYDggpTGFLAD--DEDNYADAMERILSmSPA 462
Cdd:pfam00534  72 LPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPP-EVVKDGE---TGFLVKpnNAEALAEAIDKLLE-DEE 146
                         170
                  ....*....|
gi 238624126  463 TRLEMRRRAR 472
Cdd:pfam00534 147 LRERLGENAR 156
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
63-479 1.46e-23

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: 101.85  E-value: 1.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126  63 VAFFHPYCNAG-GGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEIldgarRRFNIRLPRPVKFVFLKHRLLVEAKL 141
Cdd:cd03801    2 ILLLSPELPPPvGGAERHVRELARALAARGHDVTVLTPADPGEPPEELE-----DGVIVPLLPSLAALLRARRLLRELRP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 142 YPHFtllgqsvgsiflgwealteFVPDL-YIDSMGFAFTLPVFRYLGGCQVGSYVHYPTistdmlsvvrernPRFNNADY 220
Cdd:cd03801   77 LLRL-------------------RKFDVvHAHGLLAALLAALLALLLGAPLVVTLHGAE-------------PGRLLLLL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 221 ISSNPVLSAIKVIYYCVfallyglagscsDVIMVNSTWTLGHILAL-WRTPNRTSVVYPPCDVQAFlDVPIGEDNEEKEQ 299
Cdd:cd03801  125 AAERRLLARAEALLRRA------------DAVIAVSEALRDELRALgGIPPEKIVVIPNGVDLERF-SPPLRRKLGIPPD 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 300 KKchSLVSVGQFRPEKDHQLQIRAFKKLLDRkevepagREAVKLVLIGgcRNQEDEDRVLMLrglcqELGIADRVEFKLN 379
Cdd:cd03801  192 RP--VLLFVGRLSPRKGVDLLLEALAKLLRR-------GPDVRLVIVG--GDGPLRAELEEL-----ELGLGDRVRFLGF 255
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 380 IPFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVVPydgGPTGFLA--DDEDNYADAMERIL 457
Cdd:cd03801  256 VPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLP-EVVED---GEGGLVVppDDVEALADALLRLL 331
                        410       420
                 ....*....|....*....|...
gi 238624126 458 SmSPATRLEMRRRARLSVS-RFS 479
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 ...
63-484 3.57e-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: 97.81  E-value: 3.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126  63 VAFFHPyCNAGGGGERVLWCALRALQNRYQDVSFVVYTGdqgvtaEEILDGARRRFNIRLPRPVKFVFLKHRLLVEAKLY 142
Cdd:cd03811    2 ILFVIP-SLSGGGAERVLLNLANALDKRGYDVTLVLLRD------EGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 143 phftllgqsVGSIFLgwealtEFVPDLYIDSMGFAFTLPVFRYLGGCQVgsyvhyptistdmlsVVRERNPRFNNadYIS 222
Cdd:cd03811   75 ---------LKRILK------RAKPDVVISFLGFATYIVAKLAAARSKV---------------IAWIHSSLSKL--YYL 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 223 SNPVLSAIKVIYYCvfallyglagscsDVIMVNSTWTLGHILAL-WRTPNRTSVVYPPCDVQAFLDVPIGEDNEEKEQKK 301
Cdd:cd03811  123 KKKLLLKLKLYKKA-------------DKIVCVSKGIKEDLIRLgPSPPEKIEVIYNPIDIDRIRALAKEPILNEPEDGP 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 302 chSLVSVGQFRPEKDHQLQIRAFKKLLDRkevepagREAVKLVLIGgcrNQEDEDRvlmLRGLCQELGIADRVEF---KL 378
Cdd:cd03811  190 --VILAVGRLDPQKGHDLLIEAFAKLRKK-------YPDVKLVILG---DGPLREE---LEKLAKELGLAERVIFlgfQS 254
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 379 NiPFQELKKdltdATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVvpyDGGPTGFLADDEDNYADAMERILS 458
Cdd:cd03811  255 N-PYPYLKK----ADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPR-EIL---DDGENGLLVPDGDAAALAGILAAL 325
                        410       420
                 ....*....|....*....|....*.
