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Conserved domains on  [gi|21358031|ref|NP_649340|]
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ALG11, alpha-1,2-mannosyltransferase, isoform A [Drosophila melanogaster]

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
PubMed:  22387211|12691742|10521532|16037492
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 ...
 44-463 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: 710.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  44 INVGIFHPYCNAGGGGERVLWCAVRALQEKYQNARMVIYTGDIDASPNSILQKAKNVFNIAVDSDNVKFVFLKQRHWIEA 123
Cdd:cd03806   1 ITVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFFLLKYRKLVEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 124 KNYPHFTLLGQSIGSMVVGLEALCRFPPDIYIDTMGYAFTYPLFRYLAQSKVGCYVHYPVISTDMLKRVQQRQMSHNNKK 203
Cdd:cd03806  81 KTYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGGCPVVAYVHYPTISTDMLNKVRSREASYNNDS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 204 YVARNPFLTWTKLAYYRLFSRMYKWVGCCAETIMVNSSWTENHILQLWDVPFKTHRVYPPCEVSHLKSLQHTEKGDEFII 283
Cdd:cd03806 161 TIARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPIDEKTRENQI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 284 LSVGQFRPEKDHPLQLQAIYELRTLLAQDEalWNQIKLVIVGSCRNEDDYERLKNMQDLTKHLSLENNVQFSVNVPYEDL 363
Cdd:cd03806 241 LSIAQFRPEKNHPLQLRAFAELLKRLPESI--RSNPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEFVVDAPYEEL 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 364 LKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGPLLDIVETSAGSQNGFLATDAVEYAENILNII-VNNSEMN 442
Cdd:cd03806 319 KELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILtLSEEERL 398

                       410       420
                ....*....|....*....|.
gi 21358031 443 GIRNAARASVERFSEQEFEKN 463
Cdd:cd03806 399 QRREAARSSAERFSDEEFERD 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 ...
 44-463 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: 710.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  44 INVGIFHPYCNAGGGGERVLWCAVRALQEKYQNARMVIYTGDIDASPNSILQKAKNVFNIAVDSDNVKFVFLKQRHWIEA 123
Cdd:cd03806   1 ITVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFFLLKYRKLVEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 124 KNYPHFTLLGQSIGSMVVGLEALCRFPPDIYIDTMGYAFTYPLFRYLAQSKVGCYVHYPVISTDMLKRVQQRQMSHNNKK 203
Cdd:cd03806  81 KTYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGGCPVVAYVHYPTISTDMLNKVRSREASYNNDS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 204 YVARNPFLTWTKLAYYRLFSRMYKWVGCCAETIMVNSSWTENHILQLWDVPFKTHRVYPPCEVSHLKSLQHTEKGDEFII 283
Cdd:cd03806 161 TIARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPIDEKTRENQI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 284 LSVGQFRPEKDHPLQLQAIYELRTLLAQDEalWNQIKLVIVGSCRNEDDYERLKNMQDLTKHLSLENNVQFSVNVPYEDL 363
Cdd:cd03806 241 LSIAQFRPEKNHPLQLRAFAELLKRLPESI--RSNPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEFVVDAPYEEL 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 364 LKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGPLLDIVETSAGSQNGFLATDAVEYAENILNII-VNNSEMN 442
Cdd:cd03806 319 KELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILtLSEEERL 398

                       410       420
                ....*....|....*....|.
gi 21358031 443 GIRNAARASVERFSEQEFEKN 463
Cdd:cd03806 399 QRREAARSSAERFSDEEFERD 419
PLN02949 PLN02949
transferase, transferring glycosyl groups
 24-473 0e+00

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 536.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031   24 FLRQWLLGRKNKLHTssenginVGIFHPYCNAGGGGERVLWCAVRALQEKYQNARMVIYTGDIDASPNSILQKAKNVFNI 103
Cdd:PLN02949  21 IALSVLRARRSRKRA-------VGFFHPYTNDGGGGERVLWCAVRAIQEENPDLDCVIYTGDHDASPDSLAARARDRFGV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  104 AVDSDnVKFVFLKQRHWIEAKNYPHFTLLGQSIGSMVVGLEALCRFPPDIYIDTMGYAFTYPLFRyLAQSKVGCYVHYPV 183
Cdd:PLN02949  94 ELLSP-PKVVHLRKRKWIEEETYPRFTMIGQSLGSVYLAWEALCKFTPLYFFDTSGYAFTYPLAR-LFGCKVVCYTHYPT 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  184 ISTDMLKRVQQRQMSHNNKKYVARNPFLTWTKLAYYRLFSRMYKWVGCCAETIMVNSSWTENHILQLWDVPFKTHRVYPP 263
Cdd:PLN02949 172 ISSDMISRVRDRSSMYNNDASIARSFWLSTCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPERIKRVYPP 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  264 CEVSHLKSLQHTEKGDEFIILSVGQFRPEKDHPLQLQAIYELRTLLAQDEALWnqiKLVIVGSCRNEDDYERLKNMQDLT 343
Cdd:PLN02949 252 CDTSGLQALPLERSEDPPYIISVAQFRPEKAHALQLEAFALALEKLDADVPRP---KLQFVGSCRNKEDEERLQKLKDRA 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  344 KHLSLENNVQFSVNVPYEDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGPLLDIVETSAGSQNGFLATD 423
Cdd:PLN02949 329 KELGLDGDVEFHKNVSYRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIVLDEDGQQTGFLATT 408

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 21358031  424 AVEYAENILNII-VNNSEMNGIRNAARASVERFSEQEFEKNFLRAVSTLFT 473
Cdd:PLN02949 409 VEEYADAILEVLrMRETERLEIAAAARKRANRFSEQRFNEDFKDAIRPILN 459
ALG11_N pfam15924
ALG11 mannosyltransferase N-terminus;
46-251 2.87e-147

ALG11 mannosyltransferase N-terminus;


