NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|123784012|sp|Q3TZM9|]
View 

RecName: Full=GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase; AltName: Full=Asparagine-linked glycosylation protein 11 homolog; AltName: Full=Glycolipid 2-alpha-mannosyltransferase

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 64-480 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: 699.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012  64 VVAFFHPYCNAGGGGERVLWCALRALQKKYPEAVYVVYTGDINVSGQQILDGAFRRFNIKLAHPVQFVF-LRKRYLVEDS 142
Cdd:cd03806    2 TVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFFlLKYRKLVEAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 143 RYPHFTLLGQSLGSILLGWEALMQRVPDVYIDSMGYAFTLPLFKYVGGCRVGSYVHYPTISTDMLSVVKNQNPGFNNAAF 222
Cdd:cd03806   82 TYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGGCPVVAYVHYPTISTDMLNKVRSREASYNNDST 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 223 ISRNALLSKAKLIYYYLFAFVYGLVGSCSDIVMVNSSWTLNHILSLWKVGHCTNIVYPPCDVQTFLDIPLHEKKVTpgHL 302
Cdd:cd03806  162 IARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPIDEKTRE--NQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 303 LVSIGQFRPEKNHALQIKAFAKLLNEKAAELGHSLKLVLIGGCRNKDDEFRVNQLRSLSENLGVQENVEFKINISFDELK 382
Cdd:cd03806  240 ILSIAQFRPEKNHPLQLRAFAELLKRLPESIRSNPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEFVVDAPYEELK 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 383 NYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKLDIVIPHEGQITGFLAESEEGYADSMAHILSLSAEERLQ 462
Cdd:cd03806  320 ELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILTLSEEERLQ 399

                        410
                 ....*....|....*...
gi 123784012 463 IRKNARASISRFSDQEFE 480
Cdd:cd03806  400 RREAARSSAERFSDEEFE 417
 
Name Accession Description Interval E-value
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
 64-480 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: 699.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012  64 VVAFFHPYCNAGGGGERVLWCALRALQKKYPEAVYVVYTGDINVSGQQILDGAFRRFNIKLAHPVQFVF-LRKRYLVEDS 142
Cdd:cd03806    2 TVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFFlLKYRKLVEAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 143 RYPHFTLLGQSLGSILLGWEALMQRVPDVYIDSMGYAFTLPLFKYVGGCRVGSYVHYPTISTDMLSVVKNQNPGFNNAAF 222
Cdd:cd03806   82 TYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGGCPVVAYVHYPTISTDMLNKVRSREASYNNDST 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 223 ISRNALLSKAKLIYYYLFAFVYGLVGSCSDIVMVNSSWTLNHILSLWKVGHCTNIVYPPCDVQTFLDIPLHEKKVTpgHL 302
Cdd:cd03806  162 IARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPIDEKTRE--NQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 303 LVSIGQFRPEKNHALQIKAFAKLLNEKAAELGHSLKLVLIGGCRNKDDEFRVNQLRSLSENLGVQENVEFKINISFDELK 382
Cdd:cd03806  240 ILSIAQFRPEKNHPLQLRAFAELLKRLPESIRSNPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEFVVDAPYEELK 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 383 NYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKLDIVIPHEGQITGFLAESEEGYADSMAHILSLSAEERLQ 462
Cdd:cd03806  320 ELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILTLSEEERLQ 399

                        410
                 ....*....|....*...
gi 123784012 463 IRKNARASISRFSDQEFE 480
Cdd:cd03806  400 RREAARSSAERFSDEEFE 417
PLN02949 PLN02949
transferase, transferring glycosyl groups
 64-492 0e+00

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 546.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012  64 VVAFFHPYCNAGGGGERVLWCALRALQKKYPEAVYVVYTGDINVSGQQILDGAFRRFNIKLAHPVQFVFLRKRYLVEDSR 143
Cdd:PLN02949  35 AVGFFHPYTNDGGGGERVLWCAVRAIQEENPDLDCVIYTGDHDASPDSLAARARDRFGVELLSPPKVVHLRKRKWIEEET 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 144 YPHFTLLGQSLGSILLGWEALMQRVPDVYIDSMGYAFTLPLFKyVGGCRVGSYVHYPTISTDMLSVVKNQNPGFNNAAFI 223
Cdd:PLN02949 115 YPRFTMIGQSLGSVYLAWEALCKFTPLYFFDTSGYAFTYPLAR-LFGCKVVCYTHYPTISSDMISRVRDRSSMYNNDASI 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 224 SRNALLSKAKLIYYYLFAFVYGLVGSCSDIVMVNSSWTLNHILSLWKVGHCTNIVYPPCDVQTFLDIPLHEKKVTPghLL 303
Cdd:PLN02949 194 ARSFWLSTCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPERIKRVYPPCDTSGLQALPLERSEDPP--YI 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 304 VSIGQFRPEKNHALQIKAFAKLLNEKAAELGHSlKLVLIGGCRNKDDEFRVNQLRSLSENLGVQENVEFKINISFDELKN 383
Cdd:PLN02949 272 ISVAQFRPEKAHALQLEAFALALEKLDADVPRP-KLQFVGSCRNKEDEERLQKLKDRAKELGLDGDVEFHKNVSYRDLVR 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 384 YLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKLDIVIPHEGQITGFLAESEEGYADSMAHILSLSAEERLQI 463
Cdd:PLN02949 351 LLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIVLDEDGQQTGFLATTVEEYADAILEVLRMRETERLEI 430