gi 238624126 459 MSPATRLEMRRRARLSVSRFSDQEFE 484
Cdd:cd03811  326 LQKKLDAALRERLAKAQEAVFREYTI 351
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
244-478 2.04e-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: 89.99  E-value: 2.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 244 LAGSCSDVIMVNSTWTLGHILALWRT-PNRTSVVYPPCDVQAFldVPIGEDNEE-----KEQKKcHSLVSVGQFRPEKDH 317
Cdd:cd03800  159 QILEAADRVIASTPQEADELISLYGAdPSRINVVPPGVDLERF--FPVDRAEARrarllLPPDK-PVVLALGRLDPRKGI 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 318 QLQIRAFKKLLDRkevepagREAVKLVLIGGCRNQEDEDRVLMLRGLCQELGIADRVEFKLNIPFQELKKDLTDATIGLH 397
Cdd:cd03800  236 DTLVRAFAQLPEL-------RELANLVLVGGPSDDPLSMDREELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVV 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 398 TMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVVPydgGPTGFLAD--DEDNYADAMERILsMSPATRLEMRRRARLSV 475
Cdd:cd03800  309 PSLYEPFGLTAIEAMACGTPVVATAVGGLQ-DIVRD---GRTGLLVDphDPEALAAALRRLL-DDPALWQRLSRAGLERA 383

                 ...
gi 238624126 476 SRF 478
Cdd:cd03800  384 RAH 386
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
306-483 5.70e-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: 5.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 306 VSVGQFRPEKDHQLQIRAFKKLLDRkevepagREAVKLVLIGgcrNQEDEDRvlmLRGLCQELGIADRVEFKLNIPFQEL 385
Cdd:cd03798  204 LFVGRLIPRKGIDLLLEAFARLAKA-------RPDVVLLIVG---DGPLREA---LRALAEDLGLGDRVTFTGRLPHEQV 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 386 KKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVvpyDGGPTGFLAD--DEDNYADAMERILsMSPAT 463
Cdd:cd03798  271 PAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIP-EVV---GDPETGLLVPpgDADALAAALRRAL-AEPYL 345
                        170       180
                 ....*....|....*....|
gi 238624126 464 RLEMRRRARLSVSRFSDQEF 483
Cdd:cd03798  346 RELGEAARARVAERFSWVKA 365
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
248-479 3.58e-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: 80.10  E-value: 3.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 248 CSDVIMVNSTWTLGHILALWRTP-NRTSVVYPPCDVQAFLDVPIGEDNEEKEQKkCHSLVSVGQFRPEKDHQLQIRAFKK 326
Cdd:cd03809  138 RADAIITVSEATRDDIIKFYGVPpEKIVVIPLGVDPSFFPPESAAVLIAKYLLP-EPYFLYVGTLEPRKNHERLLKAFAL 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 327 LLDRKEVepagreaVKLVLIGGcrnqeDEDRVLMLRGLCQELGIADRVEFKLNIPFQELKKDLTDATI----GLHtmwnE 402
Cdd:cd03809  217 LKKQGGD-------LKLVIVGG-----KGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAfvfpSLY----E 280
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238624126 403 HFGIGIVECMAAGTIILAhkSGGPKLDIVVpydgGPTGFLAD--DEDNYADAMERILSmSPATRLEMRRRARLSVSRFS 479
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 ...
275-479 2.10e-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: 2.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 275 VVYPPCDVQAFLDVPIGEDNEE---KEQKKchSLVSVGQFRPEKDHQLQIRAFKKLLDRKEvepagreaVKLVLIG-GCR 350
Cdd:cd03817  173 VIPNGIDLDKFEKPLNTEERRKlglPPDEP--ILLYVGRLAKEKNIDFLLRAFAELKKEPN--------IKLVIVGdGPE 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 351 NQEdedrvlmLRGLCQELGIADRVEFKLNIPFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDI 430
Cdd:cd03817  243 REE-------LKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAAS-EL 314
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 238624126 431 VvpyDGGPTGFL-ADDEDNYADAMERILSMsPATRLEMRRRARLSVSRFS 479
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 ...
