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Conserved domains on  [gi|31982409|ref|NP_031901|]
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UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase [Mus musculus]

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List of domain hits

Name Accession Description Interval E-value
GT_GPT_euk cd06855
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from ...
31-319 4.41e-155

UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from UDP-GlcNAc to dolichol-P to form GlcNAc-P-P-dolichol. The reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for eukaryotic N-glycosylation. GPT activity has been identified in all eukaryotic cells examined to date. A series of six conserved motifs designated A through F, ranging in length from 5 to 13 amino acid residues, has been identified in this family. They have been determined to be important for stable expression, substrate binding, or catalytic activities.


:

Pssm-ID: 133465  Cd Length: 283  Bit Score: 442.46  E-value: 4.41e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  31 IPAFRSHFIAARLCGQDLNKLSQQQIPESQGVISGAVFLIILFCFIPFPFLncfveeqcKAFPHHEFVALIGALLAICCM 110
Cdd:cd06855   1 IPKFGPLFIKAGLYGIDLNKNGEEKIPESAGLVPGIVFLIVLFLFIPFPFL--------KDFPHDKLVEYLSALLSICCM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 111 IFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpFRWILGLHLDLGILYYVYMGLLAVFCTNAINILA 190
Cdd:cd06855  73 TFLGFADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 191 GINGLEAGQSLVISASIIVFNLVELEGD----YRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAV 266
Cdd:cd06855 151 GINGLEVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAV 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 31982409 267 VGILGHFSKTMLLFFMPQVFNFLYSLPQLFHIIPCPRHRMPRLNAKTGKLEMS 319
Cdd:cd06855 231 VGILGHFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLLEPS 283
 
Name Accession Description Interval E-value
GT_GPT_euk cd06855
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from ...
31-319 4.41e-155

UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from UDP-GlcNAc to dolichol-P to form GlcNAc-P-P-dolichol. The reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for eukaryotic N-glycosylation. GPT activity has been identified in all eukaryotic cells examined to date. A series of six conserved motifs designated A through F, ranging in length from 5 to 13 amino acid residues, has been identified in this family. They have been determined to be important for stable expression, substrate binding, or catalytic activities.


Pssm-ID: 133465  Cd Length: 283  Bit Score: 442.46  E-value: 4.41e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  31 IPAFRSHFIAARLCGQDLNKLSQQQIPESQGVISGAVFLIILFCFIPFPFLncfveeqcKAFPHHEFVALIGALLAICCM 110
Cdd:cd06855   1 IPKFGPLFIKAGLYGIDLNKNGEEKIPESAGLVPGIVFLIVLFLFIPFPFL--------KDFPHDKLVEYLSALLSICCM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 111 IFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpFRWILGLHLDLGILYYVYMGLLAVFCTNAINILA 190
Cdd:cd06855  73 TFLGFADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 191 GINGLEAGQSLVISASIIVFNLVELEGD----YRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAV 266
Cdd:cd06855 151 GINGLEVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAV 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 31982409 267 VGILGHFSKTMLLFFMPQVFNFLYSLPQLFHIIPCPRHRMPRLNAKTGKLEMS 319
Cdd:cd06855 231 VGILGHFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLLEPS 283
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N- acetylglucosamine-1-phosphate ...
21-286 1.37e-30

UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N- acetylglucosamine-1-phosphate transferase [Cell envelope biogenesis, outer membrane]


Pssm-ID: 223548  Cd Length: 319  Bit Score: 119.30  E-value: 1.37e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  21 LLGFVATVTLIPAFRSHFIAARLCG--QDLNKLSQQQIPESQGvisgavfLIILFCFIPFPFLncfveeqckAFPHHEFV 98
Cdd:COG0472  10 IISFVISLILTPILIKFLRKLGLGDipEDGPKSHKKGTPTMGG-------LAILLSILLASLL---------AANLLTNP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  99 ALIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLPLlMVYFTNFGNTTIVVPKPFRWILglhLDLGILYYVYMGLL 178
Cdd:COG0472  74 YVWLVLLGLLGFGLIGFLDDRLKLSPKIRGLIQKLKALLL-IIALGELPIKFLDIPLGIPFFK---LPGPLLFILFAVFA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 179 AVFCTNAINILAGINGLEAGQSLVISASIIVFnlvelegDYRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCY 258
Cdd:COG0472 150 IVGASNAVNLTDGLDGLAAGLSAIALLALALI-------ALLQGLGELALICAALAGACLGFLWFNFYPAKIFMGDTGSL 222
                       250       260
                ....*....|....*....|....*...
gi 31982409 259 FAGMTFAVVGILGHFSKTMLLFFMPQVF 286
Cdd:COG0472 223 ALGAALAAIALLLKQEILLAIIGPLGVP 250
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
100-272 1.61e-26

