NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|255089288|ref|XP_002506566|]
View 

glycosyltransferase family 33 protein, partial [Micromonas commoda]

Protein Classification

PLN02275 family protein( domain architecture ID 11476589)

PLN02275 family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02275 PLN02275
transferase, transferring glycosyl groups
1-415 0e+00

transferase, transferring glycosyl groups


:

Pssm-ID: 215155 [Multi-domain]  Cd Length: 371  Bit Score: 589.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288   1 RPRVQVVVLGDFGRSPRMQYHALSLADSLGADVDVVAYVGSEPRREVAIHPSIRMALIPPPPAWTNARHVPRIVALAVRV 80
Cdd:PLN02275   4 RGRAAVVVLGDFGRSPRMQYHALSLARQASFQVDVVAYGGSEPIPALLNHPSIHIHLMVQPRLLQRLPRVLYALALLLKV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288  81 ATQTAQMLWTTAVALPRPTHVLLQTPPCVPSFAVCWLVCLIRRAKFVIDWHNFAYTLMALKFGPSSPIVFIAKVYERMLG 160
Cdd:PLN02275  84 AIQFLMLLWFLCVKIPRPDVFLVQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYERHYG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 161 RLGHAHLAVTDAMATWLDERWGIRdAVVLHDAPPEFFRPASVTetsalmrrlapsldaspakvpgdccdailvgggdplt 240
Cdd:PLN02275 164 KMADGHLCVTKAMQHELDQNWGIR-ATVLYDQPPEFFRPASLE------------------------------------- 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 241 ttttgrggARWREGRPALVVSSTSWTPDEDFGVLLDALTLYDSVAGADANATTS------RYPDLLVIVTGKGPQRAHYE 314
Cdd:PLN02275 206 --------IRLRPNRPALVVSSTSWTPDEDFGILLEAAVMYDRRVAARLNESDSasgkqsLYPRLLFIITGKGPQKAMYE 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 315 SRMRSLRLTRVAVRTAWLESGDYPTLLGAADLGVCAHTSSSGLDLPMKVVDMFGCGLPVLAARYDVIHELVREDArfagg 394
Cdd:PLN02275 278 EKISRLNLRHVAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGK----- 352
                        410       420
                 ....*....|....*....|.
gi 255089288 395 spNGCLFGGAGELAAQLCGVL 415
Cdd:PLN02275 353 --NGLLFSSSSELADQLLELL 371
 
Name Accession Description Interval E-value
PLN02275 PLN02275
transferase, transferring glycosyl groups
1-415 0e+00

transferase, transferring glycosyl groups


Pssm-ID: 215155 [Multi-domain]  Cd Length: 371  Bit Score: 589.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288   1 RPRVQVVVLGDFGRSPRMQYHALSLADSLGADVDVVAYVGSEPRREVAIHPSIRMALIPPPPAWTNARHVPRIVALAVRV 80
Cdd:PLN02275   4 RGRAAVVVLGDFGRSPRMQYHALSLARQASFQVDVVAYGGSEPIPALLNHPSIHIHLMVQPRLLQRLPRVLYALALLLKV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288  81 ATQTAQMLWTTAVALPRPTHVLLQTPPCVPSFAVCWLVCLIRRAKFVIDWHNFAYTLMALKFGPSSPIVFIAKVYERMLG 160
Cdd:PLN02275  84 AIQFLMLLWFLCVKIPRPDVFLVQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYERHYG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 161 RLGHAHLAVTDAMATWLDERWGIRdAVVLHDAPPEFFRPASVTetsalmrrlapsldaspakvpgdccdailvgggdplt 240
Cdd:PLN02275 164 KMADGHLCVTKAMQHELDQNWGIR-ATVLYDQPPEFFRPASLE------------------------------------- 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 241 ttttgrggARWREGRPALVVSSTSWTPDEDFGVLLDALTLYDSVAGADANATTS------RYPDLLVIVTGKGPQRAHYE 314
Cdd:PLN02275 206 --------IRLRPNRPALVVSSTSWTPDEDFGILLEAAVMYDRRVAARLNESDSasgkqsLYPRLLFIITGKGPQKAMYE 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 315 SRMRSLRLTRVAVRTAWLESGDYPTLLGAADLGVCAHTSSSGLDLPMKVVDMFGCGLPVLAARYDVIHELVREDArfagg 394
Cdd:PLN02275 278 EKISRLNLRHVAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGK----- 352
                        410       420
                 ....*....|....*....|.
gi 255089288 395 spNGCLFGGAGELAAQLCGVL 415
Cdd:PLN02275 353 --NGLLFSSSSELADQLLELL 371
GT33_ALG1-like cd03816
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ...
1-457 0e+00

chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.