305-479 1.73e-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: 71.58  E-value: 1.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 305 LVSVGQFRPEKDHQLQIRAFKKLLDRkevepagREAVKLVLIG-GCRNQEDEdrvLMLRglcqELGIADRVEFKLNIpfQ 383
Cdd:cd03807  193 IGIVGRLHPVKDHSDLLRAAALLVET-------HPDLRLLLVGrGPERPNLE---RLLL----ELGLEDRVHLLGER--S 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 384 ELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGpKLDIVVPydggPTGFL--ADDEDNYADAMERILSMsP 461
Cdd:cd03807  257 DVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGG-AAELVDD----GTGFLvpAGDPQALADAIRALLED-P 330
                        170
                 ....*....|....*....
gi 238624126 462 ATRLEMRRRARLSV-SRFS 479
Cdd:cd03807  331 EKRARLGRAARERIaNEFS 349
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
250-437 1.29e-12

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: 67.43  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 250 DVIMVNSTW--TLGHILALWRTPNRTSVVYPPCDVQAFLDVPIGEDNEEKEQKKCHSLVSVGQFRPEKDHQLQIRAFKKL 327
Cdd:cd01635   56 DVVHAHSPHaaALAALLAARLLGIPIVVTVHGPDSLESTRSELLALARLLVSLPLADKVSVGRLVPEKGIDLLLEALALL 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 328 ldrkevePAGREAVKLVLIGGCRNQEDEDRVLmlrglcQELGIADRVEFKLNIPFQELKKDLT-DATIGLHTMWNEHFGI 406
Cdd:cd01635  136 -------KARLPDLVLVLVGGGGEREEEEALA------AALGLLERVVIIGGLVDDEVLELLLaAADVFVLPSRSEGFGL 202
                        170       180       190
                 ....*....|....*....|....*....|.
gi 238624126 407 GIVECMAAGTIILAHKSGGPKLDIVVPYDGG 437
Cdd:cd01635  203 VLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
265-481 2.94e-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: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 265 ALWRTPNRTSVVYPPCDVQAFLDVPIGEDNeekeqkkchsLVSVGQFRPEKDHQLQIRAFKKlldrkevepAGReavKLV 344
Cdd:cd03802  142 AATPPIDYLTVVHNGLDPADYRFQPDPEDY----------LAFLGRIAPEKGLEDAIRVARR---------AGL---PLK 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 345 LIGGCRNQEDEDRVlmlrglcQELGIADRVEFKLNIPFQELKKDLTDATIGLHT-MWNEHFGIGIVECMAAGTIILAHKS 423
Cdd:cd03802  200 IAGKVRDEDYFYYL-------QEPLPGPRIEFIGEVGHDEKQELLGGARALLFPiNWDEPFGLVMIEAMACGTPVIAYRR 272
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 424 GGPkLDIVVPydgGPTGFLADDEDNYADAMERILSMSPATrleMRRRA--RLSVSRFSDQ 481
Cdd:cd03802  273 GGL-PEVIQH---GETGFLVDSVEEMAEAIANIDRIDRAA---CRRYAedRFSAARMADR 325
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
250-487 1.72e-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: 65.38  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 250 DVIMVNSTWTLGHIlalWRTPNRTS-VVYPPCDVQAFLDVPIGEDneekeqkkchSLVSVGQFRPEKDHQLQIRAFKKLl 328
Cdd:cd03804  159 DLFIANSQFVARRI---KKFYGREStVIYPPVDTDAFAPAADKED----------YYLTASRLVPYKRIDLAVEAFNEL- 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 329 drkevepaGReavKLVLIGgcrNQEDEDRvlmLRGlcqelgIADR-VEFKLNIPFQELKKDLTDATiGLHTMWNEHFGIG 407
Cdd:cd03804  225 --------PK---RLVVIG---DGPDLDR---LRA------MASPnVEFLGYQPDEVLKELLSKAR-AFVFAAEEDFGIV 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 408 IVECMAAGTIILAHKSGGpKLDIVVPydgGPTGFLADDEDNYA--DAMERILSMSPATRLEmrrRARLSVSRFSDQEFEG 485
Cdd:cd03804  281 PVEAQACGTPVIAFGKGG-ALETVRP---GPTGILFGEQTVESlkAAVEEFEQNFDRFKPQ---AIRANAERFSRARFRQ 353

                 ..