Glycosyl transferase family 4;


Pssm-ID: 250250  Cd Length: 158  Bit Score: 103.81  E-value: 1.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409   100 LIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLPLLMVY--FTNFGnttivvpkpfrWILGLHLDLGILYYVYMGL 177
Cdd:pfam00953   1 LLGLLLGALLIGLIGLLDDLKGLSPKIRLLLQALAALLLIILGggLTSLG-----------LLFGGGLLLLGLLAILFTV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409   178 LAVFC-TNAINILAGINGLEAGQSLVISASIIVFNlvelegdYRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTF 256
Cdd:pfam00953  70 FAIVGvINAVNFMDGLDGLAGGVALIAALALAILA-------LIAGDIELALLSLALLGALLGFLLFNFPPAKIFMGDVG 142
                         170
                  ....*....|....*.
gi 31982409   257 CYFAGMTFAVVGILGH 272
Cdd:pfam00953 143 SLFLGFVLAVLAILGG 158
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
112-286 4.30e-10

phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the enzyme catalyzes the first of the lipid cycle reactions. Also known as Muramoyl-Pentapeptide Transferase (murX) [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan].


Pssm-ID: 161884  Cd Length: 321  Bit Score: 59.38  E-value: 4.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409   112 FLGFADDVLNLRW--------RHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpfrWILGLHLDLGILYYVYMGLLAVFCT 183
Cdd:TIGR00445  74 FIGFVDDYRKIKRksnkgltaKQKLFGQIIIALIFCTWLYYYGPDTFIYIP----FIKDFMFDLGLFYILLAYFVLVGTS 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409   184 NAINILAGINGLEAGQSLVISASIIVFNLVELEGDyrddhiFSLYFMIP--------FFFTT------LGLLYHNWYPSR 249
Cdd:TIGR00445 150 NAVNLTDGLDGLAIGPSAIAFGALAILAWATGNAN------FAKYLHIPylkdsgelVIFCTalvgasLGFLWFNAYPAK 223
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 31982409   250 VFVGDTFCYFAGMTFAVVGILGHfsKTMLLFFMPQVF 286
Cdd:TIGR00445 224 VFMGDTGSLALGGALGAVAILTK--NEILLVIMGGVF 258
mraY PRK00108
phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional
100-286 3.69e-08

phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional


Pssm-ID: 234638  Cd Length: 344  Bit Score: 53.22  E-value: 3.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  100 LIGALLAICCMIFLGFADDVLN--------LRWRHKLLLPTAASLP-LLMVYFTNFGNTTIVVPkpfrWILGLHLDLG-I 169
Cdd:PRK00108  83 VWLVLLVTLGFGLIGFLDDYLKvvkknnlgLSARQKLLLQILIALIfALLLYLLGSTSTSLTIP----FFKDLSLDLGvI 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  170 LYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVElegdyrDDHIFSLYFMIPFFFTT------------ 237
Cdd:PRK00108 159 LYIPFAYFVIVGTSNAVNLTDGLDGLAIGPSVIVFAALGIIAYLQ------GNAVFANYLHIPYIPGAgelaifcaalvg 232
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 31982409  238 --LGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHfsKTMLLFFMPQVF 286
Cdd:PRK00108 233 acLGFLWFNAYPAQVFMGDTGSLALGGALAAIAVLLR--QELLLLIIGGVF 281
 
Name Accession Description Interval E-value
GT_GPT_euk cd06855
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from ...
31-319 4.41e-155

UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from UDP-GlcNAc to dolichol-P to form GlcNAc-P-P-dolichol. The reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for eukaryotic N-glycosylation. GPT activity has been identified in all eukaryotic cells examined to date. A series of six conserved motifs designated A through F, ranging in length from 5 to 13 amino acid residues, has been identified in this family. They have been determined to be important for stable expression, substrate binding, or catalytic activities.