Pssm-ID: 464944  Cd Length: 209  Bit Score: 418.80  E-value: 2.87e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031    46 VGIFHPYCNAGGGGERVLWCAVRALQEKYQNARMVIYTGDIDASPNSILQKAKNVFNIAVDSDNVKFVFLKQRHWIEAKN 125
Cdd:pfam15924   4 VGFFHPYCNAGGGGERVLWCAVRATQRRYPNAICVVYTGDIDASKEEILAKVKSRFNIELDPSRIVFVYLRKRKLVEAST 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031   126 YPHFTLLGQSIGSMVVGLEALCRFPPDIYIDTMGYAFTYPLFRYLAQSKVGCYVHYPVISTDMLKRVQQRQMSHNNKKYV 205
Cdd:pfam15924  84 YPRFTLLGQSLGSIILAWEALSKLVPDVFIDTMGYAFTYPLVRLLGGCPVGAYVHYPTISTDMLSRVSSREAGYNNDSAI 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 21358031   206 ARNPFLTWTKLAYYRLFSRMYKWVGCCAETIMVNSSWTENHILQLW 251
Cdd:pfam15924 164 ASSGLLSKAKLIYYRLFALLYGLVGSFADVVMVNSSWTQNHIRSLW 209
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 360-471 9.97e-12

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 61.93  E-value: 9.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 360 YEDLLK-LYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGpLLDIVEtsaGSQNGFL--ATDAVEYAENILNIIV 436
Cdd:COG0438  10 LDLLLEaLLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGG-LPEVIE---DGETGLLvpPGDPEALAEAILRLLE 85

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 21358031 437 NNSEMNGIRNAARASVE-RFSEQEFEKNFLRAVSTL 471
Cdd:COG0438  86 DPELRRRLGEAARERAEeRFSWEAIAERLLALYEEL 121
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 380-471 7.96e-04

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 42.08  E-value: 7.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031    380 EHFGIGIVESMAAGLIMVAHKSGGPlldiVETSAGSQNGFLAT--DAVEYAENILNIIVNN-----SEMNGIRNaarasV 452
Cdd:TIGR02468  582 EPFGLTLIEAAAHGLPMVATKNGGP----VDIHRVLDNGLLVDphDQQAIADALLKLVADKqlwaeCRQNGLKN-----I 652

                           90
                   ....*....|....*....
gi 21358031    453 ERFSEQEFEKNFLRAVSTL 471
Cdd:TIGR02468  653 HLFSWPEHCKTYLSRIASC 671
 
Name Accession Description Interval E-value
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
 44-463 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: 710.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  44 INVGIFHPYCNAGGGGERVLWCAVRALQEKYQNARMVIYTGDIDASPNSILQKAKNVFNIAVDSDNVKFVFLKQRHWIEA 123
Cdd:cd03806   1 ITVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFFLLKYRKLVEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 124 KNYPHFTLLGQSIGSMVVGLEALCRFPPDIYIDTMGYAFTYPLFRYLAQSKVGCYVHYPVISTDMLKRVQQRQMSHNNKK 203
Cdd:cd03806  81 KTYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGGCPVVAYVHYPTISTDMLNKVRSREASYNNDS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 204 YVARNPFLTWTKLAYYRLFSRMYKWVGCCAETIMVNSSWTENHILQLWDVPFKTHRVYPPCEVSHLKSLQHTEKGDEFII 283
Cdd:cd03806 161 TIARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPIDEKTRENQI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 284 LSVGQFRPEKDHPLQLQAIYELRTLLAQDEalWNQIKLVIVGSCRNEDDYERLKNMQDLTKHLSLENNVQFSVNVPYEDL 363
Cdd:cd03806 241 LSIAQFRPEKNHPLQLRAFAELLKRLPESI--RSNPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEFVVDAPYEEL 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 364 LKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGPLLDIVETSAGSQNGFLATDAVEYAENILNII-VNNSEMN 442
Cdd:cd03806 319 KELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILtLSEEERL 398

                       410       420
                ....*....|....*....|.
gi 21358031 443 GIRNAARASVERFSEQEFEKN 463
Cdd:cd03806 399 QRREAARSSAERFSDEEFERD 419
PLN02949 PLN02949
transferase, transferring glycosyl groups
 24-473 0e+00

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 536.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031   24 FLRQWLLGRKNKLHTssenginVGIFHPYCNAGGGGERVLWCAVRALQEKYQNARMVIYTGDIDASPNSILQKAKNVFNI 103
Cdd:PLN02949  21 IALSVLRARRSRKRA-------VGFFHPYTNDGGGGERVLWCAVRAIQEENPDLDCVIYTGDHDASPDSLAARARDRFGV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  104 AVDSDnVKFVFLKQRHWIEAKNYPHFTLLGQSIGSMVVGLEALCRFPPDIYIDTMGYAFTYPLFRyLAQSKVGCYVHYPV 183
Cdd:PLN02949  94 ELLSP-PKVVHLRKRKWIEEETYPRFTMIGQSLGSVYLAWEALCKFTPLYFFDTSGYAFTYPLAR-LFGCKVVCYTHYPT 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  184 ISTDMLKRVQQRQMSHNNKKYVARNPFLTWTKLAYYRLFSRMYKWVGCCAETIMVNSSWTENHILQLWDVPFKTHRVYPP 263
Cdd:PLN02949 172 ISSDMISRVRDRSSMYNNDASIARSFWLSTCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPERIKRVYPP 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  264 CEVSHLKSLQHTEKGDEFIILSVGQFRPEKDHPLQLQAIYELRTLLAQDEALWnqiKLVIVGSCRNEDDYERLKNMQDLT 343
Cdd:PLN02949 252 CDTSGLQALPLERSEDPPYIISVAQFRPEKAHALQLEAFALALEKLDADVPRP---KLQFVGSCRNKEDEERLQKLKDRA 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  344 KHLSLENNVQFSVNVPYEDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGPLLDIVETSAGSQNGFLATD 423
Cdd:PLN02949 329 KELGLDGDVEFHKNVSYRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIVLDEDGQQTGFLATT 408

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 21358031  424 AVEYAENILNII-VNNSEMNGIRNAARASVERFSEQEFEKNFLRAVSTLFT 473
Cdd:PLN02949 409 VEEYADAILEVLrMRETERLEIAAAARKRANRFSEQRFNEDFKDAIRPILN 459
ALG11_N pfam15924
ALG11 mannosyltransferase N-terminus;
46-251 2.87e-147

ALG11 mannosyltransferase N-terminus;


Pssm-ID: 464944  Cd Length: 209  Bit Score: 418.80  E-value: 2.87e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031    46 VGIFHPYCNAGGGGERVLWCAVRALQEKYQNARMVIYTGDIDASPNSILQKAKNVFNIAVDSDNVKFVFLKQRHWIEAKN 125
Cdd:pfam15924   4 VGFFHPYCNAGGGGERVLWCAVRATQRRYPNAICVVYTGDIDASKEEILAKVKSRFNIELDPSRIVFVYLRKRKLVEAST 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031   126 YPHFTLLGQSIGSMVVGLEALCRFPPDIYIDTMGYAFTYPLFRYLAQSKVGCYVHYPVISTDMLKRVQQRQMSHNNKKYV 205
Cdd:pfam15924  84 YPRFTLLGQSLGSIILAWEALSKLVPDVFIDTMGYAFTYPLVRLLGGCPVGAYVHYPTISTDMLSRVSSREAGYNNDSAI 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 21358031   206 ARNPFLTWTKLAYYRLFSRMYKWVGCCAETIMVNSSWTENHILQLW 251
Cdd:pfam15924 164 ASSGLLSKAKLIYYRLFALLYGLVGSFADVVMVNSSWTQNHIRSLW 209
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 217-466 5.16e-27

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: 111.48  E-value: 5.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 217 AYYRLFSRMYKWVGCCAETImVNSSWTENHILQLWDVPF-KTHRVYPPCEVSHLKSLQHTEKG---DEFIILSVGQFRPE 292
Cdd:cd03801 126 AERRLLARAEALLRRADAVI-AVSEALRDELRALGGIPPeKIVVIPNGVDLERFSPPLRRKLGippDRPVLLFVGRLSPR 204

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 293 KDHPLQLQAIYELRtllaqdeALWNQIKLVIVGscRNEDDYERLKNMQdltkhLSLENNVQFSVNVPYEDLLKLYQTAHI 372
Cdd:cd03801 205 KGVDLLLEALAKLL-------RRGPDVRLVIVG--GDGPLRAELEELE-----LGLGDRVRFLGFVPDEELPALYAAADV 270

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 373 GIHTMWNEHFGIGIVESMAAGLIMVAHKSGGplldIVETSAGSQNGFLA--TDAVEYAENILNIIVNNSEMNGIRNAARA 450
Cdd:cd03801 271 FVLPSRYEGFGLVVLEAMAAGLPVVATDVGG----LPEVVEDGEGGLVVppDDVEALADALLRLLADPELRARLGRAARE 346

                       250
                ....*....|....*..
gi 21358031 451 SV-ERFSEQEFEKNFLR 466
Cdd:cd03801 347 RVaERFSWERVAERLLD 363
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 279-449 1.44e-26

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: 105.05  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031   279 DEFIILSVGQFRPEKDHPLQLQAiyeLRTLLAQDEalwnQIKLVIVGscrnedDYERLKNMQDLTKHLSLENNVQFSVNV 358
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKA---FALLKEKNP----NLKLVIAG------DGEEEKRLKKLAEKLGLGDNVIFLGFV 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031   359 PYEDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGPlLDIVEtsAGsQNGFLA--TDAVEYAENILNIIV 436
Cdd:pfam00534  68 SDEDLPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGP-PEVVK--DG-ETGFLVkpNNAEALAEAIDKLLE 143

                         170
                  ....*....|...
gi 21358031   437 NNSEMNGIRNAAR 449
Cdd:pfam00534 144 DEELRERLGENAR 156
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 45-464 4.06e-25

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: 106.52  E-value: 4.06e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  45 NVGIFHPYCnaG-GGGERVLWCAVRALQEkyQNARMVIYTGDIDasPNSILQKAKN-VFNIAVDSDnvkfvflkqrhWIE 122
Cdd:cd03805   2 RVAFLHPDL--GiGGAERLVVDAALALQS--RGHEVTIYTSHHD--PSHCFEETKDgTLPVRVRGD-----------WLP 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 123 AKNYPHFTLLGQSIGSMVVGLEALCRF--PPDIYI-DTMgyAFTYPLFRYLAQSKVGCYVHYPvistDMLkrVQQRQmsh 199
Cdd:cd03805  65 RSIFGRFHALCAYLRMLYLALYLLLFSgeKYDVFIvDQV--SACVPLLKLFRPSKILFYCHFP----DQL--LAQRK--- 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 200 nnkkyvarnpflTWTKLAYYRLFSRMYKWVGCCAETIMVNSSWTENHILQLW-DVPFKTHRV-YPPCEVSHLKSLQHTE- 276
Cdd:cd03805 134 ------------SLLKRLYRKPFDWLEEFTTGMADQIVVNSNFTAGVFKKTFpSLAKNPPEVlYPCVDTDSFDSTSEDPd 201

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 277 ------KGDEFIILSVGQFRPEKDHPLQLQAIYELRtllaQDEALWNQIKLVIVGSC--RNEDDYERLKNMQDL-TKHLS 347
Cdd:cd03805 202 pgdliaKSNKKFFLSINRFERKKNIALAIEAFAKLK----QKLPEFENVRLVIAGGYdpRVAENVEYLEELQRLaEELLN 277

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 348 LENNVQFSVNVPyeDLLK--LYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGPLldivETSAGSQNGFL-ATDA 424
Cdd:cd03805 278 VEDQVLFLRSIS--DSQKeqLLSSALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPL----ETVVEGVTGFLcEPTP 351