                        410       420
                 ....*....|....*....|....*....
gi 123784012 464 RKNARASISRFSDQEFEVAFLCSMEKLLT 492
Cdd:PLN02949 431 AAAARKRANRFSEQRFNEDFKDAIRPILN 459
ALG11_N pfam15924
ALG11 mannosyltransferase N-terminus;
63-269 3.35e-145

ALG11 mannosyltransferase N-terminus;


Pssm-ID: 464944  Cd Length: 209  Bit Score: 414.18  E-value: 3.35e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012   63 TVVAFFHPYCNAGGGGERVLWCALRALQKKYPEAVYVVYTGDINVSGQQILDGAFRRFNIKL-AHPVQFVFLRKRYLVED 141
Cdd:pfam15924   2 GIVGFFHPYCNAGGGGERVLWCAVRATQRRYPNAICVVYTGDIDASKEEILAKVKSRFNIELdPSRIVFVYLRKRKLVEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012  142 SRYPHFTLLGQSLGSILLGWEALMQRVPDVYIDSMGYAFTLPLFKYVGGCRVGSYVHYPTISTDMLSVVKNQNPGFNNAA 221
Cdd:pfam15924  82 STYPRFTLLGQSLGSIILAWEALSKLVPDVFIDTMGYAFTYPLVRLLGGCPVGAYVHYPTISTDMLSRVSSREAGYNNDS 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 123784012  222 FISRNALLSKAKLIYYYLFAFVYGLVGSCSDIVMVNSSWTLNHILSLW 269
Cdd:pfam15924 162 AIASSGLLSKAKLIYYRLFALLYGLVGSFADVVMVNSSWTQNHIRSLW 209
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 381-475 3.18e-10

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 57.69  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 381 LKNYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKlDIVIPHEgqiTGFLAESE--EGYADSMAHILSlSAE 458
Cdd:COG0438   14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLP-EVIEDGE---TGLLVPPGdpEALAEAILRLLE-DPE 88

                         90
                 ....*....|....*...
gi 123784012 459 ERLQIRKNARASI-SRFS 475
Cdd:COG0438   89 LRRRLGEAARERAeERFS 106
 
Name Accession Description Interval E-value
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
 64-480 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: 699.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012  64 VVAFFHPYCNAGGGGERVLWCALRALQKKYPEAVYVVYTGDINVSGQQILDGAFRRFNIKLAHPVQFVF-LRKRYLVEDS 142
Cdd:cd03806    2 TVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFFlLKYRKLVEAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 143 RYPHFTLLGQSLGSILLGWEALMQRVPDVYIDSMGYAFTLPLFKYVGGCRVGSYVHYPTISTDMLSVVKNQNPGFNNAAF 222
Cdd:cd03806   82 TYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGGCPVVAYVHYPTISTDMLNKVRSREASYNNDST 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 223 ISRNALLSKAKLIYYYLFAFVYGLVGSCSDIVMVNSSWTLNHILSLWKVGHCTNIVYPPCDVQTFLDIPLHEKKVTpgHL 302
Cdd:cd03806  162 IARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPIDEKTRE--NQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 303 LVSIGQFRPEKNHALQIKAFAKLLNEKAAELGHSLKLVLIGGCRNKDDEFRVNQLRSLSENLGVQENVEFKINISFDELK 382
Cdd:cd03806  240 ILSIAQFRPEKNHPLQLRAFAELLKRLPESIRSNPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEFVVDAPYEELK 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 383 NYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKLDIVIPHEGQITGFLAESEEGYADSMAHILSLSAEERLQ 462
Cdd:cd03806  320 ELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILTLSEEERLQ 399

                        410
                 ....*....|....*...
gi 123784012 463 IRKNARASISRFSDQEFE 480
Cdd:cd03806  400 RREAARSSAERFSDEEFE 417
PLN02949 PLN02949
transferase, transferring glycosyl groups
 64-492 0e+00

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 546.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012  64 VVAFFHPYCNAGGGGERVLWCALRALQKKYPEAVYVVYTGDINVSGQQILDGAFRRFNIKLAHPVQFVFLRKRYLVEDSR 143
Cdd:PLN02949  35 AVGFFHPYTNDGGGGERVLWCAVRAIQEENPDLDCVIYTGDHDASPDSLAARARDRFGVELLSPPKVVHLRKRKWIEEET 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 144 YPHFTLLGQSLGSILLGWEALMQRVPDVYIDSMGYAFTLPLFKyVGGCRVGSYVHYPTISTDMLSVVKNQNPGFNNAAFI 223
Cdd:PLN02949 115 YPRFTMIGQSLGSVYLAWEALCKFTPLYFFDTSGYAFTYPLAR-LFGCKVVCYTHYPTISSDMISRVRDRSSMYNNDASI 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 224 SRNALLSKAKLIYYYLFAFVYGLVGSCSDIVMVNSSWTLNHILSLWKVGHCTNIVYPPCDVQTFLDIPLHEKKVTPghLL 303
Cdd:PLN02949 194 ARSFWLSTCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPERIKRVYPPCDTSGLQALPLERSEDPP--YI 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 304 VSIGQFRPEKNHALQIKAFAKLLNEKAAELGHSlKLVLIGGCRNKDDEFRVNQLRSLSENLGVQENVEFKINISFDELKN 383
Cdd:PLN02949 272 ISVAQFRPEKAHALQLEAFALALEKLDADVPRP-KLQFVGSCRNKEDEERLQKLKDRAKELGLDGDVEFHKNVSYRDLVR 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 384 YLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKLDIVIPHEGQITGFLAESEEGYADSMAHILSLSAEERLQI 463
Cdd:PLN02949 351 LLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIVLDEDGQQTGFLATTVEEYADAILEVLRMRETERLEI 430