Pssm-ID: 340843 [Multi-domain]  Cd Length: 411  Bit Score: 512.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288   1 RPRVQVVVLGDFGRSPRMQYHALSLAdSLGADVDVVAYVGSEPRREVAIHPSIRMALIPPPPawtNARHVPRIVALAVRV 80
Cdd:cd03816    3 KKRVCVLVLGDIGRSPRMQYHALSLA-RHGWRVDLIGYLESPPHDELLSHPNITIHALPPPP---TKNKLPFLLFAPLKV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288  81 ATQTAQMLWTTAVaLPRPTHVLLQTPPCVPSFAVCWLVCLIRRAKFVIDWHNFAYTLMALKFGPSSPIVFIAKVYERMLG 160
Cdd:cd03816   79 LLQALSLLWLLYE-LRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 161 RLGHAHLAVTDAMATWLDER-WGIRDAVVLHDAPPEFFRPASVTETSALMRRLAPSLDASPakvpgdccdailvgggdpl 239
Cdd:cd03816  158 RMADAHLCVTKAMQRDLQQFeNWNIRATVLYDRPPSHFRPIPLEEKHELFLELALFRELAE------------------- 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 240 tttttgrGGARWREGRPALVVSSTSWTPDEDFGVLLDALTLYDSvagaDANATTSRYPDLLVIVTGKGPQRAHYESRMRS 319
Cdd:cd03816  219 -------GAVSYKEGRPALLVSSTSWTPDEDFSILLDALKAYES----SAATEPALLPSLLCIITGKGPLKEMYLELIKE 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 320 LRLTRVAVRTAWLESGDYPTLLGAADLGVCAHTSSSGLDLPMKVVDMFGCGLPVLAARYDVIHELVREDArfaggspNGC 399
Cdd:cd03816  288 LKLKKVTIRTPWLSAEDYPRLLASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGV-------NGL 360
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255089288 400 LFGGAGELAAQLCGVLEGFTAGTsvagemRTRMRRELEEKgGGNRWRDNWERAALPVF 457
Cdd:cd03816  361 VFGDSEELAEQLIDLLSDFDRGK------LNVLKKGAQEE-SENRWDENWDRVAGPLF 411
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
300-416 1.18e-03

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 39.03  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288  300 LVIVtGKGPQRaHYESRMRSLRlTRVaVRTAWLEsgDYPTLLGAADLGVCAHTSSSgldLPMKVVDMFGCGLPVLAARYD 379
Cdd:pfam13692  36 LVIV-GDGPEE-ELEELAAGLE-DRV-IFTGFVE--DLAELLAAADVFVLPSLYEG---FGLKLLEAMAAGLPVVATDVG 106
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 255089288  380 VIHELVREDarfaggspNGCLF--GGAGELAAQLCGVLE 416
Cdd:pfam13692 107 GIPELVDGE--------NGLLVppGDPEALAEAILRLLE 137
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
340-452 9.04e-03

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 36.12  E-value: 9.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 340 LLGAADLGVCAHTSSSgldLPMKVVDMFGCGLPVLAARYDVIHELVREDArfaggspNGCLF--GGAGELAAQLCGVLEg 417
Cdd:COG0438   17 LLAAADVFVLPSRSEG---FGLVLLEAMAAGLPVIATDVGGLPEVIEDGE-------TGLLVppGDPEALAEAILRLLE- 85
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 255089288 418 ftaGTSVAGEMRTRMRRELEEKGGGNRWRDNWERA 452
Cdd:COG0438   86 ---DPELRRRLGEAARERAEERFSWEAIAERLLAL 117
 