                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 21358031 425 VEYAENILNIIVNNSEMNGIRNAARASV-ERFSEQEFEKNF 464
Cdd:cd03805 352 EAFAEAMLKLANDPDLADRMGAAGRKRVkEKFSREAFAERL 392
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 213-459 1.25e-19

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: 90.11  E-value: 1.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 213 WTKLAYYRLFSRMYKWVGCCAETIMVNSSWTENHILQLWDVPFKTHRVYPPCeVSHLKS-------LQHTEKGDEFIILS 285
Cdd:cd03809 119 FFPKRFRLYYRLLLPISLRRADAIITVSEATRDDIIKFYGVPPEKIVVIPLG-VDPSFFppesaavLIAKYLLPEPYFLY 197

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 286 VGQFRPEKDHPLQLQAIYELRtllaqdeALWNQIKLVIVGSCRNEDDYErlknmQDLTKHLSLENNVQFSVNVPYEDLLK 365
Cdd:cd03809 198 VGTLEPRKNHERLLKAFALLK-------KQGGDLKLVIVGGKGWEDEEL-----LDLVKKLGLGGRVRFLGYVSDEDLPA 265

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 366 LYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAhkSGGPLLdiVETSAGSQNGFLATDAVEYAENILNIIVNNSEMNGIR 445
Cdd:cd03809 266 LYRGARAFVFPSLYEGFGLPVLEAMACGTPVIA--SNISVL--PEVAGDAALYFDPLDPESIADAILRLLEDPSLREELI 341

                       250
                ....*....|....
gi 21358031 446 NAARASVERFSEQE 459
Cdd:cd03809 342 RKGLERAKKFSWEK 355
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 279-456 1.40e-17

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: 84.21  E-value: 1.40e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 279 DEFIILSVGQFRPEKDHPLQLQAiyelrtlLAQDEALWNQIKLVIVGSCRNEDDYERLKNMQDLTKHLSLENNVQFSVNV 358
Cdd:cd03800 219 DKPVVLALGRLDPRKGIDTLVRA-------FAQLPELRELANLVLVGGPSDDPLSMDREELAELAEELGLIDRVRFPGRV 291

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 359 PYEDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGPlLDIVetSAGsQNGFL--ATDAVEYAENILNIIV 436
Cdd:cd03800 292 SRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGL-QDIV--RDG-RTGLLvdPHDPEALAAALRRLLD 367

                       170       180
                ....*....|....*....|.
gi 21358031 437 NNSEMNGI-RNAARASVERFS 456
Cdd:cd03800 368 DPALWQRLsRAGLERARAHYT 388
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 279-456 6.95e-15

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: 75.78  E-value: 6.95e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 279 DEFIILSVGQFRPEKDHPLQLQAIYELRTLlaqdealwNQIKLVIVGscrneDDYERlKNMQDLTKHLSLENNVQFSVNV 358
Cdd:cd03817 200 DEPILLYVGRLAKEKNIDFLLRAFAELKKE--------PNIKLVIVG-----DGPER-EELKELARELGLADKVIFTGFV 265

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 359 PYEDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGpLLDIVETsagSQNGFL-ATDAVEYAENILNIIVN 437
Cdd:cd03817 266 PREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPA-ASELVED---GENGFLfEPNDETLAEKLLHLREN 341

                       170
                ....*....|....*....
gi 21358031 438 NSEMNGIRNAARASVERFS 456
Cdd:cd03817 342 LELLRKLSKNAEISAREFA 360
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 279-471 1.17e-14

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: 75.49  E-value: 1.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 279 DEFIILSVGQFRPEKDHPLQLQAiYELRTLLAQDealwnqIKLVIVGscrnedDYERLKNMQDLTKHLSLENNVQFSVNV 358
Cdd:cd03798 199 DAFVILFVGRLIPRKGIDLLLEA-FARLAKARPD------VVLLIVG------DGPLREALRALAEDLGLGDRVTFTGRL 265

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 359 PYEDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGPlLDIVETSAgsqNGFLA--TDAVEYAEnILNIIV 436
Cdd:cd03798 266 PHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGI-PEVVGDPE---TGLLVppGDADALAA-ALRRAL 340

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 21358031 437 NNSEMNGIRNAARASV-ERFSEQEFEKNFLRAVSTL 471
Cdd:cd03798 341 AEPYLRELGEAARARVaERFSWVKAADRIAAAYRDV 376
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
280-435 2.72e-14

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 69.85  E-value: 2.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031   280 EFIILSVGQFRPEKDHPLQL-QAIYELRtllAQDealwNQIKLVIVGscrnEDDYERLKNmqdltKHLSLENNVQFsvnV 358
Cdd:pfam13692   1 RPVILFVGRLHPNVKGVDYLlEAVPLLR---KRD----NDVRLVIVG----DGPEEELEE-----LAAGLEDRVIF---T 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031   359 PY-EDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGplldIVETSAGsQNGFLAT--DAVEYAENILNII 435
Cdd:pfam13692  62 GFvEDLAELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGG----IPELVDG-ENGLLVPpgDPEALAEAILRLL 136
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 56-461 1.01e-12

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: 69.31  E-value: 1.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  56 GGGGERVLWCAVRALQEKYQNARMVIYTGDIDASPNSILQKAKNVFNIAVDSDNVKFV---FLKQRHWIEaknyphftll 132
Cdd:cd03811  11 GGGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLlkaILKLKRILK---------- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 133 gqsigsmvvglealcRFPPDIYIDTMGYAFTYPLFRYLAQSKVGCYVHYPVISTDMLKRvqqrqmshnnkkyvarnpflt 212
Cdd:cd03811  81 ---------------RAKPDVVISFLGFATYIVAKLAAARSKVIAWIHSSLSKLYYLKK--------------------- 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 213 wtKLAYYRLFSRMYKWVGCcaetimvNSSWTENHILQL-WDVPFKTHRVYPPCEVSHLKSL----QHTEKGDEFIILSVG 287
Cdd:cd03811 125 --KLLLKLKLYKKADKIVC-------VSKGIKEDLIRLgPSPPEKIEVIYNPIDIDRIRALakepILNEPEDGPVILAVG 195