                        410       420
                 ....*....|....*....|....*....
gi 123784012 464 RKNARASISRFSDQEFEVAFLCSMEKLLT 492
Cdd:PLN02949 431 AAAARKRANRFSEQRFNEDFKDAIRPILN 459
ALG11_N pfam15924
ALG11 mannosyltransferase N-terminus;
63-269 3.35e-145

ALG11 mannosyltransferase N-terminus;


Pssm-ID: 464944  Cd Length: 209  Bit Score: 414.18  E-value: 3.35e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012   63 TVVAFFHPYCNAGGGGERVLWCALRALQKKYPEAVYVVYTGDINVSGQQILDGAFRRFNIKL-AHPVQFVFLRKRYLVED 141
Cdd:pfam15924   2 GIVGFFHPYCNAGGGGERVLWCAVRATQRRYPNAICVVYTGDIDASKEEILAKVKSRFNIELdPSRIVFVYLRKRKLVEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012  142 SRYPHFTLLGQSLGSILLGWEALMQRVPDVYIDSMGYAFTLPLFKYVGGCRVGSYVHYPTISTDMLSVVKNQNPGFNNAA 221
Cdd:pfam15924  82 STYPRFTLLGQSLGSIILAWEALSKLVPDVFIDTMGYAFTYPLVRLLGGCPVGAYVHYPTISTDMLSRVSSREAGYNNDS 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 123784012  222 FISRNALLSKAKLIYYYLFAFVYGLVGSCSDIVMVNSSWTLNHILSLW 269
Cdd:pfam15924 162 AIASSGLLSKAKLIYYRLFALLYGLVGSFADVVMVNSSWTQNHIRSLW 209
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 182-479 1.45e-34

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: 133.48  E-value: 1.45e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 182 LPLFKYVGGCRVGSYVHYPtistDMLSVvknqnpgfnnaafiSRNALLskaKLIYYYLFAFVYGLVGSCSDIVMVNSSWT 261
Cdd:cd03805  107 VPLLKLFRPSKILFYCHFP----DQLLA--------------QRKSLL---KRLYRKPFDWLEEFTTGMADQIVVNSNFT 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 262 LNHIL----SLWKVGHctNIVYPPCDVQTF-----LDIPLHEKKVTPGHLLVSIGQFRPEKNHALQIKAFAKLLNEKAaE 332
Cdd:cd03805  166 AGVFKktfpSLAKNPP--EVLYPCVDTDSFdstseDPDPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQKLP-E 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 333 LGHsLKLVLIGGCrnkddEFRV-------NQLRSLSENL-GVQENVEFKINISfDELKNYL-SEATIGLHTMWNEHFGIG 403
Cdd:cd03805  243 FEN-VRLVIAGGY-----DPRVaenveylEELQRLAEELlNVEDQVLFLRSIS-DSQKEQLlSSALALLYTPSNEHFGIV 315

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123784012 404 VVECMAAGTVILAHNSGGPKLDIViphEGqITGFLAESE-EGYADSMAHILSLSaEERLQIRKNARASIS-RFSDQEF 479
Cdd:cd03805  316 PLEAMYAGKPVIACNSGGPLETVV---EG-VTGFLCEPTpEAFAEAMLKLANDP-DLADRMGAAGRKRVKeKFSREAF 388
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 302-468 6.85e-28

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: 108.90  E-value: 6.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012  302 LLVSIGQFRPEKNHALQIKAFAKLLnekaaELGHSLKLVLIGGCRNKDdefrvnQLRSLSENLGVQENVEFKINISFDEL 381
Cdd:pfam00534   4 IILFVGRLEPEKGLDLLIKAFALLK-----EKNPNLKLVIAGDGEEEK------RLKKLAEKLGLGDNVIFLGFVSDEDL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012  382 KNYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKlDIVIPHEgqiTGFLAE--SEEGYADSMAHILSLSaEE 459
Cdd:pfam00534  73 PELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPP-EVVKDGE---TGFLVKpnNAEALAEAIDKLLEDE-EL 147


                  ....*....
gi 123784012  460 RLQIRKNAR 468
Cdd:pfam00534 148 RERLGENAR 156
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 65-475 3.88e-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: 100.69  E-value: 3.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012  65 VAFFHPYCNAG-GGGERVLWCALRALQKKyPEAVYVVYTGDINVSgqqilDGAFRRFNIKLAHPVQFVFLRKRYLVEDSR 143
Cdd:cd03801    2 ILLLSPELPPPvGGAERHVRELARALAAR-GHDVTVLTPADPGEP-----PEELEDGVIVPLLPSLAALLRARRLLRELR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 144 YphftllgqslgsillgweALMQRVPD-VYIDSMGYAFTLPLFKYVGGCRVGSYVHyptistdmlsvvkNQNPGFNNAAF 222
Cdd:cd03801   76 P------------------LLRLRKFDvVHAHGLLAALLAALLALLLGAPLVVTLH-------------GAEPGRLLLLL 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 223 ISRNALLSKAKLIYYYlfafvyglvgscSDIVMVNSSWTLNHILSLWKVGHCTNIV-YPPCDVQTFLDIPLHEKKVTPGH 301
Cdd:cd03801  125 AAERRLLARAEALLRR------------ADAVIAVSEALRDELRALGGIPPEKIVViPNGVDLERFSPPLRRKLGIPPDR 192

