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Conserved domains on  [gi|504540691|ref|WP_014727793|]
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glycosyltransferase family 2 protein [Cronobacter sakazakii]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10118426)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  9445404|12691742|10508766|12200473|10521532
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 4-231 1.39e-78

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


:

Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 236.42  E-value: 1.39e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   4 RLSVVMIAKNAASLLPDCLASVAWA-DEIVVLDSGSSDDTVAVATAAGAKVFTEsDWQGYGIQRQRAQQYASGDYILMID 82
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAvDEIIVVDSGSTDRTVEIAKEYGAKVYQR-WWDGFGAQRNFALELATNDWVLSLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691  83 TDERVTPELAQAIRQVLKQPDPqAVYSIARRNLFLGRFMRHSGWYPDRVTRLYARERYRYNDNQVHESLDAPGARVVTLS 162
Cdd:cd02511   80 ADERLTPELADEILALLATDDY-DGYYVPRRNFFLGRWIRHGGWYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGIVLK 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504540691 163 GDLLHLTCRDFASFQRKQLNYATAWAQERHQQGKKVSVPGIF--GRTLAAFCKTLILRAGVLDGRQGWLLA 231
Cdd:cd02511  159 GDILHYGYKSLEEFLEKHNRYSSLEAKDLAAKGKKRSLLKGLllGRPLLAFLKMYILKRGFLDGRAGFILA 229
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 4-231 1.39e-78

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 236.42  E-value: 1.39e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   4 RLSVVMIAKNAASLLPDCLASVAWA-DEIVVLDSGSSDDTVAVATAAGAKVFTEsDWQGYGIQRQRAQQYASGDYILMID 82
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAvDEIIVVDSGSTDRTVEIAKEYGAKVYQR-WWDGFGAQRNFALELATNDWVLSLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691  83 TDERVTPELAQAIRQVLKQPDPqAVYSIARRNLFLGRFMRHSGWYPDRVTRLYARERYRYNDNQVHESLDAPGARVVTLS 162
Cdd:cd02511   80 ADERLTPELADEILALLATDDY-DGYYVPRRNFFLGRWIRHGGWYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGIVLK 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504540691 163 GDLLHLTCRDFASFQRKQLNYATAWAQERHQQGKKVSVPGIF--GRTLAAFCKTLILRAGVLDGRQGWLLA 231
Cdd:cd02511  159 GDILHYGYKSLEEFLEKHNRYSSLEAKDLAAKGKKRSLLKGLllGRPLLAFLKMYILKRGFLDGRAGFILA 229
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 2-143 2.29e-18

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 80.52  E-value: 2.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   2 RARLSVVMIAKNAASLLPDCLASVA---WAD-EIVVLDSGSSDD-----TVAVATAAGAKVFTESDWQGYGIQRQRAQQY 72
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLaqtYPDfEIIVVDDGSTDGtaeilRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504540691  73 ASGDYILMIDTDERVTPELAQAIRQVLKQPDPQAVYSiarrnlflGRFMRHSGWYPDRVT-RLYARERYRYN 143
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYG--------SRLIREGESDLRRLGsRLFNLVRLLTN 144
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-143 5.91e-13

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 65.11  E-value: 5.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691    6 SVVMIAKNAASLLPDCLASVA----WADEIVVLDSGSSDD-----TVAVATAAGAKVFTESDWQGYGIQRQRAQQYASGD 76
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLnqtyPNFEIIVVDDGSTDGtveiaEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504540691   77 YILMIDTDERVTPELAQAIRQVLKQPDPQAVY-SIARRNLFLGRFMRHSGWYPDRVTRLYARERYRYN 143
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVgSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLN 148
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 4-137 2.58e-04

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 41.44  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   4 RLSVVMIAKNAASLLPDCLASVAWA------DEIVVLDSGSSDDTVAVATAAGAKVFTESD-------WQGYGIQRQRAQ 70
Cdd:PRK13915  32 TVSVVLPALNEEETVGKVVDSIRPLlmeplvDELIVIDSGSTDATAERAAAAGARVVSREEilpelppRPGKGEALWRSL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691  71 QYASGDYILMIDTDervtpelaqairqvLKQPDPQAVYSIA----------------RRNLFLGRFMRHSGwyPDRVTRL 134
Cdd:PRK13915 112 AATTGDIVVFVDAD--------------LINFDPMFVPGLLgplltdpgvhlvkafyRRPLRVSGGVDATG--GGRVTEL 175


