NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|148235673|ref|NP_001082880|]
View 

UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase [Danio rerio]

Protein Classification

GT_GPT_euk domain-containing protein (domain architecture ID 10160631)

GT_GPT_euk domain-containing 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
GT_GPT_euk cd06855
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from ...
27-315 6.00e-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: 442.84  E-value: 6.00e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  27 IPAFKEHFISARLYGMDLNKTTKKEVPESQGVISGTVFLIILFLFIPVPFLQcfmgekcqRFPHNEFVQLIGALLAICCM 106
Cdd:cd06855    1 IPKFGPLFIKAGLYGIDLNKNGEEKIPESAGLVPGIVFLIVLFLFIPFPFLK--------DFPHDKLVEYLSALLSICCM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 107 IFLGFADDVLNLRWRHKLLLPTMASLPLLMVYFTNFGNTVIVVPkpFRLLLGMHLDLGILYYVYMGMLAVFCTNAINILA 186
Cdd:cd06855   73 TFLGFADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 187 GINGIESGQALFISGSIILFNLLELNGD----YRDDHVFSLYFMIPFFFTTLALFYHNWYPSSVFVGDTFCYFAGMTFAV 262
Cdd:cd06855  151 GINGLEVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAV 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148235673 263 VGILGHFSKTMLLFFIPQVINFIYSLPQLFHIIPCPRHRLPRLQSDTGKLGMS 315
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 ...
27-315 6.00e-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: 442.84  E-value: 6.00e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  27 IPAFKEHFISARLYGMDLNKTTKKEVPESQGVISGTVFLIILFLFIPVPFLQcfmgekcqRFPHNEFVQLIGALLAICCM 106
Cdd:cd06855    1 IPKFGPLFIKAGLYGIDLNKNGEEKIPESAGLVPGIVFLIVLFLFIPFPFLK--------DFPHDKLVEYLSALLSICCM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 107 IFLGFADDVLNLRWRHKLLLPTMASLPLLMVYFTNFGNTVIVVPkpFRLLLGMHLDLGILYYVYMGMLAVFCTNAINILA 186
Cdd:cd06855   73 TFLGFADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 187 GINGIESGQALFISGSIILFNLLELNGD----YRDDHVFSLYFMIPFFFTTLALFYHNWYPSSVFVGDTFCYFAGMTFAV 262
Cdd:cd06855  151 GINGLEVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAV 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148235673 263 VGILGHFSKTMLLFFIPQVINFIYSLPQLFHIIPCPRHRLPRLQSDTGKLGMS 315
Cdd:cd06855  231 VGILGHFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLLEPS 283
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
18-277 4.00e-27

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


Pssm-ID: 223548  Cd Length: 319  Bit Score: 110.05  E-value: 4.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  18 LGCIATVKLIPAFKEHFISARLYG--MDLNKTTKKEVPESQGVISGTVFLIILFLFIPvpflqcfmgekcqrfpHNEFVQ 95
Cdd:COG0472   11 ISFVISLILTPILIKFLRKLGLGDipEDGPKSHKKGTPTMGGLAILLSILLASLLAAN----------------LLTNPY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  96 LIGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASLPLlMVYFTNFGNTVIVVPKPFRLLLgmhLDLGILYYVYMGMLA 175
Cdd:COG0472   75 VWLVLLGLLGFGLIGFLDDRLKLSPKIRGLIQKLKALLL-IIALGELPIKFLDIPLGIPFFK---LPGPLLFILFAVFAI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 176 VFCTNAINILAGINGIESGQALFISGSIILFnllelngDYRDDHVFSLYFMIPFFFTTLALFYHNWYPSSVFVGDTFCYF 255
Cdd:COG0472  151 VGASNAVNLTDGLDGLAAGLSAIALLALALI-------ALLQGLGELALICAALAGACLGFLWFNFYPAKIFMGDTGSLA 223
                        250       260
                 ....*....|....*....|..
gi 148235673 256 AGMTFAVVGILGHFSKTMLLFF 277
Cdd:COG0472  224 LGAALAAIALLLKQEILLAIIG 245
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
96-268 8.47e-25

Glycosyl transferase family 4;