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 302 -LLVSIGQFRPEKNHALQIKAFAKLLNEkaaelGHSLKLVLIGGcrnkDDEFRvNQLRSLSenLGVQENVEFKINISFDE 380
Cdd:cd03801  193 pVLLFVGRLSPRKGVDLLLEALAKLLRR-----GPDVRLVIVGG----DGPLR-AELEELE--LGLGDRVRFLGFVPDEE 260

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 381 LKNYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKlDIVIPHEGqitGFLAESE--EGYADSMAHILSlSAE 458
Cdd:cd03801  261 LPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLP-EVVEDGEG---GLVVPPDdvEALADALLRLLA-DPE 335

                        410
                 ....*....|....*...
gi 123784012 459 ERLQIRKNARASIS-RFS 475
Cdd:cd03801  336 LRARLGRAARERVAeRFS 353
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 76-475 2.02e-18

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: 86.65  E-value: 2.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012  76 GGGERVLWCALRALQKKYPEAVYVVytgdinVSGQQILDGAFRRFNIKLAHPVQFVFLRKRYLvedsryphftllgqslG 155
Cdd:cd03809   14 TGIGRYTRELLKALAKNDPDESVLA------VPPLPGELLRLLREYPELSLGVIKIKLWRELA----------------L 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 156 SILLGWEALMQRVPDVYIdsmGYAFTLPLFKYvgGCRVGSYVHyptistDMLsvvknqnpgfnnaAFISRNALLSKAKLI 235
Cdd:cd03809   72 LRWLQILLPKKDKPDLLH---SPHNTAPLLLK--GCPQVVTIH------DLI-------------PLRYPEFFPKRFRLY 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 236 YYYLFAfvygLVGSCSDIVMVNSSWTLNHILSLWKVGhCTNIVYPPCDVQTFLDIPLHEKKVTPGHLL-----VSIGQFR 310
Cdd:cd03809  128 YRLLLP----ISLRRADAIITVSEATRDDIIKFYGVP-PEKIVVIPLGVDPSFFPPESAAVLIAKYLLpepyfLYVGTLE 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 311 PEKNHALQIKAFAKLlnekaAELGHSLKLVLIGGCRNKDDEfrvnqLRSLSENLGVQENVEFKINISFDELKNYLSEATI 390
Cdd:cd03809  203 PRKNHERLLKAFALL-----KKQGGDLKLVIVGGKGWEDEE-----LLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARA 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 391 ----GLHtmwnEHFGIGVVECMAAGTVILAHNSGgpkldiVIPHEGQITGFL--AESEEGYADSMAHILSlSAEERLQIR 464
Cdd:cd03809  273 fvfpSLY----EGFGLPVLEAMACGTPVIASNIS------VLPEVAGDAALYfdPLDPESIADAILRLLE-DPSLREELI 341

                        410
                 ....*....|.
gi 123784012 465 KNARASISRFS 475
Cdd:cd03809  342 RKGLERAKKFS 352
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 232-432 5.54e-15

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: 74.36  E-value: 5.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 232 AKLIYYYLFAFVYGLVGSCsDIVMVNSSWTLNHILSL------WKVGHCTNIVYPPCDVQTFLDIPLHEKKVTPGHLLVS 305
Cdd:cd01635   37 ALLLLALRRILKKLLELKP-DVVHAHSPHAAALAALLaarllgIPIVVTVHGPDSLESTRSELLALARLLVSLPLADKVS 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 306 IGQFRPEKNHALQIKAFAKLlnekaAELGHSLKLVLIGGCRNKDDEFRvnqlrsLSENLGVQENVEFKINISFDELKNYL 385
Cdd:cd01635  116 VGRLVPEKGIDLLLEALALL-----KARLPDLVLVLVGGGGEREEEEA------LAAALGLLERVVIIGGLVDDEVLELL 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 123784012 386 SE-ATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKLDIVIPHEG 432
Cdd:cd01635  185 LAaADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENG 232
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 275-474 1.04e-14

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: 75.74  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 275 TNIVYPPCDVQTF---LDIPLHEKKVtpghllVSIGQFRPEKNHALQIKAFAKLlnekaAELGHSLKLVLIGGCRNKDDE 351
Cdd:cd03800  198 LERFFPVDRAEARrarLLLPPDKPVV------LALGRLDPRKGIDTLVRAFAQL-----PELRELANLVLVGGPSDDPLS 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 352 FRVNQLRSLSENLGVQENVEFKINISFDELKNYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKlDIVIPhe 431
Cdd:cd03800  267 MDREELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQ-DIVRD-- 343

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 123784012 432 gQITGFLAE--SEEGYADSMAHILSlSAEERLQIRKNARASISRF 474
Cdd:cd03800  344 -GRTGLLVDphDPEALAAALRRLLD-DPALWQRLSRAGLERARAH 386
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 302-475 1.61e-14