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 288 QFRPEKDHPLQLQAIYELRTLLAqdealwnQIKLVIVGscrNEDDYERLKNmqdLTKHLSLENNVQF---SVNvPYedll 364
Cdd:cd03811 196 RLDPQKGHDLLIEAFAKLRKKYP-------DVKLVILG---DGPLREELEK---LAKELGLAERVIFlgfQSN-PY---- 257

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 365 KLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGPlLDIVEtsaGSQNGFLAT-DAVEYAENILNIIVNNSEMNG 443
Cdd:cd03811 258 PYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGP-REILD---DGENGLLVPdGDAAALAGILAALLQKKLDAA 333

                       410
                ....*....|....*...
gi 21358031 444 IRNAARASVERFSEQEFE 461
Cdd:cd03811 334 LRERLAKAQEAVFREYTI 351
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 360-471 9.97e-12

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 61.93  E-value: 9.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 360 YEDLLK-LYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGpLLDIVEtsaGSQNGFL--ATDAVEYAENILNIIV 436
Cdd:COG0438  10 LDLLLEaLLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGG-LPEVIE---DGETGLLvpPGDPEALAEAILRLLE 85

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 21358031 437 NNSEMNGIRNAARASVE-RFSEQEFEKNFLRAVSTL 471
Cdd:COG0438  86 DPELRRRLGEAARERAEeRFSWEAIAERLLALYEEL 121
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 54-458 1.13e-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: 66.11  E-value: 1.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  54 NAGGGGERVLWCAVRALQEKYQNArMVIYTGDIDASPNsilqkaknvFNIavdSDNVKFVFLKQRHwieaknYPHFTLLG 133
Cdd:cd03820  10 SNAGGAERVAINLANHLAKKGYDV-TIISLDSAEKPPF---------YEL---DDNIKIKNLGDRK------YSHFKLLL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 134 QSIGSMVVGLEALCRFPPDIYIDTMGYAFTYPLFRYLAQSKVGCYvhypvistdmlkrvqqrqmsHNNkkYVARNPFLTW 213
Cdd:cd03820  71 KYFKKVRRLRKYLKNNKPDVVISFRTSLLTFLALIGLKSKLIVWE--------------------HNN--YEAYNKGLRR 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 214 tklayYRLFSRMYKWvgccAETIMVNSSWTENHILQLWDVPFKThrVYPPC-EVSHLKSLQHTEKgdefIILSVGQFRPE 292
Cdd:cd03820 129 -----LLLRRLLYKR----ADKIVVLTEADKLKKYKQPNSNVVV--IPNPLsFPSEEPSTNLKSK----RILAVGRLTYQ 193

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 293 KDHPLQLQAIyelrTLLAQDEALWnqiKLVIVGSCrneddyERLKNMQDLTKHLSLENNVQFSVNVpyEDLLKLYQTAHI 372
Cdd:cd03820 194 KGFDLLIEAW----ALIAKKHPDW---KLRIYGDG------PEREELEKLIDKLGLEDRVKLLGPT--KNIAEEYANSSI 258

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 373 GIHTMWNEHFGIGIVESMAAGLIMVAHKS-GGPlLDIVEtsaGSQNGFL--ATDAVEYAENILNIIVNNSEMNGIRNAAR 449
Cdd:cd03820 259 FVLSSRYEGFPMVLLEAMAYGLPIISFDCpTGP-SEIIE---DGENGLLvpNGDVDALAEALLRLMEDEELRKKMGKNAR 334


                ....*....
gi 21358031 450 ASVERFSEQ 458
Cdd:cd03820 335 KNAERFSIE 343
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 284-414 1.44e-11

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: 64.35  E-value: 1.44e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 284 LSVGQFRPEKDHPLQLQAIYELRTLLAQdealwnqIKLVIVGscrneDDYERLKNMQDLTKHLSLENNVQFSVNVPYEDL 363
Cdd:cd01635 114 VSVGRLVPEKGIDLLLEALALLKARLPD-------LVLVLVG-----GGGEREEEEALAAALGLLERVVIIGGLVDDEVL 181

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 21358031 364 LKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGPLLDIVETSAG 414
Cdd:cd01635 182 ELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENG 232
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 276-456 1.47e-11

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 65.80  E-value: 1.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 276 EKGDEFIILSVGQFRPEKDHPLQLQAiyeLRTLLAQDEalwnQIKLVIVGSCRNEDDYERlknmqdLTKHLSLENNVQFS 355
Cdd:cd03807 186 LAEDRRVIGIVGRLHPVKDHSDLLRA---AALLVETHP----DLRLLLVGRGPERPNLER------LLLELGLEDRVHLL 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 356 VNVPyeDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGpLLDIVETSAGSqnGFLATDAVEYAENILNII 435
Cdd:cd03807 253 GERS--DVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGG-AAELVDDGTGF--LVPAGDPQALADAIRALL 327

                       170       180
                ....*....|....*....|..
gi 21358031 436 VNNSEMNGIRNAARASV-ERFS 456
Cdd:cd03807 328 EDPEKRARLGRAARERIaNEFS 349
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 219-459 3.53e-10

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


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 61.46  E-value: 3.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 219 YRLFSRMYKWVGCCAETIMVNSSWTENHILQLWDVPFKTHRVYPPCEV--SHLKSLQHTEKGDEFIILSVGQFRPEKDHP 296
Cdd:cd03808 126 RLLYLLLEKLALLFTDKVIFVNEDDRDLAIKKGIIKKKKTVLIPGSGVdlDRFQYSPESLPSEKVVFLFVARLLKDKGID 205

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 297 LQLQAiyeLRTLLAQDEalwnQIKLVIVGscrnedDYERLKNMQDLTKHLSLENNVQF---SVNVPyedllKLYQTAHIG 373
Cdd:cd03808 206 ELIEA---AKILKKKGP----NVRFLLVG------DGELENPSEILIEKLGLEGRIEFlgfRSDVP-----ELLAESDVF 267

