NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1386806216|ref|NP_001349916|]
View 

tRNA-queuosine alpha-mannosyltransferase [Mus musculus]

Protein Classification

DUF3524 and Glycosyltransferase_GTB_type domain-containing protein( domain architecture ID 10572306)

DUF3524 and Glycosyltransferase_GTB_type 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
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 2-164 8.87e-91

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


:

Pssm-ID: 432280  Cd Length: 165  Bit Score: 272.12  E-value: 8.87e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216   2 SIVIIEAFYGGSHRQLVELLREEL-DDCVLYTLPAKKWHWRARTAALYFSQNIPSSEHY-RTLFASSVLNLTELAALRPD 79
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSpHEVDLLTLPARKWKWRMRGSALYFAQEIPDLSAYgDLLFATSMLDLAELRALRPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216  80 LGKLKKILYFHENQLVYPVKKYQERDFQYGYNQILSCLVADVVVFNSSFNMESFLTSIGKFLKLIPDHRPKDLESIIRPK 159
Cdd:pfam12038  81 LANCPKLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRAK 160


                  ....*
gi 1386806216 160 CQVIY 164
Cdd:pfam12038 161 SRVLY 165
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 275-386 4.81e-12

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: 65.50  E-value: 4.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 275 WPHRWEHDKDPETFLKILMSLKQLNLNFHVSVLGETFTDTPDIFSEAKKALGSSVLHWGYLPRKEDYFRVLCMADVVIST 354
Cdd:cd01635   115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLP 194

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1386806216 355 AKHEFFGVAMLEAVYCGCYPLCPKALVYPEIF 386
Cdd:cd01635   195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 345-437 5.84e-04

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


:

Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 39.59  E-value: 5.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 345 LCMADVVISTAKHEFFGVAMLEAVYCGCYPLCPKALVYPEI---------FPAEylysTPEQLSKRLKSFCKRPDIIRKH 415
Cdd:COG0438    18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEViedgetgllVPPG----DPEALAEAILRLLEDPELRRRL 93

                          90       100
                  ....*....|....*....|....*
gi 1386806216 416 LYKGE---VAPFSWAALHGKFRSLL 437
Cdd:COG0438    94 GEAAReraEERFSWEAIAERLLALY 118
 
Name Accession Description Interval E-value
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 2-164 8.87e-91

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


Pssm-ID: 432280  Cd Length: 165  Bit Score: 272.12  E-value: 8.87e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216   2 SIVIIEAFYGGSHRQLVELLREEL-DDCVLYTLPAKKWHWRARTAALYFSQNIPSSEHY-RTLFASSVLNLTELAALRPD 79
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSpHEVDLLTLPARKWKWRMRGSALYFAQEIPDLSAYgDLLFATSMLDLAELRALRPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216  80 LGKLKKILYFHENQLVYPVKKYQERDFQYGYNQILSCLVADVVVFNSSFNMESFLTSIGKFLKLIPDHRPKDLESIIRPK 159
Cdd:pfam12038  81 LANCPKLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRAK 160


                  ....*
gi 1386806216 160 CQVIY 164
Cdd:pfam12038 161 SRVLY 165
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 275-386 4.81e-12

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: 65.50  E-value: 4.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 275 WPHRWEHDKDPETFLKILMSLKQLNLNFHVSVLGETFTDTPDIFSEAKKALGSSVLHWGYLPRKEDYFRVLCMADVVIST 354
Cdd:cd01635   115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLP 194

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1386806216 355 AKHEFFGVAMLEAVYCGCYPLCPKALVYPEIF 386
Cdd:cd01635   195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 277-405 3.88e-05

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 43.80  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 277 HRWEHDKDPETFLKILMSLKQLNLNFHVSVLGETFTDTPdIFSEAKKALGSSVLHW-GYLPRKE--DYFRvlcMADVVIS 353
Cdd:pfam00534   9 GRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKR-LKKLAEKLGLGDNVIFlGFVSDEDlpELLK---IADVFVL 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1386806216 354 TAKHEFFGVAMLEAVYCGCYPLCPKALVYPEIF-PAE--YLY--STPEQLSKRLKSF 405
Cdd:pfam00534  85 PSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVkDGEtgFLVkpNNAEALAEAIDKL 141
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 345-437 5.84e-04

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 39.59  E-value: 5.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 345 LCMADVVISTAKHEFFGVAMLEAVYCGCYPLCPKALVYPEI---------FPAEylysTPEQLSKRLKSFCKRPDIIRKH 415
Cdd:COG0438    18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEViedgetgllVPPG----DPEALAEAILRLLEDPELRRRL 93

                          90       100
                  ....*....|....*....|....*
gi 1386806216 416 LYKGE---VAPFSWAALHGKFRSLL 437
Cdd:COG0438    94 GEAAReraEERFSWEAIAERLLALY 118
 
Name Accession Description Interval E-value
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 2-164 8.87e-91

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


Pssm-ID: 432280  Cd Length: 165  Bit Score: 272.12  E-value: 8.87e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216   2 SIVIIEAFYGGSHRQLVELLREEL-DDCVLYTLPAKKWHWRARTAALYFSQNIPSSEHY-RTLFASSVLNLTELAALRPD 79
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSpHEVDLLTLPARKWKWRMRGSALYFAQEIPDLSAYgDLLFATSMLDLAELRALRPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216  80 LGKLKKILYFHENQLVYPVKKYQERDFQYGYNQILSCLVADVVVFNSSFNMESFLTSIGKFLKLIPDHRPKDLESIIRPK 159
Cdd:pfam12038  81 LANCPKLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRAK 160


                  ....*
gi 1386806216 160 CQVIY 164
Cdd:pfam12038 161 SRVLY 165
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 275-386 4.81e-12

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: 65.50  E-value: 4.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 275 WPHRWEHDKDPETFLKILMSLKQLNLNFHVSVLGETFTDTPDIFSEAKKALGSSVLHWGYLPRKEDYFRVLCMADVVIST 354
Cdd:cd01635   115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLP 194

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1386806216 355 AKHEFFGVAMLEAVYCGCYPLCPKALVYPEIF 386
Cdd:cd01635   195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 267-437 6.67e-06

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: 47.92  E-value: 6.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 267 PQRPLHITWPHRWEHDKDPETFLKILMSLKQLNLNFHVSVLGETFTDTPDIfSEAKKALGSSVLHWGYLPRkEDYFRVLC 346
Cdd:cd03801   189 PPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLRAEL-EELELGLGDRVRFLGFVPD-EELPALYA 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 347 MADVVISTAKHEFFGVAMLEAVYCGCYPLCPKALVYPEIFPAEYLY-----STPEQLSKRLKSFCKRPDI---IRKHLYK 418
Cdd:cd03801   267 AADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGlvvppDDVEALADALLRLLADPELrarLGRAARE 346

                         170
                  ....*....|....*....
gi 1386806216 419 GEVAPFSWAALHGKFRSLL 437
Cdd:cd03801   347 RVAERFSWERVAERLLDLY 365
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 267-372 9.96e-06

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


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 47.59  E-value: 9.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 267 PQRPLHITWPHRWEHDKDPETFLKILMSLKQLNLNFHVSVLGETFTDTPDIFSEAKKALGSSVLHWGYlprKEDYFRVLC 346
Cdd:cd03808   186 PSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGF---RSDVPELLA 262

                          90       100
                  ....*....|....*....|....*.
gi 1386806216 347 MADVVISTAKHEFFGVAMLEAVYCGC 372
Cdd:cd03808   263 ESDVFVLPSYREGLPRSLLEAMAAGR 288
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 237-428 1.25e-05

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 46.97  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 237 NPSVHKSGSLPVSKENLPLDPSTLLC-GAedpqrplhiTWPHrwehdKDPETFLKILMSLKQLNLNFHVSVLGETFTDTP 315
Cdd:cd03809   172 DPSFFPPESAAVLIAKYLLPEPYFLYvGT---------LEPR-----KNHERLLKAFALLKKQGGDLKLVIVGGKGWEDE 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 316 DIFSEAKKALGSSVLHW-GYLPrKEDYFRVLCMADVVISTAKHEFFGVAMLEAVYCGCYPLCPKALVYPEIFPAEYLY-- 392
Cdd:cd03809   238 ELLDLVKKLGLGGRVRFlGYVS-DEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDAALYfd 316

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1386806216 393 -STPEQLSKRLKSFCKRPDIIRKHLYKG--EVAPFSWAA 428
Cdd:cd03809   317 pLDPESIADAILRLLEDPSLREELIRKGleRAKKFSWEK 355
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 277-405 3.88e-05

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 43.80  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 277 HRWEHDKDPETFLKILMSLKQLNLNFHVSVLGETFTDTPdIFSEAKKALGSSVLHW-GYLPRKE--DYFRvlcMADVVIS 353
Cdd:pfam00534   9 GRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKR-LKKLAEKLGLGDNVIFlGFVSDEDlpELLK---IADVFVL 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1386806216 354 TAKHEFFGVAMLEAVYCGCYPLCPKALVYPEIF-PAE--YLY--STPEQLSKRLKSF 405
Cdd:pfam00534  85 PSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVkDGEtgFLVkpNNAEALAEAIDKL 141
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 345-437 5.84e-04

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 39.59  E-value: 5.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 345 LCMADVVISTAKHEFFGVAMLEAVYCGCYPLCPKALVYPEI---------FPAEylysTPEQLSKRLKSFCKRPDIIRKH 415
Cdd:COG0438    18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEViedgetgllVPPG----DPEALAEAILRLLEDPELRRRL 93

                          90       100
                  ....*....|....*....|....*
gi 1386806216 416 LYKGE---VAPFSWAALHGKFRSLL 437
Cdd:COG0438    94 GEAAReraEERFSWEAIAERLLALY 118
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 265-372 1.67e-03

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 40.42  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 265 EDPQRPLHITWPHRWEHDKDPETFLKILMSLKqLNLNFHVSVLGETFTDtPDIFSEAKKALGSSVLHW-GYLPRKEDYFR 343
Cdd:cd03819   177 GLPEGKPVVGYVGRLSPEKGWLLLVDAAAELK-DEPDFRLLVAGDGPER-DEIRRLVERLGLRDRVTFtGFREDVPAALA 254

                          90       100
                  ....*....|....*....|....*....
gi 1386806216 344 vlcMADVVISTAKHEFFGVAMLEAVYCGC 372
Cdd:cd03819   255 ---ASDVVVLPSLHEEFGRVALEAMACGT 280
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
279-372 2.30e-03

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 38.26  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806216 279 WEHDKDPETFLKILMSLKQLNLNFHVSVLGEtftDTPDIFSEAKKALGSSVLHWGYLPRKEDYFRvlcMADVVISTAKHE 358
Cdd:pfam13692  11 HPNVKGVDYLLEAVPLLRKRDNDVRLVIVGD---GPEEELEELAAGLEDRVIFTGFVEDLAELLA---AADVFVLPSLYE 84

                          90
                  ....*....|....
gi 1386806216 359 FFGVAMLEAVYCGC 372
Cdd:pfam13692  85 GFGLKLLEAMAAGL 98
 
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