                 ...
gi 504540691 135 YAR 137
Cdd:PRK13915 176 VAR 178
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 4-231 1.39e-78

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 236.42  E-value: 1.39e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   4 RLSVVMIAKNAASLLPDCLASVAWA-DEIVVLDSGSSDDTVAVATAAGAKVFTEsDWQGYGIQRQRAQQYASGDYILMID 82
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAvDEIIVVDSGSTDRTVEIAKEYGAKVYQR-WWDGFGAQRNFALELATNDWVLSLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691  83 TDERVTPELAQAIRQVLKQPDPqAVYSIARRNLFLGRFMRHSGWYPDRVTRLYARERYRYNDNQVHESLDAPGARVVTLS 162
Cdd:cd02511   80 ADERLTPELADEILALLATDDY-DGYYVPRRNFFLGRWIRHGGWYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGIVLK 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504540691 163 GDLLHLTCRDFASFQRKQLNYATAWAQERHQQGKKVSVPGIF--GRTLAAFCKTLILRAGVLDGRQGWLLA 231
Cdd:cd02511  159 GDILHYGYKSLEEFLEKHNRYSSLEAKDLAAKGKKRSLLKGLllGRPLLAFLKMYILKRGFLDGRAGFILA 229
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 2-143 2.29e-18

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 80.52  E-value: 2.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   2 RARLSVVMIAKNAASLLPDCLASVA---WAD-EIVVLDSGSSDD-----TVAVATAAGAKVFTESDWQGYGIQRQRAQQY 72
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLaqtYPDfEIIVVDDGSTDGtaeilRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504540691  73 ASGDYILMIDTDERVTPELAQAIRQVLKQPDPQAVYSiarrnlflGRFMRHSGWYPDRVT-RLYARERYRYN 143
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYG--------SRLIREGESDLRRLGsRLFNLVRLLTN 144
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 7-141 6.63e-15

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 69.84  E-value: 6.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   7 VVMIAKNAASLLPDCLASVAWAD----EIVVLDSGSSDD-----TVAVATAAGAKVFTESDWQGYGIQRQRAQQYASGDY 77
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTypnfEVIVVDDGSTDGtleilEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504540691  78 ILMIDTDERVTPE-LAQAIRQVLKQPDPQAVYS----IARRNLFL---GRFMRHSGWYPDRVTRLYARERYR 141
Cdd:cd00761   81 ILFLDADDLLLPDwLERLVAELLADPEADAVGGpgnlLFRRELLEeigGFDEALLSGEEDDDFLLRLLRGGK 152
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-143 5.91e-13

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 65.11  E-value: 5.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691    6 SVVMIAKNAASLLPDCLASVA----WADEIVVLDSGSSDD-----TVAVATAAGAKVFTESDWQGYGIQRQRAQQYASGD 76
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLnqtyPNFEIIVVDDGSTDGtveiaEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504540691   77 YILMIDTDERVTPELAQAIRQVLKQPDPQAVY-SIARRNLFLGRFMRHSGWYPDRVTRLYARERYRYN 143
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVgSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLN 148
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-96 2.88e-10

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 58.08  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   1 MRARLSVVMIAKNAASLLPDCLASVA----WADEIVVLDSGSSDDTVAVATAAGA---KVFTESDWQGYGIQRQRAQQYA 73
Cdd:COG1216    1 MRPKVSVVIPTYNRPELLRRCLESLLaqtyPPFEVIVVDNGSTDGTAELLAALAFprvRVIRNPENLGFAAARNLGLRAA 80

                         90       100
                 ....*....|....*....|....
gi 504540691  74 SGDYILMIDTDERVTPE-LAQAIR 96
Cdd:COG1216   81 GGDYLLFLDDDTVVEPDwLERLLA 104
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 4-132 1.09e-08

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 54.75  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   4 RLSVVMIAKNAASLLPDCLASVAWAD------EIVVLDSGSSDD-----TVAVATAAGAKVFTESDWQGYGIQRQRAQQY 72
Cdd:COG1215   30 RVSVIIPAYNEEAVIEETLRSLLAQDypkeklEVIVVDDGSTDEtaeiaRELAAEYPRVRVIERPENGGKAAALNAGLKA 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504540691  73 ASGDYILMIDTDERVTPELAQAIRQVLKQPDPQAV--YSIARRNLflgrFMRHSGWYPDRVT 132
Cdd:COG1215  110 ARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASgaNLAFRREA----LEEVGGFDEDTLG 167
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 5-122 2.06e-06

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 47.18  E-value: 2.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   5 LSVVMIAKNAASLLPDCLASVA----WADEIVVLDSGSSDDTVAVATAAGAKVFTESdwQGYGIQRQRAQQYASGDYILM 80
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRrlnpLPLEIIVVDGGSTDGTVAIARSAGVVVISSP--KGRARQMNAGAAAARGDWLLF 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 504540691  81 IDTDERVTPELAQAIRQVLKQPDPQAVY--------SIARRNLFLGRFMR 122
Cdd:cd02522   79 LHADTRLPPDWDAAIIETLRADGAVAGAfrlrfddpGPRLRLLELGANLR 128
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 6-137 7.36e-06

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 45.61  E-value: 7.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   6 SVVMIAKNAASLLPDCLASVA---WAD-EIVVLDSGSSD---DTVAVATAAGAKVFTESDwQG-Y-----GIQRqraqqy 72
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLsqtYPNiEYIVIDGGSTDgtvDIIKKYEDKITYWISEPD-KGiYdamnkGIAL------ 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504540691  73 ASGDYILMIDTDER-VTPELAQAIRQVLKQPDPQAVYSIARRNLFLGRFMRHSGWYPDRVTRLYAR 137
Cdd:cd06433   74 ATGDIIGFLNSDDTlLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFLLYG 139
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-106 1.38e-04

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 41.39  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   7 VVMIAKNAASLLPDCLASVAWAD----EIVVLDSGSSDDTVAVATAAGAKVF--TESDWQGYGIQRQRAQQYASGDYILM 80
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTypdfEVIVVDNASTDGSVELLRELFPEVRliRNGENLGFGAGNNQGIREAKGDYVLL 80

                         90       100
                 ....*....|....*....|....*.
gi 504540691  81 IDTDERVTPELAQAIRQVLKQpDPQA 106
Cdd:cd04186   81 LNPDTVVEPGALLELLDAAEQ-DPDV 105
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 4-137 2.58e-04

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 41.44  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   4 RLSVVMIAKNAASLLPDCLASVAWA------DEIVVLDSGSSDDTVAVATAAGAKVFTESD-------WQGYGIQRQRAQ 70
Cdd:PRK13915  32 TVSVVLPALNEEETVGKVVDSIRPLlmeplvDELIVIDSGSTDATAERAAAAGARVVSREEilpelppRPGKGEALWRSL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691  71 QYASGDYILMIDTDervtpelaqairqvLKQPDPQAVYSIA----------------RRNLFLGRFMRHSGwyPDRVTRL 134
Cdd:PRK13915 112 AATTGDIVVFVDAD--------------LINFDPMFVPGLLgplltdpgvhlvkafyRRPLRVSGGVDATG--GGRVTEL 175


                 ...
gi 504540691 135 YAR 137
Cdd:PRK13915 176 VAR 178
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 4-91 3.87e-03

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 38.10  E-value: 3.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   4 RLSVVMIAKNAASLLPDCLASV---AWAD-EIVVLDSGSSDDTVAVATAAGAK-----VFTESDwQGYGIQRQRAQQYAS 74
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAFMESLiaqTWTAlEIIIVNDGSTDNSVEIAKHYAENyphvrLLHQAN-AGVSVARNTGLAVAT 85

                         90
                 ....*....|....*..
gi 504540691  75 GDYILMIDTDERVTPEL 91
Cdd:PRK10073  86 GKYVAFPDADDVVYPTM 102
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 7-84 7.48e-03

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 36.40  E-value: 7.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504540691   7 VVMIAKNAASLLPDCLASV------AWADEIVVLDSGSSDD-----TVAVATAAGAKVFTESDWQGYGIQRQRAQQYASG 75
Cdd:cd04179    1 VVIPAYNEEENIPELVERLlavleeGYDYEIIVVDDGSTDGtaeiaRELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80


                 ....*....
gi 504540691  76 DYILMIDTD 84
Cdd:cd04179   81 DIVVTMDAD 89
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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