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 374 IHTMWNEHFGIGIVESMAAGLIMVAHKSGGPlLDIVEtsAGsQNGFLAT--DAVEYAENILNIIVNNSEMNGIRNAARAS 451
Cdd:cd03808 268 VLPSYREGLPRSLLEAMAAGRPVITTDVPGC-RELVI--DG-VNGFLVPpgDVEALADAIEKLIEDPELRKEMGEAARKR 343


                ....*....
gi 21358031 452 VE-RFSEQE 459
Cdd:cd03808 344 VEeKFDEEK 352
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 260-464 4.15e-10

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: 61.15  E-value: 4.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 260 VYPPCEVSHLKSLQhtEKGDEFiiLSVGQFRPEKDHPLQLQAIYELrtllaqdealwnQIKLVIVGscrNEDDYERLKNM 339
Cdd:cd03804 183 IYPPVDTDAFAPAA--DKEDYY--LTASRLVPYKRIDLAVEAFNEL------------PKRLVVIG---DGPDLDRLRAM 243

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 340 QDltkhlsleNNVQFSVNVPYEDLLKLYQTAHIGIHtMWNEHFGIGIVESMAAGLIMVAHKSGGplldIVETSAGSQNGF 419
Cdd:cd03804 244 AS--------PNVEFLGYQPDEVLKELLSKARAFVF-AAEEDFGIVPVEAQACGTPVIAFGKGG----ALETVRPGPTGI 310

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 21358031 420 LatdaveYAE---NILNIIVNNSEMNGIR---NAARASVERFSEQEFEKNF 464
Cdd:cd03804 311 L------FGEqtvESLKAAVEEFEQNFDRfkpQAIRANAERFSRARFRQEI 355
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 212-457 2.24e-09

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: 58.92  E-value: 2.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 212 TWTKLAYYRLFsrMYKWVGCcAETIMVNSSWTENHILQLWD------VPFKTHRvyPPCEVSHLKSLQHTEKGDEFIILS 285
Cdd:cd03821 135 HWKKRIALHLI--ERRNLNN-AALVHFTSEQEADELRRFGLeppiavIPNGVDI--PEFDPGLRDRRKHNGLEDRRIILF 209

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 286 VGQFRPEKDHPLQLQAiyeLRTLLAQdealWNQIKLVIVGScrNEDDYERLknMQDLTKHLsLENNVQFSVNVPYEDLLK 365
Cdd:cd03821 210 LGRIHPKKGLDLLIRA---ARKLAEQ----GRDWHLVIAGP--DDGAYPAF--LQLQSSLG-LGDRVTFTGPLYGEAKWA 277

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 366 LYQTAHIGIHTMWNEHFGIGIVESMAAGL-IMVAHKSGGPllDIVETSAGsqnGFLATDAVEYAENILNIIVNNSE---M 441
Cdd:cd03821 278 LYASADLFVLPSYSENFGNVVAEALACGLpVVITDKCGLS--ELVEAGCG---VVVDPNVSSLAEALAEALRDPADrkrL 352

                       250
                ....*....|....*.
gi 21358031 442 NGIRNAARASVERFSE 457
Cdd:cd03821 353 GEMARRARQVEENFSW 368
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 277-456 7.44e-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: 57.45  E-value: 7.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 277 KGDEFIILSVGQFRPEKDHPLQLQAIYELRTllaqdeaLWNQIKLVIVGscrnedDYERLKNMQDLTKHLSLENNVQFSV 356
Cdd:cd04951 185 KNDEFVILNVGRLTEAKDYPNLLLAISELIL-------SKNDFKLLIAG------DGPLRNELERLICNLNLVDRVILLG 251

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 357 NVpyEDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGG------PLLDIVETSagsqngflatDAVEYAEN 430
Cdd:cd04951 252 QI--SNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGvaevvgDHNYVVPVS----------DPQLLAEK 319

                       170       180
                ....*....|....*....|....*..
gi 21358031 431 ILNIIVNNSEMNGI-RNAARASVERFS 456
Cdd:cd04951 320 IKEIFDMSDEERDIlGNKNEYIAKNFS 346
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 259-456 1.15e-08

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: 56.98  E-value: 1.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 259 RVYPPCEVSHLKSlQHTEKGDEFIILSVGQFRPEKDHPLQLQAIYELRtllaqdealwNQI--KLVIVGscrnedDYERL 336
Cdd:cd04962 176 DVFKRKPAGALKR-RLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVR----------RKIpaKLLLVG------DGPER 238

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 337 KNMQDLTKHLSLENNVQFSVNVPyeDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGplldIVETSAGSQ 416
Cdd:cd04962 239 VPAEELARELGVEDRVLFLGKQD--DVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGG----IPEVVKHGE 312

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21358031 417 NGFL-----ATDAVEYAENILNIIVNNSEMNgiRNAARASVERFS 456
Cdd:cd04962 313 TGFLsdvgdVDAMAKSALSILEDDELYNRMG--RAARKRAAERFD 355
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 203-467 2.70e-08

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: 55.76  E-value: 2.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 203 KYVARN--PFLTWTKLAYYRLFSRmykwvgcCAETIMVNSSWT----ENHI---LQLWDVPFKTHRVYP-PCEVSHLKSL 272
Cdd:cd03814 121 EYLSYYtlGPLSWLAWAYLRWFHN-------PFDTTLVPSPSIarelEGHGferVRLWPRGVDTELFHPsRRDAALRRRL 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 273 QHtekGDEFIILSVGQFRPEKDHPLQLQAIyelRTLLAQDealwnQIKLVIVGSCRNEddyERLKNMQDltkhlslenNV 352
Cdd:cd03814 194 GP---PGRPLLLYVGRLAPEKNLEALLDAD---LPLAASP-----PVRLVVVGDGPAR---AELEARGP---------DV 250