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: 75.05  E-value: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 302 LLVSIGQFRPEKNHALQIKAFAKLlnekaAELGHSLKLVLIG-GCRNKDDEfrvnqlrSLSENLGVQENVEFKINISfdE 380
Cdd:cd03807  192 VIGIVGRLHPVKDHSDLLRAAALL-----VETHPDLRLLLVGrGPERPNLE-------RLLLELGLEDRVHLLGERS--D 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 381 LKNYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGpKLDIVIPHegqiTGFL--AESEEGYADSMAHILSLsAE 458
Cdd:cd03807  258 VPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGG-AAELVDDG----TGFLvpAGDPQALADAIRALLED-PE 331

                        170
                 ....*....|....*...
gi 123784012 459 ERLQIRKNARASI-SRFS 475
Cdd:cd03807  332 KRARLGRAARERIaNEFS 349
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 299-477 3.85e-14

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: 73.48  E-value: 3.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 299 PGHLLVsIGQFRPEKNHALQIKAfakllnekAAELGhsLKLVLIGGCRNKDDEFRVNQLRslsenlgVQENVEFKINISF 378
Cdd:cd03802  169 EDYLAF-LGRIAPEKGLEDAIRV--------ARRAG--LPLKIAGKVRDEDYFYYLQEPL-------PGPRIEFIGEVGH 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 379 DELKNYLSEATIGLHT-MWNEHFGIGVVECMAAGTVILAHNSGGPkLDIVIPHEgqiTGFLAESEEGYADSMAHILSLSa 457
Cdd:cd03802  231 DEKQELLGGARALLFPiNWDEPFGLVMIEAMACGTPVIAYRRGGL-PEVIQHGE---TGFLVDSVEEMAEAIANIDRID- 305

                        170       180
                 ....*....|....*....|..
gi 123784012 458 eeRLQIRKNA--RASISRFSDQ 477
Cdd:cd03802  306 --RAACRRYAedRFSAARMADR 325
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 252-483 3.62e-13

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: 70.78  E-value: 3.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 252 DIVMVNSSWTLNHIlslWKVGHCTNIV-YPPCDVQTFLdiPLHEKkvtpGHLLVSIGQFRPEKNHALQIKAFAKLlneka 330
Cdd:cd03804  159 DLFIANSQFVARRI---KKFYGRESTViYPPVDTDAFA--PAADK----EDYYLTASRLVPYKRIDLAVEAFNEL----- 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 331 aelghSLKLVLIGgcrnkdDEFRVNQLRSLSenlgvQENVEFKINISFDELKNYLSEATiGLHTMWNEHFGIGVVECMAA 410
Cdd:cd03804  225 -----PKRLVVIG------DGPDLDRLRAMA-----SPNVEFLGYQPDEVLKELLSKAR-AFVFAAEEDFGIVPVEAQAC 287

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123784012 411 GTVILAHNSGGpKLDIVIPHEgqiTGFLAesEEGYADSMAHILSLSAEERLQIRKNA-RASISRFSDQEFEVAF 483
Cdd:cd03804  288 GTPVIAFGKGG-ALETVRPGP---TGILF--GEQTVESLKAAVEEFEQNFDRFKPQAiRANAERFSRARFRQEI 355
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 302-475 7.87e-13

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: 69.62  E-value: 7.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 302 LLVSIGQFRPEKNHALQIKAFAKLLNEKAAelghslKLVLIGGcrNKDDEfrvnQLRSLSENLGVQENVEFKINISFDEL 381
Cdd:cd03817  203 ILLYVGRLAKEKNIDFLLRAFAELKKEPNI------KLVIVGD--GPERE----ELKELARELGLADKVIFTGFVPREEL 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 382 KNYLSEATIGLHTMWNEHFGIGVVECMAAGT-VILAHNSGGPklDIVipHEGqITGFLAESEEGY-ADSMAHILSLsAEE 459
Cdd:cd03817  271 PEYYKAADLFVFASTTETQGLVYLEAMAAGLpVVAAKDPAAS--ELV--EDG-ENGFLFEPNDETlAEKLLHLREN-LEL 344

                        170
                 ....*....|....*.
gi 123784012 460 RLQIRKNARASISRFS 475
Cdd:cd03817  345 LRKLSKNAEISAREFA 360
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 250-479 2.02e-12

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: 68.56  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 250 CSDIVmVNSSWTLNHILSLWKVGHCT---------------------NIVYPPCDVQTFLDIPLHE--KKVTPGHLLVSI 306
Cdd:cd03798  128 GSDIN-VFPPRSLLRKLLRWALRRAArviavskalaeelvalgvprdRVDVIPNGVDPARFQPEDRglGLPLDAFVILFV 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 307 GQFRPEKNHALQIKAFAKLlnEKAAElghSLKLVLIGGCRNKDdefrvnQLRSLSENLGVQENVEFKINISFDELKNYLS 386
Cdd:cd03798  207 GRLIPRKGIDLLLEAFARL--AKARP---DVVLLIVGDGPLRE------ALRALAEDLGLGDRVTFTGRLPHEQVPAYYR 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 387 EATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKlDIViphEGQITGFLAE--SEEGYADSMAHILSLSAEERLQIR 464
Cdd:cd03798  276 ACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIP-EVV---GDPETGLLVPpgDADALAAALRRALAEPYLRELGEA 351

                        250
                 ....*....|....*
gi 123784012 465 KNARASiSRFSDQEF 479
Cdd:cd03798  352 ARARVA-ERFSWVKA 365
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 251-475 3.52e-12