gi 238624126 486 SF 487
Cdd:cd03804  354 EI 355
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
63-479 2.13e-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: 65.34  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126  63 VAFFHPYCNAGGGGERVLWCALRALQNRYQDVSFVVYTGDQGVTAEEildgarrrfnirLPRPVKFVFLKHRLLVEAKLY 142
Cdd:cd03820    2 IAIVIPSISNAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYE------------LDDNIKIKNLGDRKYSHFKLL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 143 PHFtllgQSVGSIFLgwEALTEFVPDLYIDSMGFAFTLPvfrylggcqvgsyvhyPTISTDMLSVVRERNPRFNNADYIS 222
Cdd:cd03820   70 LKY----FKKVRRLR--KYLKNNKPDVVISFRTSLLTFL----------------ALIGLKSKLIVWEHNNYEAYNKGLR 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 223 SnpvlsaikviyYCVFALLYGLAgscsDVIMVNSTWTLghILALWRTPNRTSVVYPPCDvqaFLDVPIGEDNEEKeqkkc 302
Cdd:cd03820  128 R-----------LLLRRLLYKRA----DKIVVLTEADK--LKKYKQPNSNVVVIPNPLS---FPSEEPSTNLKSK----- 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 303 hSLVSVGQFRPEKDHQLQIRAFKKLLDRkevepagREAVKLVLIGGCrnqEDEDRvlmLRGLCQELGIADRVEFKLNIpf 382
Cdd:cd03820  183 -RILAVGRLTYQKGFDLLIEAWALIAKK-------HPDWKLRIYGDG---PEREE---LEKLIDKLGLEDRVKLLGPT-- 246
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 383 QELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKS-GGPKlDIVvpyDGGPTGFLADDED--NYADAMERILSm 459
Cdd:cd03820  247 KNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCpTGPS-EII---EDGENGLLVPNGDvdALAEALLRLME- 321
                        410       420
                 ....*....|....*....|
gi 238624126 460 SPATRLEMRRRARLSVSRFS 479
Cdd:cd03820  322 DEELRKKMGKNARKNAERFS 341
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
389-496 7.15e-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: 7.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 389 LTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVVPydgGPTGFLAD--DEDNYADAMERILSmSPATRLE 466
Cdd:COG0438   18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLP-EVIED---GETGLLVPpgDPEALAEAILRLLE-DPELRRR 92
                         90       100       110
                 ....*....|....*....|....*....|.
gi 238624126 467 MRRRAR-LSVSRFSDQEFEGSFLSAMEPLMS 496
Cdd:COG0438   93 LGEAAReRAEERFSWEAIAERLLALYEELLA 123
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
305-458 1.92e-10

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 58.68  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126  305 LVSVGQFRPE-KDHQLQIRAFKKLLDRkevepagREAVKLVLIGGCRNQEDEDRVLmlrglcqelGIADRVEFklnIPF- 382
Cdd:pfam13692   4 ILFVGRLHPNvKGVDYLLEAVPLLRKR-------DNDVRLVIVGDGPEEELEELAA---------GLEDRVIF---TGFv 64
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238624126  383 QELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVVpydgGPTGFLA--DDEDNYADAMERILS 458
Cdd:pfam13692  65 EDLAELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIP-ELVD----GENGLLVppGDPEALAEAILRLLE 137
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
237-482 4.57e-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: 61.07  E-value: 4.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 237 VFALLYGLAGSCSDVIMVNSTWTLGHILALWRTPNRTSVVYPPCDVQAFLDVPIGEDNEEKEqkkcHSLVSVGQFRPEKD 316
Cdd:cd03808  128 LYLLLEKLALLFTDKVIFVNEDDRDLAIKKGIIKKKKTVLIPGSGVDLDRFQYSPESLPSEK----VVFLFVARLLKDKG 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 317 HQLQIRAFKKLLDRKevepagrEAVKLVLIGGCRnqEDEDRVLMLrglcQELGIADRVEF---KLNIPfqelkKDLTDAT 393
Cdd:cd03808  204 IDELIEAAKILKKKG-------PNVRFLLVGDGE--LENPSEILI----EKLGLEGRIEFlgfRSDVP-----ELLAESD 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 394 IGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVVPydgGPTGFLAD--DEDNYADAMERILSmSPATRLEMRRRA 471
Cdd:cd03808  266 VFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCR-ELVID---GVNGFLVPpgDVEALADAIEKLIE-DPELRKEMGEAA 340
                        250
                 ....*....|..