Name Accession Description Interval E-value
PLN02275 PLN02275
transferase, transferring glycosyl groups
1-415 0e+00

transferase, transferring glycosyl groups


Pssm-ID: 215155 [Multi-domain]  Cd Length: 371  Bit Score: 589.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288   1 RPRVQVVVLGDFGRSPRMQYHALSLADSLGADVDVVAYVGSEPRREVAIHPSIRMALIPPPPAWTNARHVPRIVALAVRV 80
Cdd:PLN02275   4 RGRAAVVVLGDFGRSPRMQYHALSLARQASFQVDVVAYGGSEPIPALLNHPSIHIHLMVQPRLLQRLPRVLYALALLLKV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288  81 ATQTAQMLWTTAVALPRPTHVLLQTPPCVPSFAVCWLVCLIRRAKFVIDWHNFAYTLMALKFGPSSPIVFIAKVYERMLG 160
Cdd:PLN02275  84 AIQFLMLLWFLCVKIPRPDVFLVQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYERHYG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 161 RLGHAHLAVTDAMATWLDERWGIRdAVVLHDAPPEFFRPASVTetsalmrrlapsldaspakvpgdccdailvgggdplt 240
Cdd:PLN02275 164 KMADGHLCVTKAMQHELDQNWGIR-ATVLYDQPPEFFRPASLE------------------------------------- 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 241 ttttgrggARWREGRPALVVSSTSWTPDEDFGVLLDALTLYDSVAGADANATTS------RYPDLLVIVTGKGPQRAHYE 314
Cdd:PLN02275 206 --------IRLRPNRPALVVSSTSWTPDEDFGILLEAAVMYDRRVAARLNESDSasgkqsLYPRLLFIITGKGPQKAMYE 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 315 SRMRSLRLTRVAVRTAWLESGDYPTLLGAADLGVCAHTSSSGLDLPMKVVDMFGCGLPVLAARYDVIHELVREDArfagg 394
Cdd:PLN02275 278 EKISRLNLRHVAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGK----- 352
                        410       420
                 ....*....|....*....|.
gi 255089288 395 spNGCLFGGAGELAAQLCGVL 415
Cdd:PLN02275 353 --NGLLFSSSSELADQLLELL 371
GT33_ALG1-like cd03816
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ...
1-457 0e+00

chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.


Pssm-ID: 340843 [Multi-domain]  Cd Length: 411  Bit Score: 512.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288   1 RPRVQVVVLGDFGRSPRMQYHALSLAdSLGADVDVVAYVGSEPRREVAIHPSIRMALIPPPPawtNARHVPRIVALAVRV 80
Cdd:cd03816    3 KKRVCVLVLGDIGRSPRMQYHALSLA-RHGWRVDLIGYLESPPHDELLSHPNITIHALPPPP---TKNKLPFLLFAPLKV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288  81 ATQTAQMLWTTAVaLPRPTHVLLQTPPCVPSFAVCWLVCLIRRAKFVIDWHNFAYTLMALKFGPSSPIVFIAKVYERMLG 160
Cdd:cd03816   79 LLQALSLLWLLYE-LRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 161 RLGHAHLAVTDAMATWLDER-WGIRDAVVLHDAPPEFFRPASVTETSALMRRLAPSLDASPakvpgdccdailvgggdpl 239
Cdd:cd03816  158 RMADAHLCVTKAMQRDLQQFeNWNIRATVLYDRPPSHFRPIPLEEKHELFLELALFRELAE------------------- 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 240 tttttgrGGARWREGRPALVVSSTSWTPDEDFGVLLDALTLYDSvagaDANATTSRYPDLLVIVTGKGPQRAHYESRMRS 319
Cdd:cd03816  219 -------GAVSYKEGRPALLVSSTSWTPDEDFSILLDALKAYES----SAATEPALLPSLLCIITGKGPLKEMYLELIKE 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 320 LRLTRVAVRTAWLESGDYPTLLGAADLGVCAHTSSSGLDLPMKVVDMFGCGLPVLAARYDVIHELVREDArfaggspNGC 399
Cdd:cd03816  288 LKLKKVTIRTPWLSAEDYPRLLASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGV-------NGL 360
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255089288 400 LFGGAGELAAQLCGVLEGFTAGTsvagemRTRMRRELEEKgGGNRWRDNWERAALPVF 457
Cdd:cd03816  361 VFGDSEELAEQLIDLLSDFDRGK------LNVLKKGAQEE-SENRWDENWDRVAGPLF 411
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
21-453 2.84e-08