Pssm-ID: 133465  Cd Length: 283  Bit Score: 442.46  E-value: 4.41e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  31 IPAFRSHFIAARLCGQDLNKLSQQQIPESQGVISGAVFLIILFCFIPFPFLncfveeqcKAFPHHEFVALIGALLAICCM 110
Cdd:cd06855   1 IPKFGPLFIKAGLYGIDLNKNGEEKIPESAGLVPGIVFLIVLFLFIPFPFL--------KDFPHDKLVEYLSALLSICCM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 111 IFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpFRWILGLHLDLGILYYVYMGLLAVFCTNAINILA 190
Cdd:cd06855  73 TFLGFADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 191 GINGLEAGQSLVISASIIVFNLVELEGD----YRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAV 266
Cdd:cd06855 151 GINGLEVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAV 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 31982409 267 VGILGHFSKTMLLFFMPQVFNFLYSLPQLFHIIPCPRHRMPRLNAKTGKLEMS 319
Cdd:cd06855 231 VGILGHFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLLEPS 283
GT_GPT_like cd06851
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ...
45-290 2.18e-70

This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and archaeal GPT-like glycosyltransferases. Eukaryotic GPT catalyzes the transfer of GlcNAc-1-P from UDP-GlcNAc to dolichol-P to form GlcNAc-P-P-dolichol. The reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for eukaryotic N-linked glycosylation. GPT activity has been identified in all eukaryotic cells examined to date. Evidence for the existence of the N-glycosylation pathway in archaea has emerged and genes responsible for the pathway have been identified. A glycosyl transferase gene Mv1751 in M. voltae encodes for the enzyme that carries out the first step in the pathway, the attachment of GlcNAc to a dolichol lipid carrier in the membrane. A lethal mutation in the alg7 (GPT) gene in Saccharomyces cerevisiae was successfully complemented with Mv1751, the archaeal gene, indicating eukaryotic and archaeal enzymes may use the same substrates and are evolutionarily closer than the bacterial enzyme, which uses a different substrate.


Pssm-ID: 133461  Cd Length: 223  Bit Score: 223.53  E-value: 2.18e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  45 GQDLNKLSQQQIPESQGVISGAVFLIILFCFIPFPFLncfveeqckAFPHHEFVALIGALLAICCMIFLGFADDVLNLRW 124
Cdd:cd06851   2 GKDMNKKGNVMIPEPGGISILIGFVASEITLIFFPFL---------SFPHFPISEILAALITSVLGFSVGIIDDRLTMGG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 125 RHKLLLPTAASLPLLMVYFTNFGNTTIvvpkpfrwILGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVIS 204
Cdd:cd06851  73 WFKPVALAFAAAPILLLGAYDSNLDFP--------LFGGSVKIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFTTIIS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 205 ASIIVFNLVELEGdyrddhiFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQ 284
Cdd:cd06851 145 FALAISLLVQQNY-------EIGIACLCLAFASLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAILGEVEKIAAVAFIPA 217

                ....*.
gi 31982409 285 VFNFLY 290
Cdd:cd06851 218 IINFFL 223
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
91-268 5.03e-41

Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine:polyprenol phosphate D-N-acetylhexosamine-1-phosphate transferases. They catalyze the transfer of a D-N-acetylhexosamine 1-phosphate to a membrane-bound polyprenol phosphate, which is the initiation step of protein N-glycosylation in eukaryotes and peptidoglycan biosynthesis in bacteria. One member, D-N-acetylhexosamine 1-phosphate transferase (GPT) is a eukaryotic enzyme, which is specific for UDP-GlcNAc as donor substrate and dolichol-phosphate as the membrane bound acceptor. The bacterial members MraY, WecA, and WbpL/WbcO utilize undecaprenol phosphate as the acceptor substrate, but use different UDP-sugar donor substrates. MraY-type transferases are highly specific for UDP-N-acetylmuramate-pentapeptide, whereas WecA proteins are selective for UDP-N-acetylglucosamine (UDP-GlcNAc). The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic endproducts implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The eukaryotic reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for N-glycosylation. The prokaryotic reactions lead to the formation of polyprenol-linked oligosaccharides involved in bacterial cell wall and peptidoglycan assembly. Archaeal and eukaryotic enzymes may use the same substrates and are evolutionarily closer than the bacterial enzyme. Archaea possess the same N-glycosylation pathway as eukaryotes. A glycosyl transferase gene Mv1751 in M. voltae encodes for the enzyme that carries out the first step in the pathway, the attachment of GlcNAc to a dolichol lipid carrier in the membrane. A lethal mutation in the alg7 (GPT) gene in Saccharomyces cerevisiae was successfully complemented with Mv1751, the archaea gene.


Pssm-ID: 133460  Cd Length: 185  Bit Score: 144.75  E-value: 5.03e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  91 AFPHHEFVALIGALLAICCMIFLGFADDVLNL----RWRHKLLLPTAASLPLLMVyftNFGNTTIVVPkpfrwiLGLHLD 166
Cdd:cd06499  20 LYIPHSNTLILLALLSGLVAGIVGFIDDLLGLkvelSEREKLLLQILAALFLLLI---GGGHTTVTTP------LGFVLD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 167 LGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVELEGDyrddhifSLYFMIPFFFTTLGLLYHNWY 246
Cdd:cd06499  91 LGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFALLSGQTT-------SALLFIILAGACLGFLYFNFY 163
                       170       180
                ....*....|....*....|..
gi 31982409 247 PSRVFVGDTFCYFAGMTFAVVG 268
Cdd:cd06499 164 PAKIFMGDTGSYFLGAAYAAVA 185
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N- acetylglucosamine-1-phosphate ...
21-286 1.37e-30

UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N- acetylglucosamine-1-phosphate transferase [Cell envelope biogenesis, outer membrane]


Pssm-ID: 223548  Cd Length: 319  Bit Score: 119.30  E-value: 1.37e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  21 LLGFVATVTLIPAFRSHFIAARLCG--QDLNKLSQQQIPESQGvisgavfLIILFCFIPFPFLncfveeqckAFPHHEFV 98
Cdd:COG0472  10 IISFVISLILTPILIKFLRKLGLGDipEDGPKSHKKGTPTMGG-------LAILLSILLASLL---------AANLLTNP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  99 ALIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLPLlMVYFTNFGNTTIVVPKPFRWILglhLDLGILYYVYMGLL 178
Cdd:COG0472  74 YVWLVLLGLLGFGLIGFLDDRLKLSPKIRGLIQKLKALLL-IIALGELPIKFLDIPLGIPFFK---LPGPLLFILFAVFA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 179 AVFCTNAINILAGINGLEAGQSLVISASIIVFnlvelegDYRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCY 258
Cdd:COG0472 150 IVGASNAVNLTDGLDGLAAGLSAIALLALALI-------ALLQGLGELALICAALAGACLGFLWFNFYPAKIFMGDTGSL 222
                       250       260
                ....*....|....*....|....*...
gi 31982409 259 FAGMTFAVVGILGHFSKTMLLFFMPQVF 286
Cdd:COG0472 223 ALGAALAAIALLLKQEILLAIIGPLGVP 250
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
45-339 3.55e-29

UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT catalyzes the transfer of GlcNAc-1-P from UDP-GlcNAc to dolichol-P to form GlcNAc-P-P-dolichol. The reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for eukaryotic N-linked glycosylation. Evidence for the existence of the N-glycosylation pathway in archaea has emerged and genes responsible for the pathway have been identified. A glycosyl transferase gene Mv1751 in M. voltae encodes for the enzyme that carries out the first step in the pathway, the attachment of GlcNAc to a dolichol lipid carrier in the membrane. A lethal mutation in the alg7 (GPT) gene in Saccharomyces cerevisiae was successfully complemented with Mv1751, the archaea gene, indicating that eukaryotic and archaeal enzymes may use the same substrates and are evolutionarily closer than the bacterial enzyme, which uses a different substrate.