gi 238624126 472 RLSV-SRFSDQE 482
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 ...
292-479 1.31e-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: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 292 EDNEEKEQKKCHS----LVSVGQFRPEKDHQLQIRAFKKLldRKEVePAgreavKLVLIGgcrnqEDEDRVLMLRgLCQE 367
Cdd:cd04962  182 PAGALKRRLLAPPdekvVIHVSNFRPVKRIDDVVRVFARV--RRKI-PA-----KLLLVG-----DGPERVPAEE-LARE 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 368 LGIADRVEFKLNIPfqELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGpkLDIVVpyDGGPTGFLAD--D 445
Cdd:cd04962  248 LGVEDRVLFLGKQD--DVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGG--IPEVV--KHGETGFLSDvgD 321
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 238624126 446 EDNYADAMERILSmSPATRLEMRRRARL-SVSRFS 479
Cdd:cd04962  322 VDAMAKSALSILE-DDELYNRMGRAARKrAAERFD 355
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
305-492 8.78e-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: 8.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 305 LVSVGQFRPEKDhqlqIRAFKKLLDRkevePAGREAVKLVLIGGCRNQEdedrVLMLRGLCQE-LGIADRvefklnipfQ 383
Cdd:cd03814  201 LLYVGRLAPEKN----LEALLDADLP----LAASPPVRLVVVGDGPARA----ELEARGPDVIfTGFLTG---------E 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 384 ELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVvpyDGGPTGFLAD--DEDNYADAMERiLSMSP 461
Cdd:cd03814  260 ELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPR-DIV---RPGGTGALVEpgDAAAFAAALRA-LLEDP 334
                        170       180       190
                 ....*....|....*....|....*....|.
gi 238624126 462 ATRLEMRRRARLSVSRFSDQEFEGSFLSAME 492
Cdd:cd03814  335 ELRRRMAARARAEAERYSWEAFLDNLLDYYA 365
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
308-473 4.07e-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: 4.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 308 VGQFRPEKDHQLQIRAFKKLLDRKEVepagreavkLVLIGGCRNQEDEDRVLMlrglcQELGIADRVEFKLNIPfqELKK 387
Cdd:cd03819  188 VGRLSPEKGWLLLVDAAAELKDEPDF---------RLLVAGDGPERDEIRRLV-----ERLGLRDRVTFTGFRE--DVPA 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 388 DLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPkLDIVVPydgGPTGFLADDEDN--YADAMERiLSMSPATRL 465
Cdd:cd03819  252 ALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGA-REIVVH---GRTGLLVPPGDAeaLADAIRA-AKLLPEARE 326

                 ....*...