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: 55.62  E-value: 2.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288  21 HALSLADSL---GADVDVVAYVGSEPRREVAIHPSIRMALIPPPPAWTNARHVPRIVALavrvatqtaqmlwttaVALPR 97
Cdd:cd03801   19 HVRELARALaarGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPL----------------LRLRK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288  98 PTHVLLQTPPcvpSFAVCWLVCLIRRAKFVIDWHNFAYTLMALKFGPSSPivFIAKVYERMlgRLGHAHLAVTDAMATWL 177
Cdd:cd03801   83 FDVVHAHGLL---AALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERR--LLARAEALL--RRADAVIAVSEALRDEL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 178 DERWGIRDA---VVLHDAPPEFFRPASVTEtsalmrrlapsldaspakvpgdccdailvgggdpltttttgrggaRWREG 254
Cdd:cd03801  156 RALGGIPPEkivVIPNGVDLERFSPPLRRK---------------------------------------------LGIPP 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 255 RPALVVSSTSWTPDEDFGVLLDALtlydsvagadaNATTSRYPDL-LVIVTGKGPQRAHYESRMRSLRLtRVaVRTAWLE 333
Cdd:cd03801  191 DRPVLLFVGRLSPRKGVDLLLEAL-----------AKLLRRGPDVrLVIVGGDGPLRAELEELELGLGD-RV-RFLGFVP 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 334 SGDYPTLLGAADLGVCAHTSSSgldLPMKVVDMFGCGLPVLAARYDVIHELVREDArfaggspNGCLFGG--AGELAAQL 411
Cdd:cd03801  258 DEELPALYAAADVFVLPSRYEG---FGLVVLEAMAAGLPVVATDVGGLPEVVEDGE-------GGLVVPPddVEALADAL 327
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 255089288 412 CGVLEgftagtsvAGEMRTRMRRELEEKGggnRWRDNWERAA 453
Cdd:cd03801  328 LRLLA--------DPELRARLGRAARERV---AERFSWERVA 358
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
260-388 2.57e-04

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: 42.39  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 260 VSSTSWTPDEDFGVLLDALTLYdsvagadanatTSRYPDLLVIVTGKGPQRAHYESRMRSLRLTRVAVRTAWLESGD-YP 338
Cdd:cd01635  114 VSVGRLVPEKGIDLLLEALALL-----------KARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEvLE 182
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 255089288 339 TLLGAADLGVCAHTSSSgldLPMKVVDMFGCGLPVLAARYDVIHELVRED 388
Cdd:cd01635  183 LLLAAADVFVLPSRSEG---FGLVLLEAMAAGKPVIATDVGGIPEFVVDG 229
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
300-401 2.79e-04

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 43.04  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 300 LVIVtGKGPQRAHYESRMRSLRLTRVAVRTAWLESGDYPTLLGAADLGVCAHTSSSgldLPMKVVDMFGCGLPVLAARYD 379
Cdd:cd03817  234 LVIV-GDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTET---QGLVYLEAMAAGLPVVAAKDP 309
                         90       100
                 ....*....|....*....|..
gi 255089288 380 VIHELVrEDARfaggspNGCLF 401
Cdd:cd03817  310 AASELV-EDGE------NGFLF 324
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
267-392 2.81e-04

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: 43.07  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 267 PDEDFGVLLDALTLydsvagadanaTTSRYPDLLVIVTGKGPQRAHYESRMRSLRLT-RVAVRTawlESGDYPTLLGAAD 345
Cdd:cd03807  201 PVKDHSDLLRAAAL-----------LVETHPDLRLLLVGRGPERPNLERLLLELGLEdRVHLLG---ERSDVPALLPAMD 266
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 255089288 346 LGvCAHTSSSGldLPMKVVDMFGCGLPVLAARYDVIHELVREDARFA 392
Cdd:cd03807  267 IF-VLSSRTEG--FPNALLEAMACGLPVVATDVGGAAELVDDGTGFL 310
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
13-390 4.60e-04