Pssm-ID: 133466  Cd Length: 280  Bit Score: 114.27  E-value: 3.55e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  45 GQDLNKLSQQQIPESQGVISGAVFLIILFCFIPFPFLNcfveeqckafphhEFVALIGALLAICcmiFLGFADDVLNLRW 124
Cdd:cd06856   2 GRDVHKPGKPEVPEMGGIAVLLGFSLGLLFLSALTHSV-------------EALALLITSLLAG---LIGLLDDILGLSQ 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 125 RHKLLLPTAASLPLLMVyftNFGNTTIVVPkpfrwiLGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVIS 204
Cdd:cd06856  66 SEKVLLTALPAIPLLVL---KAGNPLTSLP------IGGRVLGILYYLLIVPLGITGASNAFNMLAGFNGLEAGMGIIIL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 205 ASIIVFNLveLEGDYrddhiFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQ 284
Cdd:cd06856 137 LALAIILL--INGDY-----DALIIALILVAALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLGGLEIILLILLLPY 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 31982409 285 VFNFLYSLPQLFHIIPcPRHRMPRLnAKTGKLEMSYskfktkNLSFLGTFILKVA 339
Cdd:cd06856 210 VIDFLLKLRSKGGGKE-HREKPTKV-LEDGTLYPPP------DKSSLLTLRLLLR 256
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
100-272 1.61e-26

Glycosyl transferase family 4;


Pssm-ID: 250250  Cd Length: 158  Bit Score: 103.81  E-value: 1.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409   100 LIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLPLLMVY--FTNFGnttivvpkpfrWILGLHLDLGILYYVYMGL 177
Cdd:pfam00953   1 LLGLLLGALLIGLIGLLDDLKGLSPKIRLLLQALAALLLIILGggLTSLG-----------LLFGGGLLLLGLLAILFTV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409   178 LAVFC-TNAINILAGINGLEAGQSLVISASIIVFNlvelegdYRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTF 256
Cdd:pfam00953  70 FAIVGvINAVNFMDGLDGLAGGVALIAALALAILA-------LIAGDIELALLSLALLGALLGFLLFNFPPAKIFMGDVG 142
                         170
                  ....*....|....*.
gi 31982409   257 CYFAGMTFAVVGILGH 272
Cdd:pfam00953 143 SLFLGFVLAVLAILGG 158
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
66-274 1.26e-21

This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. WecA is an UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate (Und-P) GlcNAc-1-phosphate transferase that catalyzes the formation of a phosphodiester bond between a membrane-associated undecaprenyl-phosphate molecule and N-acetylglucosamine 1-phosphate, which is usually donated by a soluble UDP-N-acetylglucosamine precursor. WecA participates in the biosynthesis of O antigen LPS in many enteric bacteria and is also involved in the biosynthesis of enterobacterial common antigen. A conserved short sequence motif and a conserved arginine at a cytosolic loop of this integral membrane protein were shown to be critical in recognition of substrate UDP-N-acetylglucosamine.


Pssm-ID: 133463  Cd Length: 249  Bit Score: 92.17  E-value: 1.26e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  66 AVFLIILFCFIPFPFLNCFVEEQckafphhefvaLIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLplLMVYFtn 145
Cdd:cd06853  15 AIFLGFLLALLLALLFPFFLLPE-----------LLGLLAGATIIVLLGLLDDLFDLSPKVKLLGQILAAL--IVVFG-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 146 fGNTTIVVPKPFrwiLGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVElegdyrdDHIF 225
Cdd:cd06853  80 -GGVILSLLGPF---GGGIILLGWLSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLN-------GQVL 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 31982409 226 SLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFS 274
Cdd:cd06853 149 VALLALALAGALLGFLPYNFHPARIFMGDAGSLFLGFLLAVLSILGTQK 197
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
100-255 1.14e-14

Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the formation of the first lipid intermediate in the synthesis of bacterial cell wall peptidoglycan. It catalyzes the formation of undecaprenyl-pyrophosphoryl-N-acetylmuramoyl-pentapeptide from UDP-MurNAc-pentapeptide and undecaprenyl-phosphate. It is an integral membrane protein with possibly ten transmembrane domains.