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: 67.76  E-value: 3.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 251 SDIVMVNSSWTLNHILSLWKVGHCTNIVYPPCDVQTFLDIP---LHEKKVTP--GHLLVSIGQFRPEKNHALQIKAFAKL 325
Cdd:cd04962  142 SDRVTAVSSSLRQETYELFDVDKDIEVIHNFIDEDVFKRKPagaLKRRLLAPpdEKVVIHVSNFRPVKRIDDVVRVFARV 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 326 LNEKAAelghslKLVLIGgcrnkDDEFRVNqLRSLSENLGVQENVEFKINisFDELKNYLSEATIGLHTMWNEHFGIGVV 405
Cdd:cd04962  222 RRKIPA------KLLLVG-----DGPERVP-AEELARELGVEDRVLFLGK--QDDVEELLSIADLFLLPSEKESFGLAAL 287

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123784012 406 ECMAAGTVILAHNSGGpkLDIVIPHegQITGFLaeSEEGYADSMA-HILSLSAEERLQIR--KNARASI-SRFS 475
Cdd:cd04962  288 EAMACGVPVVSSNAGG--IPEVVKH--GETGFL--SDVGDVDAMAkSALSILEDDELYNRmgRAARKRAaERFD 355
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
300-454 7.77e-12

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 62.91  E-value: 7.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012  300 GHLLVSIGQFRPE-KNHALQIKAFAKLLNEKaaelgHSLKLVLIGGCRNKddefrvnQLRSLSEnlGVQENVEFKINIsf 378
Cdd:pfam13692   1 RPVILFVGRLHPNvKGVDYLLEAVPLLRKRD-----NDVRLVIVGDGPEE-------ELEELAA--GLEDRVIFTGFV-- 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123784012  379 DELKNYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKlDIVIphegQITGFLAESE--EGYADSMAHILS 454
Cdd:pfam13692  65 EDLAELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIP-ELVD----GENGLLVPPGdpEALAEAILRLLE 137
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 277-480 2.08e-11

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: 65.07  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 277 IVYPPCDVQTFLDIPLHEKKVTPGH--LLVSIGQFRPEKNHALQIKAFAKLLNEkaaelGHSLKLVLIGgcrNKDDEfrv 354
Cdd:cd03811  163 VIYNPIDIDRIRALAKEPILNEPEDgpVILAVGRLDPQKGHDLLIEAFAKLRKK-----YPDVKLVILG---DGPLR--- 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 355 NQLRSLSENLGVQENVEFKinisfDELKN---YLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKlDIVIPHE 431
Cdd:cd03811  232 EELEKLAKELGLAERVIFL-----GFQSNpypYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPR-EILDDGE 305

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 123784012 432 gqiTGFLAESEEGYADSMAHILSLSAEERLQIRKNARASISRFSDQEFE 480
Cdd:cd03811  306 ---NGLLVPDGDAAALAGILAALLQKKLDAALRERLAKAQEAVFREYTI 351
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 381-475 3.18e-10

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 57.69  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 381 LKNYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKlDIVIPHEgqiTGFLAESE--EGYADSMAHILSlSAE 458
Cdd:COG0438   14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLP-EVIEDGE---TGLLVPPGdpEALAEAILRLLE-DPE 88

                         90
                 ....*....|....*...
gi 123784012 459 ERLQIRKNARASI-SRFS 475
Cdd:COG0438   89 LRRRLGEAARERAeERFS 106
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 302-475 9.60e-09

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: 57.07  E-value: 9.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 302 LLVSIGQFRPEKNHALQIKAFAKLLNEKaaelgHSLKLVLIGgcrnkDDEFRvNQLRSLSENLGVQENVEFKINISfdEL 381
Cdd:cd04951  190 VILNVGRLTEAKDYPNLLLAISELILSK-----NDFKLLIAG-----DGPLR-NELERLICNLNLVDRVILLGQIS--NI 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 382 KNYLSEATIG-LHTMWnEHFGIGVVECMAAGTVILAHNSGGPKlDIVIPHEGQITgfLAESEEgYADSMAHILSLSAEER 460
Cdd:cd04951  257 SEYYNAADLFvLSSEW-EGFGLVVAEAMACERPVVATDAGGVA-EVVGDHNYVVP--VSDPQL-LAEKIKEIFDMSDEER 331

                        170
                 ....*....|....*
gi 123784012 461 LQIRKNARASISRFS 475
Cdd:cd04951  332 DILGNKNEYIAKNFS 346
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 306-473 3.67e-08

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: 55.41  E-value: 3.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 306 IGQFRPEKNHALQIKAFAKLLNEKAaelghslKLVLIGGCRNKDDEFrvnqlrslsenLGVQENVEFKINISFDELKNYL 385
Cdd:cd03823  197 IGRLTEEKGIDLLVEAFKRLPREDI-------ELVIAGHGPLSDERQ-----------IEGGRRIAFLGRVPTDDIKDFY 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 386 SEATIGL-HTMWNEHFGIGVVECMAAGTVILAHNSGGPKLDIVIPHEGQItgFLAESEEGYADSMAHILSLSAEERLqIR 464
Cdd:cd03823  259 EKIDVLVvPSIWPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLL--FAPGDAEDLAAAMRRLLTDPALLER-LR 335


                 ....*....
gi 123784012 465 KNARASISR 473
Cdd:cd03823  336 AGAEPPRST 344
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 196-475 6.41e-08