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 353 QFsvnVPY---EDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGPlLDIVEtsaGSQNGFL--ATDAVEY 427
Cdd:cd03814 251 IF---TGFltgEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGP-RDIVR---PGGTGALvePGDAAAF 323

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 21358031 428 AENILNIIVNNSEMNGIRNAARASVERFSEQEFEKNFLRA 467
Cdd:cd03814 324 AAALRALLEDPELRRRMAARARAEAERYSWEAFLDNLLDY 363
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 219-465 3.28e-08

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: 55.43  E-value: 3.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 219 YRLFSRMYKWVGCCAETIMVNSSWTENHILQLWDVPFKTHRVYPPCEVSHLKSL------QHTEKGDEFIILSVGQFRPE 292
Cdd:cd03794 150 LKLLKKLERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPpkdelrKKLGLDDKFVVVYAGNIGKA 229

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 293 KDhplqLQAIYELRTLLAQDealwNQIKLVIVGSCRNEDDYERLKNMQDLTkhlslenNVQFSVNVPYEDLLKLYQTAHI 372
Cdd:cd03794 230 QG----LETLLEAAERLKRR----PDIRFLFVGDGDEKERLKELAKARGLD-------NVTFLGRVPKEEVPELLSAADV 294

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 373 GIHTMWNEHFGIGIV-----ESMAAGLIMVAhkSGGPLLDIVETSAGsqNGFLAT--DAVEYAENILNIIVNNSEMNGIR 445
Cdd:cd03794 295 GLVPLKDNPANRGSSpsklfEYMAAGKPILA--SDDGGSDLAVEING--CGLVVEpgDPEALADAILELLDDPELRRAMG 370

                       250       260
                ....*....|....*....|.
gi 21358031 446 NAARASV-ERFSEQEFEKNFL 465
Cdd:cd03794 371 ENGRELAeEKFSREKLADRLL 391
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 279-456 3.02e-07

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 52.79  E-value: 3.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  279 DEFIILSVGQFRPEKDhplqlqaIYELRTLLaqdEALWNqIKLVIVGscrneDDYERlknmQDLTKHLSlENNVQFSVNV 358
Cdd:PLN02871 262 EKPLIVYVGRLGAEKN-------LDFLKRVM---ERLPG-ARLAFVG-----DGPYR----EELEKMFA-GTPTVFTGML 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  359 PYEDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGpLLDIVETSAGSQNGFLAT--DAVEYAENILNIIV 436
Cdd:PLN02871 321 QGDELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGG-IPDIIPPDQEGKTGFLYTpgDVDDCVEKLETLLA 399

                        170       180
                 ....*....|....*....|
gi 21358031  437 NNSEMNGIRNAARASVERFS 456
Cdd:PLN02871 400 DPELRERMGAAAREEVEKWD 419
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 356-458 1.37e-06

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: 50.41  E-value: 1.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 356 VNVPYED----LLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGpLLDIVETsagSQNGFLAT--DAVEYAE 429
Cdd:cd03825 246 ISLGYIDddeqLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGG-SPEIVQH---GVTGYLVPpgDVQALAE 321

                        90       100       110
                ....*....|....*....|....*....|
gi 21358031 430 NILNIIVNNSEMNGIRNAARASVE-RFSEQ 458
Cdd:cd03825 322 AIEWLLANPKERESLGERARALAEnHFDQR 351
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 256-457 1.96e-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: 49.61  E-value: 1.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 256 KTHRVYPPCEVSHLKSLQHTEKGDEFIILSVGQFRPEKDHPLQLQAIYELRTLLaqdealwNQIKLVIVGSCRNEDDYer 335
Cdd:cd04949 136 PPIFTIPVGYVDQLDTAESNHERKSNKIITISRLAPEKQLDHLIEAVAKAVKKV-------PEITLDIYGYGEEREKL-- 206

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 336 lknmQDLTKHLSLENNVQFSvnvPY-EDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSG-GPlLDIVETsa 413
Cdd:cd04949 207 ----KKLIEELHLEDNVFLK---GYhSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGP-SELIED-- 276

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21358031 414 gSQNGFLAT--DAVEYAENILNIIVNNSEMNGIRNAARASVERFSE 457
Cdd:cd04949 277 -GENGYLIEknNIDALADKIIELLNDPEKLQQFSEESYKIAEKYST 321
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 277-410 2.54e-06

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: 49.28  E-value: 2.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 277 KGDEFIILSVGQFRPEKDHPLQLQAIYELRTLLaqdealwnQIKLVIVGSCRNEDDYERLKNmqdltkHLSLENNVQFSV 356
Cdd:cd03819 179 PEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEP--------DFRLLVAGDGPERDEIRRLVE------RLGLRDRVTFTG 244

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 21358031 357 NVpyEDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGpLLDIVE 410
Cdd:cd03819 245 FR--EDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGG-AREIVV 295
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 317-462 2.55e-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: 49.25  E-value: 2.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 317 NQIKLVIVGSCRNEDdyerlknmqdlTKHLSLENNVQFSVNVPYEDLLKLYQTAHIGI-HTMWNEHFGIGIVESMAAGLI 395
Cdd:cd03823 219 EDIELVIAGHGPLSD-----------ERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVvPSIWPEPFGLVVREAIAAGLP 287

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21358031 396 MVAHKSGGPLLDIVETsagsQNGFLAtdAVEYAENILNIIVNNSEMNGI--RNAARASVERFSEQEFEK 462
Cdd:cd03823 288 VIASDLGGIAELIQPG----VNGLLF--APGDAEDLAAAMRRLLTDPALleRLRAGAEPPRSTESQAEE 350
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 319-466 2.23e-05

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: 46.51  E-value: 2.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 319 IKLVIVGSCRNEDDYERLKNmqdltkhLSLENNVQFSVNVPYEDLLKLYQTAHIGIHT-MWNEHFGIGIVESMAAGLIMV 397
Cdd:cd03802 196 LPLKIAGKVRDEDYFYYLQE-------PLPGPRIEFIGEVGHDEKQELLGGARALLFPiNWDEPFGLVMIEAMACGTPVI 268