Pssm-ID: 307205  Cd Length: 160  Bit Score: 99.97  E-value: 8.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673   96 LIGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASLPLLMVYFTNFGNTVIvvpkpfrLLLGMHLDLGILYYVYMGMLA 175
Cdd:pfam00953   1 LLGLLLASLLIGLIGLIDDLKGLSARIKLLLQALAALIVIILGGIGLTSLGL-------PFGGGSLDLGPILAIPITVFA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  176 VFC-TNAINILAGINGIESGQALFISGSIILFNllelngdYRDDHVFSLYFMIPFFFTTLALFYHNWYPSSVFVGDTFCY 254
Cdd:pfam00953  74 IVGvTNAVNFIDGLDGLAGGVSLIAALALAIIA-------YLLGNIELALLSLALLGALLGFLPFNFYPAKIFMGDTGSL 146
                         170
                  ....*....|....
gi 148235673  255 FAGMTFAVVGILGH 268
Cdd:pfam00953 147 FLGFLLAVLAIIGG 160
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
108-268 2.45e-08

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: 55.14  E-value: 2.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  108 FLGFADDVLNLRW--------RHKLLLPTMASLPLLMVYFTNFGNTVIVVPkpfrLLLGMHLDLGILYYVYMGMLAVFCT 179
Cdd:TIGR00445  74 FIGFVDDYRKIKRksnkgltaKQKLFGQIIIALIFCTWLYYYGPDTFIYIP----FIKDFMFDLGLFYILLAYFVLVGTS 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  180 NAINILAGINGIESGQALFISGSIILFNLLELNGDyrddhvFSLYFMIP--------FFFTT------LALFYHNWYPSS 245
Cdd:TIGR00445 150 NAVNLTDGLDGLAIGPSAIAFGALAILAWATGNAN------FAKYLHIPylkdsgelVIFCTalvgasLGFLWFNAYPAK 223
                         170       180
                  ....*....|....*....|...
gi 148235673  246 VFVGDTFCYFAGMTFAVVGILGH 268
Cdd:TIGR00445 224 VFMGDTGSLALGGALGAVAILTK 246
mraY PRK14654
phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional
100-291 2.06e-05

phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional


Pssm-ID: 173117  Cd Length: 302  Bit Score: 45.66  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 100 LLAICCMIFLGFADDVLN--------LRWRHKLLLPTMASLPLLMvyftnfgntvIVVPKPFRLLLGMHLDLGILYYVYM 171
Cdd:PRK14654  69 LLGMFLFFLIGFLDDFLSvarkdstgLKTYQKALLQTLAALIMLL----------LIRPETNVDFFGFTIEMGKWYYLFA 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 172 GMLAVFCTNAINILAGINGIESGqaLFISGSIILFNLLELNGdyrddhvFSLYFMIPFFFTTLALFYHNWYPSSVFVGDT 251
Cdd:PRK14654 139 LLVIVGSSNAMNLTDGLDGLAGW--IYVSGSIPYWFFLKERG-------VSEDILLILGAGVLAFLVFNSKPAKIFMGDT 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 148235673 252 FCYFAGMTFAVVGILGHFSKTMLLFFIPQVINFIYSLPQL 291
Cdd:PRK14654 210 GSITLGGVLGTVSVLTKTEFYLVLFFLIPVIETLSVILQV 249
 
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 ...
27-315 6.00e-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: 442.84  E-value: 6.00e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  27 IPAFKEHFISARLYGMDLNKTTKKEVPESQGVISGTVFLIILFLFIPVPFLQcfmgekcqRFPHNEFVQLIGALLAICCM 106
Cdd:cd06855    1 IPKFGPLFIKAGLYGIDLNKNGEEKIPESAGLVPGIVFLIVLFLFIPFPFLK--------DFPHDKLVEYLSALLSICCM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 107 IFLGFADDVLNLRWRHKLLLPTMASLPLLMVYFTNFGNTVIVVPkpFRLLLGMHLDLGILYYVYMGMLAVFCTNAINILA 186
Cdd:cd06855   73 TFLGFADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 187 GINGIESGQALFISGSIILFNLLELNGD----YRDDHVFSLYFMIPFFFTTLALFYHNWYPSSVFVGDTFCYFAGMTFAV 262
Cdd:cd06855  151 GINGLEVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAV 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148235673 263 VGILGHFSKTMLLFFIPQVINFIYSLPQLFHIIPCPRHRLPRLQSDTGKLGMS 315
Cdd:cd06855  231 VGILGHFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLLEPS 283
GT_GPT_like cd06851
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ...
41-286 3.59e-68