Pssm-ID: 133462  Cd Length: 280  Bit Score: 72.52  E-value: 1.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 100 LIGALLAICCMIFLGFADDVLN--------LRWRHKLLLPTAASLpLLMVYFTNFGNTTIVVPKPFrwILGLHLDLGILY 171
Cdd:cd06852  38 VLLLLLLTLGFGLIGFLDDYLKvvkkrnlgLSARQKLLLQFLIAI-VFALLLYYFNGSGTLITLPF--FKNGLIDLGILY 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 172 YVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVELegdyrdDHIFSLYFMIPFFFTTLGLLYHNWYPSRVF 251
Cdd:cd06852 115 IPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLAG------NAVFLAVFCAALVGACLGFLWFNAYPAKVF 188

                ....
gi 31982409 252 VGDT 255
Cdd:cd06852 189 MGDT 192
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
61-283 1.71e-10

The members of this subfamily catalyze the formation of a phosphodiester bond between a membrane-associated undecaprenyl-phosphate (Und-P) molecule and N-acetylhexosamine 1-phosphate, which is usually donated by a soluble UDP-N-acetylhexosamine precursor. The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic end products implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The subgroup of bacterial UDP-HexNAc:polyprenol-P HexNAc-1-P transferases includes the WbcO protein from Yersinia enterocolitica and the WbpL protein from Pseudomonas aeruginosa. These transferases initiate LPS O-antigen biosynthesis. Similar to other GlcNAc/MurNAc-1-P transferase family members, WbpL is a highly hydrophobic protein possessing 11 predicted transmembrane segments.


Pssm-ID: 133464  Cd Length: 253  Bit Score: 59.56  E-value: 1.71e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  61 GVISGAVFLIILFCFIPFPFLNCFVeeqckafphheFVALIGALLAICcmiFLGFADDVLNLRWRHKLLLPTAASLplLM 140
Cdd:cd06854  20 GIAFVLAFLLALLLAAAAGPLNDLS-----------YLLLLIGLLLLA---AVGFIDDLRSLSPKIRLLVQLLAAA--LA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 141 VYFTNFGNTTIVVPKPFRWILGLhldlgilyyvyMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVELEGDYR 220
Cdd:cd06854  84 LYALGPLTSLLLNFLPPWLIALL-----------LLLAIVWIINLYNFMDGIDGLAGGEALVVFLALALLGYLAGEPALA 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31982409 221 DdhifslyFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSK----TMLLFFMP 283
Cdd:cd06854 153 L-------LALALAGALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLLALSGqspwAWLLLLSP 212
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
112-286 4.30e-10

phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the enzyme catalyzes the first of the lipid cycle reactions. Also known as Muramoyl-Pentapeptide Transferase (murX) [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan].


Pssm-ID: 161884  Cd Length: 321  Bit Score: 59.38  E-value: 4.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409   112 FLGFADDVLNLRW--------RHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpfrWILGLHLDLGILYYVYMGLLAVFCT 183
Cdd:TIGR00445  74 FIGFVDDYRKIKRksnkgltaKQKLFGQIIIALIFCTWLYYYGPDTFIYIP----FIKDFMFDLGLFYILLAYFVLVGTS 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409   184 NAINILAGINGLEAGQSLVISASIIVFNLVELEGDyrddhiFSLYFMIP--------FFFTT------LGLLYHNWYPSR 249
Cdd:TIGR00445 150 NAVNLTDGLDGLAIGPSAIAFGALAILAWATGNAN------FAKYLHIPylkdsgelVIFCTalvgasLGFLWFNAYPAK 223
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 31982409   250 VFVGDTFCYFAGMTFAVVGILGHfsKTMLLFFMPQVF 286
Cdd:TIGR00445 224 VFMGDTGSLALGGALGAVAILTK--NEILLVIMGGVF 258
mraY PRK00108
phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional
100-286 3.69e-08

phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional


Pssm-ID: 234638  Cd Length: 344  Bit Score: 53.22  E-value: 3.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  100 LIGALLAICCMIFLGFADDVLN--------LRWRHKLLLPTAASLP-LLMVYFTNFGNTTIVVPkpfrWILGLHLDLG-I 169
Cdd:PRK00108  83 VWLVLLVTLGFGLIGFLDDYLKvvkknnlgLSARQKLLLQILIALIfALLLYLLGSTSTSLTIP----FFKDLSLDLGvI 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  170 LYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVElegdyrDDHIFSLYFMIPFFFTT------------ 237
Cdd:PRK00108 159 LYIPFAYFVIVGTSNAVNLTDGLDGLAIGPSVIVFAALGIIAYLQ------GNAVFANYLHIPYIPGAgelaifcaalvg 232
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 31982409  238 --LGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHfsKTMLLFFMPQVF 286
Cdd:PRK00108 233 acLGFLWFNAYPAQVFMGDTGSLALGGALAAIAVLLR--QELLLLIIGGVF 281
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
89-268 3.61e-06

This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like family. This family contains both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine:polyprenol phosphate D-N-acetylhexosamine-1-phosphate transferases, which catalyze the transfer of a D-N-acetylhexosamine 1-phosphate to a membrane-bound polyprenol phosphate. This is the initiation step of protein N-glycosylation in eukaryotes and peptidoglycan biosynthesis in bacteria. The three bacterial members MraY, WecA, and WbpL/WbcO, utilize undecaprenol phosphate as the acceptor substrate, but use different UDP-sugar donor substrates. MraY-type transferases are highly specific for UDP-N-acetylmuramate-pentapeptide, whereas WecA proteins are selective for UDP-N-acetylglucosamine (UDP-GlcNAc). The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic end products implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The prokaryotic enzyme-catalyzed reactions lead to the formation of polyprenol-linked oligosaccharides involved in bacterial cell wall and peptidoglycan assembly.


Pssm-ID: 133467  Cd Length: 193  Bit Score: 46.08  E-value: 3.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  89 CKAFPHHEFVALIGALLAICCMIFLGFADDV-LNLRWRHKLLLptAASLPLLMVYFTNFGNTTIVVPkPFRWILGLHLdL 167
Cdd:cd06912  27 LLLLSLLSGSLLLLLLLAALPAFLAGLLEDItKRVSPRIRLLA--TFLSALLAVWLLGASITRLDLP-GLDLLLSFPP-F 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409 168 GILYYVymgLLAVFCTNAINILAGINGLEAGQSLVISASIIvfnLVELEGDYRDDHIFSLYFMipffFTTLGLLYHNWYP 247
Cdd:cd06912 103 AIIFTI---FAVAGVANAFNIIDGFNGLASGVAIISLLSLA---LVAFQVGDTDLAFLALLLA----GALLGFLIFNFPF 172
                       170       180
                ....*....|....*....|.
gi 31982409 248 SRVFVGDTFCYFAGMTFAVVG 268
Cdd:cd06912 173 GKIFLGDGGAYLLGFLLAWLA 193
mraY PRK14654
phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional
98-295 1.62e-05

phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional


Pssm-ID: 173117  Cd Length: 302  Bit Score: 44.89  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409   98 VALIGALLaiccMIFLGFADDVLN--------LRWRHKLLLPTAASLPLLMvyftnfgnttIVVPKPFRWILGLHLDLGI 169
Cdd:PRK14654  67 MVLLGMFL----FFLIGFLDDFLSvarkdstgLKTYQKALLQTLAALIMLL----------LIRPETNVDFFGFTIEMGK 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982409  170 LYYVYMGLLAVFCTNAINILAGINGLEAGqsLVISASIIVFNLVELEGdyrddhiFSLYFMIPFFFTTLGLLYHNWYPSR 249
Cdd:PRK14654 133 WYYLFALLVIVGSSNAMNLTDGLDGLAGW--IYVSGSIPYWFFLKERG-------VSEDILLILGAGVLAFLVFNSKPAK 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 31982409  250 VFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQVFNFLYSLPQL 295
Cdd:PRK14654 204 IFMGDTGSITLGGVLGTVSVLTKTEFYLVLFFLIPVIETLSVILQV 249
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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