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21358031 398 AHKSGGPlLDIVEtsAGSqNGFLA---TDAVEYAENILNIivnnsemngIRNAARASVE-RFSEQEFEKNFLR 466
Cdd:cd03802 269 AYRRGGL-PEVIQ--HGE-TGFLVdsvEEMAEAIANIDRI---------DRAACRRYAEdRFSAARMADRYEA 328
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 212-459 2.78e-05

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: 46.56  E-value: 2.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 212 TWTKLAYYRLFSRMYKWVGCCA--ETIMVNSSWTENHILQLWD--VPFKTHRVYPPCEVSHLK-SLQHTEKGDEFIILSV 286
Cdd:cd03813 220 TWIMGYIKKLWIRFFERLGKLAyqQADKIISLYEGNRRRQIRLgaDPDKTRVIPNGIDIQRFApAREERPEKEPPVVGLV 299

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 287 GQFRPEKDHPLQLQAIYELRtlLAQDEA-LWnqiklvIVGScrNEDDYERLKNMQDLTKHLSLENNVQFS--VNV----P 359
Cdd:cd03813 300 GRVVPIKDVKTFIRAFKLVR--RAMPDAeGW------LIGP--EDEDPEYAQECKRLVASLGLENKVKFLgfQNIkeyyP 369

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 360 YEDLLKLyqtahigihTMWNEHFGIGIVESMAAGLIMVAHKSGGpLLDIVE--TSAGSQNGFLA--TDAVEYAENILNII 435
Cdd:cd03813 370 KLGLLVL---------TSISEGQPLVILEAMASGVPVVATDVGS-CRELIYgaDDALGQAGLVVppADPEALAEALIKLL 439

                       250       260
                ....*....|....*....|....
gi 21358031 436 VNNSEMNGIRNAARASVERFSEQE 459
Cdd:cd03813 440 RDPELRQAFGEAGRKRVEKYYTLE 463
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 259-454 1.49e-04

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: 43.85  E-value: 1.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 259 RVYPPCEVShlKSLQHTEKGD--EFIILSVGQFRPEKDHPLQLQAIYELRtllAQDEALwnqiKLVIVGSCRNEDD---- 332
Cdd:cd03792 176 KDLSPADIR--YYLEKPFVIDpeRPYILQVARFDPSKDPLGVIDAYKLFK---RRAEEP----QLVICGHGAVDDPegsv 246

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 333 -YERLKNMQDLTKHLSLennvqfsVNVPYEDLL--KLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGPLLDIV 409
Cdd:cd03792 247 vYEEVMEYAGDDHDIHV-------LRLPPSDQEinALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVI 319

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21358031 410 EtsagSQNGFLATDAVEYAENILNIIVNNSEMNGIRNAARASVER 454
Cdd:cd03792 320 D----GETGFLVNSVEGAAVRILRLLTDPELRRKMGLAAREHVRD 360
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 279-439 4.25e-04

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: 42.28  E-value: 4.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 279 DEFIILSVGQFRPEKDHPLQLQAIYELRTllaqdeaLWNQIKLVIVGscrnedDYERLKNMQDLTKHLSLENNVQFSVNV 358
Cdd:cd03812 190 DKLVLGHVGRFNEQKNHSFLIDIFEELKK-------KNPNVKLVLVG------EGELKEKIKEKVKELGLEDKVIFLGFR 256

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 359 pyEDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGPlldivETSAGSQNGF--LATDAVEYAENILNIIV 436
Cdd:cd03812 257 --NDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITK-----ECDITNNVEFlpLNETPSTWAEKILKLIK 329


                ...
gi 21358031 437 NNS 439
Cdd:cd03812 330 RKR 332
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 380-471 7.96e-04

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 42.08  E-value: 7.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031    380 EHFGIGIVESMAAGLIMVAHKSGGPlldiVETSAGSQNGFLAT--DAVEYAENILNIIVNN-----SEMNGIRNaarasV 452
Cdd:TIGR02468  582 EPFGLTLIEAAAHGLPMVATKNGGP----VDIHRVLDNGLLVDphDQQAIADALLKLVADKqlwaeCRQNGLKN-----I 652

                           90
                   ....*....|....*....
gi 21358031    453 ERFSEQEFEKNFLRAVSTL 471
Cdd:TIGR02468  653 HLFSWPEHCKTYLSRIASC 671
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
279-462 3.76e-03

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 39.39  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  279 DEFIILSVGQFRPEKDHPLQLQAIYELRTllAQDEalwnqIKLVIVGSCRNEDDYERL---KNMQDLTKHLSleNNVQFS 355
Cdd:PRK15484 192 DETVLLYAGRISPDKGILLLMQAFEKLAT--AHSN-----LKLVVVGDPTASSKGEKAayqKKVLEAAKRIG--DRCIML 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031  356 VNVPYEDLLKLYQTAH-IGIHTMWNEHFGIGIVESMAAGLIMVAHKSGGplldIVETSAGSQNGFLATDAVEyAENILNI 434
Cdd:PRK15484 263 GGQPPEKMHNYYPLADlVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGG----ITEFVLEGITGYHLAEPMT-SDSIISD 337

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 21358031  435 I---VNNSEMNGIRNAARASV-ERFS----EQEFEK 462
Cdd:PRK15484 338 InrtLADPELTQIAEQAKDFVfSKYSwegvTQRFEE 373
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 319-403 6.37e-03

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


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 38.76  E-value: 6.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358031 319 IKLVIVGSCRNEDDYErlknmQDLTKHlSLENNVQFSVNVPYEDLLKLYQTAHIGIHTMWNEHFGIGIVESMAAGLIMVA 398
Cdd:cd03796 225 VRFIIGGDGPKRIELE-----EMREKY-QLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVS 298


                ....*
gi 21358031 399 HKSGG 403
Cdd:cd03796 299 TRVGG 303
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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