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: 218.52  E-value: 3.59e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  41 GMDLNKTTKKEVPESQGVISGTVFLIILFLFIPVPFLQcfmgekcqrFPHNEFVQLIGALLAICCMIFLGFADDVLNLRW 120
Cdd:cd06851    2 GKDMNKKGNVMIPEPGGISILIGFVASEITLIFFPFLS---------FPHFPISEILAALITSVLGFSVGIIDDRLTMGG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 121 RHKLLLPTMASLPLLMVYFTNFGNTVIvvpkpfrlLLGMHLDLGILYYVYMGMLAVFCTNAINILAGINGIESGQALFIS 200
Cdd:cd06851   73 WFKPVALAFAAAPILLLGAYDSNLDFP--------LFGGSVKIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFTTIIS 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 201 GSIILFNLLELNGdyrddhvFSLYFMIPFFFTTLALFYHNWYPSSVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFIPQ 280
Cdd:cd06851  145 FALAISLLVQQNY-------EIGIACLCLAFASLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAILGEVEKIAAVAFIPA 217

                 ....*.
gi 148235673 281 VINFIY 286
Cdd:cd06851  218 IINFFL 223
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
52-264 4.20e-38

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: 137.82  E-value: 4.20e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  52 VPESQGVISGTVFLIILFLFIPVPFlqcfmgekcqrfphnefVQLIGALLAICCMIFLGFADDVLNL----RWRHKLLLP 127
Cdd:cd06499    2 TPTMGGLAILLGFLLGVLLYIPHSN-----------------TLILLALLSGLVAGIVGFIDDLLGLkvelSEREKLLLQ 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 128 TMASLPLLMVYFTNFGNTVIvvpkpfrllLGMHLDLGILYYVYMGMLAVFCTNAINILAGINGIESGQALFISGSIILFN 207
Cdd:cd06499   65 ILAALFLLLIGGGHTTVTTP---------LGFVLDLGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFA 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148235673 208 LLELNGDyrddhvfSLYFMIPFFFTTLALFYHNWYPSSVFVGDTFCYFAGMTFAVVG 264
Cdd:cd06499  136 LLSGQTT-------SALLFIILAGACLGFLYFNFYPAKIFMGDTGSYFLGAAYAAVA 185
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
40-285 1.19e-28

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: 113.88  E-value: 1.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  40 YGMDLNKTTKKEVPESQGVISGTVFLIILFLFIPVPFLqcfmgekcqrfphnefVQLIGALLAICCMIFLGFADDVLNLR 119
Cdd:cd06856    1 VGRDVHKPGKPEVPEMGGIAVLLGFSLGLLFLSALTHS----------------VEALALLITSLLAGLIGLLDDILGLS 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 120 WRHKLLLPTMASLPLLmvyftnfgntVIVVPKPFRLLLGMHLDLGILYYVYMGMLAV-FCTNAINILAGINGIESGQALF 198
Cdd:cd06856   65 QSEKVLLTALPAIPLL----------VLKAGNPLTSLPIGGRVLGILYYLLIVPLGItGASNAFNMLAGFNGLEAGMGII 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 199 ISgsIILFNLLELNGDYrddhvFSLYFMIPFFFTTLALFYHNWYPSSVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFI 278
Cdd:cd06856  135 IL--LALAIILLINGDY-----DALIIALILVAALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLGGLEIILLILLL 207

                 ....*..
gi 148235673 279 PQVINFI 285
Cdd:cd06856  208 PYVIDFL 214
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
18-277 4.00e-27

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


Pssm-ID: 223548  Cd Length: 319  Bit Score: 110.05  E-value: 4.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  18 LGCIATVKLIPAFKEHFISARLYG--MDLNKTTKKEVPESQGVISGTVFLIILFLFIPvpflqcfmgekcqrfpHNEFVQ 95
Cdd:COG0472   11 ISFVISLILTPILIKFLRKLGLGDipEDGPKSHKKGTPTMGGLAILLSILLASLLAAN----------------LLTNPY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  96 LIGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASLPLlMVYFTNFGNTVIVVPKPFRLLLgmhLDLGILYYVYMGMLA 175
Cdd:COG0472   75 VWLVLLGLLGFGLIGFLDDRLKLSPKIRGLIQKLKALLL-IIALGELPIKFLDIPLGIPFFK---LPGPLLFILFAVFAI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 176 VFCTNAINILAGINGIESGQALFISGSIILFnllelngDYRDDHVFSLYFMIPFFFTTLALFYHNWYPSSVFVGDTFCYF 255
Cdd:COG0472  151 VGASNAVNLTDGLDGLAAGLSAIALLALALI-------ALLQGLGELALICAALAGACLGFLWFNFYPAKIFMGDTGSLA 223
                        250       260
                 ....*....|....*....|..
gi 148235673 256 AGMTFAVVGILGHFSKTMLLFF 277
Cdd:COG0472  224 LGAALAAIALLLKQEILLAIIG 245
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
96-268 8.47e-25