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: 42.33  E-value: 4.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288  13 GRSPRMQYHALSLADSlGADVDVVA--YVGSEPRREVAI---HPSIRMALIPPPPAWTNArhvprIVALAVRVATQTAQM 87
Cdd:cd03794   15 AAAARVYELAKELVRR-GHEVTVLTpsPNYPLGRIFAGAtetKDGIRVIRVKLGPIKKNG-----LIRRLLNYLSFALAA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288  88 LWTTAVALPRPTHVLLQTPPCVPSFAVCWLvCLIRRAKFVID----WHNFAYTLMALKfgPSSPIVFIAKVYERMLgRLG 163
Cdd:cd03794   89 LLKLLVREERPDVIIAYSPPITLGLAALLL-KKLRGAPFILDvrdlWPESLIALGVLK--KGSLLKLLKKLERKLY-RLA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 164 HAHLAVTDAMATWLDERwGIRD---AVVLHDAPPEFFRPAsvtetsalmrrlaPSLDASPAKVPGDCCDAILVGggdplt 240
Cdd:cd03794  165 DAIIVLSPGLKEYLLRK-GVPKekiIVIPNWADLEEFKPP-------------PKDELRKKLGLDDKFVVVYAG------ 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 241 ttttgrggarwregrpalvvsstSWTPDEDFGVLLDALtlydsvagadanATTSRYPDL-LVIVtGKGPQRAHYESRMRS 319
Cdd:cd03794  225 -----------------------NIGKAQGLETLLEAA------------ERLKRRPDIrFLFV-GDGDEKERLKELAKA 268
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255089288 320 LRLTRVAVRtAWLESGDYPTLLGAADLGVC--AHTSSSGLDLPMKVVDMFGCGLPVLAArYDVIHELVREDAR 390
Cdd:cd03794  269 RGLDNVTFL-GRVPKEEVPELLSAADVGLVplKDNPANRGSSPSKLFEYMAAGKPILAS-DDGGSDLAVEING 339
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
300-416 1.18e-03

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 39.03  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288  300 LVIVtGKGPQRaHYESRMRSLRlTRVaVRTAWLEsgDYPTLLGAADLGVCAHTSSSgldLPMKVVDMFGCGLPVLAARYD 379
Cdd:pfam13692  36 LVIV-GDGPEE-ELEELAAGLE-DRV-IFTGFVE--DLAELLAAADVFVLPSLYEG---FGLKLLEAMAAGLPVVATDVG 106
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 255089288  380 VIHELVREDarfaggspNGCLF--GGAGELAAQLCGVLE 416
Cdd:pfam13692 107 GIPELVDGE--------NGLLVppGDPEALAEAILRLLE 137
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
294-388 1.25e-03

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: 40.83  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 294 SRYPDLLVIVTGKGPQRAHYESRMRSLRLTRVAVRTAWLESGDYPTLLGAADLGVCAhtsSSGLDLPMKVVDMFGCGLPV 373
Cdd:cd03798  227 KARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLP---SRHEGFGLVLLEAMACGLPV 303
                         90
                 ....*....|....*
gi 255089288 374 LAARYDVIHELVRED 388
Cdd:cd03798  304 VATDVGGIPEVVGDP 318
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
18-188 6.33e-03

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 37.38  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288   18 MQYHALSLADSL---GADVDVVAYVGSEPRREVAiHPSIRMALIPPPPAWTNARHVPRIVALAvrvatqtaqmlwtTAVA 94
Cdd:pfam13579   3 IGVYVLELARALaalGHEVRVVTPGGPPGRPELV-GDGVRVHRLPVPPRPSPLADLAALRRLR-------------RLLR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288   95 LPRPTHVLLQTPPcvpSFAVCWLVCLIRRAKFVIDWHNFAYTlmalkfGPSSPIVFIAKVYERMLGRLGHAHLAVTDAMA 174
Cdd:pfam13579  69 AERPDVVHAHSPT---AGLAARLARRRRGVPLVVTVHGLALD------YGSGWKRRLARALERRLLRRADAVVVVSEAEA 139
                         170
                  ....*....|....
gi 255089288  175 TWLdERWGIRDAVV 188
Cdd:pfam13579 140 ELL-RALGVPAARV 152
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
340-452 9.04e-03

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 36.12  E-value: 9.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089288 340 LLGAADLGVCAHTSSSgldLPMKVVDMFGCGLPVLAARYDVIHELVREDArfaggspNGCLF--GGAGELAAQLCGVLEg 417
Cdd:COG0438   17 LLAAADVFVLPSRSEG---FGLVLLEAMAAGLPVIATDVGGLPEVIEDGE-------TGLLVppGDPEALAEAILRLLE- 85
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 255089288 418 ftaGTSVAGEMRTRMRRELEEKGGGNRWRDNWERA 452
Cdd:COG0438   86 ---DPELRRRLGEAARERAEERFSWEAIAERLLAL 117
 
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