gi 238624126 466 EMRRRARL 473
Cdd:cd03819  327 KLQAAAAL 334
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
270-479 1.95e-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: 53.11  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 270 PNRTSVVYPPCDVQAFLDVPIGEDNEEKEQKKCHSLVSVGQFRPEKDHQLQIRAFKKLLDRKEVepagreavKLVLIGGC 349
Cdd:cd03794  185 KEKIIVIPNWADLEEFKPPPKDELRKKLGLDDKFVVVYAGNIGKAQGLETLLEAAERLKRRPDI--------RFLFVGDG 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 350 RNQEDEDRVLMLRGLcqelgiaDRVEFKLNIPFQELKKDLTDATIGLHTMWNEHFGIGIV-----ECMAAGTIILAHKSG 424
Cdd:cd03794  257 DEKERLKELAKARGL-------DNVTFLGRVPKEEVPELLSAADVGLVPLKDNPANRGSSpsklfEYMAAGKPILASDDG 329
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 238624126 425 GPKLDIVVpydgGPTGFLADDEDN--YADAMERiLSMSPATRLEMRRRAR-LSVSRFS 479
Cdd:cd03794  330 GSDLAVEI----NGCGLVVEPGDPeaLADAILE-LLDDPELRRAMGENGReLAEEKFS 382
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
219-482 4.83e-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: 51.95  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 219 DYISSNPVLSAIKVIYYCVFALLYGLAGSCSDVIMVNSTWTLGHILALWRTPNRTSVVYPPCDVQAFLDVPigednEEKE 298
Cdd:cd03813  215 EILQSTWIMGYIKKLWIRFFERLGKLAYQQADKIISLYEGNRRRQIRLGADPDKTRVIPNGIDIQRFAPAR-----EERP 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 299 QKKCHSLVSVGQFRPEKDHQLQIRAFKKLLDRkevepagREAVKLVLIGGcrNQEDEDRVLMLRGLCQELGIADRVEFkl 378
Cdd:cd03813  290 EKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRA-------MPDAEGWLIGP--EDEDPEYAQECKRLVASLGLENKVKF-- 358
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 379 nIPFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKlDIVvpYDG----GPTGFL---ADDEDnYAD 451
Cdd:cd03813  359 -LGFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCR-ELI--YGAddalGQAGLVvppADPEA-LAE 433
                        250       260       270
                 ....*....|....*....|....*....|.
gi 238624126 452 AMERILSmSPATRLEMRRRARLSVSRFSDQE 482
Cdd:cd03813  434 ALIKLLR-DPELRQAFGEAGRKRVEKYYTLE 463
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
277-477 1.94e-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: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 277 YPPCDVQAFLDVPIGEDNEEKeqkkchSLVSVGQFRPEKDHQLQIRAFKKLLDRKEVepagreaVKLVLIGGcRNQEDED 356
Cdd:cd03792  178 LSPADIRYYLEKPFVIDPERP------YILQVARFDPSKDPLGVIDAYKLFKRRAEE-------PQLVICGH-GAVDDPE 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 357 RVLMLRGLCQELGIADRVEF-KLNIPFQELKKDLTDATIGLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKLDIVvpyd 435
Cdd:cd03792  244 GSVVYEEVMEYAGDDHDIHVlRLPPSDQEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVI---- 319
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 238624126 436 GGPTGFLADDEDNYADAMERILSmSPATRLEMRRRARLSVSR 477
Cdd:cd03792  320 DGETGFLVNSVEGAAVRILRLLT-DPELRRKMGLAAREHVRD 360
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
297-480 6.04e-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: 6.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 297 KEQKKcHSLVSVGQFRPEKDHQLQIRAFKKLldRKEVePagreAVKLVLIGgcRNQEDEDrvlmLRGLCQELGIADRVEF 376
Cdd:cd04949  156 HERKS-NKIITISRLAPEKQLDHLIEAVAKA--VKKV-P----EITLDIYG--YGEEREK----LKKLIEELHLEDNVFL 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 377 K--LNIPFQELKkdltDATIGLHTMWNEHFGIGIVECMAAGTIILAHKsggpkldivVPYdgGPTGFLADDE-------- 446
Cdd:cd04949  222 KgyHSNLDQEYQ----DAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYD---------VKY--GPSELIEDGEngyliekn 286
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 238624126 447 --DNYADAMERILSmSPATRLEMRRRARLSVSRFSD 480
Cdd:cd04949  287 niDALADKIIELLN-DPEKLQQFSEESYKIAEKYST 321
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
308-481 9.67e-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: 9.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 308 VGQFRPEKDHQLQIRAFKKLlDRKEVEpagreavkLVLIGGCRNQEdedrvlmlrglCQELGIADRVEFKLNIPFQELKK 387
Cdd:cd03823  197 IGRLTEEKGIDLLVEAFKRL-PREDIE--------LVIAGHGPLSD-----------ERQIEGGRRIAFLGRVPTDDIKD 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 388 --DLTDATIgLHTMWNEHFGIGIVECMAAGTIILAHKSGGPKLDIVvpydGGPTGFL--ADDEDNYADAMERI-----LS 458
Cdd:cd03823  257 fyEKIDVLV-VPSIWPEPFGLVVREAIAAGLPVIASDLGGIAELIQ----PGVNGLLfaPGDAEDLAAAMRRLltdpaLL 331
                        170       180
                 ....*....|....*....|...