Glycosyl transferase family 4;


Pssm-ID: 307205  Cd Length: 160  Bit Score: 99.97  E-value: 8.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673   96 LIGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASLPLLMVYFTNFGNTVIvvpkpfrLLLGMHLDLGILYYVYMGMLA 175
Cdd:pfam00953   1 LLGLLLASLLIGLIGLIDDLKGLSARIKLLLQALAALIVIILGGIGLTSLGL-------PFGGGSLDLGPILAIPITVFA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  176 VFC-TNAINILAGINGIESGQALFISGSIILFNllelngdYRDDHVFSLYFMIPFFFTTLALFYHNWYPSSVFVGDTFCY 254
Cdd:pfam00953  74 IVGvTNAVNFIDGLDGLAGGVSLIAALALAIIA-------YLLGNIELALLSLALLGALLGFLPFNFYPAKIFMGDTGSL 146
                         170
                  ....*....|....
gi 148235673  255 FAGMTFAVVGILGH 268
Cdd:pfam00953 147 FLGFLLAVLAIIGG 160
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
86-279 9.47e-18

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: 82.15  E-value: 9.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  86 QRFPHNEFVQLIGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASLplLMVYFtnfGNTVIVVPKPFrllLGMHLDLGI 165
Cdd:cd06853   28 LLFPFFLLPELLGLLAGATIIVLLGLLDDLFDLSPKVKLLGQILAAL--IVVFG---GGVILSLLGPF---GGGIILLGW 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 166 LYYVYMGMLAVFCTNAINILAGINGIESGQALFISGSIILFNLLElngdyrdDHVFSLYFMIPFFFTTLALFYHNWYPSS 245
Cdd:cd06853  100 LSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLN-------GQVLVALLALALAGALLGFLPYNFHPAR 172
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 148235673 246 VFVGDTFCYFAGMTFAVVGILGHF-SKTMLLFFIP 279
Cdd:cd06853  173 IFMGDAGSLFLGFLLAVLSILGTQkSSTAISPVVP 207
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
94-278 7.67e-11

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: 62.12  E-value: 7.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  94 VQLIGALLAICCMIFLGFADDVLN--------LRWRHKLLLPTMASLPLLMVYFTNFGNTVIVVPKPFRLLLgmhLDLGI 165
Cdd:cd06852   36 PEVLLLLLLTLGFGLIGFLDDYLKvvkkrnlgLSARQKLLLQFLIAIVFALLLYYFNGSGTLITLPFFKNGL---IDLGI 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 166 LYYVYMGMLAVFCTNAINILAGINGIESGQALFISGSIILFNLLELNgdyrddHVFSLYFMIPFFFTTLALFYHNWYPSS 245
Cdd:cd06852  113 LYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLAGN------AVFLAVFCAALVGACLGFLWFNAYPAK 186
                        170       180       190
                 ....*....|....*....|....*....|...
gi 148235673 246 VFVGDTFCYFAGMTFAVVGILghfSKTMLLFFI 278
Cdd:cd06852  187 VFMGDTGSLALGGALAALAIL---TKQELLLLI 216
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
49-279 1.75e-08

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: 54.94  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  49 KKEVPESQGVISGTVFLIILFLFIPVPFLqcfmgekcqrfPHNEFVQLIGALLAICcmiFLGFADDVLNL--RWRhkllL 126
Cdd:cd06854   12 TKPTPRGGGIAFVLAFLLALLLAAAAGPL-----------NDLSYLLLLIGLLLLA---AVGFIDDLRSLspKIR----L 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 127 PTMASLPLLMVYFTNFGNTVIVVPKPFRLLLGmhldLGILYYVYMgmlavfcTNAINILAGINGIESGQALFISGSIILF 206
Cdd:cd06854   74 LVQLLAAALALYALGPLTSLLLNFLPPWLIAL----LLLLAIVWI-------INLYNFMDGIDGLAGGEALVVFLALALL 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148235673 207 NLLELNGDYRDdhvfslyFMIPFFFTTLALFYHNWYPSSVFVGDTFCYFAGMTFAVVGILGHFSK----TMLLFFIP 279
Cdd:cd06854  143 GYLAGEPALAL-------LALALAGALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLLALSGqspwAWLLLLSP 212
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
108-268 2.45e-08