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: 54.55  E-value: 6.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 196 YVHYPTISTDMLSVVKNQNP----GFNNAAFISRNALLSKAKLI-----------YYYLFAFVYGLVGSCSDIVMVNSSW 260
Cdd:cd03820   69 LLKYFKKVRRLRKYLKNNKPdvviSFRTSLLTFLALIGLKSKLIvwehnnyeaynKGLRRLLLRRLLYKRADKIVVLTEA 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 261 TLNHILSLWKvghcTNIVYPPcdvqTFLDIPLHEKKVTP-GHLLVSIGQFRPEKNHALQIKAFAKLLNEKAAelghsLKL 339
Cdd:cd03820  149 DKLKKYKQPN----SNVVVIP----NPLSFPSEEPSTNLkSKRILAVGRLTYQKGFDLLIEAWALIAKKHPD-----WKL 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 340 VLIGGCrnkDDEfrvNQLRSLSENLGVQENVEFKINISfdELKNYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNS 419
Cdd:cd03820  216 RIYGDG---PER---EELEKLIDKLGLEDRVKLLGPTK--NIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDC 287

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 123784012 420 -GGPKlDIVIPHEgqiTGFLAESE--EGYADSMAHILSlSAEERLQIRKNARASISRFS 475
Cdd:cd03820  288 pTGPS-EIIEDGE---NGLLVPNGdvDALAEALLRLME-DEELRKKMGKNARKNAERFS 341
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 237-491 1.04e-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: 53.89  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 237 YYLFAFVYGLVGSCSDIVMVNSSWTLNHILSLWKVGHCTNIVYPPCDVQTFLDIP---LHEKKVTPGHLLV----SIGqf 309
Cdd:cd03794  150 LKLLKKLERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPkdeLRKKLGLDDKFVVvyagNIG-- 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 310 rpeKNHALQ--IKAFAKLLNEKaaelghSLKLVLIGGCRNKDdefrvnQLRSLSENLGVQeNVEFKINISFDELKNYLSE 387
Cdd:cd03794  228 ---KAQGLEtlLEAAERLKRRP------DIRFLFVGDGDEKE------RLKELAKARGLD-NVTFLGRVPKEEVPELLSA 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 388 ATIGLHTMWNEHFGIGVV-----ECMAAGTVILAHNSGGPKLDIVIphegQITGFLAESEEgyADSMAH-ILSLSA--EE 459
Cdd:cd03794  292 ADVGLVPLKDNPANRGSSpsklfEYMAAGKPILASDDGGSDLAVEI----NGCGLVVEPGD--PEALADaILELLDdpEL 365

                        250       260       270
                 ....*....|....*....|....*....|..
gi 123784012 460 RLQIRKNARasisRFSDQEFEVAFLcsMEKLL 491
Cdd:cd03794  366 RRAMGENGR----ELAEEKFSREKL--ADRLL 391
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 306-474 1.27e-07

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: 53.51  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 306 IGQFRPEKNHALQIKAFAKLLNEKAAELghslklvLIGGcrnkdDEFRVNQLRSLSENLGVQENVEFKINIsfDELKNYL 385
Cdd:cd03819  188 VGRLSPEKGWLLLVDAAAELKDEPDFRL-------LVAG-----DGPERDEIRRLVERLGLRDRVTFTGFR--EDVPAAL 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 386 SEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPkLDIVIPHEgqiTGFLaeSEEGYADSMA-----HILSLSAEER 460
Cdd:cd03819  254 AASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGA-REIVVHGR---TGLL--VPPGDAEALAdairaAKLLPEAREK 327

                        170
                 ....*....|....
gi 123784012 461 LQIRKNARASISRF 474
Cdd:cd03819  328 LQAAAALTEAVREL 341
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 221-484 1.72e-07

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: 53.07  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 221 AFISRNALLSKAKLIYYYLFAFvYGlvgsCSDIVMVNSSWTLNHI-------LSLWKVGHCTNIVYP-PCDvQTFLDIPL 292
Cdd:cd03814  121 EYLSYYTLGPLSWLAWAYLRWF-HN----PFDTTLVPSPSIARELeghgferVRLWPRGVDTELFHPsRRD-AALRRRLG 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 293 HEKKVtpghLLVSIGQFRPEKNHALQIKAFAKLLNEKaaelghSLKLVLIGGCRNKddefRVNQLRSLsenlgvqeNVEF 372
Cdd:cd03814  195 PPGRP----LLLYVGRLAPEKNLEALLDADLPLAASP------PVRLVVVGDGPAR----AELEARGP--------DVIF 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 373 KINISFDELKNYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKlDIVIPHEgqiTGFLAES--EEGYADSMA 450
Cdd:cd03814  253 TGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPR-DIVRPGG---TGALVEPgdAAAFAAALR 328

                        250       260       270
                 ....*....|....*....|....*....|....
gi 123784012 451 HiLSLSAEERLQIRKNARASISRFSDQEFEVAFL 484
Cdd:cd03814  329 A-LLEDPELRRRMAARARAEAERYSWEAFLDNLL 361
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 275-478 9.79e-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: 51.18  E-value: 9.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 275 TNIVYPPCDVQTFLDIPLHEKKVTPGHLlVSIGQFRPEKNHALQIKAFAKLLNEkaaelGHSLKLVLIGGcrNKDDEFRV 354
Cdd:cd03813  269 TRVIPNGIDIQRFAPAREERPEKEPPVV-GLVGRVVPIKDVKTFIRAFKLVRRA-----MPDAEGWLIGP--EDEDPEYA 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 355 NQLRSLSENLGVQENVEFkinISFDELKNYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKlDIViphEGQI 434
Cdd:cd03813  341 QECKRLVASLGLENKVKF---LGFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCR-ELI---YGAD 413

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 123784012 435 TGFLAESE----EGYADSMAHILSL--SAEERLQIRKNARASISRFSDQE 478
Cdd:cd03813  414 DALGQAGLvvppADPEALAEALIKLlrDPELRQAFGEAGRKRVEKYYTLE 463
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 301-476 1.51e-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: 49.99  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 301 HLLVSIGQFRPEKNHALQIKAFAKLLNEkaaelGHSLKLVLIGgcrnKDDEFrvNQLRSLSENLGVQENVEFKINISfDE 380
Cdd:cd04949  161 NKIITISRLAPEKQLDHLIEAVAKAVKK-----VPEITLDIYG----YGEER--EKLKKLIEELHLEDNVFLKGYHS-NL 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 381 LKNYlSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSG-GPKlDIVIPHEgqiTGFLAESE--EGYADSMAHILsLSA 457
Cdd:cd04949  229 DQEY-QDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPS-ELIEDGE---NGYLIEKNniDALADKIIELL-NDP 302

                        170
                 ....*....|....*....
gi 123784012 458 EERLQIRKNARASISRFSD 476
Cdd:cd04949  303 EKLQQFSEESYKIAEKYST 321
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 276-473 1.68e-05

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: 46.93  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 276 NIVYPPCDVQTFLDIPLhekKVTPGH-LLVSIGQFRPEKNHALQIKAFaKLLNEKAAELghslKLVLIGGCRNKDDEFRV 354
Cdd:cd03792  175 NKDLSPADIRYYLEKPF---VIDPERpYILQVARFDPSKDPLGVIDAY-KLFKRRAEEP----QLVICGHGAVDDPEGSV 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 355 --NQLRSLSENlgvQENVEFKINISFDELKN-YLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKLDIviphE 431
Cdd:cd03792  247 vyEEVMEYAGD---DHDIHVLRLPPSDQEINaLQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQV----I 319

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 123784012 432 GQITGFLAESEEGYAdsmAHILSLSAEERL--QIRKNARASISR 473
Cdd:cd03792  320 DGETGFLVNSVEGAA---VRILRLLTDPELrrKMGLAAREHVRD 360
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 302-477 1.27e-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: 44.24  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 302 LLVSIGQFRPEKNHALQIKAFAKLLNEKaaelghSLKLVLIGGC--RNKDDEFRVNqlrslseNLGVQENVEfkinisfd 379
Cdd:cd03825  197 LFGAESVTKPRKGFDELIEALKLLATKD------DLLLVVFGKNdpQIVILPFDII-------SLGYIDDDE-------- 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 380 ELKNYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPkLDIVIPHEgqiTGFLA--ESEEGYADSMAHILSlSA 457
Cdd:cd03825  256 QLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGS-PEIVQHGV---TGYLVppGDVQALAEAIEWLLA-NP 330

                        170       180
                 ....*....|....*....|
gi 123784012 458 EERLQIRKNARASISRFSDQ 477
Cdd:cd03825  331 KERESLGERARALAENHFDQ 350
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
288-468 1.49e-04

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 44.01  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 288 LDIPLHEKkvtpghLLVSIGQFRPEKNHALQIKAFAKLLNEKAaelghSLKLVLIGGCRNKDD----EFRvNQLRSLSEN 363
Cdd:PRK15484 187 LNISPDET------VLLYAGRISPDKGILLLMQAFEKLATAHS-----NLKLVVVGDPTASSKgekaAYQ-KKVLEAAKR 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 364 LGVQenVEFKINISFDELKNYLSEAT-IGLHTMWNEHFGIGVVECMAAGTVILAHNSGGpkldiviphegqITGFLAESE 442
Cdd:PRK15484 255 IGDR--CIMLGGQPPEKMHNYYPLADlVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGG------------ITEFVLEGI 320

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 123784012 443 EGY-------ADSMAHILS--LSAEERLQIRKNAR 468
Cdd:PRK15484 321 TGYhlaepmtSDSIISDINrtLADPELTQIAEQAK 355
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 294-426 1.24e-03

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 41.12  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 294 EKKVTPGHllvsIGQFRPEKNHALQIKAFAKLLNEkaaelGHSLKLVLIGgcrnkDDEFRvNQLRSLSENLGVQENVEF- 372
Cdd:cd03812  189 EDKLVLGH----VGRFNEQKNHSFLIDIFEELKKK-----NPNVKLVLVG-----EGELK-EKIKEKVKELGLEDKVIFl 253

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 123784012 373 --KINISfdelkNYLSEATIGLHTMWNEHFGIGVVECMAAGTVILAHNSGGPKLDI 426
Cdd:cd03812  254 gfRNDVS-----EILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDI 304
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 398-475 1.32e-03

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 41.23  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123784012 398 EHFGIGVVECMAAGTVILAHNSGGPKlDIVIPHEGQITGFLAESEEgYADSMAHILSL--SAEERLQIRKNARASISRFS 475
Cdd:PLN02871 342 ETLGFVVLEAMASGVPVVAARAGGIP-DIIPPDQEGKTGFLYTPGD-VDDCVEKLETLlaDPELRERMGAAAREEVEKWD 419
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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