gi 238624126 459 MSPATRLEMRRRARLSVSRFSDQ 481
Cdd:cd03823  332 ERLRAGAEPPRSTESQAEEYLKL 354
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
402-479 2.11e-05

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 47.01  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 402 EHFGIGIVECMAAGTIILAHKSGGPKlDIVVPYDGGPTGFLADDEDnYADAMERI--LSMSPATRLEMRRRARLSVSRFS 479
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 ...
285-479 5.77e-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: 45.13  E-value: 5.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 285 FLDVPIGEDNEEKEQKKCHSL---------VSVGQFRPEKDHQLQIRAFKKLLDRKEvepagreAVKLVLIGgcrnqEDE 355
Cdd:cd04951  162 GIDLNKFKKDINVRLKIRNKLnlkndefviLNVGRLTEAKDYPNLLLAISELILSKN-------DFKLLIAG-----DGP 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 356 DRVLMLRGLCQeLGIADRVEFklnIPFQELKKDLTDAT--IGLHTMWnEHFGIGIVECMAAGTIILAHKSGGPKlDIVVP 433
Cdd:cd04951  230 LRNELERLICN-LNLVDRVIL---LGQISNISEYYNAAdlFVLSSEW-EGFGLVVAEAMACERPVVATDAGGVA-EVVGD 303
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 238624126 434 YDggptgFLADDEDNY--ADAMERILSMSPATRLEMRRRARLSVSRFS 479
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 ...
305-479 6.90e-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: 6.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 305 LVSVGQFRPEKDHQLQIRAFKKLLDrkevepAGREaVKLVLIGgcrnqEDEDRVLMLRGLCQELGIADRVEFKLNIPFQE 384
Cdd:cd03821  207 ILFLGRIHPKKGLDLLIRAARKLAE------QGRD-WHLVIAG-----PDDGAYPAFLQLQSSLGLGDRVTFTGPLYGEA 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 385 LKKDLTDATIGLHTMWNEHFGIGIVECMAAGT-IILAHKSGGPKLdivvpYDGGpTGFLADDEDNY-ADAMERILS--MS 460
Cdd:cd03821  275 KWALYASADLFVLPSYSENFGNVVAEALACGLpVVITDKCGLSEL-----VEAG-CGVVVDPNVSSlAEALAEALRdpAD 348
                        170
                 ....*....|....*....
gi 238624126 461 PATRLEMRRRARLSVSRFS 479
Cdd:cd03821  349 RKRLGEMARRARQVEENFS 367
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
375-481 3.32e-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: 42.70  E-value: 3.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624126 375 EFKLNIPFQELKKDLTDATIGLHTMWN-----------EHFGIGIVECMAAGTIILAHKSGGPkLDIVvpyDGGPTGFLA 443
Cdd:cd03825  236 PQIVILPFDIISLGYIDDDEQLVDIYSaadlfvhpslaDNLPNTLLEAMACGTPVVAFDTGGS-PEIV---QHGVTGYLV 311
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 238624126 444 DDED--NYADAMERILsMSPATRLEMRRRAR-LSVSRFSDQ 481
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 ...
402-471 8.21e-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: 8.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238624126 402 EHFGIGIVECMAAGTIILAHKSGGPKlDIVVPYD---GGPTGFLADDEDNYA--DAMERILSM--SPATRLEMRRRA 471
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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