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: 55.14  E-value: 2.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  108 FLGFADDVLNLRW--------RHKLLLPTMASLPLLMVYFTNFGNTVIVVPkpfrLLLGMHLDLGILYYVYMGMLAVFCT 179
Cdd:TIGR00445  74 FIGFVDDYRKIKRksnkgltaKQKLFGQIIIALIFCTWLYYYGPDTFIYIP----FIKDFMFDLGLFYILLAYFVLVGTS 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  180 NAINILAGINGIESGQALFISGSIILFNLLELNGDyrddhvFSLYFMIP--------FFFTT------LALFYHNWYPSS 245
Cdd:TIGR00445 150 NAVNLTDGLDGLAIGPSAIAFGALAILAWATGNAN------FAKYLHIPylkdsgelVIFCTalvgasLGFLWFNAYPAK 223
                         170       180
                  ....*....|....*....|...
gi 148235673  246 VFVGDTFCYFAGMTFAVVGILGH 268
Cdd:TIGR00445 224 VFMGDTGSLALGGALGAVAILTK 246
mraY PRK14654
phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional
100-291 2.06e-05

phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional


Pssm-ID: 173117  Cd Length: 302  Bit Score: 45.66  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 100 LLAICCMIFLGFADDVLN--------LRWRHKLLLPTMASLPLLMvyftnfgntvIVVPKPFRLLLGMHLDLGILYYVYM 171
Cdd:PRK14654  69 LLGMFLFFLIGFLDDFLSvarkdstgLKTYQKALLQTLAALIMLL----------LIRPETNVDFFGFTIEMGKWYYLFA 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 172 GMLAVFCTNAINILAGINGIESGqaLFISGSIILFNLLELNGdyrddhvFSLYFMIPFFFTTLALFYHNWYPSSVFVGDT 251
Cdd:PRK14654 139 LLVIVGSSNAMNLTDGLDGLAGW--IYVSGSIPYWFFLKERG-------VSEDILLILGAGVLAFLVFNSKPAKIFMGDT 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 148235673 252 FCYFAGMTFAVVGILGHFSKTMLLFFIPQVINFIYSLPQL 291
Cdd:PRK14654 210 GSITLGGVLGTVSVLTKTEFYLVLFFLIPVIETLSVILQV 249
mraY PRK00108
phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional
94-278 1.06e-04

phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional


Pssm-ID: 234638  Cd Length: 344  Bit Score: 43.59  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673  94 VQLIGALLAICCMIFLGFADDVLN--------LRWRHKLLLPTMASLP-LLMVYFTNFGNTVIVVPkpfrLLLGMHLDLG 164
Cdd:PRK00108  81 PYVWLVLLVTLGFGLIGFLDDYLKvvkknnlgLSARQKLLLQILIALIfALLLYLLGSTSTSLTIP----FFKDLSLDLG 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 165 ILYYVYMGMLA-VFCTNAINILAGINGIESGQALFISGSIILFNLLELNgdyrddHVFSLYFMIPFFFTTLAL------- 236
Cdd:PRK00108 157 VILYIPFAYFViVGTSNAVNLTDGLDGLAIGPSVIVFAALGIIAYLQGN------AVFANYLHIPYIPGAGELaifcaal 230
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 148235673 237 -------FYHNWYPSSVFVGDTFCYFAGMTFAVVGILghfSKTMLLFFI 278
Cdd:PRK00108 231 vgaclgfLWFNAYPAQVFMGDTGSLALGGALAAIAVL---LRQELLLLI 276
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
108-264 1.80e-04

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: 42.23  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148235673 108 FLGFADDV-LNLRWRHKLLLPTMASLplLMVYFTNFGNTVIVVPKPFRLLLGMHLDLGILYYVYMGMlavfcTNAINILA 186
Cdd:cd06912   50 LAGLLEDItKRVSPRIRLLATFLSAL--LAVWLLGASITRLDLPGLDLLLSFPPFAIIFTIFAVAGV-----ANAFNIID 122
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148235673 187 GINGIESGQALFISGSIILFnllelngDYRDDHVFSLYFMIPFFFTTLALFYHNWYPSSVFVGDTFCYFAGMTFAVVG 264
Cdd:cd06912  123 GFNGLASGVAIISLLSLALV-------AFQVGDTDLAFLALLLAGALLGFLIFNFPFGKIFLGDGGAYLLGFLLAWLA 193
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • 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, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH